|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
585-1321 |
0e+00 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 1036.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKV---PKG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVakmFKGcRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 740
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 741 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQ 820
Cdd:cd01386 161 LERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 821 RAVWRVLAAIYHLGAAGACK---VGRKQFMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRwGLEDEETS 897
Cdd:cd01386 241 RAIWSILAAIYHLGAAGATKaasAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQ-ESPARSSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 898 SGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGKDRAATFEELCHNYAHERLQL 977
Cdd:cd01386 320 GGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERLQL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 978 LFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQNPSQVRLPAGGGAQDARGLFWVLDEEVHVEGSSDSVVLERL 1057
Cdd:cd01386 400 LFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQQALVRSDLRDEDRRGLLWLLDEEALYPGSSDDTFLERL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1058 CAAFEKKGAGTeGSSALRTCEQPLQCEIFHQLGWDPVRYDLTGWLHRAKPNLSALDAPQVLHQSKREelrslfqaraklp 1137
Cdd:cd01386 480 FSHYGDKEGGK-GHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE------------- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1138 pvcravaglegtsqqalqrsrmvrrtfassLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESRSGQESP 1217
Cdd:cd01386 546 ------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDERSTSS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1218 PPpqpgrdkpgaGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMSTSEGIDERKAV 1297
Cdd:cd01386 596 PA----------AGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVADERKAV 665
|
730 740
....*....|....*....|....
gi 51317366 1298 EELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd01386 666 EELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
586-1321 |
2.67e-96 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 326.47 E-value: 2.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKV-----PKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVmekyrGKGRSADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVS------VEKIRATFTVLRAFGsvsmaHSRS-----ATRFSMVMSLDFNATG 729
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSssassiEQQILQSNPILEAFG-----NAKTvrndnSSRFGKFIELQFDPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 730 RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL---HQMADSSSFGMGVWSKPEDKQKAAAAFAQL 806
Cdd:cd00124 157 RLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLellLSYYYLNDYLNSSGCDRIDGVDDAEEFQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 807 QGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKqfmrfEWANYAAEALGCEYEELNTATFKhhlR 876
Cdd:cd00124 237 LDALDVLGFSDEEQDSIFRILAAILHLGniefeedeedEDSSAEVADD-----ESLKAAAKLLGVDAEDLEEALTT---R 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 877 QIIqqmtfgpsrwgLEDEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFSS--HHLSMASIMVVDSPGFQNPR 953
Cdd:cd00124 309 TIK-----------VGGETITKPLTVEQaEDARDALAKALYSRLFDWLVNRINAALSPtdAAESTSFIGILDIFGFENFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 954 HQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgtTVAVVDQNPSqvrlpagggaqda 1032
Cdd:cd00124 378 VNS------FEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFiDFPDNQD--CLDLIEGKPL------------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1033 rGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagteGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSal 1112
Cdd:cd00124 437 -GILSLLDEECLFPKGTDATFLEKLYSAHGSH-----PRFFSKKRKAKLEFGIKHYAG--DVTYDADGFLEKNKDTLP-- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1113 dapqvlhqskrEELRSLFQAraklppvcravaglegtsqqalqrsrmvrrtfasslaavrrkapCSQIKLQMDALTSMIK 1192
Cdd:cd00124 507 -----------PDLVDLLRS--------------------------------------------GSQFRSQLDALMDTLN 531
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1193 RSRLHFIHCLVPNPvvesrsgqesppppqpgrdkpgAGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQ 1272
Cdd:cd00124 532 STQPHFVRCIKPND----------------------EKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKR 589
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 51317366 1273 FQVLDAPLLKKLMSTSEgiderKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd00124 590 YRILAPGATEKASDSKK-----AAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
566-1333 |
3.41e-91 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 312.94 E-value: 3.41e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 566 NPPELDQVEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAGKvpkGRRDG-LPAHIGS 638
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPykqlpiYTDEVIKKYR---GKSRGeLPPHVFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 639 MAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRF 717
Cdd:smart00242 78 IADNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGSVEdQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 718 SMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQmadSSSFG---MGVWSK-- 792
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS---PEDYRylnQGGCLTvd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 793 -PEDKqkaaAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKQFmrfewaNYAAEALGC 861
Cdd:smart00242 235 gIDDA----EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGniefeegrndNAASTVKDKEEL------SNAAELLGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 862 EYEELNTA-TFKhhlrqiiqQMTFGpsrwgleDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMA 939
Cdd:smart00242 305 DPEELEKAlTKR--------KIKTG-------GEVITKPLNVEQAlDARDALAKALYSRLFDWLVKRINQSLSFKDGSTY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 940 SIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQ----FDLpdpspGTTVAVVD 1015
Cdd:smart00242 370 FIGVLDIYGFEIFEVNS------FEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTfidfFDN-----QDCIDLIE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1016 QNPsqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCeqplqceiF---HQLGwd 1092
Cdd:smart00242 439 KKP--------------PGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKPKKKGRTE--------FiikHYAG-- 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1093 PVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcravaglegtSQQALQRSRMVRRTFASslaavr 1172
Cdd:smart00242 495 DVTYDVTGFLEKNKDTLSD-DLIELLQSSKNPLIASLF-------------------PSGVSNAGSKKRFQTVG------ 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1173 rkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEA 1252
Cdd:smart00242 549 -----SQFKEQLNELMDTLNSTNPHFIRCIKPNE--EKKPGD--------------------FDSSLVLHQLRYLGVLEN 601
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1253 LRLHRTGYADHMGLTRFRRQFQVLDAPLLKklmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLKAGVISRLEKQR 1332
Cdd:smart00242 602 IRIRRAGFPYRLPFDEFLQRYRVLLPDTWP-----PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
.
gi 51317366 1333 E 1333
Cdd:smart00242 677 E 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
510-2086 |
2.08e-75 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 278.88 E-value: 2.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 510 WYEA-EKVWLA---QKDGFTLATVlkpdEGTADLPAGRVrlwIDADKTITEVDEEhvhraNPPELDQVEDLASLISVNES 585
Cdd:COG5022 13 WIPDeEKGWIWaeiIKEAFNKGKV----TEEGKKEDGES---VSVKKKVLGNDRI-----KLPKFDGVDDLTELSYLNEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGpsVPSAG-----KVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:COG5022 81 AVLHNLEKRYNNGQIYTYSGLVLIAVNPyRD--LGIYTddiiqSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIIS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMAGSV-DGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQ 737
Cdd:COG5022 159 GESGAGKTENAKRIMQYLASVTSSStVEISSIEkQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 738 TMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISE 817
Cdd:COG5022 239 TYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLL-LLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 818 SEQRAVWRVLAAIYHLG--AAGACKVGRKQFMRFEWANYAAEALGCEYEELNTATFKhhlRQIIQqmtfgpsrwGLEDEE 895
Cdd:COG5022 318 EEQDQIFKILAAILHIGniEFKEDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVK---RQIKT---------GGEWIV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 896 TSSGLKMTgVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERL 975
Cdd:COG5022 386 VPLNLEQA-LAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNS------FEQLCINYTNEKL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 976 QLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVL 1054
Cdd:COG5022 459 QQFFNQHMFKLEQEEYVKEGIEWSFiDYFDNQP-CIDLIEKKNPL--------------GILSLLDEECVMPHATDESFT 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1055 ERLCAAFEKKgagtegSSALRTCEQPLQCEIF--HQLGwDpVRYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQA 1132
Cdd:COG5022 524 SKLAQRLNKN------SNPKFKKSRFRDNKFVvkHYAG-D-VEYDVEGFLDKNKDPLN-DDLLELLKASTNEFVSTLFDD 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1133 RaklppvcravaglegtsQQALQRSRmvRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRS 1212
Cdd:COG5022 595 E-----------------ENIESKGR--FPTLG------------SRFKESLNSLMSTLNSTQPHYIRCIKPN---EEKS 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1213 gqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMSTSEGiD 1292
Cdd:COG5022 641 -------------------PWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTWKE-D 700
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1293 ERKAVEELLETLDLEKKAVAVGHSQVFLKAGVISRLEKQREKLVSQSIVLFQAACKGFLSRQEFKKLKIRRLAAQCIQKN 1372
Cdd:COG5022 701 TKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHG 780
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1373 VAVFLAVKDWPWWQLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEK----SEKLRNELRQNTDLLESKIADltSDLAD 1448
Cdd:COG5022 781 FRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekklRETEEVEFSLKAEVLIQKFGR--SLKAK 858
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1449 ERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQkKLGDVNKQLEeaqQKIqlndLERNPTGGADewqMRFDCaQME 1528
Cdd:COG5022 859 KRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELE---SEI----IELKKSLSSD---LIENL-EFK 926
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1529 NEFLrKRLQQCEERLDSELTARKELEQK--LGELQSAydgakkmahqlkrkchhlTCDLEDTCVLLENqqsrnhELEKKq 1606
Cdd:COG5022 927 TELI-ARLKKLLNNIDLEEGPSIEYVKLpeLNKLHEV------------------ESKLKETSEEYED------LLKKS- 980
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1607 kkfdlqlaqalgesvfEKGLREKVTQENTSVRW--ELGQLQQQLKQKEQEASQLKQQVEMLQDHKREllgspslgencva 1684
Cdd:COG5022 981 ----------------TILVREGNKANSELKNFkkELAELSKQYGALQESTKQLKELPVEVAELQSA------------- 1031
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1685 glkERLWKLESSALEQQK-IQSQQENTIKQLEQLRQRFE---LEIERmkqmhQKDREDQEEELEDVRqscqkrlhqlemQ 1760
Cdd:COG5022 1032 ---SKIISSESTELSILKpLQKLKGLLLLENNQLQARYKalkLRREN-----SLLDDKQLYQLESTE------------N 1091
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1761 LEQEYEEKQMVLhEKQDLEGLIGTLcdqighrDFDVEKRLRRDL-RRTHALLSdvqLLLGTMEDGKTSVSKEELE----K 1835
Cdd:COG5022 1092 LLKTINVKDLEV-TNRNLVKPANVL-------QFIVAQMIKLNLlQEISKFLS---QLVNTLEPVFQKLSVLQLEldglF 1160
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1836 VHSQLEQSEAKCEEALKTQKVLTADleSMHSEL--ENMTRNKSLVDE--QLYRLQFE---KADLLKRIDEDQDDLNELMQ 1908
Cdd:COG5022 1161 WEANLEALPSPPPFAALSEKRLYQS--ALYDEKskLSSSEVNDLKNEliALFSKIFSgwpRGDKLKKLISEGWVPTEYST 1238
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1909 KHKDliAQSAADIGQiqelqlqlEEAKKEKHKLQEQL-QVAQMRIEYLEQSTVDRAIVsrqeavicdlenKTEFQKVQIK 1987
Cdd:COG5022 1239 SLKG--FNNLNKKFD--------TPASMSNEKLLSLLnSIDNLLSSYKLEEEVLPATI------------NSLLQYINVG 1296
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1988 RFEVLVIRLRDSLIKMGEELSQaatseSQQRESSQYYQRRLEELKADMEELVQReaeasRRCMELEKY-VEELAAVRQTL 2066
Cdd:COG5022 1297 LFNALRTKASSLRWKSATEVNY-----NSEELDDWCREFEISDVDEELEELIQA-----VKVLQLLKDdLNKLDELLDAC 1366
|
1610 1620
....*....|....*....|.
gi 51317366 2067 QTDLETSIRRI-ADLQAALEE 2086
Cdd:COG5022 1367 YSLNPAEIQNLkSRYDPADKE 1387
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
573-1321 |
4.07e-71 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 253.74 E-value: 4.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 573 VEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvpkgRRDGLPAHIGSMAQRAY 644
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPykqlpiYSEDMIKAyrGK----RRGELPPHIFAIADEAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 645 WALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVD----GRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMV 720
Cdd:pfam00063 77 RSMLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSagnvGRLE-EQILQSNPILEAFGNAKTVRNNNSSRFGKY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 721 MSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGM-GVWSKP 793
Cdd:pfam00063 156 IEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyHYLSQSGCYTIdGIDDSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 794 EDKqkaaaafaQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQfmrfEWANYAAEALGCEYEEL 866
Cdd:pfam00063 236 EFK--------ITDKAMDILGFSDEEQMGIFRIVAAILHLGniefkkeRNDEQAVPDDT----ENLQKAASLLGIDSTEL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 867 NTATFKhhlRQIiqqmtfgpsrwgledeETSSGLKMTGVDC------VEGMASGLYQELFAAVVSLINRSFSSHHLSMAS 940
Cdd:pfam00063 304 EKALCK---RRI----------------KTGRETVSKPQNVeqanyaRDALAKAIYSRLFDWLVDRINKSLDVKTIEKAS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 941 -IMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgtTVAVV 1014
Cdd:pfam00063 365 fIGVLDIYGFEifekN----------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFiDFGDNQP--CIDLI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1015 DQNPsqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEK----KGAGTEGSSALRtceqplqceIFHQLG 1090
Cdd:pfam00063 433 EKKP--------------LGILSLLDEECLFPKATDQTFLDKLYSTFSKhphfQKPRLQGETHFI---------IKHYAG 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1091 wdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFQARAKlppvcRAVAGLEGTSQQALQRSRMVRRTFASslaa 1170
Cdd:pfam00063 490 --DVEYNVEGFLEKNKDPLND-DLVSLLKSSSDPLLAELFPDYET-----AESAAANESGKSTPKRTKKKRFITVG---- 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1171 vrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHIL 1250
Cdd:pfam00063 558 -------SQFKESLGELMKTLNSTNPHYIRCIKPNE--KKRAGV--------------------FDNSLVLHQLRCNGVL 608
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51317366 1251 EALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMStsegiDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:pfam00063 609 EGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKG-----DAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
585-1321 |
4.49e-53 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 200.00 E-value: 4.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAGKVP---KGRRDGLPAHIGSMAQRAYWALLN----QRRDQS 655
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKsiPDLYSEERMLlyhGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 656 IVALGWSGAGKT-------------TCCEQVLEHLVGMAGSVDGRVSV----EKIRATFTVLRAFGSVSMAHSRSATRFS 718
Cdd:cd14890 81 IIISGESGAGKTeatkiimqylariTSGFAQGASGEGEAASEAIEQTLgsleDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 719 MVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEDKq 797
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLrGECSSIPSCDD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 798 kaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRkQFMRFewanyAAEALGCEYEELN 867
Cdd:cd14890 240 --AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGnvdfesendtTVLEDATTL-QSLKL-----AAELLGVNEDALE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 868 TATFKHHL----RQIIQQMTFGPSRwgledeetssglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMV 943
Cdd:cd14890 312 KALLTRQLfvggKTIVQPQNVEQAR-----------------DKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 944 VDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDqNPSQVRL 1023
Cdd:cd14890 375 LDIYGFEKFEWN------TFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQY----------ITFND-NQACLEL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1024 PAGGGAQDArGLFWVLDEEVHVEGS-SDSVVLERLCAAFekkGAGTEGSSALRTCEQ------P-----LQCEIFHQLGw 1091
Cdd:cd14890 438 IEGKVNGKP-GIFITLDDCWRFKGEeANKKFVSQLHASF---GRKSGSGGTRRGSSQhphfvhPkfdadKQFGIKHYAG- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1092 dPVRYDLTGWLHRAKPNLSAldapqvlhqskreELRSLfqaraklppvcravaglegtsqqalqrsrmvrrtFASSLAAV 1171
Cdd:cd14890 513 -DVIYDASGFNEKNNETLNA-------------EMKEL----------------------------------IKQSRRSI 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1172 RRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILE 1251
Cdd:cd14890 545 REVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKA----------------------PGKFDGLDCLRQLKYSGMME 602
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51317366 1252 ALRLHRTGYA---DHmglTRFRRQFQVLDapllkklmSTSEGIDErkAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14890 603 AIQIRQQGFAlreEH---DSFFYDFQVLL--------PTAENIEQ--LVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
585-1321 |
4.11e-50 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 190.99 E-value: 4.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVP----SAGKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPY-KNLPiyseNIIEMYRGKkRHEMPPHIYAISESAYRCMLQDREDQSILCT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMA--------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRI 731
Cdd:cd14920 80 GESGAGKTENTKKVIQYLAHVAsshkgrkdHNIPGELERQLLQAN-PILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 732 TAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLHQMADSSSFgMGVWSKPEDKQKAAAAFAQLQGAME 811
Cdd:cd14920 159 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDL-LLEGFNNYRF-LSNGYIPIPGQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 812 MLGISESEQRAVWRVLAAIYHLGAAGACKvGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsRWGL 891
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKL-CHLLGMNVMEFTRAI--LTPRIKVG--RDYV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 892 EDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEELCHNY 970
Cdd:cd14920 311 QKAQTKEQADFA----VEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFE------IFELNSFEQLCINY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 971 AHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEG 1047
Cdd:cd14920 381 TNEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIDLIERPANPP--------------GVLALLDEECWFPK 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1048 SSDSVVLERLcaafekkgAGTEGS-SALRTCEQP---LQCEIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLHQS 1121
Cdd:cd14920 446 ATDKTFVEKL--------VQEQGShSKFQKPRQLkdkADFCIIHYAG--KVDYKADEWLMK---NMDPLndNVATLLHQS 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1122 KREELRSLFQARAKLPPVCRAVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHC 1201
Cdd:cd14920 513 SDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVG------------QLYKESLTKLMATLRNTNPNFVRC 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1202 LVPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLL 1281
Cdd:cd14920 581 IIPNH--EKRAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 638
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 51317366 1282 KKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14920 639 PKGF-----MDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
586-1276 |
1.07e-49 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 189.45 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAgkvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPfkdvplYGNEFITA----YRQKLLDSPHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMAGSVDGrvsVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQT 738
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGGGSSG---IEnEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 739 MLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISES 818
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNL-KSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 819 EQRAVWRVLAAIYHLG--------AAGACKVGRKqfmrfEWANYAAEALGCEYEELNTATFKHHLRqiiqqmtfgpsrwg 890
Cdd:cd01383 234 DQEHIFQMLAAVLWLGnisfqvidNENHVEVVAD-----EAVSTAASLLGCNANDLMLALSTRKIQ-------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 891 LEDEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRSF-SSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 968
Cdd:cd01383 295 AGGDKIVKKLTLQqAIDARDALAKAIYASLFDWLVEQINKSLeVGKRRTGRSISILDIYGFESFQKN------SFEQLCI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 969 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdlpdpspgTTVAVVDqNPSQVRL----PAgggaqdarGLFWVLDEEVH 1044
Cdd:cd01383 369 NYANERLQQHFNRHLFKLEQEEYELDGIDW----------TKVDFED-NQECLDLiekkPL--------GLISLLDEESN 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1045 VEGSSDSVVLERL--------CAAFEKKGAGTegssalrtceqplqceIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQ 1116
Cdd:cd01383 430 FPKATDLTFANKLkqhlksnsCFKGERGGAFT----------------IRHYAG--EVTYDTSGFLEKNRDLLHS-DLIQ 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1117 VLHQSKreelRSLFQARAklppvcravAGLEGTSQQALQRSRMvrrtfasSLAAVRRKAPCSQIKLQMDALTSMIKRSRL 1196
Cdd:cd01383 491 LLSSCS----CQLPQLFA---------SKMLDASRKALPLTKA-------SGSDSQKQSVATKFKGQLFKLMQRLENTTP 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1197 HFIHCLVPNPV-VESRSGQEsppppqpgrdkpgaggpLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQV 1275
Cdd:cd01383 551 HFIRCIKPNNKqLPGVFDQD-----------------LVLQ------QLRCCGVLEVVRISRSGYPTRMTHQEFARRYGF 607
|
.
gi 51317366 1276 L 1276
Cdd:cd01383 608 L 608
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
586-1278 |
5.00e-47 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 182.46 E-value: 5.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAGKVPKGRRD-----GLPAHIGSMAQRAYWALL-------NQRRD 653
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPF-KHIPGLYDLHKYREEmpgwtALPPHVFSIAEGAYRSLRrrlhepgASKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 654 QSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDF 725
Cdd:cd14895 81 QTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGsellsanpILESFGNARTLRNDNSSRFGKFVRMFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 726 -----NATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMA--DSSSFGMGVWSKPEDKQK 798
Cdd:cd14895 161 eghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGQCYQRNDGVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 799 AAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG------------------AAGACKVGR---KQFMRFEWANYAAE 857
Cdd:cd14895 241 DDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvlfvassedegeedngaASAPCRLASaspSSLTVQQHLDIVSK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 858 ALGCEYEELNTATFKhhlRQIiqqmtfgpsrwGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLIN-----RSF 931
Cdd:cd14895 321 LFAVDQDELVSALTT---RKI-----------SVGGETFHANLSLAQCgDARDAMARSLYAFLFQFLVSKVNsaspqRQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 932 SSHHLSMAS------IMVVDSPGFQnprhqgKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP-VQFDLPD 1004
Cdd:cd14895 387 ALNPNKAANkdttpcIAVLDIFGFE------EFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKwNAVDYED 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1005 PSpgTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGagteGSSALRTCEQPLQCE 1084
Cdd:cd14895 461 NS--VCLEMLEQRPS--------------GIFSLLDEECVVPKGSDAGFARKLYQRLQEHS----NFSASRTDQADVAFQ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1085 IFHQLGwdPVRYDLTGWL--HRAKPNLSALDapqVLHQSKREELRSLfqaraklppvCRAVAGLEgTSQQALQRSRMVRR 1162
Cdd:cd14895 521 IHHYAG--AVRYQAEGFCekNKDQPNAELFS---VLGKTSDAHLREL----------FEFFKASE-SAELSLGQPKLRRR 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1163 TfaSSLAAVrrkAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRV 1242
Cdd:cd14895 585 S--SVLSSV---GIGSQFKQQLASLLDVVQQTQTHYIRCIKPND--ESASDQ--------------------FDMAKVSS 637
|
730 740 750
....*....|....*....|....*....|....*.
gi 51317366 1243 QLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDA 1278
Cdd:cd14895 638 QLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVA 673
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
586-1206 |
1.03e-45 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 177.58 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSV-----------PSAGKVPkgrrdglpaHIGSMAQRAYWALLNQRR 652
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPfkTIPGLysdemllkfiqPSISKSP---------HVFSTASSAYQGMCNNKK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 653 DQSIVALGWSGAGKTTCCEQVLEHLVgMAGSVD--GRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT- 728
Cdd:cd14888 73 SQTILISGESGAGKTESTKYVMKFLA-CAGSEDikKRSLVEaQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 729 --------GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGL-------------DLDLRTELNLHQMA-DSSSFG 786
Cdd:cd14888 152 skrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAreakntglsyeenDEKLAKGADAKPISiDMSSFE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 787 MGVWSKPEDKQKAAAAFA--------QLQGAMEMLGISESEQRAVWRVLAAIYHLG-----AAGACKVGRK-QFMRFEWA 852
Cdd:cd14888 232 PHLKFRYLTKSSCHELPDvddleefeSTLYAMQTVGISPEEQNQIFSIVAAILYLGnilfeNNEACSEGAVvSASCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 853 NYAAEALGCEYEEL-NTATFkhhlRQIIQQmtfgpsrwgleDEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRS 930
Cdd:cd14888 312 EKVASLLGVDAEDLlNALCY----RTIKTA-----------HEFYTKPLRVDeAEDVRDALARALYSCLFDKVVERTNES 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 931 FS-SHHLSMASIMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQFdl 1002
Cdd:cd14888 377 IGySKDNSLLFCGVLDIFGFEcfqlN----------SFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIswnPLDF-- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1003 pdPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTceQPLQ 1082
Cdd:cd14888 445 --PDNQDCVDLLQEKPL--------------GIFCMLDEECFVPGGKD----QGLCNKLCQKHKGHKRFDVVKT--DPNS 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1083 CEIFHQLGwdPVRYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQAraklppvcravaglegtsqqalqrsrMVRR 1162
Cdd:cd14888 503 FVIVHFAG--PVKYCSDGFLEKNKDQLS-VDAQEVIKNSKNPFISNLFSA--------------------------YLRR 553
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 51317366 1163 TFASSLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNP 1206
Cdd:cd14888 554 GTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNS 597
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
585-1321 |
1.88e-45 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 176.75 E-value: 1.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVP---------SAGKvpkgRRDGLPAHIGSMAQRAYWALLNQRRDQS 655
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTGSILVAVNPY-KELPiytqdivkqYFGK----RMGALPPHIFALAEAAYTNMQEDGKNQS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 656 IVALGWSGAGKTTCCEQVLEHLVgmagSVDGRVS-VE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 733
Cdd:cd14883 76 VIISGESGAGKTETTKLILQYLC----AVTNNHSwVEqQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 734 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAG--LDLDLRTELNLHQMAD------SSSFGMGVWSKPEDkqkaaaaFAQ 805
Cdd:cd14883 152 AIIQDYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDyhylnqSGCIRIDNINDKKD-------FDH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 806 LQGAMEMLGISESEQRAVWRVLAAIYHLG--AAGACKVGRKQFMRFEWANYAAEA--LGCEYEELNTA-TFKHhlRQIIQ 880
Cdd:cd14883 225 LRLAMNVLGIPEEMQEGIFSVLSAILHLGnlTFEDIDGETGALTVEDKEILKIVAklLGVDPDKLKKAlTIRQ--INVRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 881 QMTFGPsrwgledeetssgLKMT-GVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdr 959
Cdd:cd14883 303 NVTEIP-------------LKVQeARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVN---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 960 aaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQF-------DLPDPSPgttvavvdqnpsqvrlpaggga 1029
Cdd:cd14883 366 --SFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGInwsHIVFtdnqeclDLIEKPP---------------------- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1030 qdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQceifHQLGwdPVRYDLTGWLHRAKPNL 1109
Cdd:cd14883 422 ---LGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVK----HYAG--EVTYTVQGFLDKNKDTQ 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1110 SaLDAPQVLHQSKREELRSLFQARAKLPPVCRAVAGLEGTSQqalqrsrmvRRTfasslaavRRKAP--CSQIKLQMDAL 1187
Cdd:cd14883 493 Q-DDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTS---------RGT--------SKGKPtvGDTFKHQLQSL 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1188 TSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLT 1267
Cdd:cd14883 555 VDVLSATQPWYVRCIKPNSLKE----------------------PNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFK 612
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 51317366 1268 RFRRQFQVLDapllkKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14883 613 EFVDRYLCLD-----PRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
585-1321 |
1.89e-45 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 177.09 E-value: 1.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVP---KG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMeryKGiKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGS-----------------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSL 723
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavphpavnpavLIGELEQQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 724 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPedKQKAAAAF 803
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVP--GVDDYAEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 804 AQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEyeelNTATFK--HHLRQIIQQ 881
Cdd:cd14911 238 QATVKSMNIMGMTSEDFNSIFRIVSAVLLFGS-----------MKFRQERNNDQATLPD----NTVAQKiaHLLGLSVTD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 882 MT--FGPSRWGL-EDEETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgK 957
Cdd:cd14911 303 MTraFLTPRIKVgRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASfIGILDMAGFE------I 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 958 DRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPgtTVAVVDQnpsqvrlpagggaqdARG 1034
Cdd:cd14911 377 FELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwkfIDFGL-DLQP--TIDLIDK---------------PGG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1035 LFWVLDEEVHVEGSSDSVVLERLCAA------FEKkgAGTEGSSALrtceqplqcEIFHQLGwdPVRYDLTGWLHRakpN 1108
Cdd:cd14911 439 IMALLDEECWFPKATDKTFVDKLVSAhsmhpkFMK--TDFRGVADF---------AIVHYAG--RVDYSAAKWLMK---N 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1109 LSALDapqvlhqskrEELRSLFQArAKLPPVCR--AVAGLEGTSQQALQRSRMVRRTFASSLAAVrrkapcSQI-KLQMD 1185
Cdd:cd14911 503 MDPLN----------ENIVSLLQG-SQDPFVVNiwKDAEIVGMAQQALTDTQFGARTRKGMFRTV------SHLyKEQLA 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1186 ALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgAGGPLALDipalrvQLAGFHILEALRLHRTGYADHMG 1265
Cdd:cd14911 566 KLMDTLRNTNPNFVRCIIPNH--EKRAGK--------------IDAPLVLD------QLRCNGVLEGIRICRQGFPNRIP 623
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 51317366 1266 LTRFRRQFQVLDAPLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14911 624 FQEFRQRYELLTPNVIPKGF-----MDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
586-1318 |
4.85e-45 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 175.35 E-value: 4.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPS--AGKVPKGrrdgLPAHIGSMAQRAYWALLNQRRDQSIV 657
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPfkrlplYTPTVMDqyMHKGPKE----MPPHTYNIADDAYRAMIVDAMNQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 658 ALGWSGAGKTTCCEQVLEHLVGMAGSVDGrvsVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQL 736
Cdd:cd14872 78 ISGESGAGKTEATKQCLSFFAEVAGSTNG---VEqRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 737 QTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNlhqmaDSSSFGMGVWSKPEDKQKAAAAF--AQLQGAMEMLG 814
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWG-----SSAAYGYLSLSGCIEVEGVDDVAdfEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 815 ISESEQRAVWRVLAAIYHLG------AAGACKVGRKQFMRFEWANYAAEALGCEYEELNTAtFKHHLRQIIQQmtfGPSR 888
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGniefasGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEA-LTSRLMEIKGC---DPTR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 889 WGLEDEEtssglkmtGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQ----NprhqgkdraaTF 963
Cdd:cd14872 306 IPLTPAQ--------ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTfIGVLDIFGFEifekN----------SF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 964 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPSQVRLPAGGGaqdarGLFWVLDEEV 1043
Cdd:cd14872 368 EQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFE----------HIDFIDNQPVLDLIEKKQP-----GLMLALDDQV 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1044 HVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKR 1123
Cdd:cd14872 433 KIPKGSD----ATFMIAANQTHAAKSTFVYAEVRTSRTEFIVKHYAG--DVTYDITGFLEKNKDTLQK-DLYVLLSSSKN 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1124 EELRSLFqaraklPPvcraVAGLEGTSQQALqrsrmvrrtfasslaavrrkapCSQIKLQMDALTSMIKRSRLHFIHCLV 1203
Cdd:cd14872 506 KLIAVLF------PP----SEGDQKTSKVTL----------------------GGQFRKQLSALMTALNATEPHYIRCVK 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1204 PNpvvesrsgqesppppQPGRDKPGAGgplALDIPALRvqLAGfhILEALRLHRTGYAdhmgltrFR---RQFQVLDAPL 1280
Cdd:cd14872 554 PN---------------QEKRARLFDG---FMSLEQLR--YAG--VFEAVKIRKTGYP-------FRyshERFLKRYRFL 604
|
730 740 750
....*....|....*....|....*....|....*...
gi 51317366 1281 LKKlMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQV 1318
Cdd:cd14872 605 VKT-IAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRV 641
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
585-1277 |
8.45e-45 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 174.58 E-value: 8.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAG---KVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQwlPELYTEEqhsKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMAGSVDgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLN-DSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQ---------------MADSSSFgmgvwskpedkqkaaaafA 804
Cdd:cd14903 160 LLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANecaytganktikiegMSDRKHF------------------A 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 805 QLQGAMEMLGISESEQRAVWRVLAAIYHLGAA-----------GACKVGRkqfmrfEWANYAAEALGCEYEELNTATFKH 873
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLqiqskpnddekSAIAPGD------QGAVYATKLLGLSPEALEKALCSR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 874 HLRQIIQQMTFgpsrwGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPR 953
Cdd:cd14903 296 TMRAAGDVYTV-----PLKKDQAE--------DCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 954 HQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP-VQFDLPDPSpgTTVAVVdqnpsqvrlpagggaQDA 1032
Cdd:cd14903 363 HN------SFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRwAHIDFADNQ--DVLAVI---------------EDR 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1033 RGLFWVLDEEV-HVEGSSDSVVLeRLCAAFEKKGAGTEGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAK----P 1107
Cdd:cd14903 420 LGIISLLNDEVmRPKGNEESFVS-KLSSIHKDEQDVIEFPRTSRT-----QFTIKHYAG--PVTYESLGFLEKHKdallP 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1108 NLSALdapqvLHQSKREELRSLFQARaklppvcravAGLEGTSQQALQRSRMVRRTFASSLAAVRrkapcSQIKLQMDAL 1187
Cdd:cd14903 492 DLSDL-----MRGSSKPFLRMLFKEK----------VESPAAASTSLARGARRRRGGALTTTTVG-----TQFKDSLNEL 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1188 TSMIKRSRLHFIHCLVPNPvvesrsgqesppppqpgrdkpgAGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLT 1267
Cdd:cd14903 552 MTTIRSTNVHYVRCIKPNS----------------------IKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHE 609
|
730
....*....|
gi 51317366 1268 RFRRQFQVLD 1277
Cdd:cd14903 610 EFLDKFWLFL 619
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
585-1321 |
1.78e-44 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 174.05 E-value: 1.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVP---KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVdmyKGKkRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGS--------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRIT 732
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASShkgkkdtsITGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 733 AAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkAAAAFAQLQGAMEM 812
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQ--DDEMFQETLEAMSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 813 LGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsrwglE 892
Cdd:cd14921 238 MGFSEEEQLSILKVVSSVLQLGNI-VFKKERNTDQASMPDNTAAQKV-CHLMGINVTDFTRSI--LTPRIKVG------R 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 893 DEETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIM-VVDSPGFQnprhqgKDRAATFEELCHNYA 971
Cdd:cd14921 308 DVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFE------IFEVNSFEQLCINYT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 972 HERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGS 1048
Cdd:cd14921 382 NEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIELIERPNNPP--------------GVLALLDEECWFPKA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1049 SDSVVLERLCaafEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLHQSKREEL 1126
Cdd:cd14921 447 TDKSFVEKLC---TEQGNHPKFQKPKQLKDKTEFS-IIHYAG--KVDYNASAWLTK---NMDPLndNVTSLLNASSDKFV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1127 RSLFQARAKlppvcraVAGLEgtsqqalQRSRMVRRTFASslAAVRRKAPCSQI----KLQMDALTSMIKRSRLHFIHCL 1202
Cdd:cd14921 518 ADLWKDVDR-------IVGLD-------QMAKMTESSLPS--ASKTKKGMFRTVgqlyKEQLGKLMTTLRNTTPNFVRCI 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1203 VPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1282
Cdd:cd14921 582 IPNH--EKRSGK--------------------LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIP 639
|
730 740 750
....*....|....*....|....*....|....*....
gi 51317366 1283 KLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14921 640 KGF-----MDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
582-1320 |
2.14e-44 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 173.50 E-value: 2.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 582 VNESSVLNTLLQRYKAQLLHTCTGPD-LIVLQP--RGPSV--PSAGK-------VPKGRRDGLPAHIGSMAQRAYWALLN 649
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPykYLSSNsdASLGEygseyydTTSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 650 QRRDQSIVALGWSGAGKTTCCEQVLEHLVGM-AGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 728
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 729 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHqmaDSSSFGMGvWS--------KP--EDkqk 798
Cdd:cd14879 161 GRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLD---DPSDYALL-ASygchplplGPgsDD--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 799 aAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVgrkqfmrfewANY-----AAEALGCEY 863
Cdd:cd14879 234 -AEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGnleftydhegGEESAVV----------KNTdvldiVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 864 EELNTA-TFKhhlrqiiqqmtfgpsrwgledeetssgLKMTGVDCVEGM-------------ASGLYQELFAAVVSLINR 929
Cdd:cd14879 303 EDLETSlTYK---------------------------TKLVRKELCTVFldpegaaaqrdelARTLYSLLFAWVVETINQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 930 SFSSHHLSMAS-IMVVDSPGFQNprhQGKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdlPDPSpg 1008
Cdd:cd14879 356 KLCAPEDDFATfISLLDFPGFQN---RSSTGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSV----PATS-- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1009 ttvaVVDqNPSQVRLPAGGGAqdarGLFWVLDEEV-HVEGSSDSVVLERLCAAFEKK-------GAGTEGSSALRTceqp 1080
Cdd:cd14879 427 ----YFD-NSDCVRLLRGKPG----GLLGILDDQTrRMPKKTDEQMLEALRKRFGNHssfiavgNFATRSGSASFT---- 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1081 lqceIFHQLGwdPVRYDLTGWLHRakpNLSALDApqvlhqskreELRSLfqaraklppvcravagLEGTSQqalqrsrmv 1160
Cdd:cd14879 494 ----VNHYAG--EVTYSVEGFLER---NGDVLSP----------DFVNL----------------LRGATQ--------- 529
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1161 rrtFASSLaavrrkapcsqiklqmDALTSMIKRSRLHFIHCLVPNPvvesrsgqeSPPPPQPGRDKpgaggplaldipaL 1240
Cdd:cd14879 530 ---LNAAL----------------SELLDTLDRTRLWSVFCIRPND---------SQLPNSFDKRR-------------V 568
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1241 RVQLAGFHILEALRLHRTGYADHMGLTRFrrqfqvldaplLKKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFL 1320
Cdd:cd14879 569 KAQIRSLGLPELAARLRVEYVVSLEHAEF-----------CERYKSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
586-1130 |
7.26e-44 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 171.41 E-value: 7.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAGKVPKGR------RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKP-LPIFDKKHHEEysnlsvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMAGSVDGRVsVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSDL-LDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL-----HQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLG 814
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLedpdcHRILRDDNRNRPVFNDSEELEYYRQMFHDLTNIMKLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 815 ISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRFE---WANYAAEALGCEYEELNTAtfkhhlrqIIQQMTFgpsrwgL 891
Cdd:cd14897 240 FSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVAdeyPLHAVAKLLGIDEVELTEA--------LISNVNT------I 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 892 EDEETSSGLKM-TGVDCVEGMASGLYQELFAAVVSLINRSFSSHHL-----SMASIMVVDSPGFQNPRHQGkdraatFEE 965
Cdd:cd14897 306 RGERIQSWKSLrQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDfqimtRGPSIGILDMSGFENFKINS------FDQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 966 LCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfDLPDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHV 1045
Cdd:cd14897 380 LCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR-DIEYHDNDDVLELFFKKPL--------------GILPLLDEESTF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1046 EGSSDSVVLERLcaafEKKGagteGSSALRTCEQPLQCE--IFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKR 1123
Cdd:cd14897 445 PQSTDSSLVQKL----NKYC----GESPRYVASPGNRVAfgIRHYAE--QVTYDADGFLEKNRDNLSS-DIVGCLLNSNN 513
|
....*..
