|
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 ... |
627-1363 |
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: 1041.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKV---PKG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVakmFKGcRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 782
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 783 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQ 862
Cdd:cd01386 161 LERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 863 RAVWRVLAAIYHLGAAGACK---VGRKQFMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRwGLEDEETS 939
Cdd:cd01386 241 RAIWSILAAIYHLGAAGATKaasAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQ-ESPARSSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 940 SGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGKDRAATFEELCHNYAHERLQL 1019
Cdd:cd01386 320 GGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERLQL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1020 LFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQNPSQVRLPAGGGAQDARGLFWVLDEEVHVEGSSDSVVLERL 1099
Cdd:cd01386 400 LFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQQALVRSDLRDEDRRGLLWLLDEEALYPGSSDDTFLERL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1100 CAAFEKKGAGTeGSSALRTCEQPLQCEIFHQLGWDPVRYDLTGWLHRAKPNLSALDAPQVLQQSKREelrslfqaraklp 1179
Cdd:cd01386 480 FSHYGDKEGGK-GHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE------------- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1180 pvcravaglegtsqqalqrsrmvrrtfassLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESRSGQESP 1259
Cdd:cd01386 546 ------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDERSTSS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1260 PPpqpgrdkpgaGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMSTSEGIDERKAV 1339
Cdd:cd01386 596 PA----------AGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVADERKAV 665
|
730 740
....*....|....*....|....
gi 2462585723 1340 EELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd01386 666 EELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
628-1363 |
1.10e-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: 327.63 E-value: 1.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKV-----PKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVmekyrGKGRSADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGSVDGRVS------VEKIRATFTVLRAFGsvsmaHSRS-----ATRFSMVMSLDFNATG 771
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSssassiEQQILQSNPILEAFG-----NAKTvrndnSSRFGKFIELQFDPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 772 RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL---HQMADSSSFGMGVWSKPEDKQKAAAAFAQL 848
Cdd:cd00124 157 RLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLellLSYYYLNDYLNSSGCDRIDGVDDAEEFQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 849 QGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKqfmrfEWANYAAEALGCEYEELNTATFKhhlR 918
Cdd:cd00124 237 LDALDVLGFSDEEQDSIFRILAAILHLGniefeedeedEDSSAEVADD-----ESLKAAAKLLGVDAEDLEEALTT---R 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 919 QIIqqmtfgpsrwgLEDEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFSS--HHLSMASIMVVDSPGFQNPR 995
Cdd:cd00124 309 TIK-----------VGGETITKPLTVEQaEDARDALAKALYSRLFDWLVNRINAALSPtdAAESTSFIGILDIFGFENFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 996 HQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgtTVAVVDQNPSqvrlpagggaqda 1074
Cdd:cd00124 378 VNS------FEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFiDFPDNQD--CLDLIEGKPL------------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1075 rGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagteGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSal 1154
Cdd:cd00124 437 -GILSLLDEECLFPKGTDATFLEKLYSAHGSH-----PRFFSKKRKAKLEFGIKHYAG--DVTYDADGFLEKNKDTLP-- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1155 dapqvlqqskrEELRSLFQAraklppvcravaglegtsqqalqrsrmvrrtfasslaavrrkapCSQIKLQMDALTSMIK 1234
Cdd:cd00124 507 -----------PDLVDLLRS--------------------------------------------GSQFRSQLDALMDTLN 531
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1235 RSRLHFIHCLVPNPvvesrsgqesppppqpgrdkpgAGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQ 1314
Cdd:cd00124 532 STQPHFVRCIKPND----------------------EKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKR 589
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 2462585723 1315 FQVLDAPLLKKLMSTSEgiderKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd00124 590 YRILAPGATEKASDSKK-----AAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
608-1375 |
3.94e-92 |
|
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: 315.64 E-value: 3.94e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 608 NPPELDQVEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAGKvpkGRRDG-LPAHIGS 680
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPykqlpiYTDEVIKKYR---GKSRGeLPPHVFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 681 MAQRAYWALLNQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRF 759
Cdd:smart00242 78 IADNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGSVEdQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 760 SMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQmadSSSFG---MGVWSK-- 834
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS---PEDYRylnQGGCLTvd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 835 -PEDKqkaaAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKQFmrfewaNYAAEALGC 903
Cdd:smart00242 235 gIDDA----EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGniefeegrndNAASTVKDKEEL------SNAAELLGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 904 EYEELNTA-TFKhhlrqiiqQMTFGpsrwgleDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMA 981
Cdd:smart00242 305 DPEELEKAlTKR--------KIKTG-------GEVITKPLNVEQAlDARDALAKALYSRLFDWLVKRINQSLSFKDGSTY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 982 SIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQ----FDLpdpspGTTVAVVD 1057
Cdd:smart00242 370 FIGVLDIYGFEIFEVNS------FEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTfidfFDN-----QDCIDLIE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1058 QNPsqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCeqplqceiF---HQLGwd 1134
Cdd:smart00242 439 KKP--------------PGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKPKKKGRTE--------FiikHYAG-- 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1135 PVRYDLTGWLHRAKPNLSAlDAPQVLQQSKREELRSLFqaraklppvcravaglegtSQQALQRSRMVRRTFASslaavr 1214
Cdd:smart00242 495 DVTYDVTGFLEKNKDTLSD-DLIELLQSSKNPLIASLF-------------------PSGVSNAGSKKRFQTVG------ 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1215 rkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEA 1294
Cdd:smart00242 549 -----SQFKEQLNELMDTLNSTNPHFIRCIKPNE--EKKPGD--------------------FDSSLVLHQLRYLGVLEN 601
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1295 LRLHRTGYADHMGLTRFRRQFQVLDAPLLKklmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLKAGVISRLEKQR 1374
Cdd:smart00242 602 IRIRRAGFPYRLPFDEFLQRYRVLLPDTWP-----PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
.
gi 2462585723 1375 E 1375
Cdd:smart00242 677 E 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
552-2127 |
1.26e-75 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 279.66 E-value: 1.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 552 WYEA-EKVWLA---QKDGFTLATVlkpdEGTADLPAGRVrlcIDADKTITEVDEEhvhraNPPELDQVEDLASLISVNES 627
Cdd:COG5022 13 WIPDeEKGWIWaeiIKEAFNKGKV----TEEGKKEDGES---VSVKKKVLGNDRI-----KLPKFDGVDDLTELSYLNEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGpsVPSAG-----KVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:COG5022 81 AVLHNLEKRYNNGQIYTYSGLVLIAVNPyRD--LGIYTddiiqSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIIS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMAGSV-DGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQ 779
Cdd:COG5022 159 GESGAGKTENAKRIMQYLASVTSSStVEISSIEkQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 780 TMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISE 859