gi 51317366 1124 EELRSLF 1130
Cdd:cd14897 514 EFISDLF 520
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
586-1321 |
9.84e-44 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 171.49 E-value: 9.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvpkgRRDGLPAHIGSMAQRAYWALLNQRRDQSIV 657
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPykrlpiYTEEVIDKykGK----RREEMPPHIFAIADNAYRNMLQDRENQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 658 ALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATF--------TVLRAFGSVSMAHSRSATRFSMVMSLDFNATG 729
Cdd:cd01377 78 ITGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKGTLedqilqanPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 730 RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGM-------GVWSKPEDKqkaaaa 802
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSqgeltidGVDDAEEFK------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 803 faQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRF---EWANYAAEALGCEYEELNTATFKHHL---R 876
Cdd:cd01377 232 --LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELdgtEEADKAAHLLGVNSSDLLKALLKPRIkvgR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 877 QIIQQmtfgpsrwgledeetssGLKMTGVDC-VEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQ----N 951
Cdd:cd01377 310 EWVTK-----------------GQNKEQVVFsVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 952 prhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVD--QNPSQvrlp 1024
Cdd:cd01377 373 ----------SFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfglDLQ--------PTIDliEKPNM---- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1025 agggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtegsSALRTCEQPLQCE----IFHQLGwdPVRYDLTG 1100
Cdd:cd01377 431 ---------GILSILDEECVFPKATDKTFVEKLYSNHLGK-------SKNFKKPKPKKSEahfiLKHYAG--DVEYNIDG 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1101 WLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcrAVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQI 1180
Cdd:cd01377 493 WLEKNKDPLNE-NVVALLKKSSDPLVASLF-----------KDYEESGGGGGKKKKKGGSFRTVS------------QLH 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1181 KLQMDALTSMIKRSRLHFIHCLVPNpvvESRsgqesppppQPGR-DKpgaggPLALDipalrvQLA--GfhILEALRLHR 1257
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPN---EEK---------KPGKiDA-----PLVLH------QLRcnG--VLEGIRICR 603
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51317366 1258 TGYADHMGLTRFRRQFQVLDAPLLKKlmstseGIDERKAVEELLETLDLEKKAV-AVGHSQVFLK 1321
Cdd:cd01377 604 KGFPNRIIFAEFKQRYSILAPNAIPK------GFDDGKAACEKILKALQLDPELyRIGNTKVFFK 662
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
588-1321 |
4.34e-43 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 169.56 E-value: 4.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 588 LNTLLQRYKAQLLHTCTGPDLIVLQPRG--------PSVPSAGKVPKGRRDGLPaHIGSMAQRAYWAL----LNQRRDQS 655
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPYKsipllydvPGFDSQRKEEATASSPPP-HVFSIAERAYRAMkgvgKGQGTPQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 656 IVALGWSGAGKTTCCEQVLEHLV-------GMAGSVDGRVSVEKIRATF----TVLRAFGSVSMAHSRSATRFSMVMSLD 724
Cdd:cd14892 83 IVVSGESGAGKTEASKYIMKYLAtasklakGASTSKGAANAHESIEECVllsnLILEAFGNAKTIRNDNSSRFGKYIQIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 725 FNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSFGMGVWSKPEDKQKAAAAFA 804
Cdd:cd14892 163 YNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALEL-TPAESFLFLNQGNCVEVDGVDDATEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 805 QLQGAMEMLGISESEQRAVWRVLAAIYHLGAAgackvgrkqfmRFEwANYAAEALGCEYEELNTATFKHHLRQIIQQMTF 884
Cdd:cd14892 242 QLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNV-----------RFE-ENADDEDVFAQSADGVNVAKAAGLLGVDAAELM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 885 GPSRWgledEETSSG------LKMTGVDCVE---GMASGLYQELFAAVVSLINRSFSSH----HLSMAS------IMVVD 945
Cdd:cd14892 310 FKLVT----QTTSTArgsvleIKLTAREAKNaldALCKYLYGELFDWLISRINACHKQQtsgvTGGAASptfspfIGILD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 946 SPGFQN-PRHqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQFDlpDPSPgtTVAVVDQNPSqv 1021
Cdd:cd14892 386 IFGFEImPTN-------SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIdvsAIEFQ--DNQD--CLDLIQKKPL-- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1022 rlpagggaqdarGLFWVLDEEVHV-EGSSDSVVLERLCAAFEKKGAgtegssalrTCEQP-LQCEIF---HQLGwdPVRY 1096
Cdd:cd14892 453 ------------GLLPLLEEQMLLkRKTTDKQLLTIYHQTHLDKHP---------HYAKPrFECDEFvlrHYAG--DVTY 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1097 DLTGWLhrAKPNLSaldapqvLHqskrEELRSLfqaraklppvcravaglegtsqqaLQRSRMVRRtfasslaavrrkap 1176
Cdd:cd14892 510 DVHGFL--AKNNDN-------LH----DDLRDL------------------------LRSSSKFRT-------------- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1177 csqiklQMDALTSMIKRSRLHFIHCLVPNPVvesrsgqespppPQPGrdkpGAGGPLALDipalrvQLAGFHILEALRLH 1256
Cdd:cd14892 539 ------QLAELMEVLWSTTPSYIKCIKPNNL------------KFPG----GFSCELVRD------QLIYSGVLEVVRIR 590
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51317366 1257 RTGYADHMGLTRFRRQFQVLDAPLLKKLMS--TSEGIDERKAVeELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14892 591 REGFPIRRQFEEFYEKFWPLARNKAGVAASpdACDATTARKKC-EEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
632-1321 |
1.69e-42 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 167.72 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 632 LPAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVgmAGSVDGRVSVEKIR----ATFTVLRAFGSVS 707
Cdd:cd01378 52 VPPHVFALADSAYRNMKSEKENQCVIISGESGAGKTEASKRIMQYIA--AVSGGSESEVERVKdmllASNPLLEAFGNAK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 708 MAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQ--------- 778
Cdd:cd01378 130 TLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRpeqyyyysk 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 779 --------MADSSSFgmgvwskpedkqkaaaafAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGR 843
Cdd:cd01378 210 sgcfdvdgIDDAADF------------------KEVLNAMKVIGFTEEEQDSIFRILAAILHLGniqfaedEEGNAAISD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 844 KQFMRFewanyAAEALGCEYEELNTA-TFkhhlRQIIqqmtfgpSRWGlEDEETSSGLKMTGVDCV-EGMASGLYQELFA 921
Cdd:cd01378 272 TSVLDF-----VAYLLGVDPDQLEKAlTH----RTIE-------TGGG-GRSVYEVPLNVEQAAYArDALAKAIYSRLFD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 922 AVVSLINRSFSSHHLSMASIM-VVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---P 997
Cdd:cd01378 335 WIVERINKSLAAKSGGKKKVIgVLDIYGFEIFEKNS------FEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIewtP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 998 VQF-------DLpdpspgttvavVDQNPsqvrlpagggaqdaRGLFWVLDEEVHVEG-SSDSVVLERLCAAFEKKGAGTE 1069
Cdd:cd01378 409 IKYfnnkiicDL-----------IEEKP--------------PGIFAILDDACLTAGdATDQTFLQKLNQLFSNHPHFEC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1070 GSSALrtcEQPLQC-EIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcravagLEG 1148
Cdd:cd01378 464 PSGHF---ELRRGEfRIKHYAG--DVTYNVEGFLDKNKDLLFK-DLKELMQSSSNPFLRSLF---------------PEG 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1149 TSQQALQRSrmvrrTFASslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRSgqesppppqpgrdkpg 1228
Cdd:cd01378 523 VDLDSKKRP-----PTAG-----------TKFKNSANALVETLMKKQPSYIRCIKPN---DNKS---------------- 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1229 aggPLALDIPALRVQLAGFHILEALRLHRTGYAdhmgltrFRRQFqvlDAPLLK-KLMS--TS---EGIDeRKAVEELLE 1302
Cdd:cd01378 568 ---PGEFDEELVLHQVKYLGLLENVRVRRAGFA-------YRQTY---EKFLERyKLLSpkTWpawDGTW-QGGVESILK 633
|
730
....*....|....*....
gi 51317366 1303 TLDLEKKAVAVGHSQVFLK 1321
Cdd:cd01378 634 DLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
586-1205 |
1.59e-41 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 164.37 E-value: 1.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSV---PSAGKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGiytEEHSRLYRGAkRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 662 SGAGKTTCCEQVLEHLVGMaGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLL 741
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 742 EKSRVARQPEGESNFLVFSQMLAGLDLDLRTE---LNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISES 818
Cdd:cd01379 161 EKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGFTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 819 EQRAVWRVLAAIYHLG-------AAGACKVGRKQFMRFEWANYAAEALGCEYEElntatfkhhlrqiiqqmtfgpsrwgL 891
Cdd:cd01379 241 EVDSVYSILAAILHIGdieftevESNHQTDKSSRISNPEALNNVAKLLGIEADE-------------------------L 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 892 EDEETSSGLKMTG------------VDCVEGMASGLYQELFAAVVSLINR--SFSSHHLSMA-SIMVVDSPGFQNPRHQg 956
Cdd:cd01379 296 QEALTSHSVVTRGetiirnntveeaTDARDAMAKALYGRLFSWIVNRINSllKPDRSASDEPlSIGILDIFGFENFQKN- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 957 kdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPS-----QVRLpagggaqd 1031
Cdd:cd01379 375 -----SFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVD----------LIEYEDNRPLldmflQKPM-------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1032 arGLFWVLDEEVHVEGSSDSVVLERlcaaFEKkgaGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSA 1111
Cdd:cd01379 432 --GLLALLDEESRFPKATDQTLVEK----FHN---NIKSKYYWRPKSNALSFGIHHYAG--KVLYDASGFLEKNRDTLPP 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1112 lDAPQVLHQSKreelrslfqaraklppvcravaglegtsqqalqrSRMVRRTFAS----SLaavrrkapcsqiklqMDAL 1187
Cdd:cd01379 501 -DVVQLLRSSE----------------------------------NPLVRQTVATyfrySL---------------MDLL 530
|
650
....*....|....*...
gi 51317366 1188 TSMIKrSRLHFIHCLVPN 1205
Cdd:cd01379 531 SKMVV-GQPHFVRCIKPN 547
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
585-1205 |
2.46e-41 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 163.96 E-value: 2.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP-SVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQIlPIYTAEQIRlyRNKKIGeLPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLvgmaGSVDGRVS-VEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQT 738
Cdd:cd01381 81 ESGAGKTESTKLILQYL----AAISGQHSwIEQqILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 739 MLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVwSKPEDKQKAAAAFAQLQGAMEMLGISES 818
Cdd:cd01381 157 YLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGN-CLTCEGRDDAAEFADIRSAMKVLMFTDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 819 EQRAVWRVLAAIYHLGAAG----------ACKVGRKQFmrfewANYAAEALGCEYEELNTATFKHHLrqiiqqMTFGpsr 888
Cdd:cd01381 236 EIWDIFKLLAAILHLGNIKfeatvvdnldASEVRDPPN-----LERAAKLLEVPKQDLVDALTTRTI------FTRG--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 889 wgledEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSF---SSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 964
Cdd:cd01381 302 -----ETVVSPLSAEQaLDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENFEVN------SFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDQNPSQVRLpagggAQDARGLFWVLDEEVH 1044
Cdd:cd01381 371 QLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQH----------IEFVDNQDVLDLI-----ALKPMNIMSLIDEESK 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1045 VEGSSDSVVLERLCAAFEKKGAGTEGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKRE 1124
Cdd:cd01381 436 FPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT-----SFGINHFAG--VVFYDTRGFLEKNRDTFSA-DLLQLVQSSKNK 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1125 ELRSLFQAraklppvCRAvAGLEGtsqqalqrsrmvrrtfasslaavRRKAP--CSQIKLQMDALTSMIKRSRLHFIHCL 1202
Cdd:cd01381 508 FLKQLFNE-------DIS-MGSET-----------------------RKKSPtlSSQFRKSLDQLMKTLSACQPFFVRCI 556
|
...
gi 51317366 1203 VPN 1205
Cdd:cd01381 557 KPN 559
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
586-1321 |
3.89e-41 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 163.68 E-value: 3.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYkwlpvyNPEVVEGYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMAGSVD-GRVSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAATGDlAKKKDSKMKGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqMADSSSFGMGVWSKPE---DKQKAAAAFAQLQ 807
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELL----LITTNPYDYPFISQGEilvASIDDAEELLATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 808 GAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFgpS 887
Cdd:cd14913 236 SAIDILGFTPEEKSGLYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKTAYLMGLNSSDLLKALCF--P 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 888 RWGLEDEETSSGLKMTGVD-CVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 966
Cdd:cd14913 305 RVKVGNEYVTKGQTVDQVHhAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN------SLEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLpdpspGTTVAVVdqnpsqVRLpagggAQDARGLFWVLDEEVHV 1045
Cdd:cd14913 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFiDF-----GMDLAAC------IEL-----IEKPMGIFSILEEECMF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1046 EGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREE 1125
Cdd:cd14913 443 PKATDTSFKNKLYDQHLGKSNNFQKPKVVKG-RAEAHFSLIHYAG--TVDYSVSGWLEKNKDPLNE-TVVGLYQKSSNRL 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1126 LRSLFQ--ARAKLPPVCRAVAGLEGTSQQalqrsrmvrrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLV 1203
Cdd:cd14913 519 LAHLYAtfATADADSGKKKVAKKKGSSFQ--------------TVSALFRE--------NLNKLMSNLRTTHPHFVRCII 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1204 PNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1283
Cdd:cd14913 577 PN---ETKT-------------------PGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPE 634
|
730 740 750
....*....|....*....|....*....|....*...
gi 51317366 1284 lmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14913 635 ----GQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
585-1321 |
8.82e-41 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 162.89 E-value: 8.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKYLPIYSEEIVNmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGSVD------------GRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 728
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKtkkdqssialshGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 729 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKP--EDKqkaaAAFAQL 806
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPgqQDK----ELFAET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 807 QGAMEMLGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKhhlRQIIQ-QMTFG 885
Cdd:cd14932 236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNM-SFKKERNSDQASMPDDTAAQKV-CHLLGMNVTDFT---RAILSpRIKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 886 psRWGLEDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFE 964
Cdd:cd14932 311 --RDYVQKAQTQEQAEFA----VEALAKASYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFE------IFELNSFE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPgtTVAVVDQnpsqvrlPAGggaqdARGLFWVLDE 1041
Cdd:cd14932 379 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwsfIDFGL-DLQP--CIELIEK-------PNG-----PPGILALLDE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1042 EVHVEGSSDSVVLERLCaafEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSALD--APQVLH 1119
Cdd:cd14932 444 ECWFPKATDKSFVEKVV---QEQGNNPKFQKPKKLKDDADFC-IIHYAG--KVDYKANEWLMK---NMDPLNenVATLLN 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1120 QSKREELRSLFQARAKLPPVCRaVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFI 1199
Cdd:cd14932 515 QSTDKFVSELWKDVDRIVGLDK-VAGMGESLHGAFKTRKGMFRTVG------------QLYKEQLMNLMTTLRNTNPNFV 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1200 HCLVPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAP 1279
Cdd:cd14932 582 RCIIPNH--EKKAGKLAH--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 51317366 1280 LLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14932 640 AIPKGF-----MDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
586-1273 |
1.13e-40 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 163.14 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP--SVPSAGKV-----------PKGRRDGLPAHIGSMAQRAYWALL-NQR 651
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPLKPlpDLYSESQLnaykasmtstsPVSQLSELPPHVFAIGGKAFGGLLkPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 652 RDQSIVALGWSGAGKTTCCEQVLEHL--VG-----MAGSVDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSL 723
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLtsVGrdqssTEQEGSDAVEIGKrILQTNPILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 724 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADS---SSFGMGVWSKPEDKQKAA 800
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 801 AAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFM-------RFEWANyAAEALGCEYEELNTATFKH 873
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDAtavtaasRFHLAK-CAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 874 HLRQIIQQMTFGPSRWGLEDEETSsglkmtgvdcvegMASGLYQELFAAVVSLIN---------RSFSSHHLSMASIMVV 944
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGS-------------LAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGIL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 945 DSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfDLPDPSPGTTVAVVDQNPSqvrlp 1024
Cdd:cd14902 388 DIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWK-NISYPSNAACLALFDDKSN----- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1025 agggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGagtegssalrtceqplQCEIFHQLGwdPVRYDLTGWLHR 1104
Cdd:cd14902 456 ---------GLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAG--RVCYNVEQFVEK 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1105 AKPNLSAlDAPQVLHQSKREELRSLFQARAKLPPVCRAVAGLEgtsqqalQRSRMVRrtfASSLAAvrrkapcsQIKLQM 1184
Cdd:cd14902 509 NTDALPA-DASDILSSSSNEVVVAIGADENRDSPGADNGAAGR-------RRYSMLR---APSVSA--------QFKSQL 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1185 DALTSMIKRSRLHFIHCLVPNPVvesrsgqesppppqpgrdkpgaGGPLALDIPALRVQLAGFHILEALRLHRTGYADHM 1264
Cdd:cd14902 570 DRLIVQIGRTEAHYVRCLKPNEV----------------------KKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRL 627
|
....*....
gi 51317366 1265 GLTRFRRQF 1273
Cdd:cd14902 628 AHASFIELF 636
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
586-1260 |
1.74e-40 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 161.65 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKGRrDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPYKwidnlyGDHLHEQYLKKPR-DKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMAGSVDGRvSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDK-TIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESE 819
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 820 QRAVWRVLAAIYHLGAAGACKVGRK--QFMRFEWANYAAEALGCEYEELNTATFKhhlRQIIQQmtfgpsrwgledeETS 897
Cdd:cd14904 240 QRTLFKILSGVLHLGEVMFDKSDENgsRISNGSQLSQVAKMLGLPTTRIEEALCN---RSVVTR-------------NES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 898 SGLKMTGVDCVE---GMASGLYQELFAAVVSLINRSFSS-HHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHE 973
Cdd:cd14904 304 VTVPLAPVEAEEnrdALAKAIYSKLFDWMVVKINAAISTdDDRIKGQIGVLDIFGFEDFAHNG------FEQFCINYANE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 974 RLQLLFYQRTFVSTLQRYQEEGvpVQFD-LPDPSPGTTVAVVDQNpsqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSV 1052
Cdd:cd14904 378 KLQQKFTTDVFKTVEEEYIREG--LQWDhIEYQDNQGIVEVIDGK---------------MGIIALMNDHLRQPRGTEEA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1053 VLERLCAAFEKKGAGT--EGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLF 1130
Cdd:cd14904 441 LVNKIRTNHQTKKDNEsiDFPKVKRT-----QFIINHYAG--PVTYETVGFMEKHRDTLQN-DLLDLVLLSSLDLLTELF 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1131 QAraklppvcravagLEGTSQQALQRSRmvRRTFAsslaavrRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvES 1210
Cdd:cd14904 513 GS-------------SEAPSETKEGKSG--KGTKA-------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPN---AN 567
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 51317366 1211 RSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGY 1260
Cdd:cd14904 568 KS-------------------PTEFDKRMVVEQLRSAGVIEAIRITRSGY 598
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
585-1321 |
1.85e-40 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 161.55 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPS-AGKVPKG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPykRYPVYTNrCAKMYRGkRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK-------IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 733
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSkgsledqVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 734 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL-HQMADSSSFGMGVWSKPedKQKAAAAFAQLQGAMEM 812
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVP--NVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 813 LGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMR---FEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRw 889
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEqdgEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 890 gleDEETSSglkmtgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHN 969
Cdd:cd14909 318 ---QQVTNS---------IGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG------FEQLCIN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 970 YAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLpdpspgttVAVVDQnpsqvrlpagggAQDARGLFWVLDEEVH 1044
Cdd:cd14909 380 FTNEKLQQFFNHHMFVLEQEEYKREGIDWAFidfgmDL--------LACIDL------------IEKPMGILSILEEESM 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1045 VEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSaldaPQVLHQSKRE 1124
Cdd:cd14909 440 FPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAG--CVSYNITGWLEKNKDPLN----DTVVDQFKKS 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1125 ELRSLFQARAKLPPVCRAVAGLEGTsqqalqrsrmvRRTFASSLAAVRrkapcSQIKLQMDALTSMIKRSRLHFIHCLVP 1204
Cdd:cd14909 514 QNKLLIEIFADHAGQSGGGEQAKGG-----------RGKKGGGFATVS-----SAYKEQLNSLMTTLRSTQPHFVRCIIP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1205 NPVvesrsgqespppPQPGrdkpgaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKL 1284
Cdd:cd14909 578 NEM------------KQPG----------VVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGE 635
|
730 740 750
....*....|....*....|....*....|....*..
gi 51317366 1285 MstsegiDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14909 636 E------DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
585-1321 |
2.98e-40 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 160.91 E-value: 2.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVA 658
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKwlpvyqKEVMAAYK--GKRRSEAPPHIFAVANNAFQDMLHNRENQSILF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 659 LGWSGAGKTTCCEQVLEHLVGMAGSVDGR----VSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAA 734
Cdd:cd14929 79 TGESGAGKTVNTKHIIQYFATIAAMIESKkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 735 QLQTMLLEKSRVARQPEGESNFLVFSQMLAGldldlrtELNLHQM----ADSSSFGM---GVWSKpeDKQKAAAAFAQLQ 807
Cdd:cd14929 159 DIDIYLLEKSRVIFQQPGERNYHIFYQILSG-------KKELRDLllvsANPSDFHFcscGAVAV--ESLDDAEELLATE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 808 GAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFgpS 887
Cdd:cd14929 230 QAMDILGFLPDEKYGCYKLTGAIMHFG-----NMKFKQKPREE----QLEADGTENADKAAFLMGINSSELVKGLIH--P 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 888 RWGLEDEETSSGLKMTGVDCVEG-MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 966
Cdd:cd14929 299 RIKVGNEYVTRSQNIEQVTYAVGaLSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYN------SLEQL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEG---VPVQFDLpdpspgTTVAVVDQnpsqvrlpagggAQDARGLFWVLDEEV 1043
Cdd:cd14929 373 CINFTNEKLQQFFNQHMFVLEQEEYRKEGidwVSIDFGL------DLQACIDL------------IEKPMGIFSILEEEC 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1044 HVEGSSDSVVLERLC-AAFEKKGAGTEGSSALRTCEqpLQCEIFHQLGWDPvrYDLTGWLHRAKPNLSAlDAPQVLHQSK 1122
Cdd:cd14929 435 MFPKATDLTFKTKLFdNHFGKSVHFQKPKPDKKKFE--AHFELVHYAGVVP--YNISGWLEKNKDLLNE-TVVAVFQKSS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1123 REELRSLFQARAklppvcravaglegTSQQALQRSRMVRRTFASSlaavrrKAPCSQIKLQMDALTSMIKRSRLHFIHCL 1202
Cdd:cd14929 510 NRLLASLFENYI--------------STDSAIQFGEKKRKKGASF------QTVASLHKENLNKLMTNLKSTAPHFVRCI 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1203 VPNPvvesrsgqesppppqpgRDKPGAGGP-LALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDApll 1281
Cdd:cd14929 570 NPNV-----------------NKIPGVLDPyLVLQ------QLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP--- 623
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 51317366 1282 kKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14929 624 -RTFPKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
585-1321 |
3.60e-40 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 161.03 E-value: 3.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKNLPIYSEEIVEmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGSV-----DGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 735
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHkskkdQGELERQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 736 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKP--EDKqkaaAAFAQLQGAMEML 813
Cdd:cd14919 160 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPgqQDK----DMFQETMEAMRIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 814 GISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALGcEYEELNTATFKHHLrqIIQQMTFGpsrwglED 893
Cdd:cd14919 236 GIPEEEQMGLLRVISGVLQLGNI-VFKKERNTDQASMPDNTAAQKVS-HLLGINVTDFTRGI--LTPRIKVG------RD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 894 EETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEELCHNYAH 972
Cdd:cd14919 306 YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFE------IFDLNSFEQLCINYTN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 973 ERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVavvdqnpsqVRLPAGggaqdARGLFWVLDEEVHVEGSS 1049
Cdd:cd14919 380 EKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIDL---------IEKPAG-----PPGILALLDEECWFPKAT 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1050 DSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLHQSKREELR 1127
Cdd:cd14919 445 DKSFVEKV---VQEQGTHPKFQKPKQLKDKADFC-IIHYAG--KVDYKADEWLMK---NMDPLndNIATLLHQSSDKFVS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1128 SLFQARAKlppvcraVAGLE---GTSQQALQRSRMVRRTFASSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVP 1204
Cdd:cd14919 516 ELWKDVDR-------IIGLDqvaGMSETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFVRCIIP 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1205 NPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKL 1284
Cdd:cd14919 581 NH--EKKAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG 638
|
730 740 750
....*....|....*....|....*....|....*..
gi 51317366 1285 MstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14919 639 F-----MDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
585-1321 |
3.78e-40 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 160.58 E-value: 3.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAG----KVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPY-KWLPIYGarvaNMYKGKkRTEMPPHLFSISDNAYHDMLMDRENQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMAG----SVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAA 734
Cdd:cd14934 80 GESGAGKTENTKKVIQYFANIGGtgkqSSDGKGSLEdQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 735 QLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqMADSSSF-----GMGVWSKPEDkqkaAAAFAQLQGA 809
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLL--VPNPKEYhwvsqGVTVVDNMDD----GEELQITDVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 810 MEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRF---EWANYAAEALGCEYEELntatfkhhlrqiiqQMTFGP 886
Cdd:cd14934 234 FDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVdttEVADKVAHLMGLNSGEL--------------QKGITR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 887 SRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEE 965
Cdd:cd14934 300 PRVKVGNEFVQKGQNMEQCnNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN------SFEQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 966 LCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqvrlpagggAQDARGLFWVLD 1040
Cdd:cd14934 374 LCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFidfglDLQ--------ACIDL------------LEKPMGIFSILE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1041 EEVHVEGSSDSVV--------LERLCAAFEKKGAGTEGSSAlrtceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSal 1112
Cdd:cd14934 434 EQCVFPKATDATFkaalydnhLGKSSNFLKPKGGKGKGPEA--------HFELVHYAG--TVGYNITGWLEKNKDPLN-- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1113 dapqvlhqskrEELRSLFQARAKLppVC----RAVAGLEGTSQQALQRSRMVRRTFasslaavrrkapcsqIKLQMDALT 1188
Cdd:cd14934 502 -----------ETVVGLFQKSSLG--LLallfKEEEAPAGSKKQKRGSSFMTVSNF---------------YREQLNKLM 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1189 SMIKRSRLHFIHCLVPNPVVESRsgqesppppqpgrdkpgaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTR 1268
Cdd:cd14934 554 TTLHSTAPHFVRCIVPNEFKQSG----------------------VVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPE 611
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 51317366 1269 FRRQFQVLDAPLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14934 612 FKQRYQVLNPNVIPQGF-----VDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
587-1321 |
2.04e-39 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 158.36 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 587 VLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpvynPEVVAAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMA----------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAvtgekkkeesGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEdkQKAAAAFAQLQGA 809
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFvSQGEITVPS--IDDQEELMATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 810 MEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRW 889
Cdd:cd14918 238 IDILGFTPEEKVSIYKLTGAVMHYGN-----------MKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 890 GLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 968
Cdd:cd14918 307 KVGNEYVTKGQTVQQVyNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLCI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 969 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEVHVEGS 1048
Cdd:cd14918 381 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---------------PLGIFSILEEECMFPKA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1049 SDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSalDAPQVLHQ-SKREELR 1127
Cdd:cd14918 446 TDTSFKNKLYDQHLGKSANFQKPKVVKG-KAEAHFSLIHYAG--TVDYNITGWLDKNKDPLN--DTVVGLYQkSAMKTLA 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1128 SLFQ--ARAKLPPVCRAVAGLEGTSQQalqrsrmvrrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVPN 1205
Cdd:cd14918 521 SLFStyASAEADSGAKKGAKKKGSSFQ--------------TVSALFRE--------NLNKLMTNLRSTHPHFVRCIIPN 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1206 pvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKlm 1285
Cdd:cd14918 579 ---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE-- 634
|
730 740 750
....*....|....*....|....*....|....*.
gi 51317366 1286 stSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14918 635 --GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
585-1321 |
2.30e-39 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 158.33 E-value: 2.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSA-GKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPykQLPIYTEAiVEMYRGKkRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGSVDGR----VSVEKIRATFT---VLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 733
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRkepgVPGELERQLLQanpILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 734 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkaAAAFAQLQGAMEML 813
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE---RELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 814 GISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsrwglED 893
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNI-VLKRERNTDQATMPDNTAAQKL-CRLLGLGVTDFSRAL--LTPRIKVG------RD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 894 EETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIM-VVDSPGFQnprhqgKDRAATFEELCHNYAH 972
Cdd:cd14930 308 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFE------IFQLNSFEQLCINYTN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 973 ERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSS 1049
Cdd:cd14930 382 EKLQQLFNHTMFVLEQEEYQREGIPwtfLDFGL-DLQPCIDLIERPANPP--------------GLLALLDEECWFPKAT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1050 DSVVLERLCaafEKKGAGTEGSSAlRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKReelrsl 1129
Cdd:cd14930 447 DKSFVEKVA---QEQGGHPKFQRP-RHLRDQADFSVLHYAG--KVDYKANEWLMKNMDPLND-NVAALLHQSTD------ 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1130 fQARAKLPPVCRAVAGLEGTSQQAL-QRSRMVRRTFASSLAAVRRKApcsqiklqMDALTSMIKRSRLHFIHCLVPNPvv 1208
Cdd:cd14930 514 -RLTAEIWKDVEGIVGLEQVSSLGDgPPGGRPRRGMFRTVGQLYKES--------LSRLMATLSNTNPSFVRCIVPNH-- 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1209 ESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMsts 1288
Cdd:cd14930 583 EKRAGKLEP--------------RLVLD------QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGF--- 639
|
730 740 750
....*....|....*....|....*....|...
gi 51317366 1289 egIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14930 640 --MDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
586-1205 |
2.99e-39 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 157.80 E-value: 2.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP----RGPSVPSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyfdiPKLYSSETIKSYQGKSLGtLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 740
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIE-QRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 741 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLH--QMADSSSFGmgvwskpedkqkaaaafaQLQGAMEMLGISES 818
Cdd:cd01382 161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKdpLLDDVGDFI------------------RMDKAMKKIGLSDE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 819 EQRAVWRVLAAIYHLG----------AAGACKVGRKQFMRFEwanYAAEALGCEYEELntatfKHHLRQIIQQMTFGPS- 887
Cdd:cd01382 222 EKLDIFRVVAAVLHLGniefeengsdSGGGCNVKPKSEQSLE---YAAELLGLDQDEL-----RVSLTTRVMQTTRGGAk 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 888 ----RWGLEDEETSSGLkmtgvdcvEGMASGLYQELFAAVVSLINRS--FSShhlSMASIMVVDSPGFQNPRHQgkdraa 961
Cdd:cd01382 294 gtviKVPLKVEEANNAR--------DALAKAIYSKLFDHIVNRINQCipFET---SSYFIGVLDIAGFEYFEVN------ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 962 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQnpsqvrlpagggaQD--------AR 1033
Cdd:cd01382 357 SFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVK----------EVEYVDN-------------QDcidlieakLV 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1034 GLFWVLDEEVHVEGSSD----SVVLE------RLCAAFEKKGAGTEgssALRTCEQPLqceIFHQLGwdPVRYDLTGWLH 1103
Cdd:cd01382 414 GILDLLDEESKLPKPSDqhftSAVHQkhknhfRLSIPRKSKLKIHR---NLRDDEGFL---IRHFAG--AVCYETAQFIE 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1104 RakpNLSALDAP--QVLHQSKREELRSLFQARAKLPPVCRAVAGlegtsqqalqrsrmvRRTFASslaaVRRKapcsqIK 1181
Cdd:cd01382 486 K---NNDALHASleSLICESKDKFIRSLFESSTNNNKDSKQKAG---------------KLSFIS----VGNK-----FK 538
|
650 660
....*....|....*....|....
gi 51317366 1182 LQMDALTSMIKRSRLHFIHCLVPN 1205
Cdd:cd01382 539 TQLNLLMDKLRSTGTSFIRCIKPN 562
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
586-1321 |
1.14e-38 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 156.03 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKwlpvynAEVVAAYRGKK--RSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMAGSVD--------GRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAIGDrskkdqtpGKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPEDKQKA---AAAFAQLQ 807
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILS----NKKPELLDMLLITNNPYDYAFISQGETTVASiddAEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 808 GAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPS 887
Cdd:cd14917 236 NAFDVLGFTSEEKNSMYKLTGAIMHFGN-----------MKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 888 RWGLEDEETSSGLKMTGVDCVEG-MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 966
Cdd:cd14917 305 RVKVGNEYVTKGQNVQQVIYATGaLAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqvrlpagggAQDARGLFWVLDE 1041
Cdd:cd14917 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgmDLQ--------ACIDL------------IEKPMGIMSILEE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1042 EVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGWdpVRYDLTGWLHRAKPNLSAlDAPQVLHQS 1121
Cdd:cd14917 439 ECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKG-KPEAHFSLIHYAGT--VDYNIIGWLQKNKDPLNE-TVVGLYQKS 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1122 KREELRSLFQARAKlppvcrAVAGLEGTSQQALQRSRMvrrtfaSSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHC 1201
Cdd:cd14917 515 SLKLLSNLFANYAG------ADAPIEKGKGKAKKGSSF------QTVSALHRE--------NLNKLMTNLRSTHPHFVRC 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1202 LVPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLL 1281
Cdd:cd14917 575 IIPN---ETKS-------------------PGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAI 632
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 51317366 1282 KKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14917 633 PE----GQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
585-1321 |
2.06e-38 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 155.50 E-value: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVA 658
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYkwlpvyTAPVVAAYK--GKRRSEAPPHIYAIADNAYNDMLRNRENQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 659 LGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFT-------------VLRAFGSVSMAHSRSATRFSMVMSLDF 725
Cdd:cd14927 79 TGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTggtledqiieanpAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 726 NATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqMADSSSFGMGVWSKPE---DKQKAAAA 802
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML----LVSMNPYDYHFCSQGVttvDNMDDGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 803 FAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAgacKVGRKQfmRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQM 882
Cdd:cd14927 235 LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNM---KFKQKQ--REE----QAEADGTESADKAAYLMGVSSADLLKGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 883 TFGPSRWGleDEETSSGLKMTGVD-CVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraa 961
Cdd:cd14927 306 LHPRVKVG--NEYVTKGQSVEQVVyAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFN------ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 962 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqvrlpagggAQDARGLF 1036
Cdd:cd14927 378 SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFidfglDLQ--------ACIDL------------IEKPLGIL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1037 WVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGWDPvrYDLTGWLHRAKPNLSALDAPq 1116
Cdd:cd14927 438 SILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKYEAHFEVVHYAGVVP--YNIVGWLDKNKDPLNETVVA- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1117 VLHQSKREELRSLFQARAKLPPVCRAVAGLEGtsqqalqrsrmvRRTFASSLAAVrrkapcSQI-KLQMDALTSMIKRSR 1195
Cdd:cd14927 515 IFQKSQNKLLATLYENYVGSDSTEDPKSGVKE------------KRKKAASFQTV------SQLhKENLNKLMTNLRATQ 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1196 LHFIHCLVPNpvvESRSgqesppppqpgrdkPGAGGPLaLDIPALRVQlagfHILEALRLHRTGYADHMGLTRFRRQFQV 1275
Cdd:cd14927 577 PHFVRCIIPN---ETKT--------------PGVMDPF-LVLHQLRCN----GVLEGIRICRKGFPNRILYADFKQRYRI 634
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 51317366 1276 LDAPLLKKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14927 635 LNPSAIPD----DKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
586-1321 |
2.33e-38 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 155.27 E-value: 2.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvyNPEVVTAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMA------------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNA 727
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeaasGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 728 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPE---DKQKAAAAFA 804
Cdd:cd14915 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEitvPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 805 QLQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTF 884
Cdd:cd14915 235 ATDSAVDILGFSADEKVAIYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKAAYLTSLNSADLLKALCY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 885 gpSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTF 963
Cdd:cd14915 306 --PRVKVGNEYVTKGQTVQQVyNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 964 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEV 1043
Cdd:cd14915 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---------------PMGIFSILEEEC 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1044 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSaldapqvlhqskr 1123
Cdd:cd14915 443 MFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKG-KAEAHFSLVHYAG--TVDYNIAGWLDKNKDPLN------------- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1124 EELRSLFQaRAKLPPVCRAVAGLEGTSQQALQRSRMVRRTFAS--SLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHC 1201
Cdd:cd14915 507 ETVVGLYQ-KSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSfqTVSALFRE--------NLNKLMTNLRSTHPHFVRC 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1202 LVPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLL 1281
Cdd:cd14915 578 LIPN---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 635
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 51317366 1282 KKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14915 636 PE----GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
586-1321 |
2.39e-38 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 154.95 E-value: 2.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPyqPIAGLYEPATMEqySRRHLGeLPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK-------IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 733
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSLELSLKEKtscveqaILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 734 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL------NLHQMADSssfgmGVWSkpEDKQKAAAAFAQLQ 807
Cdd:cd14873 162 GRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFylstpeNYHYLNQS-----GCVE--DKTISDQESFREVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 808 GAMEMLGISESEQRAVWRVLAAIYHLG-----AAGACKVGRKQFMrfewaNYAAEALGCEYEELNTAtfkhhlrqIIQQM 882
Cdd:cd14873 235 TAMEVMQFSKEEVREVSRLLAGILHLGniefiTAGGAQVSFKTAL-----GRSAELLGLDPTQLTDA--------LTQRS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 883 TFgpsrwgLEDEETSSGLKM-TGVDCVEGMASGLYQELFAAVVSLINRSFSSHHlSMASIMVVDSPGFQNPRHQgkdraa 961
Cdd:cd14873 302 MF------LRGEEILTPLNVqQAVDSRDSLAMALYARCFEWVIKKINSRIKGKE-DFKSIGILDIFGFENFEVN------ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 962 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpVQFDLPDPSPGTTVAVVDQNpsqvrlpagggaqdaRGLFWVLDE 1041
Cdd:cd14873 369 HFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGL-VWEDIDWIDNGECLDLIEKK---------------LGLLALINE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1042 EVHVEGSSDSVVLERLcaafekKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQS 1121
Cdd:cd14873 433 ESHFPQATDSTLLEKL------HSQHANNHFYVKPRVAVNNFGVKHYAG--EVQYDVRGILEKNRDTFRD-DLLNLLRES 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1122 KREELRSLFQARAKlppvcravAGLEGTSQQALQRsrmvrrtfasslaavRRKAPCSQIKLQMDALTSMIKRSRLHFIHC 1201
Cdd:cd14873 504 RFDFIYDLFEHVSS--------RNNQDTLKCGSKH---------------RRPTVSSQFKDSLHSLMATLSSSNPFFVRC 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1202 LVPNpvVESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYAdhmgltrFRRQFQvldaPLL 1281
Cdd:cd14873 561 IKPN--MQKMPDQFDQ--------------AVVLN------QLRYSGMLETVRIRKAGYA-------VRRPFQ----DFY 607
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 51317366 1282 KKLMSTSEGI----DERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14873 608 KRYKVLMRNLalpeDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
587-1016 |
2.58e-38 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 154.76 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 587 VLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIAVNPfkRLPHLYDAHMMEqyKGAPLGeLSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 662 SGAGKTTCCEQVLEHLVGMAG--SVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGMGVWSKPEDkqkaaaaFAQLQGAMEML 813
Cdd:cd01384 163 LLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 814 GISESEQRAVWRVLAAIYHLG--------AAGACKVGRKQfMRFEWANyAAEALGCEYEELNTATFKhhlRQIIqqmtfg 885
Cdd:cd01384 236 GISEEEQDAIFRVVAAILHLGniefskgeEDDSSVPKDEK-SEFHLKA-AAELLMCDEKALEDALCK---RVIV------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 886 psrwgLEDEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQnprhQGKDRaaTFE 964
Cdd:cd01384 305 -----TPDGIITKPLDPDAaTLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE----SFKTN--SFE 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51317366 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQF-------DLPDPSPGTTVAVVDQ 1016
Cdd:cd01384 374 QFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDwsyIEFvdnqdvlDLIEKKPGGIIALLDE 435
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
586-1321 |
6.15e-38 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 154.12 E-value: 6.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpvynPEVVTAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMA------------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNA 727
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeitsGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 728 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPEDKQKA---AAAFA 804
Cdd:cd14912 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITS----NKKPELIEMLLITTNPYDYPFVSQGEISVASiddQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 805 QLQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEElnTATFKHHLRQIIQQMTF 884
Cdd:cd14912 235 ATDSAIDILGFTNEEKVSIYKLTGAVMHYG-----NLKFKQKQREE----QAEPDGTEVAD--KAAYLQSLNSADLLKAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 885 GPSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTF 963
Cdd:cd14912 304 CYPRVKVGNEYVTKGQTVEQVtNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 964 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEV 1043
Cdd:cd14912 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---------------PMGIFSILEEEC 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1044 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAldapQVLHQSKR 1123
Cdd:cd14912 443 MFPKATDTSFKNKLYEQHLGKSANFQKPKVVKG-KAEAHFSLIHYAG--VVDYNITGWLDKNKDPLNE----TVVGLYQK 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1124 EELRSLfqarAKLPPVCRAVAGlEGTSQQALQRSRMVRRTFASSLAAVRRkapcsqiklQMDALTSMIKRSRLHFIHCLV 1203
Cdd:cd14912 516 SAMKTL----AYLFSGAQTAEG-ASAGGGAKKGGKKKGSSFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCII 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1204 PNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1283
Cdd:cd14912 582 PN---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 639
|
730 740 750
....*....|....*....|....*....|....*...
gi 51317366 1284 lmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14912 640 ----GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
587-1276 |
1.28e-37 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 152.75 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 587 VLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAGKVPKGR-----RDGLPAHIGSMAQRAYWALLNQ----RRDQSIV 657
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKY-LHIYEKEVSQKykcekKSSLPPHIFAVADRAYQSMLGRlargPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 658 ALGWSGAGKTTCCEQVLEHLVGMAgsvDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQL 736
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELC---RGNSQLEQqILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGAKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 737 QTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKpEDKQKAAAAFAQLQGAMEMLGIS 816
Cdd:cd14889 158 NEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCK-REVQYWKKKYDEVCNAMDMVGFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 817 ESEQRAVWRVLAAIYHLGA-------AGACKVGRKQfmrFEWANYAAEALGCEYEEL-----NTATF-------KHHLRQ 877
Cdd:cd14889 237 EQEEVDMFTILAGILSLGNitfemddDEALKVENDS---NGWLKAAAGQFGVSEEDLlktltCTVTFtrgeqiqRHHTKQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 878 IIQqmtfgpsrwgledeetssglkmtgvDCVEGMASGLYQELFAAVVSLINRSFS---SHHLSMASIMVVDSPGFQnprH 954
Cdd:cd14889 314 QAE-------------------------DARDSIAKVAYGRVFGWIVSKINQLLApkdDSSVELREIGILDIFGFE---N 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 955 QGKDRaatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPSQVRLPAgggaqDARG 1034
Cdd:cd14889 366 FAVNR---FEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWK----------EITYKDNKPILDLFLN-----KPIG 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1035 LFWVLDEEVHVEGSSDSVVLERLCAAFekKGAGTEGSSALRTceqPLqCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlda 1114
Cdd:cd14889 428 ILSLLDEQSHFPQATDESFVDKLNIHF--KGNSYYGKSRSKS---PK-FTVNHYAG--KVTYNASGFLEKNRDTIPA--- 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1115 pqvlhqSKREE-LRSLFQARAKLPPVCRAVAGLEGTSQQALQRSrmvrrtfASSLAAVRRKAPCSQIKLQMDALTSMIKR 1193
Cdd:cd14889 497 ------SIRTLfINSATPLLSVLFTATRSRTGTLMPRAKLPQAG-------SDNFNSTRKQSVGAQFKHSLGVLMEKMFA 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1194 SRLHFIHCLVPNPVvesrsgqespppPQPGRdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQF 1273
Cdd:cd14889 564 ASPHFVRCIKPNHV------------KVPGQ----------LDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERY 621
|
...