Cdd:COG5022 239 TYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLL-LLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 860 SEQRAVWRVLAAIYHLG--AAGACKVGRKQFMRFEWANYAAEALGCEYEELNTATFKhhlRQIIQqmtfgpsrwGLEDEE 937
Cdd:COG5022 318 EEQDQIFKILAAILHIGniEFKEDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVK---RQIKT---------GGEWIV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 938 TSSGLKMTgVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERL 1017
Cdd:COG5022 386 VPLNLEQA-LAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNS------FEQLCINYTNEKL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1018 QLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVL 1096
Cdd:COG5022 459 QQFFNQHMFKLEQEEYVKEGIEWSFiDYFDNQP-CIDLIEKKNPL--------------GILSLLDEECVMPHATDESFT 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1097 ERLCAAFEKKgagtegSSALRTCEQPLQCEIF--HQLGwDpVRYDLTGWLHRAKPNLSaLDAPQVLQQSKREELRSLFQA 1174
Cdd:COG5022 524 SKLAQRLNKN------SNPKFKKSRFRDNKFVvkHYAG-D-VEYDVEGFLDKNKDPLN-DDLLELLKASTNEFVSTLFDD 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1175 RaklppvcravaglegtsQQALQRSRmvRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRS 1254
Cdd:COG5022 595 E-----------------ENIESKGR--FPTLG------------SRFKESLNSLMSTLNSTQPHYIRCIKPN---EEKS 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1255 gqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMSTSEGiD 1334
Cdd:COG5022 641 -------------------PWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTWKE-D 700
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1335 ERKAVEELLETLDLEKKAVAVGHSQVFLKAGVISRLEKQREKLVSQSIVLFQAACKGFLSRQEFKKLKIRRLAAQCIQKN 1414
Cdd:COG5022 701 TKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHG 780
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1415 VAVFLAVKDWPWWQLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEK----SEKLRNELRQNTDLLESKIADltSDLAD 1490
Cdd:COG5022 781 FRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekklRETEEVEFSLKAEVLIQKFGR--SLKAK 858
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1491 ERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQkKLGDVNKQLE----EAQQKIQLNDLERNptggdewqmrfdca 1566
Cdd:COG5022 859 KRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELEseiiELKKSLSSDLIENL-------------- 923
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1567 QMENEFLrKRLQQCEERLDSELTARKELEQK--LGELQSAydgakkmahqlkrkchhlTCDLEDTCVLLENqqsrnhELE 1644
Cdd:COG5022 924 EFKTELI-ARLKKLLNNIDLEEGPSIEYVKLpeLNKLHEV------------------ESKLKETSEEYED------LLK 978
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1645 KKqkkfdlqlaqalgesvfEKGLREKVTQENTSVRW--ELGQLQQQLKQKEQEASQLKQQVEMLQDHKREllgspslgen 1722
Cdd:COG5022 979 KS-----------------TILVREGNKANSELKNFkkELAELSKQYGALQESTKQLKELPVEVAELQSA---------- 1031
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1723 cvaglkERLWKLESSALEQQK-IQSQQENTIKQLEQLRQRFE---LEIERmkqmhQKDREDQEEELEDVRqscqkrlhql 1798
Cdd:COG5022 1032 ------SKIISSESTELSILKpLQKLKGLLLLENNQLQARYKalkLRREN-----SLLDDKQLYQLESTE---------- 1090
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1799 emQLEQEYEEKQMVLhEKQDLEGLIGTLcdqighrDFDVEKRLRRDL-RRTHALLSdvqLLLGTMEDGKTSVSKEELE-- 1875
Cdd:COG5022 1091 --NLLKTINVKDLEV-TNRNLVKPANVL-------QFIVAQMIKLNLlQEISKFLS---QLVNTLEPVFQKLSVLQLEld 1157
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1876 --KVHSQLEQSEAKCEEALKTQKVLTADleSMHSEL--ENMTRNKSLVDE--QLYRLQFE---KADLLKRIDEDQDDLNE 1946
Cdd:COG5022 1158 glFWEANLEALPSPPPFAALSEKRLYQS--ALYDEKskLSSSEVNDLKNEliALFSKIFSgwpRGDKLKKLISEGWVPTE 1235
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1947 LMQKHKDliAQSAADIGQiqelqlqlEEAKKEKHKLQEQL-QVAQMRIEYLEQSTVDRAIVsrqeavicdlenKTEFQKV 2025
Cdd:COG5022 1236 YSTSLKG--FNNLNKKFD--------TPASMSNEKLLSLLnSIDNLLSSYKLEEEVLPATI------------NSLLQYI 1293
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2026 QIKRFEVLVIRLRDSLIKMGEELSQaatseSQQRESSQYYQRRLEELKADMEELVQReaeasRRCMELEKY-VEELAAVR 2104
Cdd:COG5022 1294 NVGLFNALRTKASSLRWKSATEVNY-----NSEELDDWCREFEISDVDEELEELIQA-----VKVLQLLKDdLNKLDELL 1363
|
1610 1620
....*....|....*....|....