gi 51317366 1274 QVL 1276
Cdd:cd14889 622 KIL 624
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
586-1321 |
1.41e-37 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 152.91 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR---RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPyKWLPVYNAEVVAAYRgkkRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 662 SGAGKTTCCEQVLEHLVGMAG-----------SVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAigdrskkenpnANKGTLEDQIIQAN-PALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAG-----LDLDLRTElNLHQMADSSSFGMGVWSKPEDKqkaaaAFAQ 805
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNkkpelLDMLLVTN-NPYDYAFVSQGEVSVASIDDSE-----ELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 806 LQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFG 885
Cdd:cd14916 235 TDSAFDVLGFTAEEKAGVYKLTGAIMHYGN-----------MKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 886 PSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 964
Cdd:cd14916 304 HPRVKVGNEYVTKGQSVQQVyYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqvrlpagggAQDARGLFWVL 1039
Cdd:cd14916 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFidfgmDLQ--------ACIDL------------IEKPMGIMSIL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1040 DEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLH 1119
Cdd:cd14916 438 EEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKG-KQEAHFSLVHYAG--TVDYNILGWLEKNKDPLNE-TVVGLYQ 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1120 QSKREELRSLFQARAKlppvcrAVAGLEGTSQQALQRSRMVRrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFI 1199
Cdd:cd14916 514 KSSLKLMATLFSTYAS------ADTGDSGKGKGGKKKGSSFQ-----TVSALHRE--------NLNKLMTNLKTTHPHFV 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1200 HCLVPNPvvesrsgqesppppqpgRDKPGaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAP 1279
Cdd:cd14916 575 RCIIPNE-----------------RKAPG-----VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 632
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 51317366 1280 LLKKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14916 633 AIPE----GQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
586-1321 |
2.51e-37 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 152.19 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR---RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPyKWLPVYNAEVVTAYRgkkRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 662 SGAGKTTCCEQVLEHLVGMAGSVDGR---VSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKkeeATSGKMQGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEdkQKAAAAFAQLQGA 809
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFvSQGEITVPS--IDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 810 MEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRW 889
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGN-----------MKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 890 GLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 968
Cdd:cd14910 309 KVGNEYVTKGQTVQQVyNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 969 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEVHVEGS 1048
Cdd:cd14910 383 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---------------PMGIFSILEEECMFPKA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1049 SDSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCE--IFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREEL 1126
Cdd:cd14910 448 TDTSFKNKL---YEQHLGKSNNFQKPKPAKGKVEAHfsLIHYAG--TVDYNIAGWLDKNKDPLNE-TVVGLYQKSSMKTL 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1127 RSLFQARAKLPpvCRAVAGLEGTSQQAlqrsrmvrRTFASSLAAVRRkapcsqiklQMDALTSMIKRSRLHFIHCLVPNp 1206
Cdd:cd14910 522 ALLFSGAAAAE--AEEGGGKKGGKKKG--------SSFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCIIPN- 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1207 vvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKlms 1286
Cdd:cd14910 582 --ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE--- 637
|
730 740 750
....*....|....*....|....*....|....*
gi 51317366 1287 tSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14910 638 -GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
586-994 |
2.69e-37 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 151.54 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRY-KAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvPKGRRDglPaHIGSMAQRAYWALLNQRRDQSI 656
Cdd:cd01380 2 AVLHNLKVRFcQRNAIYTYCGIVLVAINPyedlpiYGEDIIQAysGQ-NMGELD--P-HIFAIAEEAYRQMARDEKNQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 657 VALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 735
Cdd:cd01380 78 IVSGESGAGKTVSAKYAMRYFATVGGSSSGETQVEeKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 736 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqmADSSSF---GMGvwSKPE-DKQKAAAAFAQLQGAME 811
Cdd:cd01380 158 MRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHL---GSAEDFfytNQG--GSPViDGVDDAAEFEETRKALT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 812 MLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRFEWA---NYAAEALGCEYEElntatFKHHL-RQIIQQMTfgps 887
Cdd:cd01380 233 LLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDehlQIACELLGIDESQ-----LAKWLcKRKIVTRS---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 888 rwgledEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRSFSSHHLS--MASIMVVDSPGFQ----Nprhqgkdra 960
Cdd:cd01380 304 ------EVIVKPLTLQqAIVARDALAKHIYAQLFDWIVDRINKALASPVKEkqHSFIGVLDIYGFEtfevN--------- 368
|
410 420 430
....*....|....*....|....*....|....
gi 51317366 961 aTFEELCHNYAHERLQLLFYQRTFvstlQRYQEE 994
Cdd:cd01380 369 -SFEQFCINYANEKLQQQFNQHVF----KLEQEE 397
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
585-1321 |
3.73e-37 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 151.76 E-value: 3.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKNLPIYSEEIVEmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGS------------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 728
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslalSHGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 729 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkAAAAFAQLQG 808
Cdd:cd15896 160 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQ--DKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 809 AMEMLGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKhhlRQIIQ-QMTFGps 887
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNM-SFKKERHTDQASMPDNTAAQKV-CHLMGMNVTDFT---RAILSpRIKVG-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 888 RWGLEDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEEL 966
Cdd:cd15896 311 RDYVQKAQTQEQAEFA----VEALAKATYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFE------IFELNSFEQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEV 1043
Cdd:cd15896 381 CINYTNEKLQQLFNHTMFILEQEEYQREGIEwsfIDFGL-DLQPCIDLIEKPASPP--------------GILALLDEEC 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1044 HVEGSSDSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKR 1123
Cdd:cd15896 446 WFPKATDKSFVEKV---LQEQGTHPKFFKPKKLKDEADFC-IIHYAG--KVDYKADEWLMKNMDPLND-NVATLLNQSTD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1124 EELRSLFQARAKLPPVCRaVAGLEGTSQQALQRSRMVRRTfasslaavrrkapcSQI-KLQMDALTSMIKRSRLHFIHCL 1202
Cdd:cd15896 519 KFVSELWKDVDRIVGLDK-VSGMSEMPGAFKTRKGMFRTV--------------GQLyKEQLSKLMATLRNTNPNFVRCI 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1203 VPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1282
Cdd:cd15896 584 IPNH--EKKAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIP 641
|
730 740 750
....*....|....*....|....*....|....*....
gi 51317366 1283 KLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd15896 642 KGF-----MDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
586-1321 |
3.18e-36 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 148.68 E-value: 3.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvyNPEVVAAYRGKK--RQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMA-----------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 728
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 729 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPE---DKQKAAAAFAQ 805
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMS----NKKPELIDLLLISTNPFDFPFVSQGEvtvASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 806 LQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFg 885
Cdd:cd14923 235 TDNAIDILGFSSEEKVGIYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKAGYLMGLNSAEMLKGLCC- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 886 pSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 964
Cdd:cd14923 305 -PRVKVGNEYVTKGQNVQQVtNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEVH 1044
Cdd:cd14923 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---------------PMGIFSILEEECM 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1045 VEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSalDAPQVLHQSKRE 1124
Cdd:cd14923 443 FPKATDTSFKNKLYDQHLGKSNNFQKPKPAKG-KAEAHFSLVHYAG--TVDYNIAGWLDKNKDPLN--ETVVGLYQKSSL 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1125 ELRS-LFQARAKlppvcrAVAGLEGTSQQALQRsrmvRRTFASSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLV 1203
Cdd:cd14923 518 KLLSfLFSNYAG------AEAGDSGGSKKGGKK----KGSSFQTVSAVFRE--------NLNKLMTNLRSTHPHFVRCLI 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1204 PNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1283
Cdd:cd14923 580 PN---ETKT-------------------PGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPE 637
|
730 740 750
....*....|....*....|....*....|....*...
gi 51317366 1284 lmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14923 638 ----GQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
586-1320 |
8.10e-36 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 147.24 E-value: 8.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-----------RGPSVPSAGKVPKGRRDgLPAHIGSMAQRAYWALLNQRR-- 652
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPfrrlplyddetKEAYYEHGERRAAGERK-LPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 653 --DQSIVALGWSGAGKTTCCEQVLEHLVGMA------GSVDGRVSV-EKIRATFTVLRAFGSVSMAHSRSATRFSMVMSL 723
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgQNATERENVrDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 724 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAF 803
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 804 AQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQfMRFEWANYAAEALGCEYEELNTATFKHHL--RQIIQQ 881
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEG-GTFSMSSLANVRAACDLLGLDMDVLEKTLctREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 882 MTFGPSRWGLEDEETSSglkmtgvdcvEGMASGLYQELFAAVVSLINRS--FSSHHLSMASIMVVDSPGF----QNprhq 955
Cdd:cd14901 320 GEYITMPLSVEQALLTR----------DVVAKTLYAQLFDWLVDRINESiaYSESTGASRFIGIVDIFGFeifaTN---- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 956 gkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdLPDPSPGTTVAVVDQNPSqvrlpagggaqdarGL 1035
Cdd:cd14901 386 ------SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTF-VEYPNNDACVAMFEARPT--------------GL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1036 FWVLDEEVHVEGSSDsvvlERLCAAFekkgagtegssalrtceqplqceifhqlgwdpvrYDLTGwlhrAKPNLSAldap 1115
Cdd:cd14901 445 FSLLDEQCLLPRGND----EKLANKY----------------------------------YDLLA----KHASFSV---- 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1116 qvlhqSKREELRSLFQARAKLPPVCRAVAGL-----EGTSQQALQRSRMVRRTFASSLAAvrrkapcSQIKLQMDALTSM 1190
Cdd:cd14901 479 -----SKLQQGKRQFVIHHYAGAVCYATDGFcdknkDHVHSEALALLRTSSNAFLSSTVV-------AKFKVQLSSLLEV 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1191 IKRSRLHFIHCLVPNPVVESRSgqesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFR 1270
Cdd:cd14901 547 LNATEPHFIRCIKPNDVLSPSE----------------------FDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFV 604
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 51317366 1271 RQFQVLDAPLLKKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFL 1320
Cdd:cd14901 605 HTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVFL 654
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
585-1205 |
1.17e-35 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 146.71 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKV-----------PKGRRDGLPAHIGSMAQRAYWALLNQR 651
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPykQIDNLFSEEVMqmykeqiiqngEYFDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 652 RDQSIVALGWSGAGKT---TCC--------------EQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRS 713
Cdd:cd14907 81 KKQAIVISGESGAGKTenaKYAmkfltqlsqqeqnsEEVLTLTSSIRATSKSTKSIEqKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 714 ATRFSMVMSLDFN-ATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqMADSSSFGMGVWSK 792
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGL--KNQLSGDRYDYLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 793 PE----DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKQFMRfewanYAAEA 858
Cdd:cd14907 239 SNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGnlqfddstldDNSPCCVKNKETLQ-----IIAKL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 859 LGCEYEELNTA-TFKhhLRQIIQQMTFGPsrwgledeetssglkMTGVDCV---EGMASGLYQELFAAVVSLINRSFSSH 934
Cdd:cd14907 314 LGIDEEELKEAlTTK--IRKVGNQVITSP---------------LSKKECInnrDSLSKELYDRLFNWLVERLNDTIMPK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 935 HLS--------MASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLP 1003
Cdd:cd14907 377 DEKdqqlfqnkYLSIGLLDIFGFEVFQNNS------FEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdylNQLSYT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1004 DPSPgtTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAafekkgagTEGSSALRTCEQPLQC 1083
Cdd:cd14907 451 DNQD--VIDLLDKPPI--------------GIFNLLDDSCKLATGTDEKLLNKIKK--------QHKNNSKLIFPNKINK 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1084 EIF---HQLGwdPVRYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQAraklppvcravaglEGTSQQALQRSRMV 1160
Cdd:cd14907 507 DTFtirHTAK--EVEYNIEGFREKNKDEIS-QSIINCIQNSKNRIISSIFSG--------------EDGSQQQNQSKQKK 569
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 51317366 1161 RRtfasslaaVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPN 1205
Cdd:cd14907 570 SQ--------KKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPN 606
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
551-1358 |
1.27e-35 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 148.25 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 551 DKTITEVDEEHVHRANPP-ELDQVEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR 628
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPfKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 629 R----DGLPAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLV-GMAGSVDGRVSvEKIRATFTVLRAF 703
Cdd:PTZ00014 155 DakdsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAsSKSGNMDLKIQ-NAIMAANPVLEAF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 704 GSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMA--- 780
Cdd:PTZ00014 234 GNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEeyk 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 781 -------------DSSSFGMGVWSkpedkqkaaaafaqlqgaMEMLGISESEQRAVWRVLAAIYHLGAA----------- 836
Cdd:PTZ00014 314 yinpkcldvpgidDVKDFEEVMES------------------FDSMGLSESQIEDIFSILSGVLLLGNVeiegkeegglt 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 837 -GACKVGRKQfmrfEWANYAAEALGCEYEELntatfKHHLrqIIQQMTFGP----SRWGLEDEETSsglkmtgvdcVEGM 911
Cdd:PTZ00014 376 dAAAISDESL----EVFNEACELLFLDYESL-----KKEL--TVKVTYAGNqkieGPWSKDESEML----------KDSL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 912 ASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVST 987
Cdd:PTZ00014 435 SKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEvfknN----------SLEQLFINITNEMLQKNFVDIVFERE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 988 LQRYQEEGVP---VQFdlpdpspgTTvavvdqNPSQVRLPAGGGaqdaRGLFWVLDEEVHVEGSSDsvvlERLCAAFEKK 1064
Cdd:PTZ00014 505 SKLYKDEGISteeLEY--------TS------NESVIDLLCGKG----KSVLSILEDQCLAPGGTD----EKFVSSCNTN 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1065 gagTEGSSALRTCE--QPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcra 1142
Cdd:PTZ00014 563 ---LKNNPKYKPAKvdSNKNFVIKHTIG--DIQYCASGFLFKNKDVLRP-ELVEVVKASPNPLVRDLF------------ 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1143 vaglEGtsqQALQRSRMVRRTFASslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRSgqesppppqp 1222
Cdd:PTZ00014 625 ----EG---VEVEKGKLAKGQLIG-----------SQFLNQLDSLMSLINSTEPHFIRCIKPN---ENKK---------- 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1223 grdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLlkklmSTSEGIDERKAVEELLE 1302
Cdd:PTZ00014 674 ---------PLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAV-----SNDSSLDPKEKAEKLLE 739
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 51317366 1303 TLDLEKKAVAVGHSQVFLKAGVISRL-EKQREKLVS-QSIV-LFQAACKGFLSRQEFKK 1358
Cdd:PTZ00014 740 RSGLPKDSYAIGKTMVFLKKDAAKELtQIQREKLAAwEPLVsVLEALILKIKKKRKVRK 798
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
586-1321 |
5.92e-35 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 144.83 E-value: 5.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSV-PSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKflPIYnPKYVKMYQNRRLGkLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 662 SGAGKTTCCEQVLEHLVgmAGSVDGRVS-VEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd01385 82 SGSGKTESTNFLLHHLT--ALSQKGYGSgVEQtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGmgvwskpEDKQKAAAAFAQLQGAMEML 813
Cdd:cd01385 160 LLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLkqpedyHYLNQSDCYT-------LEGEDEKYEFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 814 GISESEQRAVWRVLAAIYHLgaagackvGRKQFMRfeWANYAAEALGCEYEE-LNTATfkhHLRQIIQQMtfgpsrwgLE 892
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHL--------GNIEYKK--KAYHRDESVTVGNPEvLDIIS---ELLRVKEET--------LL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 893 DEETSSGLKMTGVDCV------------EGMASGLYQELFAAVV-----SLINRSFSSHHlSMASIMVVDSPGFQNPRHQ 955
Cdd:cd01385 292 EALTTKKTVTVGETLIlpyklpeaiatrDAMAKCLYSALFDWIVlrinhALLNKKDLEEA-KGLSIGVLDIFGFEDFGNN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 956 gkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFdlpdpspgttvavVDqNPSQVRLPAGggaqDA 1032
Cdd:cd01385 371 ------SFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISwhnIEY-------------TD-NTGCLQLISK----KP 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1033 RGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtegssalRTCEQPLQCE----IFHQLGwdPVRYDLTGWLHRAKPN 1108
Cdd:cd01385 427 TGLLCLLDEESNFPGATNQTLLAKFKQQHKDN----------KYYEKPQVMEpafiIAHYAG--KVKYQIKDFREKNLDL 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1109 LSAlDAPQVLHQSK----RE-------------ELRSLFQARAKLPPVCRA----VAGLEGTSQQALQRSRMVRRTfass 1167
Cdd:cd01385 495 MRP-DIVAVLRSSSsafvREligidpvavfrwaVLRAFFRAMAAFREAGRRraqrTAGHSLTLHDRTTKSLLHLHK---- 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1168 laavRRKAPCSQIKLQ--MDALTSMIKRSRLHFIHCLVPNpvvesrsgqesppppqpgRDKpgagGPLALDIPALRVQLA 1245
Cdd:cd01385 570 ----KKKPPSVSAQFQtsLSKLMETLGQAEPFFIRCIKSN------------------AEK----KPLRFDDELVLRQLR 623
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51317366 1246 GFHILEALRLHRTGYADHMGLTRFRRQFQVLdapLLKKLMSTSEGIderkavEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd01385 624 YTGMLETVRIRRSGYSVRYTFQEFITQFQVL---LPKGLISSKEDI------KDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
585-1260 |
8.24e-33 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 137.96 E-value: 8.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSV---PSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDiygLEQVQQYSGRALGeLPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAtGRITAAQLQTML 740
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLVT-EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 741 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL---------HQMADSSSFGMGvwskpedkqkAAAAFAQLQGAME 811
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLqeaekyfylNQGGNCEIAGKS----------DADDFRRLLAAMQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 812 MLGISESEQRAVWRVLAAIYHLG-----------AAGACKVGRKQFMRfewanYAAEALGCEYEELNTA-TFKhhLRQII 879
Cdd:cd01387 229 VLGFSSEEQDSIFRILASVLHLGnvyfhkrqlrhGQEGVSVGSDAEIQ-----WVAHLLQISPEGLQKAlTFK--VTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 880 QQMTFGPsrwgLEDEEtssglkmtGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdr 959
Cdd:cd01387 302 RERIFTP----LTIDQ--------ALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 960 aaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpvqfdlpdpsPGTTVAVVDQNPSQVRLpagggAQDARGLFWVL 1039
Cdd:cd01387 366 --SFEQLCINYANENLQYYFNKHVFKLEQEEYIREQI----------DWTEIAFADNQPVINLI-----SKKPVGILHIL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1040 DEEVHVEGSSDSVVLERlCaafEKKGAGTEGSSALRTCEQPLQceIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLH 1119
Cdd:cd01387 429 DDECNFPQATDHSFLEK-C---HYHHALNELYSKPRMPLPEFT--IKHYAG--QVWYQVHGFLDKNRDQLRQ-DVLELLV 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1120 QSKREELRSLF-----QARAKLPpvcravAGLEGTSQQALQRSRMVRRTFASSLaavrrkapcsqiklqMDALTSMiKRS 1194
Cdd:cd01387 500 SSRTRVVAHLFsshraQTDKAPP------RLGKGRFVTMKPRTPTVAARFQDSL---------------LQLLEKM-ERC 557
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51317366 1195 RLHFIHCLVPNpvvesrsgqesppppqpgRDKpgagGPLALDIPALRVQLAGFHILEALRLHRTGY 1260
Cdd:cd01387 558 NPWFVRCLKPN------------------HKK----EPMLFDMDVVMAQLRYSGMLETIRIRKEGY 601
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
585-1276 |
9.37e-32 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 134.52 E-value: 9.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP----SVPSAGKVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSlplfSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLVGMAGSVDgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQLQTML 740
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQT-EDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASVSHYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 741 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSF----GMGVWSKPEDKqkaaAAFAQLQGAMEMLGIS 816
Cdd:cd14896 159 LETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYlnqgGACRLQGKEDA----QDFEGLLKALQGLGLC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 817 ESEQRAVWRVLAAIYHLGaaGACkvgrkqFMRFEWANYAAEALGCEYEELNTATFKH----HLRQII-QQMTFGPSRWgl 891
Cdd:cd14896 234 AEELTAIWAVLAAILQLG--NIC------FSSSERESQEVAAVSSWAEIHTAARLLQvppeRLEGAVtHRVTETPYGR-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 892 edeeTSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFS--SHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCH 968
Cdd:cd14896 304 ----VSRPLPVEGaIDARDALAKTLYSRLFTWLLKRINAWLAppGEAESDATIGVVDAYGFEALRVNG------LEQLCI 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 969 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdLPDPSPgttvavvdQNPSQVRLPAGggaqDARGLFWVLDEEVHVEGS 1048
Cdd:cd14896 374 NLASERLQLFSSQTLLAQEEEECQRELLPW---VPIPQP--------PRESCLDLLVD----QPHSLLSILDDQTWLSQA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1049 SDSVVLErlcaafekKGAGTEGSSALRTCEQpLQCEIF---HQLGwdPVRYDLTGWLHRakpNLSALDaPQVLH---QSK 1122
Cdd:cd14896 439 TDHTFLQ--------KCHYHHGDHPSYAKPQ-LPLPVFtvrHYAG--TVTYQVHKFLNR---NRDQLD-PAVVEmlaQSQ 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1123 REELRSLFQaraklppvcravaglEGTSQQALQRSRmvrrtfaSSLAavrrkapcSQIKLQMDALTSMIKRSRLHFIHCL 1202
Cdd:cd14896 504 LQLVGSLFQ---------------EAEPQYGLGQGK-------PTLA--------SRFQQSLGDLTARLGRSHVYFIHCL 553
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51317366 1203 VPNPVvesrsgqesppppqpgrDKPGaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1276
Cdd:cd14896 554 NPNPG-----------------KLPG-----LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL 605
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
586-1209 |
6.46e-31 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 132.41 E-value: 6.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGRRD-----GLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDinqnkSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 660 GWSGAGKTTCCEQVLEHLVGMAGSV--------DGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT-G 729
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNqqqnnnnnNNNNSIEKdILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 730 RITAAQLQTMLLEKSRVARQPEGES-NFLVFSQMLAGLDLDLRTELNLHQMADS-----------SSF---GMGVWSKPE 794
Cdd:cd14906 162 KIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNDPSKyryldarddviSSFksqSSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 795 DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEwanyaAEALGCEYEELnTATFKHH 874
Cdd:cd14906 242 NKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGN-----------IEFE-----EDSDFSKYAYQ-KDKVTAS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 875 LRQIIQQMTFGPSRWglEDEETSSGLKMTGVDCV--------------EGMASGLYQELFAAVVSLINRSF----SSHHL 936
Cdd:cd14906 305 LESVSKLLGYIESVF--KQALLNRNLKAGGRGSVycrpmevaqseqtrDALSKSLYVRLFKYIVEKINRKFnqntQSNDL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 937 SMAS-------IMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpvqfdlpdpsPGT 1009
Cdd:cd14906 383 AGGSnkknnlfIGVLDIFGFENLSSN------SLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGI----------PWS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1010 TVAVVDqNPSQVRLPagggAQDARGLFWVLDEEVHVEGSSDSVVLERlcaaFEKKGAGTEgSSALRTCEQpLQCEIFHQL 1089
Cdd:cd14906 447 NSNFID-NKECIELI----EKKSDGILSLLDDECIMPKGSEQSLLEK----YNKQYHNTN-QYYQRTLAK-GTLGIKHFA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1090 GwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFQARAKLPPvcravaglegTSQQalqrsrmvRRTFASSLA 1169
Cdd:cd14906 516 G--DVTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT----------NTTK--------KQTQSNTVS 574
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 51317366 1170 avrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVE 1209
Cdd:cd14906 575 --------GQFLEQLNQLIQTINSTSVHYIRCIKPNQTMD 606
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
633-1063 |
1.36e-30 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 130.93 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 633 PAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLV--GMAGSVDGRVSVEKIRATFT------------ 698
Cdd:cd14891 55 PYAIAEMAYQQMCLGSGRMQNQSIVISGESGAGKTETSKIILRFLTtrAVGGKKASGQDIEQSSKKRKlsvtslderlmd 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 699 ---VLRAFGSVSMAHSRSATRFSMVMSLDFNATG-RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL 774
Cdd:cd14891 135 tnpILESFGNAKTLRNHNSSRFGKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKEL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 775 NLhqmadsssfgmgvwSKPEDKQKAAAAF-------------AQLQGAMEMLGISESEQRAVWRVLAAIYHLG------- 834
Cdd:cd14891 215 LL--------------LSPEDFIYLNQSGcvsddniddaanfDNVVSALDTVGIDEDLQLQIWRILAGLLHLGniefdee 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 835 --AAGACKVGRKQFMrfEWANYAAEALGCEYEELntatfkhhLRQIIQQ--MTFGPSRWGLEDEETSSGLKmtgvdcvEG 910
Cdd:cd14891 281 dtSEGEAEIASESDK--EALATAAELLGVDEEAL--------EKVITQReiVTRGETFTIKRNAREAVYSR-------DA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 911 MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNprhqgKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQR 990
Cdd:cd14891 344 IAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFES-----FETKNDFEQLLINYANEALQATFNQQVFIAEQEL 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51317366 991 YQEEGVPV-QFDLPDpspgttvavvdqNPSQVRLPagggAQDARGLFWVLDEEVHVEGSSDSVVLERLCAAFEK 1063
Cdd:cd14891 419 YKSEGIDVgVITWPD------------NRECLDLI----ASKPNGILPLLDNEARNPNPSDAKLNETLHKTHKR 476
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
635-1211 |
1.61e-30 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 131.31 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 635 HIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSV---EKIRATFTVLRAFGSVSMAHS 711
Cdd:cd14887 63 HPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQgleARLLQSGPVLEAFGNAHTVLN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 712 RSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLdlrtelnlhqmadSSSFGMGVWS 791
Cdd:cd14887 143 ANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVA-------------AATQKSSAGE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 792 K-PEdkqkaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQfmRFEWANYAAEALGC--------- 861
Cdd:cd14887 210 GdPE-----STDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPE--TSKKRKLTSVSVGCeetaadrsh 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 862 --EYEELN-----TATFKHHLRQIIQQMTFGPSRWGLED----------EETSSGLKMTGVDCVEGMAS-GLYQELFAAV 923
Cdd:cd14887 283 ssEVKCLSsglkvTEASRKHLKTVARLLGLPPGVEGEEMlrlalvsrsvRETRSFFDLDGAAAARDAACkNLYSRAFDAV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 924 VSLINRSFSSHHLSMAS--------------IMVVDSPGFQNPRHQGKDRaatFEELCHNYAHERLQLLFYQRTFVSTLQ 989
Cdd:cd14887 363 VARINAGLQRSAKPSESdsdedtpsttgtqtIGILDLFGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHM 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 990 RYQEEGVPVQFDL-PDPSPGTTVAVVDQNPSQVRLPAGGGAQDARGLFWVLDEEVHVEGSSDSVVLE-------RLCA-- 1059
Cdd:cd14887 440 LYTQEGVFQNQDCsAFPFSFPLASTLTSSPSSTSPFSPTPSFRSSSAFATSPSLPSSLSSLSSSLSSsppvwegRDNSdl 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1060 AFEKKGAGTEGSSALRTCEQPLQCE-----IFHQLGwdPVRYDLTGWLHRAKPNLSaldapqvlhqskrEELRSLFQAra 1134
Cdd:cd14887 520 FYEKLNKNIINSAKYKNITPALSREnleftVSHFAC--DVTYDARDFCRANREATS-------------DELERLFLA-- 582
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51317366 1135 klppvCRAVaglegTSQQALQRSRMVRrtfassLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESR 1211
Cdd:cd14887 583 -----CSTY-----TRLVGSKKNSGVR------AISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAG 643
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
585-1289 |
8.00e-30 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 128.39 E-value: 8.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAGKVPKGRR-DGLPAHIGSMAQRAYWALLNQRRDQSIV 657
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPykelpiYSTMVSQLYLSSSGQLcSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 658 ALGWSGAGKTTCCEQVLEHLVGMAGSvdGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDF-NATGRITAAQ 735
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS--SRTTFDsRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 736 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVwskPEDKQKAAAAFAQLQ-----GAM 810
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTM---REDVSTAERSLNREKlavlkQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 811 EMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNtatfkhhlrQIIQQMTFGPsrwg 890
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGD-----------IRFTALTEADSAFVSDLQLLE---------QVAGMLQVST---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 891 ledEETSSGLkMTGVDCVEG------------------MASGLYQELFAAVVSLINRSFSSHH----LSMASIMVVDSPG 948
Cdd:cd14878 292 ---DELASAL-TTDIQYFKGdmiirrhtiqiaefyrdlLAKSLYSRLFSFLVNTVNCCLQSQDeqksMQTLDIGILDIFG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 949 FQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLpdpSPGTTVAVVD---QNPSqvrlpa 1025
Cdd:cd14878 368 FEEFQKN------EFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAY---SPGNQTGVLDfffQKPS------ 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1026 gggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGT------EGSSALRTCEQPLQCEIFHQLGwdPVRYDLT 1099
Cdd:cd14878 433 --------GFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAvyspmkDGNGNVALKDQGTAFTVMHYAG--RVMYEIV 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1100 GWLHRAKPNLSaldapQVLhqskreelrsLFQARaklppvcravaglegTSQQALqrsrmVRRTFASSLAAVrrkapCSQ 1179
Cdd:cd14878 503 GAIEKNKDSLS-----QNL----------LFVMK---------------TSENVV-----INHLFQSKLVTI-----ASQ 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1180 IKLQMDALTSMIKRSRLHFIHCLVPNpvvesrsgqesppppqpgrdkpGAGGPLALDIPALRVQLAGFHILEALRLHRTG 1259
Cdd:cd14878 543 LRKSLADIIGKLQKCTPHFIHCIKPN----------------------NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYG 600
|
730 740 750
....*....|....*....|....*....|..
gi 51317366 1260 YADHMGLTRFRRQFQVLDAPLL--KKLMSTSE 1289
Cdd:cd14878 601 YPVRLSFSDFLSRYKPLADTLLgeKKKQSAEE 632
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
631-1273 |
2.50e-29 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 127.23 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 631 GLPAHIGSMAQRAYWALLNQ-RRDQSIVALGWSGAGKTTCCEQVLEHLVGMA----GSVDGRVSVEKIRATFT----VLR 701
Cdd:cd14875 53 LLPPHIWQVAHKAFNAIFVQgLGNQSVVISGESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDENLKwsnpVME 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 702 AFGSVSMAHSRSATRFSMVMSLDFN-ATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL-NLHQM 779
Cdd:cd14875 133 SFGNARTVRNDNSSRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 780 AD------SSSF-GMGVWSKPEDKqkaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFE-- 850
Cdd:cd14875 213 QDykclngGNTFvRRGVDGKTLDD---AHEFQNVRHALSMIGVELETQNSIFRVLASILHLME-----------VEFEsd 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 851 ------WANYAAEALGCEYEELNTATfkhhLRQIIqqmtfgpsrwgLEDEETSSGLKMTGVDCVEGM----ASGLYQELF 920
Cdd:cd14875 279 qndkaqIADETPFLTACRLLQLDPAK----LRECF-----------LVKSKTSLVTILANKTEAEGFrnafCKAIYVGLF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 921 AAVVSLINRSFSSHH--LSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPV 998
Cdd:cd14875 344 DRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNS------FEQLCINYANESLQNHYNKYTFINDEEECRREGIQI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 999 -QFDLPDPSpgTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTC 1077
Cdd:cd14875 418 pKIEFPDNS--ECVNMFDQKRT--------------GIFSMLDEECNFKGGTT----ERFTTNLWDQWANKSPYFVLPKS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1078 EQPLQCEIFHQLGWdpVRYDLTGWLHRakpNLSAL--DAPQVLHQSKREELRSLFQARAKLPpvcravaglegtsqqalQ 1155
Cdd:cd14875 478 TIPNQFGVNHYAAF--VNYNTDEWLEK---NTDALkeDMYECVSNSTDEFIRTLLSTEKGLA-----------------R 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1156 RSRMVRRTFASSLAAVRrkapcsqiklqmdaltSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLAL 1235
Cdd:cd14875 536 RKQTVAIRFQRQLTDLR----------------TELESTETQFIRCIKPNMEAS----------------------PSFL 577
|
650 660 670
....*....|....*....|....*....|....*...
gi 51317366 1236 DIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQF 1273
Cdd:cd14875 578 DNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYF 615
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
586-1205 |
4.45e-28 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 122.72 E-value: 4.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVPK--------------GRRDGLPAHIGSMAQRAYWALLN 649
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfqKLPGLYSSDTMAKyllsfearssstrnKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 650 QRR----DQSIVALGWSGAGKTTCCEQVLEHLvGMAGSVDGRVSV----------EKIRATFTVLRAFGSVSMAHSRSAT 715
Cdd:cd14900 82 GLNgvmsDQSILVSGESGSGKTESTKFLMEYL-AQAGDNNLAASVsmgkstsgiaAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 716 RFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSssfgmgvwskped 795
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKRDMYRRVMDA------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 796 kqkaaaafaqlqgaMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQFM--RFEWA-NYAAEALGCEYEE 865
Cdd:cd14900 228 --------------MDIIGFTPHERAGIFDLLAALLHIGnltfehdENSDRLGQLKSDLapSSIWSrDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 866 LNTATfkhHLRQIIQQMTFGPSRWGLEDEETSSglkmtgvdcvEGMASGLYQELFAAVVSLINRSF-----SSHHLSMAS 940
Cdd:cd14900 294 LEKAL---SVRRIRAGTDFVSMKLSAAQANNAR----------DALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 941 IMVVDSPGFQN-PRHqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDqNPS 1019
Cdd:cd14900 361 IGILDIFGFEVfPKN-------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKY----------VEFCD-NQD 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1020 QVRLPagggAQDARGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtEGSSALRTCEQPLQCEIFHQLGwdPVRYDLT 1099
Cdd:cd14900 423 CVNLI----SQRPTGILSLIDEECVMPKGSDTTLASKLYRACGSH----PRFSASRIQRARGLFTIVHYAG--HVEYSTD 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1100 GWLHRAKpnlsaldapQVLHQskreELRSLFQAraklppvcravaglegtsqqalqrsrmvrrtfasslaavrrkapCSQ 1179
Cdd:cd14900 493 GFLEKNK---------DVLHQ----EAVDLFVY--------------------------------------------GLQ 515
|
650 660
....*....|....*....|....*.
gi 51317366 1180 IKLQMDALTSMIKRSRLHFIHCLVPN 1205
Cdd:cd14900 516 FKEQLTTLLETLQQTNPHYVRCLKPN 541
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
586-996 |
1.09e-27 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 121.16 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGK--VPKGRRDGLPaHIGSMAQRAYWALLNQRrDQSIVALGWSG 663
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMkaYLKNYSHVEP-HVYDVAEASVQDLLVHG-NQTIVISGESG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 664 AGKTTCCEQVLEHLV-GMAGSVdgrvSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNatGRITAAQLQTMLL 741
Cdd:cd14898 80 SGKTENAKLVIKYLVeRTASTT----SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 742 EKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqmADSSSFGmgvwSKPEDKQKAAAAFAQLQGAMEMLGISESeqR 821
Cdd:cd14898 154 EKSRVTHHEKGERNFHIFYQFCASKRLNIKNDF-----IDTSSTA----GNKESIVQLSEKYKMTCSAMKSLGIANF--K 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 822 AVWRVLAAIYHLGAAGACKVGRKQFMRFEWANYAAEALGCEYEELNTATFKhhlrqiiqqmtfGPSRWGLEDEETSSGLK 901
Cdd:cd14898 223 SIEDCLLGILYLGSIQFVNDGILKLQRNESFTEFCKLHNIQEEDFEESLVK------------FSIQVKGETIEVFNTLK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 902 mTGVDCVEGMASGLYQELFAAVVSLINRSFSSHhlSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQ 981
Cdd:cd14898 291 -QARTIRNSMARLLYSNVFNYITASINNCLEGS--GERSISVLDIFGFEIFESNG------LDQLCINWTNEKIQNDFIK 361
|
410
....*....|....*
gi 51317366 982 RTFVSTLQRYQEEGV 996
Cdd:cd14898 362 KMFRAKQGMYKEEGI 376
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
585-1205 |
1.34e-27 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 121.50 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAgKVPKGRRD--------GLPAHIGSMAQRAYWALLNQRR--DQ 654
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKP-VPQL-YSPELMREyhaapqpqKLKPHIFTVGEQTYRNVKSLIEpvNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 655 SIVALGWSGAGKTTCCEQVLEHLVGMAGSV---DGRVSVEKIRATF----TVLRAFGSVSMAHSRSATRFSMVMSLDFNA 727
Cdd:cd14880 79 SIVVSGESGAGKTWTSRCLMKFYAVVAASPtswESHKIAERIEQRIlnsnPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 728 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSsfgmgvWSKPEDKQKAAAAFAQLQ 807
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFS------WLPNPERNLEEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 808 GAMEMLGISESEQRAVWRVLAAIYHLG---------AAGACKV--GRKQFMRFewanyAAEALGCEYEELNTATFKHHLR 876
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGniqfadsedEAQPCQPmdDTKESVRT-----SALLLKLPEDHLLETLQIRTIR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 877 QIIQQMTF-GPSRWGLEDeetssglkmTGVDCvegMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQNPRH 954
Cdd:cd14880 308 AGKQQQVFkKPCSRAECD---------TRRDC---LAKLIYARLFDWLVSVINSSICADTDSWTTfIGLLDVYGFESFPE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 955 QgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSpgTTVAVVDQNPSQVrlpagggaqdar 1033
Cdd:cd14880 376 N------SLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFiNYQDNQ--TCLDLIEGSPISI------------ 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1034 glFWVLDEEVHVEGSSDSVVLErlcAAFEKKGAGTEGSSALRTCEQPlQCEIFHQLGwdPVRYDLTGWLHRAK----PNL 1109
Cdd:cd14880 436 --CSLINEECRLNRPSSAAQLQ---TRIESALAGNPCLGHNKLSREP-SFIVVHYAG--PVRYHTAGLVEKNKdpvpPEL 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1110 SaldapQVLHQSKREELRSLFQARAKlppvcravaglEGTSQQALQRSRmvrrtfASSLAAVrrkapcSQIKLQMDALTS 1189
Cdd:cd14880 508 T-----RLLQQSQDPLLQKLFPANPE-----------EKTQEEPSGQSR------APVLTVV------SKFKASLEQLLQ 559
|
650
....*....|....*.
gi 51317366 1190 MIKRSRLHFIHCLVPN 1205
Cdd:cd14880 560 VLHSTTPHYIRCIKPN 575
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
587-1321 |
3.58e-26 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 117.01 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 587 VLNTLLQRYKAQLLHTCTGPDLIVLQP-------------RGPSVPSAGKvpkgrrdgLPAHIGSMAQRAYWALLNQRRD 653
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirKYRDAPDLTK--------LPPHVFYTARRALENLHGVNKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 654 QSIVALGWSGAGKTTCCEQVLEHL-VGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRIT 732
Cdd:cd14876 75 QTIIVSGESGAGKTEATKQIMRYFaSAKSGNMDLRIQ-TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 733 AAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMAD-----SSSFGMGVWSKPEDkqkaaaaFAQLQ 807
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEykflnPKCLDVPGIDDVAD-------FEEVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 808 GAMEMLGISESEQRAVWRVLAAIYHLGAAgacKVGRKQFMRFEwanYAAEALGCEYEELNTATFKHHL------RQIIQQ 881
Cdd:cd14876 227 ESLKSMGLTEEQIDTVFSIVSGVLLLGNV---KITGKTEQGVD---DAAAISNESLEVFKEACSLLFLdpealkRELTVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 882 MTF-GP----SRWGLEDEETssgLKMTgvdcvegMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQg 956
Cdd:cd14876 301 VTKaGGqeieGRWTKDDAEM---LKLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNN- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 957 kdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPvqfdlpdpspgTTVAVVDQNPSQVRLPAGGGaqdaRGLF 1036
Cdd:cd14876 370 -----SLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIP-----------TAELEYTSNAEVIDVLCGKG----KSVL 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1037 WVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQ 1116
Cdd:cd14876 430 SILEDQCLAPGGSD----EKFVSACVSKLKSNGKFKPAKV-DSNINFIVVHTIG--DIQYNAEGFLFKNKDVLRA-ELVE 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1117 VLHQSKREELRSLFqaraklppvcravaglEGtsqQALQRSRMVRrtfaSSLAAvrrkapcSQIKLQMDALTSMIKRSRL 1196
Cdd:cd14876 502 VVQASTNPVVKALF----------------EG---VVVEKGKIAK----GSLIG-------SQFLKQLESLMGLINSTEP 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1197 HFIHCLVPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1276
Cdd:cd14876 552 HFIRCIKPN---ETKK-------------------PLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL 609
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 51317366 1277 DAPLlkklmSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14876 610 DLGI-----ANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
586-1283 |
4.64e-25 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 113.46 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAGK--VPKGRRDG------------LPAHIGSMAQRAYWALLN-Q 650
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPF-QRLPLYGKeiLESYRQEGllrsqgiespqaLGPHVFAIADRSYRQMMSeI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 651 RRDQSIVALGWSGAGKTTCCEQVLEHL--VGMAGSV-------DGRVSV-EKIRATFTVLRAFGSVSMAHSRSATRFSMV 720
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLttLGNGEEGapnegeeLGKLSImDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 721 MSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFG------MGVWSKPE 794
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQLpnefhyTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 795 -DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-----------AAGACKVGRKQFMrfewaNYAAEALGCE 862
Cdd:cd14908 241 lREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGqlefeskeedgAAEIAEEGNEKCL-----ARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 863 YEELNTAtfkhhLRQIIQQMTFGPSRWGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLS--MAS 940
Cdd:cd14908 316 VDKLLRA-----LTSKIIVVRGKEITTKLTPHKAY--------DARDALAKTIYGALFLWVVATVNSSINWENDKdiRSS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 941 IMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDpspgttvavvdqNPS 1019
Cdd:cd14908 383 VGVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFiEFPD------------NQD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1020 QVRLPAGggaqDARGLFWVLDEEvhvegssdsvvlerlCAAFEKkgaGTEGSSALRTCEQPLQceifhqlgwdpvrydlt 1099
Cdd:cd14908 445 CLDTIQA----KKKGILTMLDDE---------------CRLGIR---GSDANYASRLYETYLP----------------- 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1100 gwlhrakpnlsalDAPQVLHQSKREELRSLfqARAKLppvCRAVAGLEGTSQQALQRSRMVRRTFASSLAAVRRKAPCSQ 1179
Cdd:cd14908 486 -------------EKNQTHSENTRFEATSI--QKTKL---IFAVRHFAGQVQYTVETTFCEKNKDEIPLTADSLFESGQQ 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1180 IKLQMDALTSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTG 1259
Cdd:cd14908 548 FKAQLHSLIEMIEDTDPHYIRCIKPNDAAK----------------------PDLVTRKRVTEQLRYGGVLEAVRVARSG 605
|
730 740
....*....|....*....|....