gi 2462585723 2105 QTLQTDLETSIRRI-ADLQAALEE 2127
Cdd:COG5022 1364 DACYSLNPAEIQNLkSRYDPADKE 1387
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
615-1363 |
1.86e-72 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 257.59 E-value: 1.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 615 VEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvpkgRRDGLPAHIGSMAQRAY 686
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPykqlpiYSEDMIKAyrGK----RRGELPPHIFAIADEAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 687 WALLNQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSVD----GRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMV 762
Cdd:pfam00063 77 RSMLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSagnvGRLE-EQILQSNPILEAFGNAKTVRNNNSSRFGKY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 763 MSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGM-GVWSKP 835
Cdd:pfam00063 156 IEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyHYLSQSGCYTIdGIDDSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 836 EDKqkaaaafaQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQfmrfEWANYAAEALGCEYEEL 908
Cdd:pfam00063 236 EFK--------ITDKAMDILGFSDEEQMGIFRIVAAILHLGniefkkeRNDEQAVPDDT----ENLQKAASLLGIDSTEL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 909 NTATFKhhlRQIiqqmtfgpsrwgledeETSSGLKMTGVDC------VEGMASGLYQELFAAVVSLINRSFSSHHLSMAS 982
Cdd:pfam00063 304 EKALCK---RRI----------------KTGRETVSKPQNVeqanyaRDALAKAIYSRLFDWLVDRINKSLDVKTIEKAS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 983 -IMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgtTVAVV 1056
Cdd:pfam00063 365 fIGVLDIYGFEifekN----------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFiDFGDNQP--CIDLI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1057 DQNPsqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEK----KGAGTEGSSALRtceqplqceIFHQLG 1132
Cdd:pfam00063 433 EKKP--------------LGILSLLDEECLFPKATDQTFLDKLYSTFSKhphfQKPRLQGETHFI---------IKHYAG 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1133 wdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKREELRSLFQARAKlppvcRAVAGLEGTSQQALQRSRMVRRTFASslaa 1212
Cdd:pfam00063 490 --DVEYNVEGFLEKNKDPLND-DLVSLLKSSSDPLLAELFPDYET-----AESAAANESGKSTPKRTKKKRFITVG---- 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1213 vrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHIL 1292
Cdd:pfam00063 558 -------SQFKESLGELMKTLNSTNPHYIRCIKPNE--KKRAGV--------------------FDNSLVLHQLRCNGVL 608
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462585723 1293 EALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMStsegiDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:pfam00063 609 EGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKG-----DAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
627-1363 |
1.82e-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: 201.16 E-value: 1.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAGKVP---KGRRDGLPAHIGSMAQRAYWALLN----QRRDQS 697
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKsiPDLYSEERMLlyhGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 698 IVALGRSGAGKT-------------TCCEQVLEHLVGMAGSVDGRVSV----EKIRATFTVLRAFGSVSMAHSRSATRFS 760
Cdd:cd14890 81 IIISGESGAGKTeatkiimqylariTSGFAQGASGEGEAASEAIEQTLgsleDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 761 MVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEDKq 839
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLrGECSSIPSCDD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 840 kaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRkQFMRFewanyAAEALGCEYEELN 909
Cdd:cd14890 240 --AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGnvdfesendtTVLEDATTL-QSLKL-----AAELLGVNEDALE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 910 TATFKHHL----RQIIQQMTFGPSRwgledeetssglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMV 985
Cdd:cd14890 312 KALLTRQLfvggKTIVQPQNVEQAR-----------------DKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 986 VDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDqNPSQVRL 1065
Cdd:cd14890 375 LDIYGFEKFEWN------TFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQY----------ITFND-NQACLEL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1066 PAGGGAQDArGLFWVLDEEVHVEGS-SDSVVLERLCAAFekkGAGTEGSSALRTCEQ------P-----LQCEIFHQLGw 1133
Cdd:cd14890 438 IEGKVNGKP-GIFITLDDCWRFKGEeANKKFVSQLHASF---GRKSGSGGTRRGSSQhphfvhPkfdadKQFGIKHYAG- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1134 dPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKReelrslfqaraklppvcravaglegtsqqalqrsrmvrrtfasslaAV 1213
Cdd:cd14890 513 -DVIYDASGFNEKNNETLNA-EMKELIKQSRR----------------------------------------------SI 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1214 RRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILE 1293