gi 51317366 1260 YADHMGLTRFRRQFQVLdAPLLKK 1283
Cdd:cd14908 606 YPVRLPHKDFFKRYRML-LPLIPE 628
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
587-996 |
3.97e-23 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 107.28 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 587 VLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVPKGRR--------DGLPAHIGSMAQRAYWALLNQRRDQSI 656
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfkQIRNLYGTEVIGRYRQadtsrgfpSDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 657 VALGWSGAGKTTCCEQVLEHLVgmAGSVDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 735
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFA--YGHSTSSTDVQSlILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 736 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMaDSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLgI 815
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSL-ESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-F 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 816 SESEQRAVWRVLAAIYHLGAAGACKVGRkqfMRFEwaNYAAEALGCEYEEL------NTATFKHHLRQ---IIQQMTFgp 886
Cdd:cd14886 239 SKNEIDSFYKCISGILLAGNIEFSEEGD---MGVI--NAAKISNDEDFGKMcellgiESSKAAQAIITkvvVINNETI-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 887 srwgledeeTSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 966
Cdd:cd14886 312 ---------ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN------TYEQL 376
|
410 420 430
....*....|....*....|....*....|
gi 51317366 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEGV 996
Cdd:cd14886 377 LINYANERLQQYFINQVFKSEIQEYEIEGI 406
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1401-2086 |
5.37e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.83 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1401 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAERLQAFREVQELKSK 1480
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER-------LANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1481 HEQVQKKLGDVNKQLEEAQQKIqlndlernptggaDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGEL 1560
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEEL-------------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1561 QSAYDGAKKMAHQLKRKchhltcdledtcvlLENQQSRNHELEKKQKKFDLQLAQALGESVfEKGLREKVTQENT----- 1635
Cdd:TIGR02168 399 NNEIERLEARLERLEDR--------------RERLQQEIEELLKKLEEAELKELQAELEEL-EEELEELQEELERleeal 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1636 -SVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGspsLGENCVAGLKERLWKlessaleqqkiqSQQENTIKQL 1714
Cdd:TIGR02168 464 eELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG---FSEGVKALLKNQSGL------------SGILGVLSEL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1715 EQLRQRFELEIE-----RMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDqi 1789
Cdd:TIGR02168 529 ISVDEGYEAAIEaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD-- 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1790 gHRDFDVEKRL------------------RRDLRRTHALLSDVQL---LLG-----TMEDGKTSVS----KEELEKVHSQ 1839
Cdd:TIGR02168 607 -LVKFDPKLRKalsyllggvlvvddldnaLELAKKLRPGYRIVTLdgdLVRpggviTGGSAKTNSSilerRREIEELEEK 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1840 LEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAA 1919
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1920 DIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRD 1998
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1999 SLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIA 2078
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
....*...
gi 51317366 2079 DLQAALEE 2086
Cdd:TIGR02168 926 QLELRLEG 933
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
585-1274 |
5.80e-23 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 106.98 E-value: 5.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP---SVPSAGKVPKGRRDGL-----------PAHIGSMAQRAYWALLNQ 650
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPlpiYTPDHMQAYNKSREQTplyekdtvndaPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 651 RRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-----------KIRATFTVLRAFGSVSMAHSRSATRFSM 719
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEgasgvlhpigqQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 720 VMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLD--LRTELNLHQMADssSFGMGVWSKPE--D 795
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVN--EFVMLKQADPLatN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 796 KQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQfmrfewANYAAEALGCEYEELNT 868
Cdd:cd14893 239 FALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGnvdfvpdPEGGKSVGGAN------STTVSDAQSCALKDPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 869 ATFKHHLRQ---IIQQMTFGPSRWGLED-EETSSGLKMTGV----DCVEGMASGLYQELFAAVVSLIN-------RSFSS 933
Cdd:cd14893 313 ILLAAKLLEvepVVLDNYFRTRQFFSKDgNKTVSSLKVVTVhqarKARDTFVRSLYESLFNFLVETLNgilggifDRYEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 934 HHLSMAS--IMVVDSPGFQN--PRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDpspGT 1009
Cdd:cd14893 393 SNIVINSqgVHVLDMVGFENltPSQNS------FDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVENRLTV---NS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1010 TVAVVDQNPSQVRLpaggGAQDARGLFWVLDEEVHVEGSSDSVVLERLCAAFEK--------KGAGTEGSSALRTCEQPL 1081
Cdd:cd14893 464 NVDITSEQEKCLQL----FEDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAvgglsrpnMGADTTNEYLAPSKDWRL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1082 QCEIFHQLGwdPVRYDLTGWLHRAKPNLSALDApQVLHQSKREELRSLFQARAklppvcrAVAGLEGTSQQALQRSRmVR 1161
Cdd:cd14893 540 LFIVQHHCG--KVTYNGKGLSSKNMLSISSTCA-AIMQSSKNAVLHAVGAAQM-------AAASSEKAAKQTEERGS-TS 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1162 RTFASSLAAVRR-----KAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESRsgqesppppqpgrdkpgaggplALD 1236
Cdd:cd14893 609 SKFRKSASSAREsknitDSAATDVYNQADALLHALNHTGKNFLVCIKPNETLEEG----------------------VFD 666
|
730 740 750
....*....|....*....|....*....|....*...
gi 51317366 1237 IPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQ 1274
Cdd:cd14893 667 SAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
585-1276 |
1.24e-21 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 102.26 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVPKgrrdglPAHIGSMAQRAYWALL-NQRRDQSIVALGWSG 663
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIK------KCHISGVAENALDRIKsMSSNAESIVFGGESG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 664 AGKTTCCEQVLEHLVGMAGSvdgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQLQ-TMLLE 742
Cdd:cd14874 75 SGKSYNAFQVFKYLTSQPKS---KVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLTGLNLKyTVPLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 743 KSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMadSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQRA 822
Cdd:cd14874 151 VPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDDHCIS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 823 VWRVLAAIYHLGaagackvgrKQFMRFEWANYAAEALGcEYEELNTATFKHHLRQI-IQQMtfgpSRWGLEDEETSSGLK 901
Cdd:cd14874 229 IYKIISTILHIG---------NIYFRTKRNPNVEQDVV-EIGNMSEVKWVAFLLEVdFDQL----VNFLLPKSEDGTTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 902 M-TGVDCVEGMASGLYQELFAAVVSLINRSFSShHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFY 980
Cdd:cd14874 295 LnAALDNRDSFAMLIYEELFKWVLNRIGLHLKC-PLHTGVISILDHYGFEKYNNNG------VEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 981 QRTFVSTLQRYQEEGVPVQFDLPDP-SPGTTVAVVDQNPsqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCA 1059
Cdd:cd14874 368 KHSFHDQLVDYAKDGISVDYKVPNSiENGKTVELLFKKP--------------YGLLPLLTDECKFPKGSHESYLEHCNL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1060 AFEKKGAGTEGSSALRtceqpLQCEIFHQLG--WdpvrYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQARAKlp 1137
Cdd:cd14874 434 NHTDRSSYGKARNKER-----LEFGVRHCIGttW----YNVTDFFSRNKRIIS-LSAVQLLRSSKNPIIGLLFESYSS-- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1138 pvcravagleGTSQQALQRSRMVRRTfASSLAavrrkapcsqiklqmdaltSMIKRSRLHFIHCLvpnpvvesRSGQESp 1217
Cdd:cd14874 502 ----------NTSDMIVSQAQFILRG-AQEIA-------------------DKINGSHAHFVRCI--------KSNNER- 542
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 51317366 1218 pppQPGRdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1276
Cdd:cd14874 543 ---QPKK----------FDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
586-1053 |
8.28e-21 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 99.80 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgpsvpsagkvpkgRRDGLPAHIGSMAQRA-YWALLN-------QRRD---- 653
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY-------------RDVGNPLTLTSTRSSPlAPQLLKvvqeavrQQSEtgyp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 654 QSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATR---FSMVMSLDfnatGR 730
Cdd:cd14881 69 QAIILSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRighFIEVQVTD----GA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL--HQMADSS--SFGMGVWSKPEDKqkaaAAFAQL 806
Cdd:cd14881 145 LYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLdgYSPANLRylSHGDTRQNEAEDA----ARFQAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 807 QGAMEMLGISESEqraVWRVLAAIYHLG--------AAGACKVGRKQFmrfewaNYAAEALGCE----YEELNTATfkHH 874
Cdd:cd14881 221 KACLGILGIPFLD---VVRVLAAVLLLGnvqfidggGLEVDVKGETEL------KSVAALLGVSgaalFRGLTTRT--HN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 875 LR-QIIQQmtfgpsrwgLEDEETSSGLKmtgvDCvegMASGLYQELFAAVVSLINR-----SFSSHHLSMASIMVVDSPG 948
Cdd:cd14881 290 ARgQLVKS---------VCDANMSNMTR----DA---LAKALYCRTVATIVRRANSlkrlgSTLGTHATDGFIGILDMFG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 949 FQNPrhqgkdRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDlpdpspgttVAVVDQNP-----SQVRL 1023
Cdd:cd14881 354 FEDP------KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVE---------VDYVDNVPcidliSSLRT 418
|
490 500 510
....*....|....*....|....*....|
gi 51317366 1024 pagggaqdarGLFWVLDEEVHVEGSSDSVV 1053
Cdd:cd14881 419 ----------GLLSMLDVECSPRGTAESYV 438
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1326-2095 |
1.84e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 99.76 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1326 SRLEKQREKL--VSQSIVLFQAACKgfLSRQEFKKLKIRRLAAQCIQknvAVFLAVKDWPWWQLLGSLQPLLsatigtEQ 1403
Cdd:TIGR02169 170 RKKEKALEELeeVEENIERLDLIID--EKRQQLERLRREREKAERYQ---ALLKEKREYEGYELLKEKEALE------RQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1404 LRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADerfkgdvacqvLESERAERLQafREVQELKSKHEQ 1483
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD-----------LGEEEQLRVK--EKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1484 VQKKLGDVNKQLEEAQQKIQLNDLERnptggaDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSA 1563
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEI------DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1564 YDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEKKQKKFDLQLAQALgesvfeKGLREKVTQ---ENTSVRWE 1640
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINE----LKRELDRLQEELQRLSEELADLNAAI------AGIEAKINEleeEKEDKALE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1641 LgqlqqqlKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLES--SALEQQKIQSQQE---------- 1708
Cdd:TIGR02169 450 I-------KKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQRelAEAEAQARASEERvrggraveev 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1709 ---------NTIKQLEQLRQRFELEIE-----RMKQMHQKDREDQEEELEDVRQSCQKRLHQL---EMQLEQEYEEkqmV 1771
Cdd:TIGR02169 516 lkasiqgvhGTVAQLGSVGERYATAIEvaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLplnKMRDERRDLS---I 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1772 LHEkqdlEGLIGTLCDQIghrDFDVEKR-----------LRRDLRRTHALLSDVQLLL---------GTM------EDGK 1825
Cdd:TIGR02169 593 LSE----DGVIGFAVDLV---EFDPKYEpafkyvfgdtlVVEDIEAARRLMGKYRMVTlegelfeksGAMtggsraPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1826 TSVSKEELEKVHS------QLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLvdeQLYRLQFEKADLLKRIDED 1899
Cdd:TIGR02169 666 ILFSRSEPAELQRlrerleGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK---EIEQLEQEEEKLKERLEEL 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1900 QDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLqvAQMRIEYLEQSTVD-RAIVSRQEAVICDLENK 1978
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKlEEEVSRIEARLREIEQK 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1979 tefqkvqIKRFEVLVIRLRDsliKMGEELSQAATSESQQREssqyYQRRLEELKADMEELVQREAEASRRCMELEKYVEE 2058
Cdd:TIGR02169 821 -------LNRLTLEKEYLEK---EIQELQEQRIDLKEQIKS----IEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
810 820 830
....*....|....*....|....*....|....*..
gi 51317366 2059 LAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTE 2095
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
585-1205 |
4.14e-20 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 97.86 E-value: 4.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPS--AGKVPKG--------------RRDGLPAHIGSMAQRAYWALL 648
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPF-QDLPQlyGDEILRGyaydhnsqfgdrvtSTDPREPHLFAVARAAYIDIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 649 NQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGS---------------VDGRVSVE-KIRATFTVLRAFGSVSMAHSR 712
Cdd:cd14899 80 QNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTgnnnltnsesisppaSPSRTTIEeQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 713 SATRFSMVMSLDFNATGR-ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELN--LHQMADSSSFGM-- 787
Cdd:cd14899 160 NSSRFGKFIELRFRDERRrLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEQKqvLALSGGPQSFRLln 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 788 -GVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGA---------------AGACKVGRKQFMRFEW 851
Cdd:cd14899 240 qSLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNvdfeqiphkgddtvfADEARVMSSTTGAFDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 852 ANYAAEALGCEYEELNTATFKhhlrqiiqqmtfgpsRWGLEDEETSsglkMTGVDCVEG------MASGLYQELFAAVVS 925
Cdd:cd14899 320 FTKAAELLGVSTEALDHALTK---------------RWLHASNETL----VVGVDVAHArntrnaLTMECYRLLFEWLVA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 926 LINRSFSSH---------------HLSMASIMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQR 990
Cdd:cd14899 381 RVNNKLQRQasapwgadesdvddeEDATDFIGLLDIFGFEDMAEN------SFEQLCINYANEALQHQFNQYIFEEEQRL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 991 YQEEGVPVQFdLPDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEG 1070
Cdd:cd14899 455 YRDEGIRWSF-VDFPNNRACLELFEHRPI--------------GIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHF 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1071 SSAlRTCEQPLQCEIFHQLGWdpVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLfqARAKLPPVCRAVAGLEGTS 1150
Cdd:cd14899 520 RSA-PLIQRTTQFVVAHYAGC--VTYTIDGFLAKNKDSFCE-SAAQLLAGSSNPLIQAL--AAGSNDEDANGDSELDGFG 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 51317366 1151 QQALQRSRmvrrtfaSSLAAVrrkAPCSQIKLQMDALTSMIKRSRLHFIHCLVPN 1205
Cdd:cd14899 594 GRTRRRAK-------SAIAAV---SVGTQFKIQLNELLSTVRATTPRYVRCIKPN 638
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1386-2071 |
1.67e-19 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 96.40 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1386 QLLGSLQPLLSATIGTEQLRAK-EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvaCQVLESER 1464
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKlEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK----NIKLSKDV 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1465 AERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDCAQMENefLRKRLQQCEERLD 1544
Cdd:pfam01576 464 SSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD--MKKKLEEDAGTLE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1545 SELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQalgesvfEK 1624
Cdd:pfam01576 542 ALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAE-------EK 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1625 GLREKVTQENTSVRWElgqlqqqLKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLESS-------- 1696
Cdd:pfam01576 615 AISARYAEERDRAEAE-------AREKETRALSLARALEEALEAKEEL-------ERTNKQLRAEMEDLVSSkddvgknv 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1697 --------ALEQQ----KIQSQQ-ENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQ 1763
Cdd:pfam01576 681 helerskrALEQQveemKTQLEElEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELED 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1764 EYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRdLRRTHALLSDVQlllgtmedgktsvskEELEKVHSQLEQS 1843
Cdd:pfam01576 761 ERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQ-LKKLQAQMKDLQ---------------RELEEARASRDEI 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1844 EAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMqkhkdliaqsaadiGQ 1923
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLE--------------AR 890
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1924 IQELQLQLEEAKKEKHKLQEQLQVAQMRIEYL------EQSTVDRAIVSRQEAVICDLENKTEFQKV--QIK-RFEVLVI 1994
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLttelaaERSTSQKSESARQQLERQNKELKAKLQEMegTVKsKFKSSIA 970
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1995 RLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEEL--------------KADMEELVQREAEASRRCMELEKYVEELA 2060
Cdd:pfam01576 971 ALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVllqvederrhadqyKDQAEKGNSRMKQLKRQLEEAEEEASRAN 1050
|
730
....*....|.
gi 51317366 2061 AVRQTLQTDLE 2071
Cdd:pfam01576 1051 AARRKLQRELD 1061
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1403-2090 |
2.98e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 92.55 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1403 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVA----------CQVLESERAERLQAFR 1472
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAekqrrdlgeeLEALKTELEDTLDTTA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1473 EVQELKSKHEQvqkKLGDVNKQLEEAQQ--KIQLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEE--------- 1541
Cdd:pfam01576 317 AQQELRSKREQ---EVTELKKALEEETRshEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESenaelqael 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1542 ------RLDSElTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQL-- 1613
Cdd:pfam01576 394 rtlqqaKQDSE-HKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLqd 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1614 AQALG--ESVFEKGLREKVTQ---ENTSVRWELGQLQQQLKQKEQEASQLKQQvemLQDHKREllgspslgencvagLKE 1688
Cdd:pfam01576 473 TQELLqeETRQKLNLSTRLRQledERNSLQEQLEEEEEAKRNVERQLSTLQAQ---LSDMKKK--------------LEE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1689 RLWKLESSALEQQKIQSQQENTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVRQSC------QKRLHQL---EM 1759
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD-KLEKTKNRLQQELDDLLVDLDHQRQLVsnlekkQKKFDQMlaeEK 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1760 QLEQEY-EEKQMVLHEKQDLEGLIGTLCdqighRDFDVEKRLRRDLRRTHALL-SDVQLLLGTMEDGKTSVskEELEKVH 1837
Cdd:pfam01576 615 AISARYaEERDRAEAEAREKETRALSLA-----RALEEALEAKEELERTNKQLrAEMEDLVSSKDDVGKNV--HELERSK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1838 SQLEQSeakcEEALKTQkvltadLESMHSELEnMTRNKSL---VDEQLYRLQFE-------------KADLLKRIDEDQD 1901
Cdd:pfam01576 688 RALEQQ----VEEMKTQ------LEELEDELQ-ATEDAKLrleVNMQALKAQFErdlqardeqgeekRRQLVKQVRELEA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1902 DLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLeQSTVDRAIVSRQEAVICDLENKTef 1981
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-QRELEEARASRDEILAQSKESEK-- 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1982 qkvQIKRFEVLVIRLRDSLI--------------KMGEELSQAATSESQQRESsqyyQRRLEELKADMEELVQREAEAS- 2046
Cdd:pfam01576 834 ---KLKNLEAELLQLQEDLAaserarrqaqqerdELADEIASGASGKSALQDE----KRRLEARIAQLEEELEEEQSNTe 906
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 51317366 2047 -------RRCMELEKYVEELAAVRQTLQTD---LETSIRRIADLQAALEEVASS 2090
Cdd:pfam01576 907 llndrlrKSTLQVEQLTTELAAERSTSQKSesaRQQLERQNKELKAKLQEMEGT 960
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
586-999 |
2.23e-17 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 88.64 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVP-----SAGKVPKGRRDGLPaHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEypqefHAKYRCKSRSDNAP-HIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 661 WSGAGKTTCCEQVLEHLvGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 740
Cdd:cd14882 81 ESYSGKTTNARLLIKHL-CYLGDGNRGAT-GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 741 LEKSRVARQPEGESNFLVFSQMLAGL-------DLDLRTELNLHQM----ADSSSFGMGVWSKPEDKQKAAAAFAQLQGA 809
Cdd:cd14882 159 LEKLRVSTTDGNQSNFHIFYYFYDFIeaqnrlkEYNLKAGRNYRYLrippEVPPSKLKYRRDDPEGNVERYKEFEEILKD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 810 MEMlgiSESEQRAVWRVLAAIYHLGAAGACKV-GRKQFMRFEWANYAAEALGceyeeLNTATFKHHLRQIIQQMTFGPSR 888
Cdd:cd14882 239 LDF---NEEQLETVRKVLAAILNLGEIRFRQNgGYAELENTEIASRVAELLR-----LDEKKFMWALTNYCLIKGGSAER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 889 WGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINrsfssHHLSMA--------SIMVVDSPGFQNPRHQGkdra 960
Cdd:cd14882 311 RKHTTEEAR--------DARDVLASTLYSRLVDWIINRIN-----MKMSFPravfgdkySISIHDMFGFECFHRNR---- 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 51317366 961 atFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQ 999
Cdd:cd14882 374 --LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTI 410
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
585-999 |
2.34e-17 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 88.92 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALGWSGA 664
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 665 GKTTCCEQVLE-HLVGMagSVDGRVSVEKIRATFtVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEK 743
Cdd:cd14937 81 GKTEASKLVIKyYLSGV--KEDNEISNTLWDSNF-ILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 744 SRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPE-DKQKAAAAFAQLQGAMEMLGISESeqra 822
Cdd:cd14937 158 IRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEiDDAKDFGNLMISFDKMNMHDMKDD---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 823 VWRVLAAIYHLG--------AAGACKVGRKQFMRFEWANYAAEALGCEYEEL-NTATFKHhlRQIIQQMTFGPsrwgLED 893
Cdd:cd14937 234 LFLTLSGLLLLGnveyqeieKGGKTNCSELDKNNLELVNEISNLLGINYENLkDCLVFTE--KTIANQKIEIP----LSV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 894 EETSSGLKMTGVDcvegmasgLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCHNYAHE 973
Cdd:cd14937 308 EESVSICKSISKD--------LYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKN------SLEQLLINIANE 373
|
410 420
....*....|....*....|....*.
gi 51317366 974 RLQLLFYQRTFVSTLQRYQEEGVPVQ 999
Cdd:cd14937 374 EIHSIYLYIVYEKETELYKAEDILIE 399
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
586-1205 |
2.65e-17 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 88.81 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP-------------------SVPSAGKVPkgrrdglPAHIGSMAQRAYWA 646
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPlkelydqdvmnvylhkksnSAASAAPFP-------KAHIYDIANMAYKN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 647 LLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFN 726
Cdd:cd14884 75 MRGKLKRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 727 A---------TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGL-DLDL---RTELNLH----------QMADSS 783
Cdd:cd14884 155 EventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLsDEDLarrNLVRNCGvygllnpdesHQKRSV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 784 SFGMGVWSK-----PEDKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGackvgrkqfmrfewANYAAEA 858
Cdd:cd14884 235 KGTLRLGSDsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRA--------------YKAAAEC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 859 LGCEYEELNTaTFKHHLRQIIQQMTFGPSRwglEDEETSSglkmtgvdcVEGMASGLYQELFAAVVSLINR--------- 929
Cdd:cd14884 301 LQIEEEDLEN-VIKYKNIRVSHEVIRTERR---KENATST---------RDTLIKFIYKKLFNKIIEDINRnvlkckekd 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 930 SFSSHHLSM---ASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpVQFDLPDPS 1006
Cdd:cd14884 368 ESDNEDIYSineAIISILDIYGFEELSGND------FDQLCINLANEKLNNYYINNEIEKEKRIYARENI-ICCSDVAPS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1007 PGTTVAVVDQNPSQV----RLPAgGGAQDARGLFW---------VLDEEVHVEGSsdsvVLERLCAAFEKKGAGTEGSSA 1073
Cdd:cd14884 441 YSDTLIFIAKIFRRLdditKLKN-QGQKKTDDHFFryllnnerqQQLEGKVSYGF----VLNHDADGTAKKQNIKKNIFF 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1074 LRtceqplqceifHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSlfqaraklppvcravAGLEGTSQQA 1153
Cdd:cd14884 516 IR-----------HYAG--LVTYRINNWIDKNSDKIET-SIETLISCSSNRFLRE---------------ANNGGNKGNF 566
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 51317366 1154 LQRSRMVrrtfasslaavrrkapcsqIKlQMDALTSMIKRSRLHFIHCLVPN 1205
Cdd:cd14884 567 LSVSKKY-------------------IK-ELDNLFTQLQSTDMYYIRCFLPN 598
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1402-1957 |
8.59e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 87.00 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLAD---ERFKGDVACQVLES--ERAERLQAfrEVQE 1476
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKiknKLLKLELLLSNLKKkiQKNKSLES--QISE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1477 LKSKH-------EQVQKKLGDVNKQLEEAQQKI-QLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLdSELT 1548
Cdd:TIGR04523 223 LKKQNnqlkdniEKKQQEINEKTTEISNTQTQLnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI-SDLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1549 ARKE-------------LEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQ-QSRNHELEKKQKKfdLQLA 1614
Cdd:TIGR04523 302 NQKEqdwnkelkselknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN----SESEnSEKQRELEEKQNE--IEKL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1615 QALGESVFEKglREKVTQENTSVRWELgqlqqqlKQKEQEASQLKQQVEMLQDHKRELLGspslgencvaglkerlwkle 1694
Cdd:TIGR04523 376 KKENQSYKQE--IKNLESQINDLESKI-------QNQEKLNQQKDEQIKKLQQEKELLEK-------------------- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1695 ssalEQQKIQSQ---QENTIKQLEQLRQRFELEIERMKQMhqkdREDQEEELEDVRQSCQKRLHQLEmQLEQEYEEKQ-- 1769
Cdd:TIGR04523 427 ----EIERLKETiikNNSEIKDLTNQDSVKELIIKNLDNT----RESLETQLKVLSRSINKIKQNLE-QKQKELKSKEke 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1770 --MVLHEKQDLEGLIGTLCDQIghrdfdvekrlrrdlrrthallsdvqlllgtmedgktSVSKEELEKVHSQLEQSEAKC 1847
Cdd:TIGR04523 498 lkKLNEEKKELEEKVKDLTKKI-------------------------------------SSLKEKIEKLESEKKEKESKI 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1848 EEalktqkvLTADLESMHSEL--ENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQ 1925
Cdd:TIGR04523 541 SD-------LEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
570 580 590
....*....|....*....|....*....|..
gi 51317366 1926 ELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1957
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1408-2086 |
1.34e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.03 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1408 EEELTTLRRKLEKSEKLRnELRQntDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKK 1487
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYK-ELKA--ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1488 LGDVNKQLEEAQQK-----IQLNDLERNptggADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQS 1562
Cdd:TIGR02168 276 VSELEEEIEELQKElyalaNEISRLEQQ----KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1563 AYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQalgesvfekgLREKVTQentsvrwelg 1642
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER----------LEARLER---------- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1643 qlqqqlkqkeqeasqLKQQVEMLQDHKRELLGSPSLGEncvagLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFE 1722
Cdd:TIGR02168 412 ---------------LEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1723 LEIERMKQmhqkdREDQEEELedvrQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghrdfDVEKRLRR 1802
Cdd:TIGR02168 472 EAEQALDA-----AERELAQL----QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-----SVDEGYEA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1803 DLRRthALLSDVQLLLgtMEDgktsvsKEELEKVHSQLEQSEAK----CEEALKTQKVLTADLESMHSELENMTRNKSLV 1878
Cdd:TIGR02168 538 AIEA--ALGGRLQAVV--VEN------LNAAKKAIAFLKQNELGrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1879 DEqlYRLQFEKA--DLLKR--IDEDQDDLNELMQKHK----------DLIA-------QSAADIGQIQELQLQLEEAKKE 1937
Cdd:TIGR02168 608 VK--FDPKLRKAlsYLLGGvlVVDDLDNALELAKKLRpgyrivtldgDLVRpggvitgGSAKTNSSILERRREIEELEEK 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1938 KHKLQEQLQVAQMRIEYLEQSTVDraivsrqeavicdLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQ 2017
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEE-------------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51317366 2018 ressqyyQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2086
Cdd:TIGR02168 753 -------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
586-1057 |
2.88e-16 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 85.14 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAGKVPK-GRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALGWS 662
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRylPFLHSQELVRNyNQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 663 GAGKTTCCEQVLEHLVGMAGSvDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLE 742
Cdd:cd14905 82 GSGKSENTKIIIQYLLTTDLS-RSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 743 KSRVARQPEGESNFLVFSQMLAGLDLDlrtELNLHQMADSSSF-------GMGVWSKPEDKqkaaaAFAQLQGAMEMLGI 815
Cdd:cd14905 161 ENRVTYQNKGERNFHIFYQFLKGITDE---EKAAYQLGDINSYhylnqggSISVESIDDNR-----VFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 816 SESEQRAVWRVLAAIYHLGAAgackvgrkQFMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRWGLEDEE 895
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNV--------TFFQKNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENRD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 896 TssglkmtgvdcvegMASGLYQELFAAVVSLINRSFSSHHLSMaSIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERL 975
Cdd:cd14905 305 S--------------LARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQESSQLNG------YEQFSINFLEERL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 976 QLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgTTVAVVDQNPSqvrlpagggAQDARGLFWVLDEEVHVEGSSDSVVLE 1055
Cdd:cd14905 364 QQIYLQTVLKQEQREYQTERIPWM---------TPISFKDNEES---------VEMMEKIINLLDQESKNINSSDQIFLE 425
|
..
gi 51317366 1056 RL 1057
Cdd:cd14905 426 KL 427
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1384-2022 |
5.05e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 85.02 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1384 WW--QLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQntdllESKIADLTSDLADERFKGDVACQVLE 1461
Cdd:TIGR00618 243 AYltQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK-----AAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1462 SERAERLQAFrevqelkSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEE 1541
Cdd:TIGR00618 318 SKMRSRAKLL-------MKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1542 RLDSELTARKELEQKLGEL-QSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQ-LAQALGE 1619
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQeSAQSLKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1620 SVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQE--ASQLKQQVEMLQDHKRELLGSPSL-GENCVAGLKERLWKLE-- 1694
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRMQrGEQTYAQLETSEEDVYhq 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1695 -SSALEQQKIQSQQENTIKQ----LEQLRQRFELEIERMKQMHQKDREDQEEELEDvRQSCQKRLHQLEMQLEQEYEEKQ 1769
Cdd:TIGR00618 551 lTSERKQRASLKEQMQEIQQsfsiLTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA-EDMLACEQHALLRKLQPEQDLQD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1770 MVLHEKQ----------DLEGLIGTLCDQighrdfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVS--KEELEKVH 1837
Cdd:TIGR00618 630 VRLHLQQcsqelalkltALHALQLTLTQE------RVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywKEMLAQCQ 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1838 SQLEQSEAKCEEALKTQKVLTADLESMHSELEnmtRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS 1917
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIENASSSLGSDLA---AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1918 AADIGQIQELQLQLEEAKKEKHKLQEQLQvaQMRIEYLEQSTV-DRAIVSRQEAVICDLENKTEfqkvqikrfevLVIRL 1996
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLLKTLEAEIG--QEIPSDEDILNLqCETLVQEEEQFLSRLEEKSA-----------TLGEI 847
|
650 660
....*....|....*....|....*.
gi 51317366 1997 RDSLIKMGEELSQAATSESQQRESSQ 2022
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1472-2102 |
2.03e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.80 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1472 REVQELKSKHEQVQKKLGDVNKQLEEAQQKI-QLNDLERNPTGGADEWQMRFDcaqmENEFLRKRLQQCEERLDSELTAR 1550
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREInEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1551 KELEQKLGELQSAYDGAKKMAHQLKRKCHHLTcdledtcvllenqqsrnhELEKKQKKFdlqlaQALGEsvfekgLREKV 1630
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELK------------------ELKEKAEEY-----IKLSE------FYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1631 TQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgencvAGLKERLWKLESSALEQQKIQSQQENt 1710
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-----------KELEKRLEELEERHELYEEAKAKKEE- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1711 ikqLEQLRQRFE-LEIERMKQMHQKDREDQEEELEDVRQSCQKRlhqleMQLEQEYEEKQMVLHEkqdLEGLIGTlCDQI 1789
Cdd:PRK03918 374 ---LERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARI-----GELKKEIKELKKAIEE---LKKAKGK-CPVC 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1790 GhRDFDVEKRLRRdLRRTHALLSDVqlllgtmedgktSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTAdLESMHSELE 1869
Cdd:PRK03918 442 G-RELTEEHRKEL-LEEYTAELKRI------------EKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1870 NmtrnkslVDEQLYRLQFEKadlLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQ 1949
Cdd:PRK03918 507 E-------LEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1950 MRIEYLEQSTVDraivsrqeavicDLENKTEFQKVQIKRFevlvIRLRDSLIKMGEELSQAATSESQQRESSQYYQR--- 2026
Cdd:PRK03918 577 KELEELGFESVE------------ELEERLKELEPFYNEY----LELKDAEKELEREEKELKKLEEELDKAFEELAEtek 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2027 RLEELKADMEEL-----VQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTAV 2101
Cdd:PRK03918 641 RLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKAL 720
|
.
gi 51317366 2102 D 2102
Cdd:PRK03918 721 E 721
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1402-2071 |
3.14e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 82.53 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNEL-RQNTDLLESKIA---------DLTSDLADERFKGDVACQVLES---ERAERL 1468
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELeKKHQQLCEEKNAlqeqlqaetELCAEAEEMRARLAARKQELEEilhELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1469 QAFRE-VQELKSKHEQVQKKLGDVNKQLEE---AQQKIQLNDLernpTGGADEWQMRFDCAQME--NEFLRKRLQQCEER 1542
Cdd:pfam01576 85 EEEEErSQQLQNEKKKMQQHIQDLEEQLDEeeaARQKLQLEKV----TTEAKIKKLEEDILLLEdqNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1543 LDSELTARKELEQKLgelqsaydgakKMAHQLKRKCHHLTCDLEDTcvlLENQQSRNHELEKKQKKFDLQLAQALGESVF 1622
Cdd:pfam01576 161 ISEFTSNLAEEEEKA-----------KSLSKLKNKHEAMISDLEER---LKKEEKGRQELEKAKRKLEGESTDLQEQIAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1623 EKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELL---------------GSPSLGENCVAgLK 1687
Cdd:pfam01576 227 LQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQedleseraarnkaekQRRDLGEELEA-LK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1688 ERLWKLESSALEQQKIQSQQENTI----KQLEQLRQRFELEIERMKQMHQKDREDQEEELED---VRQSCQKRLHQLEMQ 1760
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVtelkKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQakrNKANLEKAKQALESE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1761 LEQEYEEKQMVLHEKQDLEgligtlcdqigHRdfdvEKRLRRDLRRTHALLSDVQLLLGTMEDgKTSVSKEELEKVHSQL 1840
Cdd:pfam01576 386 NAELQAELRTLQQAKQDSE-----------HK----RKKLEGQLQELQARLSESERQRAELAE-KLSKLQSELESVSSLL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1841 EQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAAD 1920
Cdd:pfam01576 450 NEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1921 IGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEY------------------LEQSTVDraiVSRQEAVICDLENKTefq 1982
Cdd:pfam01576 530 KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEkaaaydklektknrlqqeLDDLLVD---LDHQRQLVSNLEKKQ--- 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1983 kvqiKRFEVLVIRLRDSLIKMGEELSQA----------ATSESQQRESSQYYQRRLEE----LKADMEELVQREAEASRR 2048
Cdd:pfam01576 604 ----KKFDQMLAEEKAISARYAEERDRAeaeareketrALSLARALEEALEAKEELERtnkqLRAEMEDLVSSKDDVGKN 679
|
730 740
....*....|....*....|...
gi 51317366 2049 CMELEKYVEELAAVRQTLQTDLE 2071
Cdd:pfam01576 680 VHELERSKRALEQQVEEMKTQLE 702
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1394-2087 |
9.55e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.88 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1394 LLSATIGTEQLRAKEEELttlRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFRE 1473
Cdd:TIGR02169 296 IGELEAEIASLERSIAEK---ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1474 VQELKSKHEQVQKKLGDVNKQLEEAQQKIqlNDLERNPTGGADEWQ-MRFDCAQMENEFLRKRLQQCEerLDSEL-TARK 1551
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREI--NELKRELDRLQEELQrLSEELADLNAAIAGIEAKINE--LEEEKeDKAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1552 ELEQKLGELQSAYDGAKKMAHQLKRkchhltcdledtcvLLENQQSRNHELEKKQKKFDLQLAQ--ALGESVFEKGLREK 1629
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYD--------------LKEEYDRVEKELSKLQRELAEAEAQarASEERVRGGRAVEE 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1630 VTQENT-----SVRwELGQLQQQLKQKEQEASQLKQQVEMLQDHkrellgspSLGENCVAGLKER---------LWKLES 1695
Cdd:TIGR02169 515 VLKASIqgvhgTVA-QLGSVGERYATAIEVAAGNRLNNVVVEDD--------AVAKEAIELLKRRkagratflpLNKMRD 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1696 SALEQQKI---------------QSQQENTIKQLEQ---LRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQL 1757
Cdd:TIGR02169 586 ERRDLSILsedgvigfavdlvefDPKYEPAFKYVFGdtlVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGG 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1758 EMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRD---FDVEKRLRRDLRRTHALLSDVQLLlgtmeDGKTSVSKEELE 1834
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQL-----EQEEEKLKERLE 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1835 KVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENmtrnkslVDEQLYRLqfEKADLLKRIDEDQDDLNELMQKHKDLI 1914
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK-------LEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIE 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1915 AQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdraivsRQEAVICDLENKTEfqkvQIKRFEVLVI 1994
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK---------EIENLNGKKEELEE----ELEELEAALR 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1995 RLRDSLI-------KMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRqtlq 2067
Cdd:TIGR02169 879 DLESRLGdlkkerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE---- 954
|
730 740
....*....|....*....|
gi 51317366 2068 tDLETSIRRIADLQAALEEV 2087
Cdd:TIGR02169 955 -DVQAELQRVEEEIRALEPV 973
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1402-1943 |
1.71e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLR---NELRQNTDLLESKIADLTSDLaderfkgdvacqvleSERAERLqafrevQELK 1478
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKeeiEELEKELESLEGSKRKLEEKI---------------RELEERI------EELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1479 SKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEE---RLDSELTARKELEQ 1555
Cdd:PRK03918 273 KEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1556 KLGELQS---AYDGAKKMAHQLKRKCHHLTC-DLEDTCVLLENQQSRNHELEKKQKKfdlqLAQALGESVFEKGLREKVT 1631
Cdd:PRK03918 353 RLEELEErheLYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISK----ITARIGELKKEIKELKKAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1632 QENTSVRWELGQLQQqlkqkeqeasqlkqqvEMLQDHKRELLGSPSLG----ENCVAGLKERLWKLESSALEQQKIQSQQ 1707
Cdd:PRK03918 429 EELKKAKGKCPVCGR----------------ELTEEHRKELLEEYTAElkriEKELKEIEEKERKLRKELRELEKVLKKE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1708 ENTIKQLEQLRQRFELEiERMKQMHQKDREDQEEELEDVRQ---SCQKRLHQLEMQLEQEYE---EKQMVLHEKQDLEGL 1781
Cdd:PRK03918 493 SELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEYEKLKEkliKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEE 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1782 IGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGtmedgktsvSKEELEKVHSQLEQSEAKCEEALKTQKVLTADL 1861
Cdd:PRK03918 572 LAELLKELEELGFESVEELEERLKELEPFYNEYLELKD---------AEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1862 ESMHSELENMTRNKSLVD-EQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHK 1940
Cdd:PRK03918 643 EELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER 722
|
...
gi 51317366 1941 LQE 1943
Cdd:PRK03918 723 VEE 725
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1830-2098 |
2.30e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1830 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1909
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1910 HKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLENKTEFQKVQIKRF 1989
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA------LLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1990 EVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTD 2069
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260
....*....|....*....|....*....