Cdd:cd14890 545 REVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKA----------------------PGKFDGLDCLRQLKYSGMME 602
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462585723 1294 ALRLHRTGYA---DHmglTRFRRQFQVLDapllkklmSTSEGIDErkAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14890 603 AIQIRQQGFAlreEH---DSFFYDFQVLL--------PTAENIEQ--LVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
628-1318 |
4.95e-50 |
|
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: 190.22 E-value: 4.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAgkvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPfkdvplYGNEFITA----YRQKLLDSPHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMAGSVDGrvsVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQT 780
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGGGSSG---IEnEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 781 MLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISES 860
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNL-KSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 861 EQRAVWRVLAAIYHLG--------AAGACKVGRKqfmrfEWANYAAEALGCEYEELNTATFKHHLRqiiqqmtfgpsrwg 932
Cdd:cd01383 234 DQEHIFQMLAAVLWLGnisfqvidNENHVEVVAD-----EAVSTAASLLGCNANDLMLALSTRKIQ-------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 933 LEDEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRSF-SSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 1010
Cdd:cd01383 295 AGGDKIVKKLTLQqAIDARDALAKAIYASLFDWLVEQINKSLeVGKRRTGRSISILDIYGFESFQKN------SFEQLCI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1011 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdlpdpspgTTVAVVDqNPSQVRL----PAgggaqdarGLFWVLDEEVH 1086
Cdd:cd01383 369 NYANERLQQHFNRHLFKLEQEEYELDGIDW----------TKVDFED-NQECLDLiekkPL--------GLISLLDEESN 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1087 VEGSSDSVVLERL--------CAAFEKKGAGTegssalrtceqplqceIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQ 1158
Cdd:cd01383 430 FPKATDLTFANKLkqhlksnsCFKGERGGAFT----------------IRHYAG--EVTYDTSGFLEKNRDLLHS-DLIQ 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1159 VLQQSKreelRSLFQARAklppvcravAGLEGTSQQALQRSRMvrrtfasSLAAVRRKAPCSQIKLQMDALTSMIKRSRL 1238
Cdd:cd01383 491 LLSSCS----CQLPQLFA---------SKMLDASRKALPLTKA-------SGSDSQKQSVATKFKGQLFKLMQRLENTTP 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1239 HFIHCLVPNPV-VESRSGQEsppppqpgrdkpgaggpLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQV 1317
Cdd:cd01383 551 HFIRCIKPNNKqLPGVFDQD-----------------LVLQ------QLRCCGVLEVVRISRSGYPTRMTHQEFARRYGF 607
|
.
gi 2462585723 1318 L 1318
Cdd:cd01383 608 L 608
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
627-1363 |
2.07e-49 |
|
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: 189.07 E-value: 2.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVP----SAGKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPY-KNLPiyseNIIEMYRGKkRHEMPPHIYAISESAYRCMLQDREDQSILCT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMA--------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRI 773
Cdd:cd14920 80 GESGAGKTENTKKVIQYLAHVAsshkgrkdHNIPGELERQLLQAN-PILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 774 TAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLHQMADSSSFgMGVWSKPEDKQKAAAAFAQLQGAME 853
Cdd:cd14920 159 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDL-LLEGFNNYRF-LSNGYIPIPGQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 854 MLGISESEQRAVWRVLAAIYHLGAAGACKvGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsRWGL 933
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKL-CHLLGMNVMEFTRAI--LTPRIKVG--RDYV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 934 EDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEELCHNY 1012
Cdd:cd14920 311 QKAQTKEQADFA----VEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFE------IFELNSFEQLCINY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1013 AHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEG 1089
Cdd:cd14920 381 TNEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIDLIERPANPP--------------GVLALLDEECWFPK 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1090 SSDSVVLERLcaafekkgAGTEGS-SALRTCEQP---LQCEIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLQQS 1163
Cdd:cd14920 446 ATDKTFVEKL--------VQEQGShSKFQKPRQLkdkADFCIIHYAG--KVDYKADEWLMK---NMDPLndNVATLLHQS 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1164 KREELRSLFQARAKLPPVCRAVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHC 1243
Cdd:cd14920 513 SDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVG------------QLYKESLTKLMATLRNTNPNFVRC 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1244 LVPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLL 1323
Cdd:cd14920 581 IIPNH--EKRAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 638
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 2462585723 1324 KKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14920 639 PKGF-----MDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
628-1320 |
2.15e-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: 183.62 E-value: 2.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAGKVPKGRRD-----GLPAHIGSMAQRAYWALL-------NQRRD 695
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPF-KHIPGLYDLHKYREEmpgwtALPPHVFSIAEGAYRSLRrrlhepgASKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 696 QSIVALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDF 767
Cdd:cd14895 81 QTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGsellsanpILESFGNARTLRNDNSSRFGKFVRMFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 768 -----NATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMA--DSSSFGMGVWSKPEDKQK 840
Cdd:cd14895 161 eghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGQCYQRNDGVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 841 AAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG------------------AAGACKVGR---KQFMRFEWANYAAE 899
Cdd:cd14895 241 DDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvlfvassedegeedngaASAPCRLASaspSSLTVQQHLDIVSK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 900 ALGCEYEELNTATFKhhlRQIiqqmtfgpsrwGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLIN-----RSF 973
Cdd:cd14895 321 LFAVDQDELVSALTT---RKI-----------SVGGETFHANLSLAQCgDARDAMARSLYAFLFQFLVSKVNsaspqRQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 974 SSHHLSMAS------IMVVDSPGFQnprhqgKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP-VQFDLPD 1046
Cdd:cd14895 387 ALNPNKAANkdttpcIAVLDIFGFE------EFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKwNAVDYED 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1047 PSpgTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGagteGSSALRTCEQPLQCE 1126
Cdd:cd14895 461 NS--VCLEMLEQRPS--------------GIFSLLDEECVVPKGSDAGFARKLYQRLQEHS----NFSASRTDQADVAFQ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1127 IFHQLGwdPVRYDLTGWL--HRAKPNLSALDapqVLQQSKREELRSLfqaraklppvCRAVAGLEgTSQQALQRSRMVRR 1204
Cdd:cd14895 521 IHHYAG--AVRYQAEGFCekNKDQPNAELFS---VLGKTSDAHLREL----------FEFFKASE-SAELSLGQPKLRRR 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1205 TfaSSLAAVrrkAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRV 1284
Cdd:cd14895 585 S--SVLSSV---GIGSQFKQQLASLLDVVQQTQTHYIRCIKPND--ESASDQ--------------------FDMAKVSS 637
|
730 740 750
....*....|....*....|....*....|....*.
gi 2462585723 1285 QLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDA 1320
Cdd:cd14895 638 QLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVA 673
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
628-1248 |
2.80e-46 |
|
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: 179.50 E-value: 2.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSV-----------PSAGKVPkgrrdglpaHIGSMAQRAYWALLNQRR 694
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPfkTIPGLysdemllkfiqPSISKSP---------HVFSTASSAYQGMCNNKK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 695 DQSIVALGRSGAGKTTCCEQVLEHLVgMAGSVD--GRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT- 770
Cdd:cd14888 73 SQTILISGESGAGKTESTKYVMKFLA-CAGSEDikKRSLVEaQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 771 --------GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGL-------------DLDLRTELNLHQMA-DSSSFG 828
Cdd:cd14888 152 skrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAreakntglsyeenDEKLAKGADAKPISiDMSSFE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 829 MGVWSKPEDKQKAAAAFA--------QLQGAMEMLGISESEQRAVWRVLAAIYHLG-----AAGACKVGRK-QFMRFEWA 894
Cdd:cd14888 232 PHLKFRYLTKSSCHELPDvddleefeSTLYAMQTVGISPEEQNQIFSIVAAILYLGnilfeNNEACSEGAVvSASCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 895 NYAAEALGCEYEEL-NTATFkhhlRQIIQQmtfgpsrwgleDEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRS 972
Cdd:cd14888 312 EKVASLLGVDAEDLlNALCY----RTIKTA-----------HEFYTKPLRVDeAEDVRDALARALYSCLFDKVVERTNES 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 973 FS-SHHLSMASIMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQFdl 1044
Cdd:cd14888 377 IGySKDNSLLFCGVLDIFGFEcfqlN----------SFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIswnPLDF-- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1045 pdPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTceQPLQ 1124
Cdd:cd14888 445 --PDNQDCVDLLQEKPL--------------GIFCMLDEECFVPGGKD----QGLCNKLCQKHKGHKRFDVVKT--DPNS 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1125 CEIFHQLGwdPVRYDLTGWLHRAKPNLSaLDAPQVLQQSKREELRSLFQAraklppvcravaglegtsqqalqrsrMVRR 1204
Cdd:cd14888 503 FVIVHFAG--PVKYCSDGFLEKNKDQLS-VDAQEVIKNSKNPFISNLFSA--------------------------YLRR 553
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2462585723 1205 TFASSLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNP 1248
Cdd:cd14888 554 GTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNS 597