gi 51317366 2070 LETSIRRIADLQAALEEVASSDSDTESVQ 2098
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1687-2123 |
2.34e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 79.45 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1687 KERLWKLESSALEQQKIQSQ--QENTIKQlEQLRQRFEL--EIERMKQMhqkdREDQEEELEDVrqscqkrLHQLEMQLE 1762
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQlcEEKNALQ-EQLQAETELcaEAEEMRAR----LAARKQELEEI-------LHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1763 QEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEE--LEKVHSQL 1840
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLEEQLDEEE-AARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERklLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1841 EQSEAKCEEALKTQKVLTADLESMHSELENMTRNkslvdEQLYRLQFEKADllKRIDEDQDDLNElmqkhkdliaqsaad 1920
Cdd:pfam01576 165 TSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK-----EEKGRQELEKAK--RKLEGESTDLQE--------------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1921 igQIQELQLQLEEAKKEKHKLQEQLQVAQMRieyLEQSTVDRAIVSRQ----EAVICDLE----------NKTEFQKVQI 1986
Cdd:pfam01576 223 --QIAELQAQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKirelEAQISELQedleseraarNKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1987 -KRFEVLVIRLRDSL----------IKMGEELSQ--------AATSESQQRESSQYYQRRLEELKADMEELVQREAEASR 2047
Cdd:pfam01576 298 gEELEALKTELEDTLdttaaqqelrSKREQEVTElkkaleeeTRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51317366 2048 RCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQT-AVDCGSSGRKEMDNVSILSSQPEG 2123
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAeLAEKLSKLQSELESVSSLLNEAEG 454
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1408-2089 |
1.77e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1408 EEELTTLRRKLEKSEKLRNELRQNTDLLE--SKIA----DLTSDLadERFKGDVACQVLESERAERLQAFREVQELKSKH 1481
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLErqAEKAeryrELKEEL--KELEAELLLLKLRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1482 EQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGAdewqmrfdcaqmENEfLRKRLQQCEERLDSELTARKELEQKLGELQ 1561
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAE------------EYE-LLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1562 SAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWEL 1641
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1642 GQLQQQLKQKEQEASQLKQQVEMLQDHKRELLgspslgencvAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRF 1721
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELE----------EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1722 ELEiermkqmhQKDREDQEEELEDVRQscqKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEK--- 1798
Cdd:COG1196 473 ALL--------EAALAELLEELAEAAA---RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAale 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1799 -----RLRRDLRRTHALLSDVQLLLGTMEDGKtsVSKEELEKVHsQLEQSEAKCEEALKTQKVLTADLESMHSELENMTR 1873
Cdd:COG1196 542 aalaaALQNIVVEDDEVAAAAIEYLKAAKAGR--ATFLPLDKIR-ARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1874 NKSLVDEQLYRLQFEKAD-LLKRIDEDQDDLNELMqkhkDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRI 1952
Cdd:COG1196 619 GDTLLGRTLVAARLEAALrRAVTLAGRLREVTLEG----EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1953 EYLEQSTVDRAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDsLIKMGEELSQAATSESQQRESSQYYQRRLEELK 2032
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE-LLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51317366 2033 ADMEEL------VQREAEasrrcmELEKYVEELAAVRQTLQ---TDLETSIRRI-----ADLQAALEEVAS 2089
Cdd:COG1196 774 REIEALgpvnllAIEEYE------ELEERYDFLSEQREDLEearETLEEAIEEIdretrERFLETFDAVNE 838
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1433-2098 |
2.15e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.55 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1433 DLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREvQELKSKHEQVQKkLGDVNKQLEEAQQKIQLndlernpt 1512
Cdd:TIGR00618 171 NLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTP-CMPDTYHERKQV-LEKELKHLREALQQTQQ-------- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1513 ggADEWQMRFDCAQMENEFLRKRLQQCEERLDsELTArkeLEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLL 1592
Cdd:TIGR00618 241 --SHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRA---QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1593 EnQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEA-----SQLKQQVEMLQD 1667
Cdd:TIGR00618 315 E-LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqhiHTLQQQKTTLTQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1668 HKRELLGSPSLGENCVAGLKERLwkLESSALEQQKI--QSQQENTIKQLEQLRQRFE--LEIERMKQMHQKDREDQEEEL 1743
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRT--SAFRDLQGQLAhaKKQQELQQRYAELCAAAITctAQCEKLEKIHLQESAQSLKER 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1744 EdvrqscqKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDfdvekrlrrdlrrTHALLSDvqlllgtmED 1823
Cdd:TIGR00618 472 E-------QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN-------------PARQDID--------NP 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1824 GKTSVSKEELEKVHSQLEQSEAK----CEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRID-- 1897
Cdd:TIGR00618 524 GPLTRRMQRGEQTYAQLETSEEDvyhqLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEkl 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1898 -EDQDDLNELMQKHKDLIAQSAADIGQIQEL-QLQLEEAKKEKHKLQEQLQVAQMRI-EYLEQSTVDRA-IVSRQEAVIC 1973
Cdd:TIGR00618 604 sEAEDMLACEQHALLRKLQPEQDLQDVRLHLqQCSQELALKLTALHALQLTLTQERVrEHALSIRVLPKeLLASRQLALQ 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1974 DLENKTEF---------QKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESS------QYYQRRLEELKADMEEL 2038
Cdd:TIGR00618 684 KMQSEKEQltywkemlaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAlnqslkELMHQARTVLKARTEAH 763
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2039 VQREAEASRRCMELEKYvEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQ 2098
Cdd:TIGR00618 764 FNNNEEVTAALQTGAEL-SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1402-2086 |
3.60e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRnELRQNTDLLESKIADLTSDL--ADERFKGDVACQVLESERAERLQAFREVQ--EL 1477
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAE-EARKAEDAKKAEAARKAEEVrkAEELRKAEDARKAEAARKAEEERKAEEARkaED 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1478 KSKHEQVqKKLGDVNKQLEEAQQKiqlnDLERNptggaDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKL 1557
Cdd:PTZ00121 1223 AKKAEAV-KKAEEAKKDAEEAKKA----EEERN-----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1558 GELQSAYDgaKKMAHQLKRKChhltcdledtcvllenQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQ-ENTS 1636
Cdd:PTZ00121 1293 DEAKKAEE--KKKADEAKKKA----------------EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaEAEA 1354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1637 VRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLK--ERLWKLESSALEQQKIQSQQENtIKQL 1714
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkaDELKKAAAAKKKADEAKKKAEE-KKKA 1433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1715 EQLRQRFEleiERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEmqLEQEYEEKQMVLHEKQDLEgligtlcdqighrdf 1794
Cdd:PTZ00121 1434 DEAKKKAE---EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAE--------------- 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1795 dvEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSvskEELEKVHSQLEQSEA-KCEEALKTQKVLTADLESMHSELENMTR 1873
Cdd:PTZ00121 1494 --EAKKKADEAKKAAEAKKKADEAKKAEEAKKA---DEAKKAEEAKKADEAkKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1874 NKSlvDEQLYRLQFEKADLLKRIDEDQddLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKhklQEQLQVAQMRIE 1953
Cdd:PTZ00121 1569 AKK--AEEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKK 1641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1954 YLEQstVDRAIVSRQEavicdlENKTEFQKVQIKRFEvlvirlrDSLIKMGEELSQAatsESQQRESSQYYQRRLEElKA 2033
Cdd:PTZ00121 1642 EAEE--KKKAEELKKA------EEENKIKAAEEAKKA-------EEDKKKAEEAKKA---EEDEKKAAEALKKEAEE-AK 1702
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 51317366 2034 DMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2086
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1401-1946 |
3.91e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1401 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacQVLESERAERLQAFREVQELKSK 1480
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-------ERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1481 HEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggadewqmrfDCAQMENEFLRKRLQQcEERLDSELTARKELEQKLGEL 1560
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELA------------EAEEALLEAEAELAEA-EEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1561 QSAYDGAKKMAHQLKRKCHHLTCDLEDtcvLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWE 1640
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1641 LGQLQQQLKQKEQEASQLKQQVEMLQDH------KRELLGSPSLGENCVAGLKERLWKLESSALEQqkiqsqqentikql 1714
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYegflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE-------------- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1715 eqlrqrfELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDF 1794
Cdd:COG1196 542 -------AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1795 ------------DVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLE 1862
Cdd:COG1196 615 yyvlgdtllgrtLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1863 SMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELqLQLEEAKKEKHKLQ 1942
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELERELERLE 773
|
....
gi 51317366 1943 EQLQ 1946
Cdd:COG1196 774 REIE 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1823-2088 |
1.93e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.10 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1823 DGKTSVSKEELEKVHSQLEQSEAKCEE-------------------ALKTQK------VLTADLESMHSELENMTRNKSL 1877
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEkrqqlerlrrerekaeryqALLKEKreyegyELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1878 VDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI--------GQIQELQLQLEEAKKEKHKLQEQLQVAQ 1949
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1950 MRIEyleqstvdraivsRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLE 2029
Cdd:TIGR02169 329 AEID-------------KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 51317366 2030 ELKADMEELvqrEAEASRRCMELEKYVEELAAVRQtlqtDLETSIRRIADLQAALEEVA 2088
Cdd:TIGR02169 396 KLKREINEL---KRELDRLQEELQRLSEELADLNA----AIAGIEAKINELEEEKEDKA 447
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1402-2069 |
4.02e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELttlrrklEKSEKLRN--ELRQNTDLLESKIADLTSDL-ADERFKGD---VACQVLESERAERLQAFREVQ 1475
Cdd:PTZ00121 1233 EEAKKDAEEA-------KKAEEERNneEIRKFEEARMAHFARRQAAIkAEEARKADelkKAEEKKKADEAKKAEEKKKAD 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1476 ELKSKHEQvQKKLGDVNKQLEEAQQKiqlndlernptggADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQ 1555
Cdd:PTZ00121 1306 EAKKKAEE-AKKADEAKKKAEEAKKK-------------ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1556 KLGELQSAYDGAKKMAHQlKRKCHHLTCDLEDTCVLLENQQSRNHELEK----KQKKFDLQLAQALGESVFEKGLREKVT 1631
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEE-KKKADEAKKKAEEDKKKADELKKAAAAKKKadeaKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1632 QENTSVRweLGQLQQQLKQKEQEASQLKQQVEmlqdHKRELLGSPSLGENCvaglKERLWKLESSALEQQKI-QSQQENT 1710
Cdd:PTZ00121 1451 KKAEEAK--KAEEAKKKAEEAKKADEAKKKAE----EAKKADEAKKKAEEA----KKKADEAKKAAEAKKKAdEAKKAEE 1520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1711 IKQLEQLRQRFEL-EIERMKQMHQKDREDQEEELEDVRQSCQKRLHQlemQLEQEYEEKQMVLHEKQDLEGLIGTLCDQI 1789
Cdd:PTZ00121 1521 AKKADEAKKAEEAkKADEAKKAEEKKKADELKKAEELKKAEEKKKAE---EAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1790 GHRDFDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMH---- 1865
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDkkka 1677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1866 SELENMTRNKSLVDEQLYRLQFEKadllKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQ--- 1942
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEA----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkde 1753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1943 -EQLQVAQMRIEYLEQSTVDRaivSRQEAVICD-LENKTEFQKVQIKR--------FEVLV-------IRLRDSLIKMGE 2005
Cdd:PTZ00121 1754 eEKKKIAHLKKEEEKKAEEIR---KEKEAVIEEeLDEEDEKRRMEVDKkikdifdnFANIIeggkegnLVINDSKEMEDS 1830
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51317366 2006 ELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTD 2069
Cdd:PTZ00121 1831 AIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1403-2058 |
5.01e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 68.59 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1403 QLRAKEEELTTLRRKLEK---------------SEKLRNELRQNTDLLESKIAD--LTSDLADERFKGDVACQVLESERA 1465
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAqrkaiqelqfenekvSLKLEEEIQENKDLIKENNATrhLCNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1466 ERLQAFREV-----------QELKSKHEQVQKKLgdvNKQLEEAQQKIQlnDLErnptggaDEWQMRFDCAQMENEFLRK 1534
Cdd:pfam05483 180 ETRQVYMDLnnniekmilafEELRVQAENARLEM---HFKLKEDHEKIQ--HLE-------EEYKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1535 RLQQCEERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKkqkkfDLQLA 1614
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE-----DLQIA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1615 QalgESVFEkglrekVTQENTSVRWELGqlqQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLE 1694
Cdd:pfam05483 323 T---KTICQ------LTEEKEAQMEELN---KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1695 SSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQ--EEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVL 1772
Cdd:pfam05483 391 SELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgkEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1773 HEKQDLEgligTLCDQIGHRDFDVEKRLRRDLRRTHALL---SDVQLLLGTMEDGKTSVSKEElEKVHSQLEQSEakcee 1849
Cdd:pfam05483 471 KEVEDLK----TELEKEKLKNIELTAHCDKLLLENKELTqeaSDMTLELKKHQEDIINCKKQE-ERMLKQIENLE----- 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1850 alKTQKVLTADLESMHSEL---------------ENMTRNKSLV---DEQLYRLQFEKADLLKRIDEDQDDLNELMQKHK 1911
Cdd:pfam05483 541 --EKEMNLRDELESVREEFiqkgdevkckldkseENARSIEYEVlkkEKQMKILENKCNNLKKQIENKNKNIEELHQENK 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1912 DLIAQSAADIGQ-------IQELQLQLEEAKKekhKLQEQLQVAQMRIEYLEQS------TVDRAIVSRQEAVICDLENK 1978
Cdd:pfam05483 619 ALKKKGSAENKQlnayeikVNKLELELASAKQ---KFEEIIDNYQKEIEDKKISeeklleEVEKAKAIADEAVKLQKEID 695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1979 TEFQKvQIKRFEVLVIRLRDSLIKMGEEL-SQAATSESQQRESSQyyqrrleeLKADME-ELVQREAE--ASRRCMELEK 2054
Cdd:pfam05483 696 KRCQH-KIAEMVALMEKHKHQYDKIIEERdSELGLYKNKEQEQSS--------AKAALEiELSNIKAEllSLKKQLEIEK 766
|
....
gi 51317366 2055 YVEE 2058
Cdd:pfam05483 767 EEKE 770
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1402-1891 |
1.54e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTT---LRRKLEKSEKLRNELRQNTDllESKIADLTSDLADERFKGDVACQVLESER-AERL----QAFRE 1473
Cdd:PTZ00121 1381 DAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAA--AKKKADEAKKKAEEKKKADEAKKKAEEAKkADEAkkkaEEAKK 1458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1474 VQELKSKHEQvQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDcAQMENEFLRK--------RLQQCEERLDS 1545
Cdd:PTZ00121 1459 AEEAKKKAEE-AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE-AKKKADEAKKaeeakkadEAKKAEEAKKA 1536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1546 ELTARKELEQKLGELQSAYDGAK----KMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESV 1621
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKaeekKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1622 FEKGLREKVTQENtSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLK----------ERLW 1691
Cdd:PTZ00121 1617 EAKIKAEELKKAE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaeedekkaaEALK 1695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1692 KLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQE--EEL---EDVRQSCQKRLHQLEMQLEQEYE 1766
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKkaEEAkkdEEEKKKIAHLKKEEEKKAEEIRK 1775
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1767 EKQMVLHEKQDLE-------------------------GLIGTLCDQIGHRDFDVEKR---LRRDLRRTHALLSDVQLLL 1818
Cdd:PTZ00121 1776 EKEAVIEEELDEEdekrrmevdkkikdifdnfaniiegGKEGNLVINDSKEMEDSAIKevaDSKNMQLEEADAFEKHKFN 1855
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51317366 1819 GTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKAD 1891
Cdd:PTZ00121 1856 KNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRD 1928
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1402-2086 |
2.35e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.61 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTS-DLADERFKGDVACQVLE-----SERAERLQAF--RE 1473
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMK----LDNEIKALKSrKKQMEKDNSELELKMEKvfqgtDEQLNDLYHNhqRT 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1474 VQELKSKHEQVQKKLGDVNKQLEE-AQQKIQLNDLERNPTGGADEWQ---MRFDCAQMENEfLRKRLQQCEERLDSELTA 1549
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKERRLlNQEKTELLVEQGRLQLQADRHQehiRARDSLIQSLA-TRLELDGFERGPFSERQI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1550 R--------------KELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSrnhelEKKQKKFDLQLAQ 1615
Cdd:TIGR00606 393 KnfhtlvierqedeaKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQE-----ELKFVIKELQQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1616 ALGESVFEKglrekvTQENTSVRWELgqlqqQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGL---KERLWK 1692
Cdd:TIGR00606 468 GSSDRILEL------DQELRKAEREL-----SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhTTTRTQ 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1693 LESSALEQ----QKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQ--EEELEDVRQSCQKrLHQLEMQLEQEYE 1766
Cdd:TIGR00606 537 MEMLTKDKmdkdEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtRDRLAKLNKELAS-LEQNKNHINNELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1767 EKQMVLHEKQDlegligTLCDQIGHRDFDVE-KRLRRDLRRTHALLSdvqlllgtMEDGKTSVSKEELEKVHSQLEQSEA 1845
Cdd:TIGR00606 616 SKEEQLSSYED------KLFDVCGSQDEESDlERLKEEIEKSSKQRA--------MLAGATAVYSQFITQLTDENQSCCP 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1846 KCEEALKTQKVL---TADLESM-------HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIA 1915
Cdd:TIGR00606 682 VCQRVFQTEAELqefISDLQSKlrlapdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1916 QSAADIGQiQELQLQLEEAKKEKHKLQeQLQVAQMRIEYLEQSTVDRAI---VSRQEAVICDLENKTEFQKVQIKRFEVl 1992
Cdd:TIGR00606 762 RLKNDIEE-QETLLGTIMPEEESAKVC-LTDVTIMERFQMELKDVERKIaqqAAKLQGSDLDRTVQQVNQEKQEKQHEL- 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1993 virlrDSLIKMGEELSQAAtseSQQRESSQYYQRRLEELKADMEELvqreAEASRRCMELEKYVEELAAVRQTLQTDLET 2072
Cdd:TIGR00606 839 -----DTVVSKIELNRKLI---QDQQEQIQHLKSKTNELKSEKLQI----GTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
730
....*....|....
gi 51317366 2073 SIRRIADLQAALEE 2086
Cdd:TIGR00606 907 AKEQDSPLETFLEK 920
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1408-1785 |
3.17e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1408 EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKK 1487
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1488 LGDVNKQLEEAQQKIQlndlernptggADEWQMRFDCAQMENefLRKRLQQCEERLDSELTARKELEQKLGELQSAYDGA 1567
Cdd:TIGR02168 763 IEELEERLEEAEEELA-----------EAEAEIEELEAQIEQ--LKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1568 KKMAHQLKRkchHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVfekgLREKVTQENTSVRWELGQLQQQ 1647
Cdd:TIGR02168 830 ERRIAATER---RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN----ERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1648 LKQKEQEASQLKQQVEMLQDHkrellgspslgencvaglkerlwkLESSALEQQKIQSQQENtikQLEQLRQRFELEIER 1727
Cdd:TIGR02168 903 LRELESKRSELRRELEELREK------------------------LAQLELRLEGLEVRIDN---LQERLSEEYSLTLEE 955
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51317366 1728 MKQMHQKDREDQEEeledvrqsCQKRLHQLEMQLE----------QEYEE----KQMVLHEKQDLEGLIGTL 1785
Cdd:TIGR02168 956 AEALENKIEDDEEE--------ARRRLKRLENKIKelgpvnlaaiEEYEElkerYDFLTAQKEDLTEAKETL 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1697-2093 |
3.67e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1697 ALEQQKIQSQQENTIKQLEQLRQRFELEIERmkqmHQKDREDQEEELEDVRQSCQ----KRLHQLEMQLEQEYEEKQMVL 1772
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELER----LEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1773 HEKQDLEgligTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVqlllgtmedgktsvsKEELEKVHSQLEQSEAKceealk 1852
Cdd:COG4913 359 RRRARLE----ALLAALGLPLPASAEEFAALRAEAAALLEAL---------------EEELEALEEALAEAEAA------ 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1853 tQKVLTADLESMHSELENMTRNKSLVDEQLYRLqfeKADLLKRIDEDQDDLN---ELMQ-KHKDLIAQSAAdigqiqELQ 1928
Cdd:COG4913 414 -LRDLRRELRELEAEIASLERRKSNIPARLLAL---RDALAEALGLDEAELPfvgELIEvRPEEERWRGAI------ERV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1929 L------------QLEEAKK--EKHKLQEQLQVAQMRIEYLEQSTVD---------------------RAIVSRQEAVIC 1973
Cdd:COG4913 484 LggfaltllvppeHYAAALRwvNRLHLRGRLVYERVRTGLPDPERPRldpdslagkldfkphpfrawlEAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1974 dLENKTEFQKVqikRFEVlvirLRDSLIKMGEELSQAATsesQQRESSQYY-----QRRLEELKADMEELVQREAEASRR 2048
Cdd:COG4913 564 -VDSPEELRRH---PRAI----TRAGQVKGNGTRHEKDD---RRRIRSRYVlgfdnRAKLAALEAELAELEEELAEAEER 632
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 51317366 2049 CMELEKYVEELAAVRQTLQT---------DLETSIRRIADLQAALEEVASSDSD 2093
Cdd:COG4913 633 LEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDASSDD 686
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1479-2086 |
4.67e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.43 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1479 SKHEQVQKKLGDVNKQLEEAQQKIQlnDLERNPTGGADEWQmrfdcaQMENEFlrKRLQQCEERLDSELTARKeleQKLG 1558
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELK--NLDKNLNKDEEKIN------NSNNKI--KILEQQIKDLNDKLKKNK---DKIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1559 ELQSaydGAKKMAHQLKRKchhltcdlEDTCVLLENQQSRnheLEKKQKKFDLQLAQALGESVFEKGLREKVTQENtsvr 1638
Cdd:TIGR04523 100 KLNS---DLSKINSEIKND--------KEQKNKLEVELNK---LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1639 welgqlqqqlkqkeqeaSQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLR 1718
Cdd:TIGR04523 162 -----------------NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1719 QRFElEIERMKQMHQKDREDQEEELEDVRQscqkrlhQLEmQLEQEYEEKQMVLHEKQ-DLE---GLIGTLCDQIghrdf 1794
Cdd:TIGR04523 225 KQNN-QLKDNIEKKQQEINEKTTEISNTQT-------QLN-QLKDEQNKIKKQLSEKQkELEqnnKKIKELEKQL----- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1795 dvekrlrrdlrrtHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRN 1874
Cdd:TIGR04523 291 -------------NQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1875 KSLVDEQLYrlqfEKADLLKRIDEDQDDLNELMQKHKDliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEY 1954
Cdd:TIGR04523 358 NSEKQRELE----EKQNEIEKLKKENQSYKQEIKNLES----------QINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1955 LEQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEvlviRLRDSLIKMGEELSQAATSESQQRESSqyyQRRLEELKA 2033
Cdd:TIGR04523 424 LEKEIERlKETIIKNNSEIKDLTNQDSVKELIIKNLD----NTRESLETQLKVLSRSINKIKQNLEQK---QKELKSKEK 496
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 51317366 2034 DMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2086
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1683-2103 |
4.75e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1683 VAGLKERlwKLESsaleQQKIQSQQENtIKQLEQLRqrFELE-----IERMKQMHQKDRE--DQEEELEdvRQSCQKRLH 1755
Cdd:TIGR02168 167 ISKYKER--RKET----ERKLERTREN-LDRLEDIL--NELErqlksLERQAEKAERYKElkAELRELE--LALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1756 QLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQI-GHRDFDVEkrLRRDLRRTHALLSDVQLLLGTMEdGKTSVSKEELE 1834
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLeELRLEVSE--LEEEIEELQKELYALANEISRLE-QQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1835 KVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLI 1914
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1915 AQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAvicdLENKTEfqkvqikRFEVLVI 1994
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE----LEELQE-------ELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1995 RLrdslikmgEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSi 2074
Cdd:TIGR02168 462 AL--------EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD- 532
|
410 420 430
....*....|....*....|....*....|..
gi 51317366 2075 rriADLQAALEEVASSDSD---TESVQTAVDC 2103
Cdd:TIGR02168 533 ---EGYEAAIEAALGGRLQavvVENLNAAKKA 561
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1402-2287 |
1.18e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 64.37 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKS-EKLRNELRQNTDLLESKIADLTSDLAderfkgdVACQVLESERAERLQAFREVQELKsk 1480
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTvSQLRSELREAKRMYEDKIEELEKQLV-------LANSELTEARTERDQFSQESGNLD-- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1481 hEQVQKKLGDVNKQ-----LEEAQQKiQLNDLERNPTGGADEWQMRFDCAQMENEflrkRLQQCEERLDSEltARKELEQ 1555
Cdd:pfam15921 377 -DQLQKLLADLHKRekelsLEKEQNK-RLWDRDTGNSITIDHLRRELDDRNMEVQ----RLEALLKAMKSE--CQGQMER 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1556 KLGELQSAYDGAKKMAhqlkrkchHLTCDLEDTCVLL----ENQQSRNHELEKKQKKFDlQLAQALGESvfEKGLrEKVT 1631
Cdd:pfam15921 449 QMAAIQGKNESLEKVS--------SLTAQLESTKEMLrkvvEELTAKKMTLESSERTVS-DLTASLQEK--ERAI-EATN 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1632 QENTSVRwelgqlqqqlkqkeqeaSQLKQQVEMLQDHKREllgspslGENcvaglkerlwkLESSALEQQKIQSQQENTI 1711
Cdd:pfam15921 517 AEITKLR-----------------SRVDLKLQELQHLKNE-------GDH-----------LRNVQTECEALKLQMAEKD 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1712 KQLEQLRQrfelEIERMKQM-HQKDREDQEEELEdvrqscqkrlhqlEMQLEQEYEEKQMVLHEKQDLEgligtlcdqig 1790
Cdd:pfam15921 562 KVIEILRQ----QIENMTQLvGQHGRTAGAMQVE-------------KAQLEKEINDRRLELQEFKILK----------- 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1791 hrdfdvEKRLRRdLRRTHALLSDVQL----LLGTMEDGKTSVS--KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESM 1864
Cdd:pfam15921 614 ------DKKDAK-IRELEARVSDLELekvkLVNAGSERLRAVKdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNK 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1865 HSELEnMTRNKslvdeqlYRLQFEKADllkridedqddlNELMQKHKDLIAQSAADiGQIQELQLQLEEAKKEKhklQEQ 1944
Cdd:pfam15921 687 SEEME-TTTNK-------LKMQLKSAQ------------SELEQTRNTLKSMEGSD-GHAMKVAMGMQKQITAK---RGQ 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1945 LQVAQMRIEYLEQSTVDraivsrqeavicdlENKTefqkvqiKRFevlvirLRDSLIKMGEELSQAATSESQ---QRESS 2021
Cdd:pfam15921 743 IDALQSKIQFLEEAMTN--------------ANKE-------KHF------LKEEKNKLSQELSTVATEKNKmagELEVL 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2022 QYYQRRLEELKADMEELVQREAEASRRCMELEKYvEELAAVRQTLQTDLETS------IRRIADLQAALEEVASSDSDTE 2095
Cdd:pfam15921 796 RSQERRLKEKVANMEVALDKASLQFAECQDIIQR-QEQESVRLKLQHTLDVKelqgpgYTSNSSMKPRLLQPASFTRTHS 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2096 SVQTAVDCGSSGRKEMDNVSILSSQPEGSLQSWLSCTLSL-----ATDTMRTPSRQSATSSRILSPRINEEAgdterTQS 2170
Cdd:pfam15921 875 NVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVineepTVQLSKAEDKGRAPSLGALDDRVRDCI-----IES 949
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2171 ALALSRARSTNVHSKTSGDKpVSPHFVRRQKYCHFGDGEVLAVQRKSTERLEPASSPLASRSTNTSPlsrEKLPSPSaAL 2250
Cdd:pfam15921 950 SLRSDICHSSSNSLQTEGSK-SSETCSREPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSP---KKSPVHS-LL 1024
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 51317366 2251 SEFVEGLRRKRAQRGQGSTL----GLEDWPTLPIyQTTGAS 2287
Cdd:pfam15921 1025 TSSAEGSIGSSSQYRSAKTIhspdSVKDSQSLPI-ETTGKT 1064
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1655-2097 |
1.51e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1655 ASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLES------SALEQQKIQSQQENtiKQLEQLRQRFELEIERM 1728
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDrdeelrDRLEECRVAAQAHN--EEAESLREDADDLEERA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1729 KQMHQK----------------DREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghr 1792
Cdd:PRK02224 359 EELREEaaeleseleeareaveDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL--- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1793 dfdveKRLRRDLRRTHALLsdvqlllgtmEDGKTSVSKEELEKvhSQLEQSEAKCEEALKTQKVLTADLESMHSELEN-M 1871
Cdd:PRK02224 436 -----RTARERVEEAEALL----------EAGKCPECGQPVEG--SPHVETIEEDRERVEELEAELEDLEEEVEEVEErL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1872 TRNKSLV--DEQLYRLQfEKADLLK--------RIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKL 1941
Cdd:PRK02224 499 ERAEDLVeaEDRIERLE-ERREDLEeliaerreTIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1942 QEQLQVAQMRIEYLEqstvdraivsRQEAVICDLENktefqkvqikrfevlvirLRDSLIKMGEELSQAATSESQQRESS 2021
Cdd:PRK02224 578 NSKLAELKERIESLE----------RIRTLLAAIAD------------------AEDEIERLREKREALAELNDERRERL 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2022 QYYQRRLEELKAD-----MEELVQREAEASRRCMELEKYVEELAAVRQTLQTD---LETSIRRIADLQAALEEVASSDSD 2093
Cdd:PRK02224 630 AEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEA 709
|
....
gi 51317366 2094 TESV 2097
Cdd:PRK02224 710 LEAL 713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1590-2085 |
1.70e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1590 VLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1669
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1670 R--ELLGSPSLGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR 1747
Cdd:COG4717 126 QllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1748 QSCQkrlhqlemQLEQEYEEKQMVLHE-KQDLEGLigtlcdQIGHRDFDVEKRLRRdLRRTHALLSDVQLLLGTMEDGKT 1826
Cdd:COG4717 206 QRLA--------ELEEELEEAQEELEElEEELEQL------ENELEAAALEERLKE-ARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1827 SVskeelekvhsqleqseakceeaLKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQfekaDLLKRIDEDQDDLNEL 1906
Cdd:COG4717 271 LI----------------------LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ----ALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1907 MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEylEQSTVDRAIVSRQEAVICDLENKTEFQKVQi 1986
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAGVEDEEELRAALEQAEEYQELK- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1987 KRFEVLVIRLRDSLIKMGEELsqAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEK--YVEELAAVRQ 2064
Cdd:COG4717 402 EELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELE 479
|
490 500
....*....|....*....|.
gi 51317366 2065 TLQTDLETSIRRIADLQAALE 2085
Cdd:COG4717 480 ELKAELRELAEEWAALKLALE 500
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1398-1859 |
1.95e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1398 TIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTSDLADERfkgdvacqvlesERAERLQAFREVQEL 1477
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELR------------EELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1478 KSKHEQVQKKLGDVNKQLEEAQQKIQ-LNDLERnptggadewqmrfDCAQMENEFLRKRLQQCEERLDSELTARKELEQ- 1555
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEeLRELEE-------------ELEELEAELAELQEELEELLEQLSLATEEELQDl 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1556 --KLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQE 1633
Cdd:COG4717 198 aeELEELQQRLAELEEELEEAQEELEELEEELEQ----LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1634 N-----------TSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK-RELLGSPSLGENcvaGLKERLWKLESSALEQQ 1701
Cdd:COG4717 274 TiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEElEELLAALGLPPD---LSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1702 KIQSQQENTIKQLEQlrQRFELEIER-MKQMHQKDREDQEEELEDVRQSCQ--KRLHQLEMQLEQEYEEKQMVL--HEKQ 1776
Cdd:COG4717 351 ELLREAEELEEELQL--EELEQEIAAlLAEAGVEDEEELRAALEQAEEYQElkEELEELEEQLEELLGELEELLeaLDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1777 DLEGLIGTLCDQIghrdfdveKRLRRDLRRTHALLSDVQLLLGTMEDGktsvskEELEKVHSQLEQSEAKCEEALKTQKV 1856
Cdd:COG4717 429 ELEEELEELEEEL--------EELEEELEELREELAELEAELEQLEED------GELAELLQELEELKAELRELAEEWAA 494
|
...
gi 51317366 1857 LTA 1859
Cdd:COG4717 495 LKL 497
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1540-2086 |
2.22e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 63.45 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1540 EERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTcdLEDTCVLLENQ--QSRNHELEKKQKKFDLQLAQAL 1617
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELE--EEYLLYLDYLKlnEERIDLLQELLRDEQEEIESSK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1618 GESVFEKglrEKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspSLGENCVAGLKERLWKLESSA 1697
Cdd:pfam02463 258 QEIEKEE---EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK----VDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1698 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEE---ELEDVRQSCQKRLHQLEMQLEQEYEEKQMV--L 1772
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEllaKKKLESERLSSAAKLKEEELELKSEEEKEAqlL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1773 HEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKT-SVSKEELEKVHSQLEQSEAKCEEAL 1851
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDElELKKSEDLLKETQLVKLQEQLELLL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1852 KTQKVLTAD-LESMHSELENMtrNKSLVDEQLYRLQFEKADLLKRIDE-DQDDLNELMQKHKDLIAQSAADIGQIQELQL 1929
Cdd:pfam02463 491 SRQKLEERSqKESKARSGLKV--LLALIKDGVGGRIISAHGRLGDLGVaVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1930 QLEEAKKEKHKLQEQLQVAQMRIeyleqstVDRAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQ 2009
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPL-------KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESA 641
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51317366 2010 AATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2086
Cdd:pfam02463 642 KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1410-2097 |
2.67e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 62.93 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1410 ELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDL--ADERFKGDVA-CQVLESER--------------AERLQAFR 1472
Cdd:pfam12128 274 IASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaADAAVAKDRSeLEALEDQHgafldadietaaadQEQLPSWQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1473 -EVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLnDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLdseltaRK 1551
Cdd:pfam12128 354 sELENLEERLKALTGKHQDVTAKYNRRRSKIKE-QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL------RE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1552 ELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDlEDTCVLLENQQSRNHELEKKQKK-----FDLQLAQALGESVFEKGL 1626
Cdd:pfam12128 427 QLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAanaevERLQSELRQARKRRDQAS 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1627 rEKVTQENTSVRWELGQLQQQLKQKEQEASQL----KQQVEMLQDH-----KRELLG----SPSLGENCVAG-------- 1685
Cdd:pfam12128 506 -EALRQASRRLEERQSALDELELQLFPQAGTLlhflRKEAPDWEQSigkviSPELLHrtdlDPEVWDGSVGGelnlygvk 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1686 -----------------LKERLWKLESSALEQQKIQSQQEntiKQLEQLRQRFE---LEIERMKQMHQKDREDQeEELED 1745
Cdd:pfam12128 585 ldlkridvpewaaseeeLRERLDKAEEALQSAREKQAAAE---EQLVQANGELEkasREETFARTALKNARLDL-RRLFD 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1746 VRQSCQKRLHQlemqleQEYEEKQMVLHEKQDLEGLIGTLcdQIGHRDFDVEKRlRRDLRRTHALLSDVQLLLGTMEDGK 1825
Cdd:pfam12128 661 EKQSEKDKKNK------ALAERKDSANERLNSLEAQLKQL--DKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQL 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1826 TSVsKEELEKVHSQLEQSEAKCEEALKT---------QKV--LTADLESMHSELENMTRNKSLVDE--QLYRLQF--EKA 1890
Cdd:pfam12128 732 ALL-KAAIAARRSGAKAELKALETWYKRdlaslgvdpDVIakLKREIRTLERKIERIAVRRQEVLRyfDWYQETWlqRRP 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1891 DLLKRIDEDQDDLNELMQkhkDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYL----EQSTVDRAIVS 1966
Cdd:pfam12128 811 RLATQLSNIERAISELQQ---QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatlkEDANSEQAQGS 887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1967 RQEAVIC--DLENKTEFQKVQIKRFevlvIRLRDSLI--KMGEELsqAATSESqQRESSQYYQRRLEELKADMEELVQRE 2042
Cdd:pfam12128 888 IGERLAQleDLKLKRDYLSESVKKY----VEHFKNVIadHSGSGL--AETWES-LREEDHYQNDKGIRLLDYRKLVPYLE 960
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 51317366 2043 AEASRRCMELEKYVEELAAVRQTLQTD----LETSIRRIADLQAALEEVASSDSDTESV 2097
Cdd:pfam12128 961 QWFDVRVPQSIMVLREQVSILGVDLTEfydvLADFDRRIASFSRELQREVGEEAFFEGV 1019
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1405-1872 |
5.82e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 61.73 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1405 RAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDladerfKGDVACQVLESERAERLqAFREVQELKSKHEQV 1484
Cdd:pfam01576 632 REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSS------KDDVGKNVHELERSKRA-LEQQVEEMKTQLEEL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1485 QKKLG---------DVNKQLEEAQqkiqlndLERnptggadEWQMRFDCAQMENEFLRKRLQQCEERLDSE-------LT 1548
Cdd:pfam01576 705 EDELQatedaklrlEVNMQALKAQ-------FER-------DLQARDEQGEEKRRQLVKQVRELEAELEDErkqraqaVA 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1549 ARKELEQKLGELQSAYDGA-----------KKMAHQLKrkchHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQAL 1617
Cdd:pfam01576 771 AKKKLELDLKELEAQIDAAnkgreeavkqlKKLQAQMK----DLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQ 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1618 GESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLgencvagLKERLWKLESSA 1697
Cdd:pfam01576 847 EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTEL-------LNDRLRKSTLQV 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1698 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQkdredqeeELEDVRQSCQK--------RLHQLEMQLEQEYEEKQ 1769
Cdd:pfam01576 920 EQLTTELAAERSTSQKSESARQQLERQNKELKAKLQ--------EMEGTVKSKFKssiaaleaKIAQLEEQLEQESRERQ 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1770 MVlhekqdlegligtlcdqighrdfdvekrlRRDLRRTHALLSDVqLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEE 1849
Cdd:pfam01576 992 AA-----------------------------NKLVRRTEKKLKEV-LLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEE 1041
|
490 500
....*....|....*....|...
gi 51317366 1850 ALKTQKVLTADLESMHSELENMT 1872
Cdd:pfam01576 1042 AEEEASRANAARRKLQRELDDAT 1064
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1884-2086 |
6.34e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1884 RLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdra 1963
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1964 ivsrqeavicDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREA 2043
Cdd:COG4942 98 ----------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 51317366 2044 EASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2086
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1402-2080 |
6.80e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1481
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1482 EQVQKKLGDVNKQLEEAQQKiqLNDLERnptggadewqmRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQ------ 1555
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEE--YDRVEK-----------ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvh 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1556 ----KLGELQSAYDGAKKMAhqLKRKCHHLTCDLEDTCV-----LLENQQSRNHEL---EKKQKKFDLQLAQALGESVFE 1623
Cdd:TIGR02169 525 gtvaQLGSVGERYATAIEVA--AGNRLNNVVVEDDAVAKeaielLKRRKAGRATFLplnKMRDERRDLSILSEDGVIGFA 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1624 KGLREKVTQENTSVRWELGQLQQqlkqkeqeasqlkqqVEMLqDHKRELLGspslgencvaglKERLWKLESSALEQQKI 1703
Cdd:TIGR02169 603 VDLVEFDPKYEPAFKYVFGDTLV---------------VEDI-EAARRLMG------------KYRMVTLEGELFEKSGA 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1704 QSQQENTIKQLEQLRQRFELEIERMKqmhqkdreDQEEELEDVRQSCQKRLHQLEMQLEQeyeekqmVLHEKQDLEGLIG 1783
Cdd:TIGR02169 655 MTGGSRAPRGGILFSRSEPAELQRLR--------ERLEGLKRELSSLQSELRRIENRLDE-------LSQELSDASRKIG 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1784 TLCDQIghrdfdveKRLRRDLRRTHALLSDVQLLLGTMEDGKTSV--SKEELEKVHSQLEQSEAKCEEALktqkvltADL 1861
Cdd:TIGR02169 720 EIEKEI--------EQLEQEEEKLKERLEELEEDLSSLEQEIENVksELKELEARIEELEEDLHKLEEAL-------NDL 784
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1862 ESM--HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKH 1939
Cdd:TIGR02169 785 EARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1940 KLQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQ------AAT 2012
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLGDlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkgEDE 944
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51317366 2013 SESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADL 2080
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1683-2189 |
1.24e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.90 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1683 VAGLKERLwkLESSAL-EQQKIQSQQenTIKQLEQLRQRFELEIERMKQMHQKDREDQEeeleDVRQSCQKRLHQLEmql 1761
Cdd:pfam15921 87 VKDLQRRL--NESNELhEKQKFYLRQ--SVIDLQTKLQEMQMERDAMADIRRRESQSQE----DLRNQLQNTVHELE--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1762 eqeyEEKQMvlheKQDLEGLIGTLCDQighrdfdvekrLRRDLRRTHALLSDVQLLLGTMEDGKTsvskeelEKVHSQLE 1841
Cdd:pfam15921 156 ----AAKCL----KEDMLEDSNTQIEQ-----------LRKMMLSHEGVLQEIRSILVDFEEASG-------KKIYEHDS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1842 QSeakceealktqkvlTADLESMHSELENMTRNkslVDEQLYRLQ---FEKADLLKRI-DEDQDDLNELMQKHKDLIAQ- 1916
Cdd:pfam15921 210 MS--------------TMHFRSLGSAISKILRE---LDTEISYLKgriFPVEDQLEALkSESQNKIELLLQQHQDRIEQl 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1917 -SAADIgQIQELQLQLEEAKKEKHKLQEQLQVAQmrieylEQSTVDRAIVSRQeavICDLEN-----KTEFQKVQiKRFE 1990
Cdd:pfam15921 273 iSEHEV-EITGLTEKASSARSQANSIQSQLEIIQ------EQARNQNSMYMRQ---LSDLEStvsqlRSELREAK-RMYE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1991 VLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEelvQREAEASrrcmeLEKYVEELAAVRQT----- 2065
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH---KREKELS-----LEKEQNKRLWDRDTgnsit 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2066 ---LQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVDCGSSgrKEMDNVSILSSQPEGSLQSWLSCTLSLATDTMRT 2142
Cdd:pfam15921 414 idhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKN--ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 51317366 2143 PSRQSATSSriLSPRINEEAGDTERTQSALALSRAR-----STNVHSKTSGD 2189
Cdd:pfam15921 492 ESSERTVSD--LTASLQEKERAIEATNAEITKLRSRvdlklQELQHLKNEGD 541
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1830-2086 |
1.90e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1830 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1909
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1910 HKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKTEFQKVQIKR- 1988
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIe 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1989 FEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQT 2068
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250
....*....|....*...
gi 51317366 2069 DLETSIRRIADLQAALEE 2086
Cdd:COG4372 291 AALELKLLALLLNLAALS 308
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1403-1951 |
7.38e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.19 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1403 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSdladerfKGDVACQVLESERAErLQafREVQELKSKHE 1482
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE-------KKDHLTKELEDIKMS-LQ--RSMSTQKALEE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1483 QVQKKLGDVNKQLEEAQQKIQlndlERNPTGGADEW---QMRFDCAQMEnEFLRKRLQQCEERLDSELTARKELEQKLGE 1559
Cdd:pfam05483 318 DLQIATKTICQLTEEKEAQME----ELNKAKAAHSFvvtEFEATTCSLE-ELLRTEQQRLEKNEDQLKIITMELQKKSSE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1560 LQSAydgaKKMAHQLKRKCHHLTCDL-EDTCVLLENQQSRNHELEKKQKKFDLQ-LAQALGESVFEkgLREKVTQENTSV 1637
Cdd:pfam05483 393 LEEM----TKFKNNKEVELEELKKILaEDEKLLDEKKQFEKIAEELKGKEQELIfLLQAREKEIHD--LEIQLTAIKTSE 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1638 RWelgqlqqqlkqkeqeasQLKQQVEMLQDHKRELLGSPSLGENCvaglkeRLWKLESSALEQQ------KIQSQQENTI 1711
Cdd:pfam05483 467 EH-----------------YLKEVEDLKTELEKEKLKNIELTAHC------DKLLLENKELTQEasdmtlELKKHQEDII 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1712 KQLEQlRQRFELEIERMKQMHQKDREdqeeELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGH 1791
Cdd:pfam05483 524 NCKKQ-EERMLKQIENLEEKEMNLRD----ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1792 RDFDVEKRLR--RDLRRTHALLSDVqlllGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKT-QKVLTADLESMHSEL 1868
Cdd:pfam05483 599 LKKQIENKNKniEELHQENKALKKK----GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNyQKEIEDKKISEEKLL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1869 ENMTRNKSLVDEQLyRLQFEkadLLKRIDEDQDDLNELMQKHK---DLIA----------------QSAADIGQIQEL-- 1927
Cdd:pfam05483 675 EEVEKAKAIADEAV-KLQKE---IDKRCQHKIAEMVALMEKHKhqyDKIIeerdselglyknkeqeQSSAKAALEIELsn 750
|
570 580 590
....*....|....*....|....*....|....
gi 51317366 1928 ----------QLQLEEAKKEKHKLQEQLQVAQMR 1951
Cdd:pfam05483 751 ikaellslkkQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1424-2010 |
9.09e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1424 LRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQ 1503
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1504 LNDLERnptggadewqmrfdcaqmENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTC 1583
Cdd:COG4717 127 LLPLYQ------------------ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1584 ----DLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGE--SVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASq 1657
Cdd:COG4717 189 ateeELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1658 lkqqvemLQDHKRELLGSPSLgencVAGLkerLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDRE 1737
Cdd:COG4717 268 -------LLSLILTIAGVLFL----VLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1738 DQEEELEDVRQSCQKrLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGhrdfDVEKRLRRDLRRthallsdVQLl 1817
Cdd:COG4717 334 LSPEELLELLDRIEE-LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE----ELRAALEQAEEY-------QEL- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1818 lgtmedgktsvsKEELEKVHSQLEQSEAKCEEALKtqkvlTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRID 1897
Cdd:COG4717 401 ------------KEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1898 --EDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLE--EAKKEKHKLQEQLQVAQMRIEYLEQSTVDRaivsrqeavic 1973
Cdd:COG4717 464 qlEEDGELAELLQELEELKAELRELAEEWAALKLALEllEEAREEYREERLPPVLERASEYFSRLTDGR----------- 532
|
570 580 590
....*....|....*....|....*....|....*..
gi 51317366 1974 dlenkteFQKVQIKRFEVLVIRLRDSLIKMGEELSQA 2010
Cdd:COG4717 533 -------YRLIRIDEDLSLKVDTEDGRTRPVEELSRG 562
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1797-2087 |
1.18e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1797 EKRLRRDLRRTHALlsdvqlllgtmedGKTSVSK-EELEKVHSQLEQSEAKCEEALKTQKVLTADLE---SMHSELENMT 1872
Cdd:COG4913 591 EKDDRRRIRSRYVL-------------GFDNRAKlAALEAELAELEEELAEAEERLEALEAELDALQerrEALQRLAEYS 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1873 RNKSLVDEQLYRLQfEKADLLKRIDEDQDDLNELMQKHKDLIAQsaadigqIQELQLQLEEAKKEKHKLQEQLQVAQMRI 1952
Cdd:COG4913 658 WDEIDVASAEREIA-ELEAELERLDASSDDLAALEEQLEELEAE-------LEELEEELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1953 EYLeQSTVDRAIVSRQEAVICDLENKteFQKVQI-KRFEVLVIRLRDSLIKMGEELSQAATS-ESQQR------------ 2018
Cdd:COG4913 730 DEL-QDRLEAAEDLARLELRALLEER--FAAALGdAVERELRENLEERIDALRARLNRAEEElERAMRafnrewpaetad 806
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51317366 2019 -----ESSQYYQRRLEELKADmeELVQREAEASRRCMELEKyvEELAAVRQTLQTDLETSIRRIADLQAALEEV 2087
Cdd:COG4913 807 ldadlESLPEYLALLDRLEED--GLPEYEERFKELLNENSI--EFVADLLSKLRRAIREIKERIDPLNDSLKRI 876
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1404-1913 |
1.24e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1404 LRAKEEELTTLRRKLEksEKLRNELRQNTDLLESKIADLTSDLadERFkgdvacqvlESERAERLQAFREVQELKSKHEQ 1483
Cdd:PRK02224 182 LSDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEI--ERY---------EEQREQARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1484 VQKKLGDVNKQLEEAQQKI-------------------QLNDLERNPTGGADEwqMRFDCAQMEN-----EFLRKRLQQC 1539
Cdd:PRK02224 249 RREELETLEAEIEDLRETIaeterereelaeevrdlreRLEELEEERDDLLAE--AGLDDADAEAvearrEELEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1540 EERLDselTARKELEQKLGELQSAYDGAKKM---AHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKK----QKKF--- 1609
Cdd:PRK02224 327 RDRLE---ECRVAAQAHNEEAESLREDADDLeerAEELREEAAELESELEEAREAVEDRREEIEELEEEieelRERFgda 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1610 --DLQLAQALGESVFEKglREKVTQENTSVRWELgqlqqqlkqkEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLK 1687
Cdd:PRK02224 404 pvDLGNAEDFLEELREE--RDELREREAELEATL----------RTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1688 ERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELE--IERMKQMHQ---KDREDQEEELEDVRQSCQ---KRLHQLEM 1759
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrIERLEERREdleELIAERRETIEEKRERAEelrERAAELEA 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1760 QLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEK--RLRRDLRRTHALLSDVQLL------LGTMEDGKTSVSKE 1831
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLrekreaLAELNDERRERLAE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1832 ELEKvHSQLEQS--EAKCEEAlktqkvlTADLESMHSELENmtrnkslVDEQLYRLQFEKADLLKRI---DEDQDDLNEL 1906
Cdd:PRK02224 632 KRER-KRELEAEfdEARIEEA-------REDKERAEEYLEQ-------VEEKLDELREERDDLQAEIgavENELEELEEL 696
|
....*..
gi 51317366 1907 MQKHKDL 1913
Cdd:PRK02224 697 RERREAL 703
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1402-1909 |
1.58e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdllesKIADLTSDLADerfkgdvacqvLESERAERlqafreVQELKSKH 1481
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNE-------QISQLKKELTN-----------SESENSEK------QRELEEKQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1482 EQVQKKLGDVNKQLEEAQQ-KIQLNDLE---RNPTGGADEWQMRFDCAQMENEFLRKRLQQC-EERLDSELTArKELEQK 1556
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNlESQINDLEskiQNQEKLNQQKDEQIKKLQQEKELLEKEIERLkETIIKNNSEI-KDLTNQ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1557 LGELQSAYDGAKKMAHQLKRKchhltcdLEDtcvlLENQ-QSRNHELEKKQKKFDLQlaqalgesvfekglrekvtqent 1635
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQ-------LKV----LSRSiNKIKQNLEQKQKELKSK----------------------- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1636 svrwelgqlqqqlkqkeqeasqlKQQVEMLQDHKRELlgspslgENCVAGLKErlwKLESSALEQQKIqsqqENTIKQLE 1715
Cdd:TIGR04523 495 -----------------------EKELKKLNEEKKEL-------EEKVKDLTK---KISSLKEKIEKL----ESEKKEKE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1716 QLRQRFELEIERMKQMHQKdredqeEELEDVRQSCQKRLHQLEMQ---LEQEYEEKQMVLHEKQDlegLIGTLCDQIGHR 1792
Cdd:TIGR04523 538 SKISDLEDELNKDDFELKK------ENLEKEIDEKNKEIEELKQTqksLKKKQEEKQELIDQKEK---EKKDLIKEIEEK 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1793 DFDVEKrLRRDLRRTHALLSDVQLLLGTMEDGKTSVsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLE---------- 1862
Cdd:TIGR04523 609 EKKISS-LEKELEKAKKENEKLSSIIKNIKSKKNKL-KQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDdiielmkdwl 686
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 51317366 1863 ---SMHSE--LENMTRNKSLvdEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1909
Cdd:TIGR04523 687 kelSLHYKkyITRMIRIKDL--PKLEEKYKEIEKELKKLDEFSKELENIIKN 736
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1712-2091 |
1.60e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.04 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1712 KQLEQLRqRFELEIE-RMKQMHQKDREDQE--EELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEK---QDLEGLIGTL 1785
Cdd:pfam05483 85 KEAEKIK-KWKVSIEaELKQKENKLQENRKiiEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnatRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1786 CDQIGHRDFDVEKRlRRDLRRTHA-LLSDVQLLLGTMEDGKTSVSKEELEkVHSQLEQSEAKCEEALktqkvltadlESM 1864
Cdd:pfam05483 164 CARSAEKTKKYEYE-REETRQVYMdLNNNIEKMILAFEELRVQAENARLE-MHFKLKEDHEKIQHLE----------EEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1865 HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHK-------DLIAQSAADIGQIQELQLQLEEAKKE 1937
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1938 KHKLQEQLQVAQMRIEYL--------EQSTVDRA----IVSRQEAVICDLEnktEFQKVQIKRFEvlviRLRDSLIKMGE 2005
Cdd:pfam05483 312 QKALEEDLQIATKTICQLteekeaqmEELNKAKAahsfVVTEFEATTCSLE---ELLRTEQQRLE----KNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2006 ELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALE 2085
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK----QFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
....*.
gi 51317366 2086 EVASSD 2091
Cdd:pfam05483 461 AIKTSE 466
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1402-1564 |
1.67e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQ----------------NTDLLESKIADLTSDLADERfKGDVACQVLEsERA 1465
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeiDVASAEREIAELEAELERLD-ASSDDLAALE-EQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1466 ERLQAfrEVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDCAQM-ENEFLRKRLQQCEERLD 1544
Cdd:COG4913 695 EELEA--ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfAAALGDAVERELRENLE 772
|
170 180
....*....|....*....|....
gi 51317366 1545 SEL----TARKELEQKLGELQSAY 1564
Cdd:COG4913 773 ERIdalrARLNRAEEELERAMRAF 796
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1386-2060 |
2.11e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.98 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1386 QLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEKSEKlrnelRQNTDLLESKIADLTSDLADerfkgdvacqVLESERA 1465
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-----NSLTETLKKEVKSLQNEKAD----------LDRKLRK 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1466 ErlqafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNdlernptggadEWQMRFDCAQMENEFLRKRlqQCEERLDS 1545
Cdd:TIGR00606 520 L-----DQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI-----------KSRHSDELTSLLGYFPNKK--QLEDWLHS 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1546 ELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLE-------DTCVlLENQQSRNHELEKKQKKFDLQLAQALG 1618
Cdd:TIGR00606 582 KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklfDVCG-SQDEESDLERLKEEIEKSSKQRAMLAG 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1619 ESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLESSAL 1698
Cdd:TIGR00606 661 ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST-------ESELKKKEKRRDEMLGLAP 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1699 EQQKIQSQQENTIKQLEQLRQRFELEIERMKQmhqkDREDQEEELEDVR------QSCQKRLHQLEMQLEQEYEEKQMVL 1772
Cdd:TIGR00606 734 GRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN----DIEEQETLLGTIMpeeesaKVCLTDVTIMERFQMELKDVERKIA 809
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1773 HEKQDLEGLIGTLCDQighrdfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVskEELEKVHSQLEQSEAKCEEALK 1852
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQ------QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI--QHLKSKTNELKSEKLQIGTNLQ 881
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1853 TQKVLTADLESMHSELENM------TRNKSLVDEQ-LYRLQFEKADLLKRIDED----QDDLNELMQKHKDLIAQSAADI 1921
Cdd:TIGR00606 882 RRQQFEEQLVELSTEVQSLireikdAKEQDSPLETfLEKDQQEKEELISSKETSnkkaQDKVNDIKEKVKNIHGYMKDIE 961
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1922 GQIQE---------------LQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTV---DRAIVSRQEAVICDLENKTEFQK 1983
Cdd:TIGR00606 962 NKIQDgkddylkqketelntVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERwlqDNLTLRKRENELKEVEEELKQHL 1041
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51317366 1984 VQIKRFEVLviRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELA 2060
Cdd:TIGR00606 1042 KEMGQMQVL--QMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELV 1116
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1828-2087 |
2.59e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1828 VSKEELEKVHSQLEQSEaKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNEL- 1906
Cdd:PRK03918 142 ESDESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELr 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1907 --MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraivsrqeavICDLENKTEFQKv 1984
Cdd:PRK03918 221 eeLEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE-------------IEELEEKVKELK- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1985 QIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEEL---KADMEELVQREAEASRRCMELEKYVEELAA 2061
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELeekEERLEELKKKLKELEKRLEELEERHELYEE 366
|
250 260 270
....*....|....*....|....*....|.
gi 51317366 2062 VRQtLQTDLET-----SIRRIADLQAALEEV 2087
Cdd:PRK03918 367 AKA-KKEELERlkkrlTGLTPEKLEKELEEL 396
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1703-2084 |
2.98e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 55.67 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1703 IQSQQENTIKQLEQLRQRFEL---EIERMKQMHQKDREDQEEELEDVRQSCQkRLHQLEMQLEQEYEEKQMVLHEKQDLE 1779
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAanrQREKEKERYKRDREQWERQRRELESRVA-ELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1780 GLIGTLCDQIGHRDFDVEKRLRRdlrrthaLLSDVQLLLGTMEDGKTSVS--KEELEKVHSQLEQSEAKCEEALKTQKVL 1857
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRE-------LEEDIKTLTQRVLERETELErmKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1858 TADLESMHSELENMTRNKSLVDEQLYRLQfekadllkridedqDDLNELMQKhkdliaqsaadIGQIQELQLQLEEAKKE 1937
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQ--------------DTITTLTQK-----------LTTAHRKEAENEALLEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1938 KHKLQEQLQVAQMRIEYLEQSTvdRAIVSRQEAVICDLeNKTEFQKVQikrfevLVIRLRDSLIKMGEELSQAATSESQQ 2017
Cdd:pfam07888 239 LRSLQERLNASERKVEGLGEEL--SSMAAQRDRTQAEL-HQARLQAAQ------LTLQLADASLALREGRARWAQERETL 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2018 RESSQYYQRRLEELKAD---MEELVQREAeasrrcMELEKYVEELAAVRQTLQTDLETSIRRIADLQAAL 2084
Cdd:pfam07888 310 QQSAEADKDRIEKLSAElqrLEERLQEER------MEREKLEVELGREKDCNRVQLSESRRELQELKASL 373
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1683-2172 |
3.64e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1683 VAGLKERLWKLESSaLEQQKIQSQQentikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLE 1762
Cdd:pfam15921 233 ISYLKGRIFPVEDQ-LEALKSESQN-----KIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1763 QEYEEKQMVLHEKQDLEGLIgtlcdqighrdfdveKRLRRDLRRTHALLSDvqlllgtmedgktsvSKEELEK--VHSQL 1840
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTV---------------SQLRSELREAKRMYED---------------KIEELEKqlVLANS 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1841 EQSEAKCEEALKTQKV--LTADLESMHSELENMTRNKSLVDEQLYRLQFEKA------DLLKRideDQDDLNELMQKHKD 1912
Cdd:pfam15921 357 ELTEARTERDQFSQESgnLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitiDHLRR---ELDDRNMEVQRLEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1913 LIA------------QSAADIG------QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQsTVDRAIVSRQEAvicd 1974
Cdd:pfam15921 434 LLKamksecqgqmerQMAAIQGknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER-TVSDLTASLQEK---- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1975 lENKTEFQKVQIKRFEVLV-IRLRD--SLIKMGEELSQAATSESQQRESSQYYQRRLEELKADME--------------- 2036
Cdd:pfam15921 509 -ERAIEATNAEITKLRSRVdLKLQElqHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgrtaga 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2037 ---ELVQREAEASRRCMELEKYveelaavrQTLQTDLETSIR----RIADLQaaLEEVASSDSDTESVQTAVDCgssgRK 2109
Cdd:pfam15921 588 mqvEKAQLEKEINDRRLELQEF--------KILKDKKDAKIReleaRVSDLE--LEKVKLVNAGSERLRAVKDI----KQ 653
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51317366 2110 EMDNVSILSSQPEGSLQSwLSCTLSLATDTMRTPSRQSATSSRILSPRINEEAGDTERTQSAL 2172
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNS-LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1924-2178 |
3.82e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 55.42 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1924 IQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIV----------SRQEAVICDLEN-KTEFQKVQiKRFEVL 1992
Cdd:pfam05701 79 IEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEASVaakaqlevakARHAAAVAELKSvKEELESLR-KEYASL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1993 VIRlRDSLIKMGEElsqaATSESQQREssqyyqRRLEELKAD----MEEL-----VQREAEASRRC-------------- 2049
Cdd:pfam05701 158 VSE-RDIAIKRAEE----AVSASKEIE------KTVEELTIEliatKESLesahaAHLEAEEHRIGaalareqdklnwek 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2050 ------MELEKYVEELAAVRQtLQTDLETSIRRIADLQA--------ALEEVASSDSDTE----SVQTAVDcgsSGRKEM 2111
Cdd:pfam05701 227 elkqaeEELQRLNQQLLSAKD-LKSKLETASALLLDLKAelaaymesKLKEEADGEGNEKktstSIQAALA---SAKKEL 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51317366 2112 DNV--SILSSQPE--------GSLQSWLSCTLS-LATdtmrtpSRQSATSSRILSPRINEEagdTERTQSALALSRAR 2178
Cdd:pfam05701 303 EEVkaNIEKAKDEvnclrvaaASLRSELEKEKAeLAS------LRQREGMASIAVSSLEAE---LNRTKSEIALVQAK 371
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1831-2100 |
3.91e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1831 EELEKvhsQLEQSEAKCEEALKTQKvLTADLEsmhselenmtrnksLVDEQLYRLQFEKADllKRIDEDQDDLNELMQKH 1910
Cdd:COG1196 196 GELER---QLEPLERQAEKAERYRE-LKEELK--------------ELEAELLLLKLRELE--AELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1911 KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdraivsrqeavicdlenktefqkvQIKRFE 1990
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ---------------------------DIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1991 VLVIRLRDSLIKMGEELSQAATSESQQREssqyyqrRLEELKADMEELvqrEAEASRRCMELEKYVEELAAVRQTLQTDL 2070
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEE-------ELEELEEELEEA---EEELEEAEAELAEAEEALLEAEAELAEAE 378
|
250 260 270
....*....|....*....|....*....|
gi 51317366 2071 ETSIRRIADLQAALEEVASSDSDTESVQTA 2100
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEA 408
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1512-1898 |
4.14e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1512 TGGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEdtcvl 1591
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA----- 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1592 lenqqsrnhELEKKQKKFDLQLAQALGEsvfekglREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHkre 1671
Cdd:TIGR02168 737 ---------RLEAEVEQLEERIAQLSKE-------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE--- 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1672 llgspslgencVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHqKDREDQEEELEDVRQSCQ 1751
Cdd:TIGR02168 798 -----------LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI-EELSEDIESLAAEIEELE 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1752 KRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIgHRDFDVEKRLRRDLRRTHALLSDVQLLLGTME--------- 1822
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEEL-RELESKRSELRRELEELREKLAQLELRLEGLEvridnlqer 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1823 -DGKTSVSKEELEKVHSQLEQSEAKCEEALKT-QKVLTA----DLESMhSELENMTRNKSLVDEQLYRLQFEKADLLKRI 1896
Cdd:TIGR02168 945 lSEEYSLTLEEAEALENKIEDDEEEARRRLKRlENKIKElgpvNLAAI-EEYEELKERYDFLTAQKEDLTEAKETLEEAI 1023
|
..
gi 51317366 1897 DE 1898
Cdd:TIGR02168 1024 EE 1025
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1900-2088 |
4.87e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1900 QDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ--STVDRAIVSRQEAvicdLEN 1977
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeiAEAEAEIEERREE----LGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1978 KTEFQKVQIKRFEVLvirlrdSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVE 2057
Cdd:COG3883 91 RARALYRSGGSVSYL------DVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190
....*....|....*....|....*....|.
gi 51317366 2058 ELAAVRQTLQTDLETSIRRIADLQAALEEVA 2088
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1848-2083 |
7.61e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1848 EEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAqsaadigQIQEL 1927
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1928 QLQLEEAKKEkhkLQEQLQVAQM--RIEYLE----QSTVDRAIVSRQ--EAVICDLENKTEFQKVQIKRfevlVIRLRDS 1999
Cdd:COG4942 96 RAELEAQKEE---LAELLRALYRlgRQPPLAlllsPEDFLDAVRRLQylKYLAPARREQAEELRADLAE----LAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2000 LIKMGEELSQAATSESQQRessqyyqRRLEELKADMEELVqreAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD 2079
Cdd:COG4942 169 LEAERAELEALLAELEEER-------AALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
....
gi 51317366 2080 LQAA 2083
Cdd:COG4942 239 AAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1812-2086 |
9.04e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1812 SDVQLLLGTMEDGKtsvsKEELEKVHSQLEQSEAKceEALKTQKVLTADLESMHSELENMTRNKSLVDEQLyrlqfEKAD 1891
Cdd:PRK02224 172 SDARLGVERVLSDQ----RGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETR-----DEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1892 L-LKRIDEDQDDLNELMQkhkdliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLE--------QSTVDR 1962
Cdd:PRK02224 241 EvLEEHEERREELETLEA--------------EIEDLRETIAETEREREELAEEVRDLRERLEELEeerddllaEAGLDD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1963 AIVSRQEAVICDLENKTEF-------QKVQIKRFEVLVIRLRDSLIKMGEEL----SQAATSESQ---QRESSQYYQRRL 2028
Cdd:PRK02224 307 ADAEAVEARREELEDRDEElrdrleeCRVAAQAHNEEAESLREDADDLEERAeelrEEAAELESEleeAREAVEDRREEI 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51317366 2029 EELKADMEELVQREAEASRRCMELEKYVEELAAVRQ-------TLQTDLETSIRRIADLQAALEE 2086
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDelrereaELEATLRTARERVEEAEALLEA 451
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1464-2115 |
9.27e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.84 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1464 RAERLQAfrEVQELKSKHEQVQK-KLGDVNKQLEEA-QQKIQ---LNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQ 1538
Cdd:pfam12128 242 EFTKLQQ--EFNTLESAELRLSHlHFGYKSDETLIAsRQEERqetSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1539 CEERLDSeLTARKELEQKLGELQSAYDgaKKMAHQLKRKCHHLTCDLEdtcVLLENQQSRNHELEKKQKKFDLQLAQALg 1618
Cdd:pfam12128 320 DRSELEA-LEDQHGAFLDADIETAAAD--QEQLPSWQSELENLEERLK---ALTGKHQDVTAKYNRRRSKIKEQNNRDI- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1619 eSVFEKGLREkvtQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKREL---LGSPSLGENCVAGLKERLWKLES 1695
Cdd:pfam12128 393 -AGIKDKLAK---IREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLksrLGELKLRLNQATATPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1696 SALEQQKIQSQQENTIKQLE-------QLRQRFELEIERMKQMHQKdredqeeeLEDVRQSCQKRLHQLEMQleqeyeeK 1768
Cdd:pfam12128 469 FDERIERAREEQEAANAEVErlqselrQARKRRDQASEALRQASRR--------LEERQSALDELELQLFPQ-------A 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1769 QMVLH----EKQDLEGLIGTLCD--QIGHRDFDVEKrlrrdlrrTHALLSDVQLLLGTMEDGKtSVSKEELEKVHSQLEQ 1842
Cdd:pfam12128 534 GTLLHflrkEAPDWEQSIGKVISpeLLHRTDLDPEV--------WDGSVGGELNLYGVKLDLK-RIDVPEWAASEEELRE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1843 SEAKCEEALKTQKVLTADLESMHSELenmtrNKSLvDEQLYRLQFEKADlLKRIDEDQDDLNELMQKHKDLIAQSAADIG 1922
Cdd:pfam12128 605 RLDKAEEALQSAREKQAAAEEQLVQA-----NGEL-EKASREETFARTA-LKNARLDLRRLFDEKQSEKDKKNKALAERK 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1923 QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQST-------------------VDRAIVSRQEAV-----ICDLENK 1978
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTekqaywqvvegaldaqlalLKAAIAARRSGAkaelkALETWYK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1979 TEFQKVQIKrfEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQR-----------RLEELKADMEEL------VQR 2041
Cdd:pfam12128 758 RDLASLGVD--PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQEtwlqrrprlatQLSNIERAISELqqqlarLIA 835
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51317366 2042 EAEASRRCMELEKYVEELAAVRQT-LQTDLETSIRRIADLQaaleEVASSDSDTESVQTAVDCGSSGRKEMDNVS 2115
Cdd:pfam12128 836 DTKLRRAKLEMERKASEKQQVRLSeNLRGLRCEMSKLATLK----EDANSEQAQGSIGERLAQLEDLKLKRDYLS 906
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1869-2098 |
1.05e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1869 ENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHK--DLIAQSAADIGQIQELQLQLEEAkkekhklQEQLQ 1946
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA-------RAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1947 VAQMRIEYLEQ---STVDRAIVSRQEAVICDLenKTEFQKVQIKRFEVLViRLRDSLIKMGEELSQAATSESQQRESSqy 2023
Cdd:COG3206 237 EAEARLAALRAqlgSGPDALPELLQSPVIQQL--RAQLAELEAELAELSA-RYTPNHPDVIALRAQIAALRAQLQQEA-- 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51317366 2024 yQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQT---LQTDLETSIRRIADLQAALEEV-ASSDSDTESVQ 2098
Cdd:COG3206 312 -QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARELYESLLQRLEEArLAEALTVGNVR 389
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1597-1878 |
2.00e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.20 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1597 SRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQ--DHKRELlg 1674
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRqeERKREL-- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1675 sPSLGENCVAGLKERLWKLESSALEQQ----KIQSQQENTIKQ--LEQLRQR------FELEIERMKQMHQKDR------ 1736
Cdd:pfam17380 363 -ERIRQEEIAMEISRMRELERLQMERQqkneRVRQELEAARKVkiLEEERQRkiqqqkVEMEQIRAEQEEARQRevrrle 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1737 EDQEEELEDVRQSCQKRLHQLEM--QLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDv 1814
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK- 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51317366 1815 qlllgTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESmHSELENMTRNKSLV 1878
Cdd:pfam17380 521 -----EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE-RSRLEAMEREREMM 578
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1402-1836 |
2.33e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTS----------------DLADERFKGDVACQVLESERA 1465
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiklsefyeEYLDELREIEKRLSRLEEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1466 ERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDCAQMEN-----EFLRKRLQQCE 1540
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKlekelEELEKAKEEIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1541 ERLdSELTARK-ELEQKLGELQSAYDGAKKMahqlKRKC---------HH-------LTCDLED---------------- 1587
Cdd:PRK03918 405 EEI-SKITARIgELKKEIKELKKAIEELKKA----KGKCpvcgrelteEHrkelleeYTAELKRiekelkeieekerklr 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1588 -------TCVLLENQQSRNH-------ELEKKQKKFDLQLAQALGESvFEKGLRE--KVTQENTSVRWELGQLQQQLKQK 1651
Cdd:PRK03918 480 kelreleKVLKKESELIKLKelaeqlkELEEKLKKYNLEELEKKAEE-YEKLKEKliKLKGEIKSLKKELEKLEELKKKL 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1652 EQEASQLKQQVEMLQDHKRELLgspSLGENCVAGLKERLWKLES------------SALE-----QQKIQSQQENTIKQL 1714
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELE---ELGFESVEELEERLKELEPfyneylelkdaeKELEreekeLKKLEEELDKAFEEL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1715 EQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVlheKQDLEGLigtlcdqigHRDF 1794
Cdd:PRK03918 636 AETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEI---KKTLEKL---------KEEL 703
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 51317366 1795 DVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKV 1836
Cdd:PRK03918 704 EEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKV 745
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1692-1957 |
2.53e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1692 KLESSALEQQKIQSQQENTIKQLEQLRQR----------FELEIERMKQM--HQKDREDQEE--ELEDVRQSCQKRLHQL 1757
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARieeleedlhkLEEALNDLEARlsHSRIPEIQAElsKLEEEVSRIEARLREI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1758 EMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKE------ 1831
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKErdelea 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1832 ELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELenmtrnkSLVDEQLYRLQFEKADLLKrIDEDQDDLNELMQKHK 1911
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-------SEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIR 968
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 51317366 1912 DLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1957
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1408-2017 |
2.63e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1408 EEELTTLRRKLEKSEKLRNELRQNTDLLES---KIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQV 1484
Cdd:PRK01156 172 KDVIDMLRAEISNIDYLEEKLKSSNLELENikkQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1485 QKklgdVNKQLEEAQQKIQLNDLERNPTGGADEWQMRF--DCAQMENEFLRK---------RLQQCEERLDSELTARKEL 1553
Cdd:PRK01156 252 NR----YESEIKTAESDLSMELEKNNYYKELEERHMKIinDPVYKNRNYINDyfkykndieNKKQILSNIDAEINKYHAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1554 EQKLGELQSAYDGAKKMAHQ---LKRKCHHLTCDLEDTCVLLENQQSRN---HELEKKQKKFDLQLAQALGESVFE---- 1623
Cdd:PRK01156 328 IKKLSVLQKDYNDYIKKKSRyddLNNQILELEGYEMDYNSYLKSIESLKkkiEEYSKNIERMSAFISEILKIQEIDpdai 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1624 KGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGE----NCVAGLKERLWKLESSALE 1699
Cdd:PRK01156 408 KKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEeksnHIINHYNEKKSRLEEKIRE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1700 QQKIQSQQENTIKQLEQLRQRFEL-EIERMKQMHQKdREDQEEELEDVRQScQKRLHQLEMQLEQEYEE-KQMVLhekQD 1777
Cdd:PRK01156 488 IEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNK-IESARADLEDIKIK-INELKDKHDKYEEIKNRyKSLKL---ED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1778 LEGLIGTLCDQIGHRD-FDVEK-RLRRDlrrthallsDVQLLLGTMEDGKTSVsKEELEKVHSQLEQSEAKCEEALKTqk 1855
Cdd:PRK01156 563 LDSKRTSWLNALAVISlIDIETnRSRSN---------EIKKQLNDLESRLQEI-EIGFPDDKSYIDKSIREIENEANN-- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1856 vltadLESMHSELENmtrNKSLVDEqlyrLQFEKADLLKRI---DEDQDDLNELMQKhkdlIAQSAADIGQIQElqlQLE 1932
Cdd:PRK01156 631 -----LNNKYNEIQE---NKILIEK----LRGKIDNYKKQIaeiDSIIPDLKEITSR----INDIEDNLKKSRK---ALD 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1933 EAKKEKHKLQEQLQVAQMRIEYLEQSTVDRaivsrqeavicdleNKTEFQKVQIKRFEVLVIRLRDSLIKMG------EE 2006
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDI--------------NETLESMKKIKKAIGDLKRLREAFDKSGvpamirKS 757
|
650
....*....|.
gi 51317366 2007 LSQAATSESQQ 2017
Cdd:PRK01156 758 ASQAMTSLTRK 768
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1388-1760 |
2.82e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1388 LGSLQPLLSATigTEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAER 1467
Cdd:pfam15921 463 VSSLTAQLEST--KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1468 lqafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQlNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERL--DS 1545
Cdd:pfam15921 541 ----DHLRNVQTECEALKLQMAEKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIlkDK 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1546 ELTARKELEQKLGELQ--------------SAYDGAKKMAHQLKRKCHHLTCDL----EDTCVLLENQQSRNHELEKKQK 1607
Cdd:pfam15921 616 KDAKIRELEARVSDLElekvklvnagserlRAVKDIKQERDQLLNEVKTSRNELnslsEDYEVLKRNFRNKSEEMETTTN 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1608 KFDLQLAQALGEsvfekglREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDhKRELLGSPSLGENcvaglK 1687
Cdd:pfam15921 696 KLKMQLKSAQSE-------LEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQS-KIQFLEEAMTNAN-----K 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1688 ER-LWKLESSALEQQ--KIQSQQENTIKQLEQLR---QRFELEIERMK--------QMHQKDREDQEEELEDVRQSCQKR 1753
Cdd:pfam15921 763 EKhFLKEEKNKLSQElsTVATEKNKMAGELEVLRsqeRRLKEKVANMEvaldkaslQFAECQDIIQRQEQESVRLKLQHT 842
|
....*..
gi 51317366 1754 LHQLEMQ 1760
Cdd:pfam15921 843 LDVKELQ 849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1686-2092 |
5.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1686 LKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFEL---EIERMKQMHQKDREDQE-EELEDVRQSCQKRLHQLEMQL 1761
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1762 eQEYEEKQmvlHEKQDLEGLIGTLCDQI----GHRDFDVEKRLRRDLRRTHALLSDVQLLLGTMEDgktsvSKEELEKVH 1837
Cdd:COG4717 156 -EELRELE---EELEELEAELAELQEELeellEQLSLATEEELQDLAEELEELQQRLAELEEELEE-----AQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1838 SQLEQSEAKCEEALKTQK---------------------------------VLTADLESMHSELENMTRNKSLVDEQLYR 1884
Cdd:COG4717 227 EELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1885 LQfekaDLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQvaqmrIEYLEQstvdrai 1964
Cdd:COG4717 307 LQ----ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-----LEELEQ------- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1965 vsrqeavicdlENKTEFQKVQIKrfevlvirLRDSLIKMGEELSQAAtsesQQRESSQYYQRRLEELKADMEELVQREAE 2044
Cdd:COG4717 371 -----------EIAALLAEAGVE--------DEEELRAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLEALDE 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 51317366 2045 AsrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDS 2092
Cdd:COG4717 428 E-----ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1418-2087 |
6.33e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 52.14 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1418 LEKSEKLRNELRQNTDLLESKIADL---TSDLADERFKGDVacQVLESERAERLQ----------AFREVQELKSKHEQV 1484
Cdd:PTZ00440 597 IQQIEELINEALFNKEKFINEKNDLqekVKYILNKFYKGDL--QELLDELSHFLDdhkylyheakSKEDLQTLLNTSKNE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1485 QKKLGDVN------------------KQLEEAQQKIQLNDLERNPTGGAD-------EWQMRFDCAQMENEFLRKRLQQC 1539
Cdd:PTZ00440 675 YEKLEFMKsdnidniiknlkkelqnlLSLKENIIKKQLNNIEQDISNSLNqytikynDLKSSIEEYKEEEEKLEVYKHQI 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1540 EERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEdtcVLLENQQSRNHELEKKQKKfDLQLAQALGE 1619
Cdd:PTZ00440 755 INRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDIN---ILKENKKNNQDLLNSYNIL-IQKLEAHTEK 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1620 SVFE-KGLREKVTQENTSVRweLGQLQQQLKQKEQEASQLKQQVEmLQDHKRELLGSPSLGENcvaglkerlwkleSSAL 1698
Cdd:PTZ00440 831 NDEElKQLLQKFPTEDENLN--LKELEKEFNENNQIVDNIIKDIE-NMNKNINIIKTLNIAIN-------------RSNS 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1699 EQQKIQSQQENTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVRQSCQKRL-----HQLEMQLEQ--EYEEKQmv 1771
Cdd:PTZ00440 895 NKQLVEHLLNNKIDLKNKLEQHMK-IINTDNIIQKNEKLNLLNNLNKEKEKIEKQLsdtkiNNLKMQIEKtlEYYDKS-- 971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1772 lheKQDLEGLIGTLCDQighrdFDVEKRLRRDLRRT-HALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEa 1850
Cdd:PTZ00440 972 ---KENINGNDGTHLEK-----LDKEKDEWEHFKSEiDKLNVNYNILNKKIDDLIKKQHDDIIELIDKLIKEKGKEIEE- 1042
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1851 lKTQKVLTAdLESMHSELENMTRNK-------SLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS------ 1917
Cdd:PTZ00440 1043 -KVDQYISL-LEKMKTKLSSFHFNIdikkyknPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNAdkeknk 1120
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1918 --------AADIG----QIQELQLQLEEAKKEKHKLQEqlqVAQMRIEYleqstvDRAIVSRQEAVICDLENKTEFQKVQ 1985
Cdd:PTZ00440 1121 qtehynkkKKSLEkiykQMEKTLKELENMNLEDITLNE---VNEIEIEY------ERILIDHIVEQINNEAKKSKTIMEE 1191
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1986 IKRFEVLVIRLRDSLIKmgEELSQAATSESQQressqyYQRRLEELKADMEELVQrEAEASRRCMELEKYVEELAAVRQT 2065
Cdd:PTZ00440 1192 IESYKKDIDQVKKNMSK--ERNDHLTTFEYNA------YYDKATASYENIEELTT-EAKGLKGEANRSTNVDELKEIKLQ 1262
|
730 740
....*....|....*....|..
gi 51317366 2066 LQTDLETSIRRIADLQAALEEV 2087
Cdd:PTZ00440 1263 VFSYLQQVIKENNKMENALHEI 1284
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1411-1948 |
8.60e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.28 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1411 LTTLRRKLEKSEKlrnELRQNTDLLESKIADLTSDLADERFKG---DVACQVLESERAERLQAFREVQELkskHEQVQKK 1487
Cdd:pfam05557 11 LSQLQNEKKQMEL---EHKRARIELEKKASALKRQLDRESDRNqelQKRIRLLEKREAEAEEALREQAEL---NRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1488 LGDVNKQLEE-AQQKIQLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYDG 1566
Cdd:pfam05557 85 LEALNKKLNEkESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1567 AKKMAHQLKRKCHHLtCDLEDTCVLLENQQS---RNHELEKKQKKFDLQLAQaLGESVFEKG-LREKVTQENTSVRWELG 1642
Cdd:pfam05557 165 LAEAEQRIKELEFEI-QSQEQDSEIVKNSKSelaRIPELEKELERLREHNKH-LNENIENKLlLKEEVEDLKRKLEREEK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1643 QLQQQLK---QKEQEASQLKQQVEMLQDHKRELLGSPSLGENCV------AGLKERLWKLESSALEQQKIQSQQENTIKQ 1713
Cdd:pfam05557 243 YREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEqlqqreIVLKEENSSLTSSARQLEKARRELEQELAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1714 LeqLRQRFELEIERMKQMHQKDR---------------------EDQE--------------EELEDVRQSCQKRLHQLE 1758
Cdd:pfam05557 323 Y--LKKIEDLNKKLKRHKALVRRlqrrvllltkerdgyrailesYDKEltmsnyspqlleriEEAEDMTQKMQAHNEEME 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1759 MQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRthallsDVQLLLgtMEDGKTSVSKEELEkvhS 1838
Cdd:pfam05557 401 AQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRR------KLETLE--LERQRLREQKNELE---M 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1839 QLEQSEAKCEEALKTQKVLtadlesmHSELENMTRNKSLVDEQLYRLQFEKA---DLLKRIDEDQDDLNELMQKHKDLIA 1915
Cdd:pfam05557 470 ELERRCLQGDYDPKKTKVL-------HLSMNPAAEAYQQRKNQLEKLQAEIErlkRLLKKLEDDLEQVLRLPETTSTMNF 542
|
570 580 590
....*....|....*....|....*....|...
gi 51317366 1916 QSAADigqiqeLQLQLEEAKKEKHKLQEQLQVA 1948
Cdd:pfam05557 543 KEVLD------LRKELESAELKNQRLKEVFQAK 569
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1473-1962 |
9.37e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 51.01 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1473 EVQELKSK-HEQVQKKLGDVNKQLEEAQQkiqLNDlernptggadewQMRFDCAQMENEFLRKRLQQCEERLDSELTARK 1551
Cdd:pfam06160 46 KFEEWRKKwDDIVTKSLPDIEELLFEAEE---LND------------KYRFKKAKKALDEIEELLDDIEEDIKQILEELD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1552 ELEQKLGELQSAYDGAKKMAHQLKRKchhltcdledtcvLLENqqsrNHELEKKQKKFDLQLAQAlgESVFEKglrekVT 1631
Cdd:pfam06160 111 ELLESEEKNREEVEELKDKYRELRKT-------------LLAN----RFSYGPAIDELEKQLAEI--EEEFSQ-----FE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1632 QENTSvrwelgqlqqqlkQKEQEASQLKQQVEMLQDHKRELLGS-PSLGENCVAGLKERLWKLES--SALEQQKIQSQQE 1708
Cdd:pfam06160 167 ELTES-------------GDYLEAREVLEKLEEETDALEELMEDiPPLYEELKTELPDQLEELKEgyREMEEEGYALEHL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1709 NTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDvrqscqkRLHQLEMQLEQEYEEKQMVLHEKQDLEgligtlcDQ 1788
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEE-------RIDQLYDLLEKEVDAKKYVEKNLPEIE-------DY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1789 IGHRDfDVEKRLRRDLRRT---------------------HALLSDVQLLLGTMEDGKTSVS--KEELEKVHSQLEQSEA 1845
Cdd:pfam06160 300 LEHAE-EQNKELKEELERVqqsytlnenelervrglekqlEELEKRYDEIVERLEEKEVAYSelQEELEEILEQLEEIEE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1846 KCEEALKTQKVLTAD-------LESMHSELENM-----TRNKSLVDEQlYRLQFEKA-DLLKRIDED------------- 1899
Cdd:pfam06160 379 EQEEFKESLQSLRKDelearekLDEFKLELREIkrlveKSNLPGLPES-YLDYFFDVsDEIEDLADElnevplnmdevnr 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1900 -----QDDLNELMQKHKDLIaQSAADIGQ-IQ----------ELQLQLEEAKK--EKHKLQEQLQVAQMRIEYLEQSTVD 1961
Cdd:pfam06160 458 lldeaQDDVDTLYEKTEELI-DNATLAEQlIQyanryrssnpEVAEALTEAELlfRNYDYEKALEIAATALEKVEPGAYE 536
|
.
gi 51317366 1962 R 1962
Cdd:pfam06160 537 R 537
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1703-2028 |
1.30e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.67 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1703 IQSQQENTIKQLEQLrqrfeleiERMKQMHQKDrEDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLI 1782
Cdd:PLN02939 102 MQRDEAIAAIDNEQQ--------TNSKDGEQLS-DFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1783 GTLcdqighrdfdvEKRLRRdlrrthallSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQ---SEAKCEEA-------LK 1852
Cdd:PLN02939 173 NIL-----------EMRLSE---------TDARIKLAAQEKIHVEILEEQLEKLRNELLIrgaTEGLCVHSlskeldvLK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1853 TQKV-LTADLESMHSELENMT----------RNKSLVDEQLYRLQFE----KADLLK----RID---EDQDDLNELMQKH 1910
Cdd:PLN02939 233 EENMlLKDDIQFLKAELIEVAeteervfkleKERSLLDASLRELESKfivaQEDVSKlsplQYDcwwEKVENLQDLLDRA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1911 KDLIAQSAADIGQ-------IQELQLQLEEAKKEKHKLqEQLQVAQMRIEYLEqstvdraivSRQEAviCDLENKTefqk 1983
Cdd:PLN02939 313 TNQVEKAALVLDQnqdlrdkVDKLEASLKEANVSKFSS-YKVELLQQKLKLLE---------ERLQA--SDHEIHS---- 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 51317366 1984 vQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRL 2028
Cdd:PLN02939 377 -YIQLYQESIKEFQDTLSKLKEESKKRSLEHPADDMPSEFWSRIL 420
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1698-2102 |
1.56e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.51 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1698 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDRE-DQEEELEDVRQSCQKRLH--------QLEM--------- 1759
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDREsDRNQELQKRIRLLEKREAeaeealreQAELnrlkkkyle 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1760 ---QLEQEYEEKQMVLHEKQD-LEGLIGTLCDQIGHRDFDVE------KRLRRDLRRTHALLSDVQLLLGTMEdGKTSVS 1829
Cdd:pfam05557 87 alnKKLNEKESQLADAREVIScLKNELSELRRQIQRAELELQstnselEELQERLDLLKAKASEAEQLRQNLE-KQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1830 KEELEKVhSQLE---QSEAKCEEALKTQKVLTADLESMHSELE----------NMTRNKSLVDEQLYRLQFEkadlLKRI 1896
Cdd:pfam05557 166 AEAEQRI-KELEfeiQSQEQDSEIVKNSKSELARIPELEKELErlrehnkhlnENIENKLLLKEEVEDLKRK----LERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1897 DEDQDDLNELMQKHKDLIA--QSAADIGQIQEL-------------QLQLEEA--KKEKHKLQEQLQVAQMRIEYLEQSt 1959
Cdd:pfam05557 241 EKYREEAATLELEKEKLEQelQSWVKLAQDTGLnlrspedlsrrieQLQQREIvlKEENSSLTSSARQLEKARRELEQE- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1960 vdraiVSRQEAVICDLENKTEFQKVQIKRFE---VLVIRLRDSLIKMGEELSqaatSESQQRESSQYYQRRLEELkADME 2036
Cdd:pfam05557 320 -----LAQYLKKIEDLNKKLKRHKALVRRLQrrvLLLTKERDGYRAILESYD----KELTMSNYSPQLLERIEEA-EDMT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51317366 2037 ELVQREAEASRrcMELEKYVEELAAVRQTLQTD-LETSIRRiadLQAALEEVASSDSDTESVQTAVD 2102
Cdd:pfam05557 390 QKMQAHNEEME--AQLSVAEEELGGYKQQAQTLeRELQALR---QQESLADPSYSKEEVDSLRRKLE 451
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1402-1763 |
2.16e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.83 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKL-EKSEKLRNELRQNT-------DLLESKIADLTSDLadERFkgdvacqVLESERAERLQAFRE 1473
Cdd:PRK04778 129 QELLESEEKNREEVEQLkDLYRELRKSLLANRfsfgpalDELEKQLENLEEEF--SQF-------VELTESGDYVEAREI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1474 VQELKSKHEQVQKKLGDVNKQLEEAQQKI--QLNDLERnptgGADEWQM---RFDCAQMENEF--LRKRLQQC------- 1539
Cdd:PRK04778 200 LDQLEEELAALEQIMEEIPELLKELQTELpdQLQELKA----GYRELVEegyHLDHLDIEKEIqdLKEQIDENlalleel 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1540 ------------EERLDS-------ELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLtcdledtcvllenQQSR-- 1598
Cdd:PRK04778 276 dldeaeekneeiQERIDQlydilerEVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRV-------------KQSYtl 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1599 NHELEKKQKKFDLQLAQAlgESVFEKgLREKVTQENTSvrwelgqlqqqlkqkeqeASQLKQQVEMLQDHkrellgspsl 1678
Cdd:PRK04778 343 NESELESVRQLEKQLESL--EKQYDE-ITERIAEQEIA------------------YSELQEELEEILKQ---------- 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1679 gencvaglkerlwklessaLEQqkIQSQQENTIKQLEQLR----------QRFELEIERMKQMHQKDR-----EDQEEEL 1743
Cdd:PRK04778 392 -------------------LEE--IEKEQEKLSEMLQGLRkdeleareklERYRNKLHEIKRYLEKSNlpglpEDYLEMF 450
|
410 420
....*....|....*....|
gi 51317366 1744 EDVrqscQKRLHQLEMQLEQ 1763
Cdd:PRK04778 451 FEV----SDEIEALAEELEE 466
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1830-2046 |
2.67e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1830 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESmHSELENMTRnkslVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1909
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA-KLLLQQLSE----LESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1910 HKDLIAQSAAD--IGQIQELQLQLEEAKK---EKH----KLQEQLQVAQmrieyleqstvdRAIVSRQEAVICDLENKTE 1980
Cdd:COG3206 256 LPELLQSPVIQqlRAQLAELEAELAELSArytPNHpdviALRAQIAALR------------AQLQQEAQRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51317366 1981 FQKVQIKrfevlviRLRDSLIKMGEELSQAATSESQQREssqyYQRRLEELKADMEELVQREAEAS 2046
Cdd:COG3206 324 ALQAREA-------SLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1401-1562 |
3.09e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1401 TEQLRAKEEELTTLR-----RKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacQVLESERAERLQA-FREV 1474
Cdd:COG4913 268 RERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALR-------EELDELEAQIRGNgGDRL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1475 QELKSKHEQVQKKLGDVNKQLEEAQQkiQLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELE 1554
Cdd:COG4913 341 EQLEREIERLERELEERERRRARLEA--LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
....*...
gi 51317366 1555 QKLGELQS 1562
Cdd:COG4913 419 RELRELEA 426
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1831-2059 |
3.27e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 47.72 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1831 EELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKH 1910
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1911 KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStVDRAI--VSRQEAVICDLENKTEFQKVQIKR 1988
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGD-LERAEerAELAESKIVELEEELKVVGNNLKS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51317366 1989 FEVlvirlrdslikmgeelsqaATSESQQRESSqyYQRRLEELKADMEELVQREAEASRRCMELEKYVEEL 2059
Cdd:pfam00261 160 LEA-------------------SEEKASEREDK--YEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRL 209
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1859-2092 |
5.97e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1859 ADLESMHSELENMTRnkslvdeqlyrlqfeKADLLKRIDEDQDDLNELMQKHKDLiaQSAADIGQIQELQLQLEEAKKEK 1938
Cdd:COG4913 235 DDLERAHEALEDARE---------------QIELLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1939 HKLQEQLQVAQMRIEYLEQsTVDRAIVSRQEAVICDLENKTEfqkvQIKRFEvlvirlrdslikmgEELSQAATSESQQR 2018
Cdd:COG4913 298 EELRAELARLEAELERLEA-RLDALREELDELEAQIRGNGGD----RLEQLE--------------REIERLERELEERE 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51317366 2019 ESSQYYQRRLEELK----ADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDS 2092
Cdd:COG4913 359 RRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1747-2086 |
6.28e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.58 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1747 RQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQlllGTMEDGKT 1826
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR---EQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1827 SvsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMtrnkslvDEQLYRLQFEKADLLKRIDEDQDDLNEL 1906
Cdd:pfam05557 81 K--KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA-------ELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1907 MQKHKDLIAQ---SAADIGQIQEL--QLQLEEAKKE--KHKLQEQLQVAQMRIEyLEQSTVDRAIVSRQEAVICDLENKT 1979
Cdd:pfam05557 152 EQLRQNLEKQqssLAEAEQRIKELefEIQSQEQDSEivKNSKSELARIPELEKE-LERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1980 EFQKVQIKRFEvlviRLRDSLIKMGEELSQAATSESQQRESSQYYQ---RRLEELKADMEELVQREAEASRRCMELEKYV 2056
Cdd:pfam05557 231 EDLKRKLEREE----KYREEAATLELEKEKLEQELQSWVKLAQDTGlnlRSPEDLSRRIEQLQQREIVLKEENSSLTSSA 306
|
330 340 350
....*....|....*....|....*....|
gi 51317366 2057 EELAAVRQTLQTDLETSIRRIADLQAALEE 2086
Cdd:pfam05557 307 RQLEKARRELEQELAQYLKKIEDLNKKLKR 336
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1623-2115 |
8.21e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1623 EKGLREKVTQENTSvRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLESSALEQQK 1702
Cdd:TIGR00618 228 LKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1703 IQSQQENTIKQleqlRQRFELEIERMK-QMHQKDREDQEE----------ELEDVRQSCQKRLHQLEmQLEQEYEEKQMV 1771
Cdd:TIGR00618 307 QQAQRIHTELQ----SKMRSRAKLLMKrAAHVKQQSSIEEqrrllqtlhsQEIHIRDAHEVATSIRE-ISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1772 LHEKQDLEGLIGTLcdQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGTME-DGKTSVSKEELEKVHSQLEQSEAKCEE- 1849
Cdd:TIGR00618 382 HTLQQQKTTLTQKL--QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKi 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1850 -------ALKTQKVLTADLESMHselENMTRNKSLVDEQLYRLQFEKADLLKRIDEdqddLNELMQKHKDLIAQSAADIG 1922
Cdd:TIGR00618 460 hlqesaqSLKEREQQLQTKEQIH---LQETRKKAVVLARLLELQEEPCPLCGSCIH----PNPARQDIDNPGPLTRRMQR 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1923 QIQELQLQLEEAKKEKHKLQEQLQVAQmriEYLEQSTvdRAIVSRQEAVICDLENKTEFQKVQIKRFEVL-VIRLRDSLI 2001
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRA---SLKEQMQ--EIQQSFSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2002 KMGEELSQAATSESQ-----------QRESSQYYQRRLEELKADMEELVQ-REAEASRRCMELEkyvEELAAVRQTLQTD 2069
Cdd:TIGR00618 608 DMLACEQHALLRKLQpeqdlqdvrlhLQQCSQELALKLTALHALQLTLTQeRVREHALSIRVLP---KELLASRQLALQK 684
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 51317366 2070 LETSIRRIADLqaaLEEVASSDSDTESVQTAVDCGSSGRKEMDNVS 2115
Cdd:TIGR00618 685 MQSEKEQLTYW---KEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1657-2087 |
1.06e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1657 QLKQQVEMLQDHKREllgspslGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIE-RMKQMHQKD 1735
Cdd:TIGR04523 51 NKEKELKNLDKNLNK-------DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKnDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1736 RE--DQEEELEDVRQSCQK---RLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRRTHAL 1810
Cdd:TIGR04523 124 VElnKLEKQKKENKKNIDKfltEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK-IKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1811 LSDVQLLlgtMEDGKTSVSK-EELEKVHSQLEQSEAKceealKTQKV--LTADLESMHSELENMTRNKSLVDEQLYRLQF 1887
Cdd:TIGR04523 203 LSNLKKK---IQKNKSLESQiSELKKQNNQLKDNIEK-----KQQEIneKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1888 EKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIgqIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ---------- 1957
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEqisqlkkelt 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1958 ------STVDRAIVSRQEAVIcDLENKTEFQKVQIKRFEVLVIRLRdSLIKMGEELSQAATSESQQRESS-QYYQRRLEE 2030
Cdd:TIGR04523 353 nsesenSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLESQINDLE-SKIQNQEKLNQQKDEQIKKLQQEkELLEKEIER 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 51317366 2031 LKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEV 2087
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1415-1888 |
1.20e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.54 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1415 RRKLEKSEKLRNELRQNTDLLESKIADLTSDLAderfkgdvacQVLESERAERLqafrEVQELKSKHEQVQKKLGDVNKQ 1494
Cdd:pfam06160 78 KYRFKKAKKALDEIEELLDDIEEDIKQILEELD----------ELLESEEKNRE----EVEELKDKYRELRKTLLANRFS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1495 LEEAQQKI--QLNDLE--------RNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLDselTARKELEQKLGELQSAY 1564
Cdd:pfam06160 144 YGPAIDELekQLAEIEeefsqfeeLTESGDYLEAREVLEKLEEETDALEELMEDIPPLYE---ELKTELPDQLEELKEGY 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1565 DgakkmahQLKRKCHHLT-CDLEDTCVLLENQQSRNHELEKKqkkfdLQLAQAlgesvfEKGLREkvtqentsvrwelgq 1643
Cdd:pfam06160 221 R-------EMEEEGYALEhLNVDKEIQQLEEQLEENLALLEN-----LELDEA------EEALEE--------------- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1644 lqqqlkqkeqEASQLKQQVEMLQdhkRELLGSPSLGENcVAGLKERLwklessaleqQKIQSQQENTIKQLEQLRQRFEL 1723
Cdd:pfam06160 268 ----------IEERIDQLYDLLE---KEVDAKKYVEKN-LPEIEDYL----------EHAEEQNKELKEELERVQQSYTL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1724 eiermkqmhqkdredQEEELEDVRQScQKRLHQLE---MQLEQEYEEKQMVLHEKQD-LEGLIGTLcDQI--GHRDFDVE 1797
Cdd:pfam06160 324 ---------------NENELERVRGL-EKQLEELEkryDEIVERLEEKEVAYSELQEeLEEILEQL-EEIeeEQEEFKES 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1798 -KRLRRDLRRTHALLSDVQLLLGTMedgKTSVSK------------------EELEKVHSQLEQS-------EAKCEEAl 1851
Cdd:pfam06160 387 lQSLRKDELEAREKLDEFKLELREI---KRLVEKsnlpglpesyldyffdvsDEIEDLADELNEVplnmdevNRLLDEA- 462
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 51317366 1852 ktqkvlTADLESMHSELENMTRNKSLVdEQL------YRLQFE 1888
Cdd:pfam06160 463 ------QDDVDTLYEKTEELIDNATLA-EQLiqyanrYRSSNP 498
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1329-1762 |
1.34e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1329 EKQREKLVSQSIVLFQAACKGFLSRQEFKKLKIRRLAAQCIQKNV-AVFLAVKDWPWWQLLGSLQPLLSATIGTEQLRAK 1407
Cdd:TIGR00618 415 RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIhLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1408 -EEELTTLRRKLEKSEKLRNELRQNTDL----------LESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQE 1476
Cdd:TIGR00618 495 rLLELQEEPCPLCGSCIHPNPARQDIDNpgpltrrmqrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1477 LKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQK 1556
Cdd:TIGR00618 575 LTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1557 LG------------ELQSAYDGAKKMAHQ-LKRKCHHLTCDLEDtcvlLENQQSRNHELEKKQKKFDL---QLAQALGES 1620
Cdd:TIGR00618 655 LTqervrehalsirVLPKELLASRQLALQkMQSEKEQLTYWKEM----LAQCQTLLRELETHIEEYDRefnEIENASSSL 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1621 VFEKGLREKVTQENTS-----VRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLES 1695
Cdd:TIGR00618 731 GSDLAAREDALNQSLKelmhqARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51317366 1696 SALEQQKIQS-QQENTIKQLEQLRQRFEleiERMKQMHQKDRedQEEELEDVRQ------SCQKRLHQLEMQLE 1762
Cdd:TIGR00618 811 EIPSDEDILNlQCETLVQEEEQFLSRLE---EKSATLGEITH--QLLKYEECSKqlaqltQEQAKIIQLSDKLN 879
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1880-2071 |
1.43e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1880 EQLYRLQfekaDLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQst 1959
Cdd:COG1579 7 RALLDLQ----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1960 vdraivsRQEAV-----ICDLENKTEFQKVQIKRFEvlvirlrDSLIKMGEELSQAATSESQQREssqyyqrRLEELKAD 2034
Cdd:COG1579 81 -------QLGNVrnnkeYEALQKEIESLKRRISDLE-------DEILELMERIEELEEELAELEA-------ELAELEAE 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 51317366 2035 MEELvqrEAEASRRCMELEKYVEELAAVRQTLQTDLE 2071
Cdd:COG1579 140 LEEK---KAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1692-1942 |
1.74e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 46.10 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1692 KLESSALEQQKiqsqQENTIKqlEQLRQRFELEIERMKQMHQKDredqeeeledvrqscQKRLHQLEMQLEQEYEEKQMV 1771
Cdd:pfam09728 71 KLEKLCRELQK----QNKKLK--EESKKLAKEEEEKRKELSEKF---------------QSTLKDIQDKMEEKSEKNNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1772 LHEKQDLEGLIGTLCDQIGHRDFDVEKRLR-RDLrrthallsDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEA 1850
Cdd:pfam09728 130 REENEELREKLKSLIEQYELRELHFEKLLKtKEL--------EVQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1851 LKTQKVLTADLeSMHS----ELENmTRNKSLVDEQLYRLQFEK-ADLLKRIDEDqddlNELMQKHKDLIAQSAADIGQ-I 1924
Cdd:pfam09728 202 SETEKELREQL-NLYVekfeEFQD-TLNKSNEVFTTFKKEMEKmSKKIKKLEKE----NLTWKRKWEKSNKALLEMAEeR 275
|
250
....*....|....*...
gi 51317366 1925 QELQLQLEEAKKEKHKLQ 1942
Cdd:pfam09728 276 QKLKEELEKLQKKLEKLE 293
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1708-2045 |
1.90e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1708 ENTIKQLEQLRQRFELEIERMKQMHQKDREdQEEELEDVRQSCQKRL----HQ-------LEMQLEQ------------- 1763
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLESEEKNRE-EVEQLKDLYRELRKSLlanrFSfgpaldeLEKQLENleeefsqfvelte 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1764 --EYEEKQMVLHEKQDLEGLIGTLCDQI--------------------GHRD----------FDVEKRLRR---DLRRTH 1808
Cdd:PRK04778 190 sgDYVEAREILDQLEEELAALEQIMEEIpellkelqtelpdqlqelkaGYRElveegyhldhLDIEKEIQDlkeQIDENL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1809 ALLSdvQLLLGTMEDGKTSVSkEELEKVHSQLEQS-EAKcEEALKTQKVLTADLEsmHSElenmTRNKSLVDE-----QL 1882
Cdd:PRK04778 270 ALLE--ELDLDEAEEKNEEIQ-ERIDQLYDILEREvKAR-KYVEKNSDTLPDFLE--HAK----EQNKELKEEidrvkQS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1883 YRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQ--VAQMRIEylEQSTV 1960
Cdd:PRK04778 340 YTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSemLQGLRKD--ELEAR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1961 DRAIVSRQEavicdLENktefqkvqIKRfevLVIRLR---------DSLIKMGEELSQAATSESQQRESSQYYQRRLEEL 2031
Cdd:PRK04778 418 EKLERYRNK-----LHE--------IKR---YLEKSNlpglpedylEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEA 481
|
410
....*....|....
gi 51317366 2032 KADMEELvQREAEA 2045
Cdd:PRK04778 482 TEDVETL-EEETEE 494
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1603-1975 |
1.91e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.87 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1603 EKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLgENC 1682
Cdd:COG5185 232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI-KKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1683 VAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMhqKDREDQEEELEDVRQScQKRLHQLEMQLE 1762
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAI--KEEIENIVGEVELSKS-SEELDSFKDTIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1763 ---QEYEEKQMVLhEKQDLEGLIgTLCDQIGHRDFDVEkRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQ 1839
Cdd:COG5185 388 stkESLDEIPQNQ-RGYAQEILA-TLEDTLKAADRQIE-ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSR 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1840 LEQSEAKCEEALKTQK-VLTADLESMHSELENMTRNkslVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1918
Cdd:COG5185 465 LEEAYDEINRSVRSKKeDLNEELTQIESRVSTLKAT---LEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 51317366 1919 ADIGQIQELQLQLEEakkekHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDL 1975
Cdd:COG5185 542 ENLIPASELIQASNA-----KTDGQAANLRTAVIDELTQYLSTIESQQAREDPIPDQ 593
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1801-2101 |
2.03e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1801 RRDLRRTHALLSDVQLLLGTME----------DGKTSVSKEELEKVHSQLEQSEAKCEealKTQKVLTADLESMHSELEn 1870
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMElehkrarielEKKASALKRQLDRESDRNQELQKRIR---LLEKREAEAEEALREQAE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1871 MTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDL-NELMQKHKdliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQ 1949
Cdd:pfam05557 77 LNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSELRR-----------QIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1950 MRIEYLEQstvdraivsrqeaVICDLENKTEFQKVQIKRFEVLVIRLR----DSLI--KMGEELSQAATSESQQR----- 2018
Cdd:pfam05557 146 AKASEAEQ-------------LRQNLEKQQSSLAEAEQRIKELEFEIQsqeqDSEIvkNSKSELARIPELEKELErlreh 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2019 ---------------ESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSiRRIADLQ-- 2081
Cdd:pfam05557 213 nkhlnenienklllkEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLS-RRIEQLQqr 291
|
330 340
....*....|....*....|..
gi 51317366 2082 --AALEEVASSDSDTESVQTAV 2101
Cdd:pfam05557 292 eiVLKEENSSLTSSARQLEKAR 313
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1657-2066 |
2.91e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 46.22 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1657 QLKQQVEMLQDHKRELLGspslgENcvAGLKERLWKLES------------SALEQQKIQSQQENTikQLEQLRQRFELE 1724
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQ-----EN--KKLQERLDQLESgddsgtpggkkyLLLQKQLEQLQEENF--RLETARDDYRIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1725 IERMK------QMHQKDREDQEEELE------DVRQSCQKRLHQLEMQLE------QEYEE--KQMVLHEKQDLEGLIGT 1784
Cdd:pfam05622 89 CEELEkevlelQHRNEELTSLAEEAQalkdemDILRESSDKVKKLEATVEtykkklEDLGDlrRQVKLLEERNAEYMQRT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1785 LcdqighrdfdvekRLRRDLRRTHALLSDVQLLlgtmedgktsvsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESM 1864
Cdd:pfam05622 169 L-------------QLEEELKKANALRGQLETY------------KRQVQELHGKLSEESKKADKLEFEYKKLEEKLEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1865 HSELENMTRN----KSLVDE----QLYRLQFEKAD-LLKRIDEDQDDLN-ELM------------QKHKDL-IAQSAADI 1921
Cdd:pfam05622 224 QKEKERLIIErdtlRETNEElrcaQLQQAELSQADaLLSPSSDPGDNLAaEIMpaeireklirlqHENKMLrLGQEGSYR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1922 GQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStVDRAIVSRQEAvicdlENKTEFQKVQIKRFEVLVIRLRdsli 2001
Cdd:pfam05622 304 ERLTELQQLLEDANRRKNELETQNRLANQRILELQQQ-VEELQKALQEQ-----GSKAEDSSLLKQKLEEHLEKLH---- 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51317366 2002 KMGEELS--QAATSESQQRESSQyYQRRLEELkadMEELVQREAEAsrRCME--LEKYVEELAAVRQTL 2066
Cdd:pfam05622 374 EAQSELQkkKEQIEELEPKQDSN-LAQKIDEL---QEALRKKDEDM--KAMEerYKKYVEKAKSVIKTL 436
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1408-1795 |
3.47e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1408 EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvleseraERLQAFREVQELKSKHEQVQKK 1487
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAS---------------DHLNLVQTALRQQEKIERYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1488 LGDVNKQLEEAQQKIQLndlernptggADEWQMRfdcaqmenefLRKRLQQCEERLDseltarkELEQKLGELQSAYDGA 1567
Cdd:PRK04863 357 LEELEERLEEQNEVVEE----------ADEQQEE----------NEARAEAAEEEVD-------ELKSQLADYQQALDVQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1568 KKMAHQ------LKRKCHHLtCDLEDtcVLLENQQSRNHELEKKQKKFD---LQLAQALGESVFEKGLREKVTQENTSVR 1638
Cdd:PRK04863 410 QTRAIQyqqavqALERAKQL-CGLPD--LTADNAEDWLEEFQAKEQEATeelLSLEQKLSVAQAAHSQFEQAYQLVRKIA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1639 WELgqlqqqlkqkeqEASQLKQQ-VEMLQDHKRELLGSPSLGencvaGLKERLWKLESSALEQQkiqsQQENTIKQLEQl 1717
Cdd:PRK04863 487 GEV------------SRSEAWDVaRELLRRLREQRHLAEQLQ-----QLRMRLSELEQRLRQQQ----RAERLLAEFCK- 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1718 RQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQ------EYEEKQMVLHEKQD-LEgligTLCDQIG 1790
Cdd:PRK04863 545 RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQlqariqRLAARAPAWLAAQDaLA----RLREQSG 620
|
....*
gi 51317366 1791 HRDFD 1795
Cdd:PRK04863 621 EEFED 625
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
221-513 |
4.40e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 45.76 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 221 LGDPGQGTVAlkkgeEGQSivgKGLGTPKTTEL-KEAEPQGKDRQGTrpQAQGPGEGVRPGKAEKEGAEPTNtvEKGNVS 299
Cdd:TIGR00927 627 LGDLSKGDVA-----EAEH---TGERTGEEGERpTEAEGENGEESGG--EAEQEGETETKGENESEGEIPAE--RKGEQE 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 300 KDVGSEGKhvRPQIPGRKWGGFLGRRSKWDGPQNKKDKEGVLLSKAEKTG-EPQTQMEKTSQVQGElGDDLRMGEKAGEL 378
Cdd:TIGR00927 695 GEGEIEAK--EADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEdEGEGEAEGKHEVETE-GDRKETEHEGETE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 379 RSTTGKAGESWDKKEKMGQPQGKSG--NAGEARSQTEKGCEAPKEVSTMVESPAAPGKGGwPGSRGQEAEEPCSRAGDGA 456
Cdd:TIGR00927 772 AEGKEDEDEGEIQAGEDGEMKGDEGaeGKVEHEGETEAGEKDEHEGQSETQADDTEVKDE-TGEQELNAENQGEAKQDEK 850
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 51317366 457 GAlETELEGPSQPALEKDAERPRIRKENQDGPAPQEEGKGGQSRDSDQAPEDRWYEA 513
Cdd:TIGR00927 851 GV-DGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQKQA 906
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1461-1779 |
5.05e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1461 ESERAERLQAFREVQELKSKHEQvQKKLGDVNKQLEEAQQKIQLNDLERNPTG--GADEWQMRFDCAQMENEFLRKRLQQ 1538
Cdd:pfam02029 3 DEEEAARERRRRAREERRRQKEE-EEPSGQVTESVEPNEHNSYEEDSELKPSGqgGLDEEEAFLDRTAKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1539 CEER---LDSELTARKE---LEQKLGELQSAYDGAKkmahQLKRKCHHLTCDLEDTcvllenqqsrnHELEKKQKKFDLQ 1612
Cdd:pfam02029 82 ALERqkeFDPTIADEKEsvaERKENNEEEENSSWEK----EEKRDSRLGRYKEEET-----------EIREKEYQENKWS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1613 LAQALGESVFEKglREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELL-GSPSLGENCVAGLK---E 1688
Cdd:pfam02029 147 TEVRQAEEEGEE--EEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPeVKSQNGEEEVTKLKvttK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1689 RLWKLESSALEQQKIQSQQENTIKQLEQLRQRF-ELEIERMKQMHQKDRE-DQE-EELEDVRQSCQKRLHQLEMQLEQEY 1765
Cdd:pfam02029 225 RRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRqEKESEEFEKLRQKQQEaELElEELKKKREERRKLLEEEEQRRKQEE 304
|
330
....*....|....*....
gi 51317366 1766 EEKQMVLHE-----KQDLE 1779
Cdd:pfam02029 305 AERKLREEEekrrmKEEIE 323
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1680-2089 |
5.06e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1680 ENCVAGLKERLWKLE---SSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQ 1756
Cdd:TIGR00606 244 ENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1757 LEMQLEQEYEEKQMVLHEKQDLEGLIGTLC-------DQIGHRDFD-----------------------------VEKRL 1800
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKTELLVEQGRLQlqadrhqEHIRARDSLiqslatrleldgfergpfserqiknfhtlVIERQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1801 RRDLRRTHALLSDVQ------------------LLLGTMEDGKTSVSKE--ELEKVHSQLEQSEAKCEEALKTQKVLTAD 1860
Cdd:TIGR00606 404 EDEAKTAAQLCADLQskerlkqeqadeirdekkGLGRTIELKKEILEKKqeELKFVIKELQQLEGSSDRILELDQELRKA 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1861 LESMhSELENMTRNKSLVDEQLYrLQFEKADLLK---RIDEDQDDLN------------------------ELMQKHKDL 1913
Cdd:TIGR00606 484 EREL-SKAEKNSLTETLKKEVKS-LQNEKADLDRklrKLDQEMEQLNhhtttrtqmemltkdkmdkdeqirKIKSRHSDE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1914 IAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTeFQKVQIKRFEVL 1992
Cdd:TIGR00606 562 LTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHiNNELESKEEQLSSYEDKL-FDVCGSQDEESD 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1993 VIRLRDSLIKMGEELSQAATsesqqreSSQYYQRRLEELkadmeelvqreAEASRRCMELEKYVEELAAVRQTLQTDLET 2072
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAG-------ATAVYSQFITQL-----------TDENQSCCPVCQRVFQTEAELQEFISDLQS 702
|
490
....*....|....*..
gi 51317366 2073 SIRRIADLQAALEEVAS 2089
Cdd:TIGR00606 703 KLRLAPDKLKSTESELK 719
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1401-1569 |
6.12e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1401 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAERLQAFREVQELKSK 1480
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE-------AQELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1481 HEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGgadewQMRFDCAQMENEFLRKRLQQCEERldsELTAR-KELEQKLGE 1559
Cdd:COG1340 80 RDELNEKLNELREELDELRKELAELNKAGGSID-----KLRKEIERLEWRQQTEVLSPEEEK---ELVEKiKELEKELEK 151
|
170
....*....|
gi 51317366 1560 LQSAYDGAKK 1569
Cdd:COG1340 152 AKKALEKNEK 161
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1692-1946 |
6.39e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1692 KLESSALEQQKIQSQQENTIKQLEQLRQRFELEIermkqmhqKDREDQEEELEDVRQSCQK----RLhQLEMQLE--QEY 1765
Cdd:pfam00038 62 QLDTLTVERARLQLELDNLRLAAEDFRQKYEDEL--------NLRTSAENDLVGLRKDLDEatlaRV-DLEAKIEslKEE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1766 EEKQMVLHEKQdleglIGTLCDQIGHRDFDVEKRLRRDLRRTHALlSDVQlllgTMEDGKTSVSKEELEkvhsqlEQSEA 1845
Cdd:pfam00038 133 LAFLKKNHEEE-----VRELQAQVSDTQVNVEMDAARKLDLTSAL-AEIR----AQYEEIAAKNREEAE------EWYQS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1846 KCEEALKTQKVLTADLESMHSELENMTRnkslvdeQLYRLQFEKADLLKRIDEDQDDLNELMQKHkdliaqsAADIGQIQ 1925
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEEITELRR-------TIQSLEIELQSLKKQKASLERQLAETEERY-------ELQLADYQ 262
|
250 260
....*....|....*....|..
gi 51317366 1926 ELQLQLEEAKKE-KHKLQEQLQ 1946
Cdd:pfam00038 263 ELISELEAELQEtRQEMARQLR 284
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1874-2096 |
6.46e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1874 NKSLVDEQlyrlqfekADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQ-IQELQLQLEEAKKEKHKLQEQLQVAQMRI 1952
Cdd:PHA02562 172 NKDKIREL--------NQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1953 EYLEQSTVDRAivsrqeAVICDLENKTEFQKVQIKRFevlvirlrDSLIKMGEE----------LSQAATSESQQRESSQ 2022
Cdd:PHA02562 244 LNLVMDIEDPS------AALNKLNTAAAKIKSKIEQF--------QKVIKMYEKggvcptctqqISEGPDRITKIKDKLK 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51317366 2023 YYQRRLEELKADMEELVQREAEASrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTES 2096
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFN----EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1880-2086 |
7.62e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1880 EQLYRL---QFEKA-DLLKRIdedQ-----DDLNELMQKH-------KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQE 1943
Cdd:COG4913 180 ARLRRRlgiGSEKAlRLLHKT---QsfkpiGDLDDFVREYmleepdtFEAADALVEHFDDLERAHEALEDAREQIELLEP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1944 QLQVAQMRIEYLEQSTVDRAIVSRQEAvicdlenktEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRES--- 2020
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRL---------WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREElde 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51317366 2021 --SQYYQ---RRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2086
Cdd:COG4913 328 leAQIRGnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1402-1782 |
7.85e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdlleskiadltsdladerfkgdvacqvlESERA-ERLQAFREVQELKSK 1480
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQ------------------------------DYQAAsDHLNLVQTALRQQEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1481 HEQVQKKLGDVNKQLEEAQQKIQLNDlernptGGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGEL 1560
Cdd:PRK04863 350 IERYQADLEELEERLEEQNEVVEEAD------EQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1561 QSA----------YDGAKKMAHQLKRKCHHLTCDLEDtcvlLEnQQSRNHELEKKQKKFDLQLAQALGESV--------F 1622
Cdd:PRK04863 424 ERAkqlcglpdltADNAEDWLEEFQAKEQEATEELLS----LE-QKLSVAQAAHSQFEQAYQLVRKIAGEVsrseawdvA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1623 EKGLREKVTQENTSVRweLGQLQQQLKQKEQEASQLKQQVEMLQDHKREL---LGSPSLGENCVAGLKERLWKLESSALE 1699
Cdd:PRK04863 499 RELLRRLREQRHLAEQ--LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgknLDDEDELEQLQEELEARLESLSESVSE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1700 QQKIQSQQENTIKQLEQLRQRFEleiERMKQMHQKD------REDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQmVLH 1773
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLA---ARAPAWLAAQdalarlREQSGEEFEDSQDVTEYMQQLLERERELTVERDE-LAA 652
|
....*....
gi 51317366 1774 EKQDLEGLI 1782
Cdd:PRK04863 653 RKQALDEEI 661
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1829-1938 |
8.64e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 44.67 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1829 SKEELEKVHSQ---LEQSEAKCEEALKTQKVLTADLE----SMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQD 1901
Cdd:pfam05911 686 LKEEFEQLKSEkenLEVELASCTENLESTKSQLQESEqliaELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEA 765
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 51317366 1902 DLNELMQK--------------HKDLIAQSaadigqiQELQLQLEEAKKEK 1938
Cdd:pfam05911 766 ELNELRQKfealeveleeekncHEELEAKC-------LELQEQLERNEKKE 809
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1704-1919 |
1.15e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1704 QSQQENTIKQLEQLRQRFELEIERMKQMhQKDREDQEEELEDVRQSCQKRLHQLEmQLEQEYEEKQMVLhekQDLEGLIG 1783
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAEL---AELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1784 TLCDQIGHRDFDVEKRLRRDLRrtHALLSDVQLLLGTmEDGKTSVSK---------------EELEKVHSQLEQSEAKCE 1848
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYR--LGRQPPLALLLSP-EDFLDAVRRlqylkylaparreqaEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51317366 1849 EALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAA 1919
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1838-2108 |
1.20e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1838 SQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS 1917
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1918 AADIGQIQELQLQLEeakkekhklQEQLQVAQMRIEYLEQ-STVDRAIVSRQEAVICDLENKTEFQKVQIKrfevlviRL 1996
Cdd:COG3883 96 YRSGGSVSYLDVLLG---------SESFSDFLDRLSALSKiADADADLLEELKADKAELEAKKAELEAKLA-------EL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1997 RDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRR 2076
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270
....*....|....*....|....*....|..
gi 51317366 2077 IADLQAALEEVASSDSDTESVQTAVDCGSSGR 2108
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1701-2098 |
1.22e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1701 QKIQSQQENTIKQlEQLRQRFELEIERmKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEG 1780
Cdd:PTZ00440 546 KYYLQSIETLIKD-EKLKRSMKNDIKN-KIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQE 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1781 LIGTLCDQIGHRDFDvekrlrrdlrrthALLSDvqlLLGTMEDGKTSV----SKEELEKVHSQLEQSEAKCEEalKTQKV 1856
Cdd:PTZ00440 624 KVKYILNKFYKGDLQ-------------ELLDE---LSHFLDDHKYLYheakSKEDLQTLLNTSKNEYEKLEF--MKSDN 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1857 LTADLESMHSELENM-TRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKdliaqsaADIGQIQELQLQLEEAK 1935
Cdd:PTZ00440 686 IDNIIKNLKKELQNLlSLKENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYK-------EEEEKLEVYKHQIINRK 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1936 KE--------KHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQeAVICDlENKTEFQKvQIKRFEVLVIRLRDSLIKMGEEL 2007
Cdd:PTZ00440 759 NEfilhlyenDKDLPDGKNTYEEFLQYKDTILNKENKISND-INILK-ENKKNNQD-LLNSYNILIQKLEAHTEKNDEEL 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2008 SQaatsesqqreSSQYYQRRLEELKADmeelvqreaeasrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEV 2087
Cdd:PTZ00440 836 KQ----------LLQKFPTEDENLNLK----------------ELEKEFNENNQIVDNIIKDIENMNKNINIIKTLNIAI 889
|
410
....*....|.
gi 51317366 2088 ASSDSDTESVQ 2098
Cdd:PTZ00440 890 NRSNSNKQLVE 900
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1885-2102 |
1.41e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1885 LQFEKADLLKRIDEDQDDLnelmqkHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQvaqmRIEYLEQStvdrai 1964
Cdd:COG4717 40 LAFIRAMLLERLEKEADEL------FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEE------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1965 VSRQEAVICDLENKTEFQKVQIKRFEVLvirlrdslikmgEELSQAatsesqqRESSQYYQRRLEELKADMEELVQREAE 2044
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLY------------QELEAL-------EAELAELPERLEELEERLEELRELEEE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 51317366 2045 ASRRCMELEKYVEELAAVRQTLQTDLETSIRRIA-DLQAALEEVASSDSDTESVQTAVD 2102
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELE 223
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1707-2086 |
1.42e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1707 QENTIKQLEQLRQRFElEIERMkqmhqkdreDQEEELEDVRQscqkrLHqLEMQLEQEYEEKqmvlheKQDLEGLIGTLC 1786
Cdd:PRK04778 24 RKRNYKRIDELEERKQ-ELENL---------PVNDELEKVKK-----LN-LTGQSEEKFEEW------RQKWDEIVTNSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1787 DQIGHRDFDVEKRLRR-DLRRTHALLSDVQLLLGTMEDGKTSVSKE-----ELEKVHSQL-EQSEAKCEEALKT------ 1853
Cdd:PRK04778 82 PDIEEQLFEAEELNDKfRFRKAKHEINEIESLLDLIEEDIEQILEElqellESEEKNREEvEQLKDLYRELRKSllanrf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1854 -----QKVLTADLESMHSELENMTRNKSLVDEQlyrlqfEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI-GQIQEL 1927
Cdd:PRK04778 162 sfgpaLDELEKQLENLEEEFSQFVELTESGDYV------EAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1928 QL---QLEEAK---------KEKHKLQEQLQVAQMRIEYLEqstVDRAivsrqEAVICDLENKTE-----FQK-VQIKRF 1989
Cdd:PRK04778 236 KAgyrELVEEGyhldhldieKEIQDLKEQIDENLALLEELD---LDEA-----EEKNEEIQERIDqlydiLEReVKARKY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1990 -EVLVIRLRDSLIKMGEELSQ--AATSESQQR--------ESSQYYQRRLEELKADMEELVQREAEASRRCMELEkyvEE 2058
Cdd:PRK04778 308 vEKNSDTLPDFLEHAKEQNKElkEEIDRVKQSytlneselESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQ---EE 384
|
410 420
....*....|....*....|....*...
gi 51317366 2059 LAAVRQTLqTDLETSIRRIADLQAALEE 2086
Cdd:PRK04778 385 LEEILKQL-EEIEKEQEKLSEMLQGLRK 411
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1831-2082 |
1.53e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1831 EELEKVHSQLEQSEAKCEEAlktqkvltadlesmHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQ---------- 1900
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEA--------------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQtraiqyqqav 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1901 ---DDLNELMQKhKDLIAQSAADIgqIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ--STVDRAI--VSRQEA--V 1971
Cdd:PRK04863 421 qalERAKQLCGL-PDLTADNAEDW--LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayQLVRKIAgeVSRSEAwdV 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1972 ICDLENKTEFQKVQIKRFEVLVIRLRDslikMGEELSQAATSESQQRESSQYYQRRLEElkADMEELVQREAEASRRcmE 2051
Cdd:PRK04863 498 ARELLRRLREQRHLAEQLQQLRMRLSE----LEQRLRQQQRAERLLAEFCKRLGKNLDD--EDELEQLQEELEARLE--S 569
|
250 260 270
....*....|....*....|....*....|.
gi 51317366 2052 LEKYVEELAAVRQTLQTDLETSIRRIADLQA 2082
Cdd:PRK04863 570 LSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1603-1953 |
1.56e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 43.51 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1603 EKKQKKFDLQLAQALGESVfEKGLR---EKVT----------QENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1669
Cdd:pfam15742 14 EVQQLRQNLQRLQILCTSA-EKELRyerGKNLdlkqhnsllqEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1670 REllgspslgencvaglkerlwkLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQS 1749
Cdd:pfam15742 93 RE---------------------LELEVLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKVCLTDTCIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1750 CQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghrdfdveKRLRRDLRRTHALLsdvqlllgTMEDGKTSVS 1829
Cdd:pfam15742 152 EKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNEL--------QQQVRSLQDKEAQL--------EMTNSQQQLR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1830 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELEnmtrnkslvdeqlyRLQFEKADLLKRIDEDQDDLNELMQK 1909
Cdd:pfam15742 216 IQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEKE--------------ALQEELQQVLKQLDVHVRKYNEKHHH 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 51317366 1910 HKdliaqsaADIGQIQELQLQLEEAKKEKHK-LQEQLQVAQMRIE 1953
Cdd:pfam15742 282 HK-------AKLRRAKDRLVHEVEQRDERIKqLENEIGILQQQSE 319
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
324-506 |
1.57e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.42 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 324 RRSKWDGPQNKKDKEGVLLSKAEKTGEPQTQMEKTSQVQGELGDDLRMGEKAGElrsttGKAGESWDKKEKMGQPQGKSG 403
Cdd:PHA03169 34 GRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEER-----GQGGPSGSGSESVGSPTPSPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 404 NAGEAR----SQTEKGCEAPKEVSTMVESPAAPGKGGwPGSRGQEAEEPCSRAGDGAGALETELEGPSQPALEKDAERPR 479
Cdd:PHA03169 109 GSAEELasglSPENTSGSSPESPASHSPPPSPPSHPG-PHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEP 187
|
170 180
....*....|....*....|....*..
gi 51317366 480 IRKENQDGPAPQEEGKGGQSRDSDQAP 506
Cdd:PHA03169 188 DSPGPPQSETPTSSPPPQSPPDEPGEP 214
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1402-1576 |
1.68e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkGDVACQVLESERAER-------------L 1468
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK--EELAELLRALYRLGRqpplalllspedfL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1469 QAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggadewqmrfdcaqmENEFLRKRLQQCEERLDSELT 1548
Cdd:COG4942 133 DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA-----------------ELEALLAELEEERAALEALKA 195
|
170 180 190
....*....|....*....|....*....|..
gi 51317366 1549 ARK----ELEQKLGELQSAYDGAKKMAHQLKR 1576
Cdd:COG4942 196 ERQkllaRLEKELAELAAELAELQQEAEELEA 227
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1888-2080 |
1.77e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1888 EKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQlqvaqmrieyleqstvdRAIVSR 1967
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNL-----------------KARLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1968 QEAVICDLEnktEFQKVQIKRFEVLViRLRDSLIKMGEElsqaATSESQQRES--SQYYQRRLEELKADMEelvQREAea 2045
Cdd:pfam13851 97 LEKELKDLK---WEHEVLEQRFEKVE-RERDELYDKFEA----AIQDVQQKTGlkNLLLEKKLQALGETLE---KKEA-- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 51317366 2046 srrcmELEKYV-------EELAAVRQTLQTDLETSIRRIADL 2080
Cdd:pfam13851 164 -----QLNEVLaaanldpDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1657-2102 |
1.87e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1657 QLKQQVEMLQDHKR-----------ELLGSPSLGENCVaglkerlWKLESSALEQQKIQSQQENTIKQLEQLR---QRFE 1722
Cdd:pfam10174 71 HLQLTIQALQDELRaqrdlnqllqqDFTTSPVDGEDKF-------STPELTEENFRRLQSEHERQAKELFLLRktlEEME 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1723 LEIERMKQ--------------MHQKD---REDQEEELEDVRQ--SCQKRLHQLEMQLEQEYEEKQMV---LHEK---QD 1777
Cdd:pfam10174 144 LRIETQKQtlgardesikklleMLQSKglpKKSGEEDWERTRRiaEAEMQLGHLEVLLDQKEKENIHLreeLHRRnqlQP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1778 LEGLIGTLCDQIGHRDFDVEKrLRRDLRRthaLLSDVQLL----LGTMEDGKTSVSKEELEKVHS--------QLEQSEA 1845
Cdd:pfam10174 224 DPAKTKALQTVIEMKDTKISS-LERNIRD---LEDEVQMLktngLLHTEDREEEIKQMEVYKSHSkfmknkidQLKQELS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1846 KCEEALKTqkvLTADLESMHSELENMTRNKSLVDEQLYR-------LQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1918
Cdd:pfam10174 300 KKESELLA---LQTKLETLTNQNSDCKQHIEVLKESLTAkeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1919 ADIGQIQELQ--LQLEEAK-----KEKHKLQEQL-----QVAQM--RIEYLEQ--STVDRAIVSRQEAvICDLENKTEFQ 1982
Cdd:pfam10174 377 TLAGEIRDLKdmLDVKERKinvlqKKIENLQEQLrdkdkQLAGLkeRVKSLQTdsSNTDTALTTLEEA-LSEKERIIERL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1983 KVQIKRFEVLVIRLRDSLIKMGEELSQAATS---ESQQRESSqyyqrrLEELKADMEELVQREAEASRRC----MELEKY 2055
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEKVSAlqpELTEKESS------LIDLKEHASSLASSGLKKDSKLksleIAVEQK 529
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 51317366 2056 VEELAAVRQTLQT-----DLETSIRRIADLQAALE-EVASSDSDTESVQTAVD 2102
Cdd:pfam10174 530 KEECSKLENQLKKahnaeEAVRTNPEINDRIRLLEqEVARYKEESGKAQAEVE 582
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1402-1665 |
1.91e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1481
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1482 EQVQKKLGDVNKQLEEAQQKI-----QLNDLERNPTggadewQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQK 1556
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIaereeELKELEEQLE------SLQEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1557 LGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTS 1636
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260
....*....|....*....|....*....
gi 51317366 1637 VRWELGQLQQQLKQKEQEASQLKQQVEML 1665
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1844-2101 |
1.92e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1844 EAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRlqfEKADLLKRIDEDQDDLNELMQKHKDLIAQSaadigq 1923
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWER---QRRELESRVAELKEELRQSREKHEELEEKY------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1924 iQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdraivsrqeavicdlENKTEFQKVQIKrfEVLVIRLRDSLIKM 2003
Cdd:pfam07888 104 -KELSASSEELSEEKDALLAQRAAHEARIRELEE------------------DIKTLTQRVLER--ETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2004 GEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVeelaavrQTLQTDLETSIRRIADLQAA 2083
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTI-------TTLTQKLTTAHRKEAENEAL 235
|
250
....*....|....*...
gi 51317366 2084 LEEVASSDSDTESVQTAV 2101
Cdd:pfam07888 236 LEELRSLQERLNASERKV 253
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1378-1581 |
1.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1378 AVKDWPWWQLLGSLQplLSATIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQNtDLLESKIADLTSDLADErfkgdvac 1457
Cdd:COG4717 315 ELEEEELEELLAALG--LPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED-------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1458 qvlESERAERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLErnptggadewqmrfdcAQMENefLRKRLQ 1537
Cdd:COG4717 384 ---EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE----------------EELEE--LEEELE 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 51317366 1538 QCEERLDSELTARKELEQKLGELQS--AYDGAKKMAHQLKRKCHHL 1581
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELREL 488
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1403-1543 |
2.03e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1403 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDL--------LESKIADLTSDLADerfkgdvacqvLESERAERLQAFREV 1474
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEasferlaeLRDELAELEEELEA-----------LKARWEAEKELIEEI 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1475 QELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADE-------W------QMrfdcaqMENEflRKRLQQCEE 1541
Cdd:COG0542 474 QELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDiaevvsrWtgipvgKL------LEGE--REKLLNLEE 545
|
..
gi 51317366 1542 RL 1543
Cdd:COG0542 546 EL 547
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1923-2087 |
2.08e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1923 QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdrAIVSRQEAVicdlenktEFQKVQIKRFEVLVIRLRDSLIK 2002
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEA-----RLEAAKTEL--------EDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2003 MGEELSQAATsesqQRESsQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRR----IA 2078
Cdd:COG1579 78 YEEQLGNVRN----NKEY-EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEldeeLA 152
|
....*....
gi 51317366 2079 DLQAALEEV 2087
Cdd:COG1579 153 ELEAELEEL 161
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1402-2054 |
2.08e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.59 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRrKLEKSEKLRNElRQNTDLLESKIADLTSDLADERFKGDVA-CQVLESERAERLQafREVQELKSK 1480
Cdd:pfam07111 73 QELRRLEEEVRLLR-ETSLQQKMRLE-AQAMELDALAVAEKAGQAEAEGLRAALAgAEMVRKNLEEGSQ--RELEEIQRL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1481 HeqvQKKLGDVNKQLEEAQQKI---------QLNDLERNPTGGADEWQMrfdcAQMENEFLRKRLQQCEERLDSELTARK 1551
Cdd:pfam07111 149 H---QEQLSSLTQAHEEALSSLtskaeglekSLNSLETKRAGEAKQLAE----AQKEAELLRKQLSKTQEELEAQVTLVE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1552 ELEQKLGElqSAYDGAKKMAHQLKRK-----CHHLT---CDLEDTCVLLENQ-QSRNHELEKKQKKF--DLQLAQALgES 1620
Cdd:pfam07111 222 SLRKYVGE--QVPPEVHSQTWELERQelldtMQHLQedrADLQATVELLQVRvQSLTHMLALQEEELtrKIQPSDSL-EP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1621 VFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQdhkrellgspslgencvaglkerlwklessalEQ 1700
Cdd:pfam07111 299 EFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQ--------------------------------EQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1701 QKIQSQQENTIKQLEQLRQRfELEIERMKQMHQKDREDQEEEledVRQSCQKRLHQLEMQLeqeyeeKQMVLHEKQDLEG 1780
Cdd:pfam07111 347 VTSQSQEQAILQRALQDKAA-EVEVERMSAKGLQMELSRAQE---ARRRQQQQTASAEEQL------KFVVNAMSSTQIW 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1781 LIGTLC--DQIGHRDFDVEKRLRRDLRRTHALLsdvqlllGTMEDgKTSVSKEELEkvhsqleqSEAKCEEALKTQKVLT 1858
Cdd:pfam07111 417 LETTMTrvEQAVARIPSLSNRLSYAVRKVHTIK-------GLMAR-KVALAQLRQE--------SCPPPPPAPPVDADLS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1859 ADLESMHSElenmtRNKSLVDEQL--YRLQFEKADLLKRIDEDQDDLNELMQkhkdliaqsaadigqiqELQLQLEEAKK 1936
Cdd:pfam07111 481 LELEQLREE-----RNRLDAELQLsaHLIQQEVGRAREQGEAERQQLSEVAQ-----------------QLEQELQRAQE 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1937 EKHKLQEQLQVAQMRieylEQSTVDRAIVSRQEavicdLENKTEF--QKVQIKRFEVLViRLRDSLIKMGEELSQAATSE 2014
Cdd:pfam07111 539 SLASVGQQLEVARQG----QQESTEEAASLRQE-----LTQQQEIygQALQEKVAEVET-RLREQLSDTKRRLNEARREQ 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 51317366 2015 SQQRESSQYYQRRLEELKADMEELVQREAEA--------SRRCMELEK 2054
Cdd:pfam07111 609 AKAVVSLRQIQHRATQEKERNQELRRLQDEArkeegqrlARRVQELER 656
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1378-1836 |
2.09e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1378 AVKDWPWWQLLGSLQpllsatigtEQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTSDLADERfkgdvac 1457
Cdd:COG4717 124 LLQLLPLYQELEALE---------AELAELPERLEELEERLEELRELEEELEE----LEAELAELQEELEELL------- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1458 qvleseRAERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQlnDLERnptggadewqmrfDCAQMENEFLRKRLQ 1537
Cdd:COG4717 184 ------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE--ELEE-------------ELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1538 QCEERLDSELTARKELEQKLGELQSAYDGAKKMAhqlkrkchhltcdlEDTCVLLENQQSRNHELEKKQKKFDLQLAQAL 1617
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSLLSLILTIA--------------GVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1618 GESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSpSLGENCVAGLKERLWKLESSA 1697
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1698 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQ-MHQKDREDQEEELEDVRQscqkRLHQLEMQLEQEYEEKQMVLHEKQ 1776
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEElLEALDEEELEEELEELEE----ELEELEEELEELREELAELEAELE 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1777 DLEGliGTLCDQIGHRDFDVEKRLRRDLRRTHALlsdvQLLLGTMEDGKTSVSKEELEKV 1836
Cdd:COG4717 464 QLEE--DGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYREERLPPV 517
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1550-2126 |
2.09e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1550 RKELEQKLGELQSAYDGAKKmahqLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKkfdlQLAQAlgESVFEKGLREK 1629
Cdd:PRK01156 151 RKKILDEILEINSLERNYDK----LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKK----QIADD--EKSHSITLKEI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1630 vtqENTSVrwELGQLQQQLKQKEQEASQLKQQVEMLQDHKREL------LGSPSLGENCVAGLKERLWKLESSALeqqki 1703
Cdd:PRK01156 221 ---ERLSI--EYNNAMDDYNNLKSALNELSSLEDMKNRYESEIktaesdLSMELEKNNYYKELEERHMKIINDPV----- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1704 qsqqentIKQLEQLRQRFELeiermkqmhQKDREDQEEELEDVRQSCQK--RLHQLEMQLEQEYEEKQMVLHEKQDLegl 1781
Cdd:PRK01156 291 -------YKNRNYINDYFKY---------KNDIENKKQILSNIDAEINKyhAIIKKLSVLQKDYNDYIKKKSRYDDL--- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1782 igtlcdqighrdfdveKRLRRDLRRTHallSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEakceealkTQKVLTADL 1861
Cdd:PRK01156 352 ----------------NNQILELEGYE---MDYNSYLKSIESLKKKIEEYSKNIERMSAFISE--------ILKIQEIDP 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1862 ESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNEL--------------MQKHKDLIAQSAADIGQIQEl 1927
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEE- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1928 qlQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSrqeavicdlENKTEFQKVQIKRFEVLVIRLRDSLIKmgeel 2007
Cdd:PRK01156 484 --KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINE---------YNKIESARADLEDIKIKINELKDKHDK----- 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 2008 SQAATSESQQRESSQYYQRRLEELKA-------DMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD- 2079
Cdd:PRK01156 548 YEEIKNRYKSLKLEDLDSKRTSWLNAlavisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENe 627
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 51317366 2080 ---LQAALEEVASSDSDTESVQTAVDCGSSGRKEMDnvSILSSQPEGSLQ 2126
Cdd:PRK01156 628 annLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID--SIIPDLKEITSR 675
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1401-1730 |
2.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1401 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLEskiadltsdladerfkgdvacqvlesERAERLQAFREVQELKSK 1480
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ--------------------------ERREALQRLAEYSWDEID 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1481 HEQVQKKLGDVNKQLEEAQQkiqlndlernptgGADEWQMrfdcaqmenefLRKRLQQCEERLDseltarkELEQKLGEL 1560
Cdd:COG4913 663 VASAEREIAELEAELERLDA-------------SSDDLAA-----------LEEQLEELEAELE-------ELEEELDEL 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1561 QSAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEkkqkkFDLQLAQALGESVfEKGLREKVTQENTSVRwe 1640
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEA----AEDLARLELRAL-----LEERFAAALGDAV-ERELRENLEERIDALR-- 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1641 lgqlqqqlkqkeQEASQLKQQVE-MLQDHKRE-----LLGSPSLGENcvAGLKERLWKLESSAL---EQQKIQSQQENTI 1711
Cdd:COG4913 780 ------------ARLNRAEEELErAMRAFNREwpaetADLDADLESL--PEYLALLDRLEEDGLpeyEERFKELLNENSI 845
|
330
....*....|....*....
gi 51317366 1712 KQLEQLRQRFELEIERMKQ 1730
Cdd:COG4913 846 EFVADLLSKLRRAIREIKE 864
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1415-1790 |
2.37e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1415 RRKLEKSEKLRNELRQNTDLLESKIADLTsDLADERFKGDVACQVLESE---RAERLQAFREVQELKSKHEQVQKKLGDV 1491
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLV-EMARELEELSARESDLEQDyqaASDHLNLVQTALRQQEKIERYQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1492 NKQLEEAQQKIQlndlernptgGADEWQMRfdcaqmenefLRKRLQQCEERLDSELTARKELEQKLGELQSAyDGAKKMA 1571
Cdd:COG3096 360 TERLEEQEEVVE----------EAAEQLAE----------AEARLEAAEEEVDSLKSQLADYQQALDVQQTR-AIQYQQA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1572 HQLKRKCHHLtCDLEDtcVLLENQQSRNHELEKKQKKFD---LQLAQALGESVFEKGLREKVtqentsvrWELGQLQQQL 1648
Cdd:COG3096 419 VQALEKARAL-CGLPD--LTPENAEDYLAAFRAKEQQATeevLELEQKLSVADAARRQFEKA--------YELVCKIAGE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1649 KQKEQEASQLKQQVEMLQDHKrellgspSLGENcVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFElEIERM 1728
Cdd:COG3096 488 VERSQAWQTARELLRRYRSQQ-------ALAQR-LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-ELEEL 558
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51317366 1729 KQMHQKDREDQEEELEDvrqsCQKRLHQLEMQLEQ------EYEEKQMVLHEKQD-LEgligTLCDQIG 1790
Cdd:COG3096 559 LAELEAQLEELEEQAAE----AVEQRSELRQQLEQlrarikELAARAPAWLAAQDaLE----RLREQSG 619
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1680-1775 |
2.60e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.56 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1680 ENCVAGLKERLWKLESSALEQQKIQSQQentikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKrlhQLEM 1759
Cdd:cd16269 199 EIEAERAKAEAAEQERKLLEEQQRELEQ-----KLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLK---EQEA 270
|
90
....*....|....*.
gi 51317366 1760 QLEQEYEEKQMVLHEK 1775
Cdd:cd16269 271 LLEEGFKEQAELLQEE 286
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1830-1972 |
2.95e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1830 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELE-NMTRNKSLVDEQLYRLQFEKADLLKR----IDEDQDDLN 1904
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEeKKEKLQEEEDKLLEEAEKEAQQAIKEakkeADEIIKELR 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51317366 1905 ELMQ-KHKDLIAQSAADI-GQIQELQLQLEEAKKEKHKLQEQLQVAQ-MRIEYLEQSTVDRAIVSRQEAVI 1972
Cdd:PRK00409 595 QLQKgGYASVKAHELIEArKRLNKANEKKEKKKKKQKEKQEELKVGDeVKYLSLGQKGEVLSIPDDKEAIV 665
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1692-1934 |
3.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1692 KLESSALEQQKIQSQQENTIKQLEQLRQrfelEIERMkqmhQKDREDQEEELEDVRQscqkrlhQLEmQLEQEYEEKQMV 1771
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA----ELEEL----NEEYNELQAELEALQA-------EID-KLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1772 LHEKQDlegligtlcdqighrdfDVEKRLRrDLRRTHALLSDVQLLLG-----TMEDGKTSVSK---------EELEKVH 1837
Cdd:COG3883 81 IEERRE-----------------ELGERAR-ALYRSGGSVSYLDVLLGsesfsDFLDRLSALSKiadadadllEELKADK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1838 SQLEQSEAKCEEALKTQKVLTADLESMHSELEnmtRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS 1917
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELE---AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
250
....*....|....*..
gi 51317366 1918 AADIGQIQELQLQLEEA 1934
Cdd:COG3883 220 AAAAAAAAAAAAAAAAA 236
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1683-2086 |
3.79e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1683 VAGLKERLWKLESsALEQQKIQSQQENTikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR-------------QS 1749
Cdd:COG3096 838 LAALRQRRSELER-ELAQHRAQEQQLRQ--QLDQLKEQLQLLNKLLPQANLLADETLADRLEELReeldaaqeaqafiQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1750 CQKRLHQLEM-------------QLEQEYEEKQmvlHEKQDLEGLIGTLCDQIGhrdfdvekrlrrdlRRTHALLSDVQL 1816
Cdd:COG3096 915 HGKALAQLEPlvavlqsdpeqfeQLQADYLQAK---EQQRRLKQQIFALSEVVQ--------------RRPHFSYEDAVG 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1817 LLGTmedgktsvSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELenmtrnkslvdeqlyrlqfekADLLKRI 1896
Cdd:COG3096 978 LLGE--------NSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVL---------------------ASLKSSR 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1897 DEDQDDLNELMQKHKDLIAQSAADIgqiqelqlqLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLE 1976
Cdd:COG3096 1029 DAKQQTLQELEQELEELGVQADAEA---------EERARIRRDELHEELSQNRSRRSQLEKQ------LTRCEAEMDSLQ 1093
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1977 N---KTEfQKVQIKRFEV--------LVIRL-RDSLIKMG---EELsqAATSESQQRESSQYYQRRLEELKADMEEL--V 2039
Cdd:COG3096 1094 KrlrKAE-RDYKQEREQVvqakagwcAVLRLaRDNDVERRlhrREL--AYLSADELRSMSDKALGALRLAVADNEHLrdA 1170
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 51317366 2040 QREAEASRRCmelEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2086
Cdd:COG3096 1171 LRLSEDPRRP---ERKVQFYIAVYQHLRERIRQDIIRTDDPVEAIEQ 1214
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
1806-1914 |
3.91e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 40.29 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1806 RTHALLSDVQLLLGTMEDGKTsvskeELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELEnmTRNKSLVDEQLYRL 1885
Cdd:pfam09744 44 RNQEHNVELEELREDNEQLET-----QYEREKALRKRAEEELEEIEDQWEQETKDLLSQVESLE--EENRRLEADHVSRL 116
|
90 100
....*....|....*....|....*....
gi 51317366 1886 QFEKADLLKRIDEDQDDLNELMQKHKDLI 1914
Cdd:pfam09744 117 EEKEAELKKEYSKLHERETEVLRKLKEVV 145
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
1830-1963 |
3.94e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 40.96 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1830 KEELEKvhSQLEQSEAK-CEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQ 1908
Cdd:pfam06785 62 KEKFEK--SFLEEKEAKlTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRL 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 51317366 1909 KHKDLIAQSAAdigQIQELQLQLEEAKKEKHKLQEQlqvaqmrIEYLEQSTVDRA 1963
Cdd:pfam06785 140 ESEEQLAEKQL---LINEYQQTIEEQRSVLEKRQDQ-------IENLESKVRDLN 184
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1416-1628 |
3.96e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1416 RKLEKSEKLRNELRQNTDLLeskIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKKLGDVNKQL 1495
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1496 EEAQQKIQLNDLERNPTggadewQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYDGAKKMAHQLK 1575
Cdd:COG4372 83 EELNEQLQAAQAELAQA------QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 51317366 1576 RKCHHLTCDLEDTcvlleNQQSRNHELEKKQKKFDLQLAQALGESVFEKGLRE 1628
Cdd:COG4372 157 EQLESLQEELAAL-----EQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1600-2109 |
4.10e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1600 HELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLG 1679
Cdd:pfam12128 241 PEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1680 ENCVAGLKERLWKLESSALEQQKIQSQQENTIK-QLEQLRQRFELEIERmkqmHQKDREDQEEELEDVRQSCQKRLHQLE 1758
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQLPSWQsELENLEERLKALTGK----HQDVTAKYNRRRSKIKEQNNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1759 MQLEQEYEEKQMVLH-EKQDLEGLIGTLCDQI--GHRDF-DVEKRLRRDLRRTHALLSDVQlllgtmedgktsVSKEELE 1834
Cdd:pfam12128 397 DKLAKIREARDRQLAvAEDDLQALESELREQLeaGKLEFnEEEYRLKSRLGELKLRLNQAT------------ATPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1835 kvhsQLEQSEAKCEEALKTQKVLTADLESMHSELenmTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLI 1914
Cdd:pfam12128 465 ----QLENFDERIERAREEQEAANAEVERLQSEL---RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1915 A---QSAAD----IGQI----QELQLQLEEAKKEKHKLQEQ----LQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKT 1979
Cdd:pfam12128 538 HflrKEAPDweqsIGKVispeLLHRTDLDPEVWDGSVGGELnlygVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAR 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1980 EfqkvQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELV---QREAEASRRCMELEKYV 2056
Cdd:pfam12128 618 E----KQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALaerKDSANERLNSLEAQLKQ 693
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 51317366 2057 EELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVDCGSSGRK 2109
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAK 746
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
633-723 |
4.10e-03 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 40.41 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 633 PAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGR--------------VSVEKIRATFT 698
Cdd:cd01363 32 QPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgetegwvylteitvTLEDQILQANP 111
|
90 100
....*....|....*....|....*
gi 51317366 699 VLRAFGSVSMAHSRSATRFSMVMSL 723
Cdd:cd01363 112 ILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1402-1615 |
4.65e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLaderfkgdvacQVLESERAErlqAFREVQELKSKH 1481
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----------RALEQELAA---LEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1482 EQVQKKLGDVNKQLEEAQQKIQLNDLERNPT-----GGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQK 1556
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 51317366 1557 LGELQSAYDGAKKMAHQLKRkchhltcdledtcvLLENQQSRNHELEKKQKKFDLQLAQ 1615
Cdd:COG4942 173 RAELEALLAELEEERAALEA--------------LKAERQKLLARLEKELAELAAELAE 217
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1893-2100 |
4.67e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1893 LKRIDEDQDDLNELmqkhKDLIAQSAAdigQIQELQLQLEEAKKeKHKLQEQLQVAQMRIEYLEqstvDRAIVSRQEAvi 1972
Cdd:COG1196 178 ERKLEATEENLERL----EDILGELER---QLEPLERQAEKAER-YRELKEELKELEAELLLLK----LRELEAELEE-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1973 cdLENKTEFQKVQIKRFEvlvirlrdslikmgEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMEL 2052
Cdd:COG1196 244 --LEAELEELEAELEELE--------------AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 51317366 2053 EKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTA 2100
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1416-1778 |
4.76e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.20 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1416 RKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgDVACQVLESERAERLQAF----REVQELKSKHEQVQKKLGDV 1491
Cdd:pfam15964 353 KALIQCEQLKSELERQKERLEKELASQQEKRAQEK---EALRKEMKKEREELGATMlalsQNVAQLEAQVEKVTREKNSL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1492 NKQLEEAQQKIQLNDLERNPTGGadewQMRF--DCAQMENEFLRKRLQQCEERLDSELTARkelEQKLGELQSAYDGAKK 1569
Cdd:pfam15964 430 VSQLEEAQKQLASQEMDVTKVCG----EMRYqlNQTKMKKDEAEKEHREYRTKTGRQLEIK---DQEIEKLGLELSESKQ 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1570 MAHQLKRKCHHLTCDLEDTCVLLENQQSRNH----ELEKKQKKFDLQL-AQALGESVFEKGLREKVTQENTSVRWELGQL 1644
Cdd:pfam15964 503 RLEQAQQDAARAREECLKLTELLGESEHQLHltrlEKESIQQSFSNEAkAQALQAQQREQELTQKMQQMEAQHDKTVNEQ 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1645 QQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgencvaglkerlwkLESSALEQQKIQSQQENTIKQLEQLRQRFElE 1724
Cdd:pfam15964 583 YSLLTSQNTFIAKLKEECCTLAKKLEEI--------------------TQKSRSEVEQLSQEKEYLQDRLEKLQKRNE-E 641
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 51317366 1725 IERMKQMHQKDREDQEEELEDVRQSCQ---KRLHQLEMQLEQEYEEKQMVLHEKQDL 1778
Cdd:pfam15964 642 LEEQCVQHGRMHERMKQRLRQLDKHCQataQQLVQLLSKQNQLFKERQNLTEEVQSL 698
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1402-1607 |
4.89e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELT---TLRRKLEKSEKLRNEL--RQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERL----QAFR 1472
Cdd:pfam17380 299 ERLRQEKEEKArevERRRKLEEAEKARQAEmdRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIameiSRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1473 EVQEL----KSKHEQVQKKLGDVNKQL---EEAQQKIQLNDLE----RNPTGGADEWQMRFDCAQMENEFLRKRLQQCEE 1541
Cdd:pfam17380 379 ELERLqmerQQKNERVRQELEAARKVKileEERQRKIQQQKVEmeqiRAEQEEARQREVRRLEEERAREMERVRLEEQER 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51317366 1542 RLDSELTARKELEQKLGELQSAYDG-AKKMAHQLKRKChhLTCDLEDT-CVLLENQQSRN---HELEKKQK 1607
Cdd:pfam17380 459 QQQVERLRQQEEERKRKKLELEKEKrDRKRAEEQRRKI--LEKELEERkQAMIEEERKRKlleKEMEERQK 527
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
261-514 |
6.09e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.49 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 261 KDRQGTRPQAQGPGEGVRPGKAEKeGAEPTNTVEKGNVSKDVGSEGKHVRPQIPGRKWGGFLGRRSKwDGPQNKKDKEGV 340
Cdd:PHA03169 24 KRHGGTREQAGRRRGTAARAAKPA-PPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQ-GGPSGSGSESVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 341 LLSKAEKTGEPQTQMEKTSQVQGELGDDLRMGEkaGELRSTTGKAGESWDKKEKMGQPQGKSGNAGEARSQTEKGCEAPK 420
Cdd:PHA03169 102 SPTPSPSGSAEELASGLSPENTSGSSPESPASH--SPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 421 EVSTMVESPAA-------PGKGGWPGSRGQEAEEPCSRAGDGA--------GALETELEGPSQPALEKDAERPRIRKENQ 485
Cdd:PHA03169 180 PPTSEPEPDSPgppqsetPTSSPPPQSPPDEPGEPQSPTPQQApspntqqaVEHEDEPTEPEREGPPFPGHRSHSYTVVG 259
|
250 260 270
....*....|....*....|....*....|....*.
gi 51317366 486 DGPAPQEEG-------KGGQSRDSDQAPEDRWYEAE 514
Cdd:PHA03169 260 WKPSTRPGGvpklclrCTSHPSHRSRLPEGQQSEDK 295
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1392-1764 |
6.49e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1392 QPLLSATIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADL-----TSDLADERFKgdVACQVLESERae 1466
Cdd:PRK10929 48 EALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVppnmsTDALEQEILQ--VSSQLLEKSR-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1467 rlqafrEVQELKSKHEQVQKKLGDVNKQLEEAQQkiQLNDLERN----PTGGADEWQMRFDCAQMENEFLRKRLQQCEEr 1542
Cdd:PRK10929 124 ------QAQQEQDRAREISDSLSQLPQQQTEARR--QLNEIERRlqtlGTPNTPLAQAQLTALQAESAALKALVDELEL- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1543 ldSELTA--RKELEQKLGELqsaydgakkmahqLKRKCHHLTCDLEDTCVLLENQQSRNHE--LEK-------------- 1604
Cdd:PRK10929 195 --AQLSAnnRQELARLRSEL-------------AKKRSQQLDAYLQALRNQLNSQRQREAEraLEStellaeqsgdlpks 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1605 --KQKKFDLQLAQALGESVFEKGL----REKVTQENTSVRWELgqlqqqlkqkeqeaSQLKQQVEMLQDhkrellgSPSL 1678
Cdd:PRK10929 260 ivAQFKINRELSQALNQQAQRMDLiasqQRQAASQTLQVRQAL--------------NTLREQSQWLGV-------SNAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1679 GEncvaGLKERLWKLEssalEQQKIQsQQENTIKQLEQLRQRFELEIERMKQMHQKdREDQEEELEdvrqSCQKRLHQLE 1758
Cdd:PRK10929 319 GE----ALRAQVARLP----EMPKPQ-QLDTEMAQLRVQRLRYEDLLNKQPQLRQI-RQADGQPLT----AEQNRILDAQ 384
|
....*.
gi 51317366 1759 MQLEQE 1764
Cdd:PRK10929 385 LRTQRE 390
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1655-1959 |
6.62e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1655 ASQLKQQV-EMLQDHKRELLGSPSLGEncvaglkERLWKLESSALEQQKIQsQQENTIKQLEQLRQRFELEIERMKQ--- 1730
Cdd:pfam07888 89 LRQSREKHeELEEKYKELSASSEELSE-------EKDALLAQRAAHEARIR-ELEEDIKTLTQRVLERETELERMKErak 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1731 ---MHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIG--HRDFDVEKRLRRDLR 1805
Cdd:pfam07888 161 kagAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtaHRKEAENEALLEELR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1806 RTHALLSdvqlllgtMEDGKTSVSKEELEKV-----HSQLEQSEAKCEEALKTQKVLTADLE------SMHSELENMTRN 1874
Cdd:pfam07888 241 SLQERLN--------ASERKVEGLGEELSSMaaqrdRTQAELHQARLQAAQLTLQLADASLAlregraRWAQERETLQQS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1875 KSLVDEQLYRLQFEKADLLKRIDEDQDDLN----ELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQM 1950
Cdd:pfam07888 313 AEADKDRIEKLSAELQRLEERLQEERMEREklevELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
....*....
gi 51317366 1951 RIEYLEQST 1959
Cdd:pfam07888 393 YIRQLEQRL 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1403-1569 |
6.89e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1403 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvLESERAErlqafREVQELKSKHE 1482
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---------KEIKRLE-----LEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1483 QVQKKLGDV--NKQLEEAQQKIQLndlernptggadewqmrfdcAQMENEFLRKRLQQCEERLDSELTARKELEQKLGEL 1560
Cdd:COG1579 77 KYEEQLGNVrnNKEYEALQKEIES--------------------LKRRISDLEDEILELMERIEELEEELAELEAELAEL 136
|
....*....
gi 51317366 1561 QSAYDGAKK 1569
Cdd:COG1579 137 EAELEEKKA 145
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1697-2086 |
7.42e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1697 ALEQQKIQSQQENtiKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR-------------QSCQKRLHQLEMQL-- 1761
Cdd:PRK04863 852 ALADHESQEQQQR--SQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIReqldeaeeakrfvQQHGNALAQLEPIVsv 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1762 ----EQEYEE-KQMVLHEKQDLegligtlcdqighRDFDVEKRLRRDL--RRTHALLSDVQLLLGtmedgKTSVSKEELE 1834
Cdd:PRK04863 930 lqsdPEQFEQlKQDYQQAQQTQ-------------RDAKQQAFALTEVvqRRAHFSYEDAAEMLA-----KNSDLNEKLR 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1835 KVHSQLEQSEAKCEEALKTQKvltadlesmhselENMTRNKslvdeQLYrlqfekADLLKRIDEDQDDLNELMQKHKDLI 1914
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQAQ-------------AQLAQYN-----QVL------ASLKSSYDAKRQMLQELKQELQDLG 1047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1915 AQsaADIGQIQELQLQLEEakkekhkLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLENK-TEFQK--VQIKRFEV 1991
Cdd:PRK04863 1048 VP--ADSGAEERARARRDE-------LHARLSANRSRRNQLEKQ------LTFCEAEMDNLTKKlRKLERdyHEMREQVV 1112
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1992 -------LVIRL-RDSLIK---MGEELsqAATSESQQRESSQYYQRRLEELKADMEEL--VQREAEASRRcmeLEKYVEE 2058
Cdd:PRK04863 1113 nakagwcAVLRLvKDNGVErrlHRREL--AYLSADELRSMSDKALGALRLAVADNEHLrdVLRLSEDPKR---PERKVQF 1187
|
410 420
....*....|....*....|....*...
gi 51317366 2059 LAAVRQTLQTDLETSIRRIADLQAALEE 2086
Cdd:PRK04863 1188 YIAVYQHLRERIRQDIIRTDDPVEAIEQ 1215
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1402-2077 |
7.89e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDL-------------LESKIADLTSDLADERFKGDVACQVLE------S 1462
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLEELTERLEEQEEVVEeaaeqlA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1463 ERAERLQAFR-EVQELKSKHEQVQKKLgDVN-----------KQLEEAQQKIQLNDLERNptgGADEWQMRFDcAQmENE 1530
Cdd:COG3096 379 EAEARLEAAEeEVDSLKSQLADYQQAL-DVQqtraiqyqqavQALEKARALCGLPDLTPE---NAEDYLAAFR-AK-EQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1531 FLRKRLQQcEERLDSELTARKELEQKLGELQSAYDG-AKKMAHQLKRKchhLTCDLEDTCVLLENQQS---RNHELEKK- 1605
Cdd:COG3096 453 ATEEVLEL-EQKLSVADAARRQFEKAYELVCKIAGEvERSQAWQTARE---LLRRYRSQQALAQRLQQlraQLAELEQRl 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1606 ---QKKFDL--QLAQALGESVFEKGLREKVTQENTSVRWELgqlQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslge 1680
Cdd:COG3096 529 rqqQNAERLleEFCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARIKEL-------- 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1681 ncvaGLKERLWKLESSALEQ------------QKIQSQQENTIK----------QLEQLRQRFELEIERmkqMHQKD-RE 1737
Cdd:COG3096 598 ----AARAPAWLAAQDALERlreqsgealadsQEVTAAMQQLLErereatverdELAARKQALESQIER---LSQPGgAE 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1738 DQE--------------EELEDV---------------RQ--------SCQKRLHQLEMQLEQEYeekqMVLHEKQ---- 1776
Cdd:COG3096 671 DPRllalaerlggvllsEIYDDVtledapyfsalygpaRHaivvpdlsAVKEQLAGLEDCPEDLY----LIEGDPDsfdd 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1777 ---DLEGLIGTLCDQIGHRDFDVEK-----RLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQ------ 1842
Cdd:COG3096 747 svfDAEELEDAVVVKLSDRQWRYSRfpevpLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghl 826
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1843 ---SEAKCEEALKTQKVLTADLESMHSELE-NMTRNKSLVD------EQLYRLQ-----FEKADLLKRIDEDQDDLNEL- 1906
Cdd:COG3096 827 avaFAPDPEAELAALRQRRSELERELAQHRaQEQQLRQQLDqlkeqlQLLNKLLpqanlLADETLADRLEELREELDAAq 906
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1907 -----MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKTef 1981
Cdd:COG3096 907 eaqafIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSD-- 984
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1982 qkvqikrfevLVIRLRDSLIKMGEELSQAATS-ESQQRESSQYYQRR-------------LEELKADMEEL-VQREAEAS 2046
Cdd:COG3096 985 ----------LNEKLRARLEQAEEARREAREQlRQAQAQYSQYNQVLaslkssrdakqqtLQELEQELEELgVQADAEAE 1054
|
810 820 830
....*....|....*....|....*....|.
gi 51317366 2047 RRCMELEKYVEELAAVRQTLQTDLETSIRRI 2077
Cdd:COG3096 1055 ERARIRRDELHEELSQNRSRRSQLEKQLTRC 1085
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1371-1507 |
8.39e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1371 KNVAVFLAVKDW-PW-WQLLGSLQPLLSATIGT-----EQLRAKEEELTTLRRKLEKS-----EKLRNELRQNTDLLESK 1438
Cdd:smart00787 123 KTFARLEAKKMWyEWrMKLLEGLKEGLDENLEGlkedyKLLMKELELLNSIKPKLRDRkdaleEELRQLKQLEDELEDCD 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51317366 1439 IADLtsDLADERFKGDVACQVLESERAERLQafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDL 1507
Cdd:smart00787 203 PTEL--DRAKEKLKKLLQEIMIKVKKLEELE--EELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1402-1503 |
8.42e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvleSERAERLQAFREVQELKSKH 1481
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKDREISRLDREI 474
|
90 100
....*....|....*....|..
gi 51317366 1482 EQVQKKLGDVNKQLEEAQQKIQ 1503
Cdd:COG2433 475 ERLERELEEERERIEELKRKLE 496
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
1510-1632 |
9.41e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.46 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1510 NPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYdGAKKMAHQ-------LKRKCHHLT 1582
Cdd:pfam15294 123 NEGGGSALLHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQ-GAKKDVKSnlkeisdLEEKMAALK 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 51317366 1583 CDLEDTCVLLENQQ--------SRNHELEKKQKkfdlQLAQAlgesvfEKGLREKVTQ 1632
Cdd:pfam15294 202 SDLEKTLNASTALQksleedlaSTKHELLKVQE----QLEMA------EKELEKKFQQ 249
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1402-1569 |
9.79e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAER-LQAF-REVQELKS 1479
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-------LGNVRNNKeYEALqKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51317366 1480 KHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggadewQMRFDCAQMENEfLRKRLQQCEERLDSELTARKELEQKLGE 1559
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELA--------ELEAELEEKKAE-LDEELAELEAELEELEAEREELAAKIPP 174
|
170
....*....|.
gi 51317366 1560 -LQSAYDGAKK 1569
Cdd:COG1579 175 eLLALYERIRK 185
|
|
| |