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
627-1363 |
8.02e-46 |
|
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: 178.25 E-value: 8.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVP---KG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMeryKGiKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGS-----------------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSL 765
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavphpavnpavLIGELEQQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 766 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPedKQKAAAAF 845
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVP--GVDDYAEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 846 AQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEyeelNTATFK--HHLRQIIQQ 923
Cdd:cd14911 238 QATVKSMNIMGMTSEDFNSIFRIVSAVLLFGS-----------MKFRQERNNDQATLPD----NTVAQKiaHLLGLSVTD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 924 MT--FGPSRWGL-EDEETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgK 999
Cdd:cd14911 303 MTraFLTPRIKVgRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASfIGILDMAGFE------I 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1000 DRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPgtTVAVVDQnpsqvrlpagggaqdARG 1076
Cdd:cd14911 377 FELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwkfIDFGL-DLQP--TIDLIDK---------------PGG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1077 LFWVLDEEVHVEGSSDSVVLERLCAA------FEKkgAGTEGSSALrtceqplqcEIFHQLGwdPVRYDLTGWLHRakpN 1150
Cdd:cd14911 439 IMALLDEECWFPKATDKTFVDKLVSAhsmhpkFMK--TDFRGVADF---------AIVHYAG--RVDYSAAKWLMK---N 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1151 LSALDapqvlqqskrEELRSLFQArAKLPPVCR--AVAGLEGTSQQALQRSRMVRRTFASSLAAVrrkapcSQI-KLQMD 1227
Cdd:cd14911 503 MDPLN----------ENIVSLLQG-SQDPFVVNiwKDAEIVGMAQQALTDTQFGARTRKGMFRTV------SHLyKEQLA 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1228 ALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgAGGPLALDipalrvQLAGFHILEALRLHRTGYADHMG 1307
Cdd:cd14911 566 KLMDTLRNTNPNFVRCIIPNH--EKRAGK--------------IDAPLVLD------QLRCNGVLEGIRICRQGFPNRIP 623
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462585723 1308 LTRFRRQFQVLDAPLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
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 ... |
628-1360 |
1.37e-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: 176.89 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPS--AGKVPKGrrdgLPAHIGSMAQRAYWALLNQRRDQSIV 699
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPfkrlplYTPTVMDqyMHKGPKE----MPPHTYNIADDAYRAMIVDAMNQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 700 ALGRSGAGKTTCCEQVLEHLVGMAGSVDGrvsVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQL 778
Cdd:cd14872 78 ISGESGAGKTEATKQCLSFFAEVAGSTNG---VEqRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 779 QTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNlhqmaDSSSFGMGVWSKPEDKQKAAAAF--AQLQGAMEMLG 856
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWG-----SSAAYGYLSLSGCIEVEGVDDVAdfEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 857 ISESEQRAVWRVLAAIYHLG------AAGACKVGRKQFMRFEWANYAAEALGCEYEELNTAtFKHHLRQIIQQmtfGPSR 930
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGniefasGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEA-LTSRLMEIKGC---DPTR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 931 WGLEDEEtssglkmtGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQ----NprhqgkdraaTF 1005
Cdd:cd14872 306 IPLTPAQ--------ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTfIGVLDIFGFEifekN----------SF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1006 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPSQVRLPAGGGaqdarGLFWVLDEEV 1085
Cdd:cd14872 368 EQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFE----------HIDFIDNQPVLDLIEKKQP-----GLMLALDDQV 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1086 HVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKR 1165
Cdd:cd14872 433 KIPKGSD----ATFMIAANQTHAAKSTFVYAEVRTSRTEFIVKHYAG--DVTYDITGFLEKNKDTLQK-DLYVLLSSSKN 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1166 EELRSLFqaraklPPvcraVAGLEGTSQQALqrsrmvrrtfasslaavrrkapCSQIKLQMDALTSMIKRSRLHFIHCLV 1245
Cdd:cd14872 506 KLIAVLF------PP----SEGDQKTSKVTL----------------------GGQFRKQLSALMTALNATEPHYIRCVK 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1246 PNpvvesrsgqesppppQPGRDKPGAGgplALDIPALRvqLAGfhILEALRLHRTGYAdhmgltrFR---RQFQVLDAPL 1322
Cdd:cd14872 554 PN---------------QEKRARLFDG---FMSLEQLR--YAG--VFEAVKIRKTGYP-------FRyshERFLKRYRFL 604
|
730 740 750
....*....|....*....|....*....|....*...
gi 2462585723 1323 LKKlMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQV 1360
Cdd:cd14872 605 VKT-IAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRV 641
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
627-1363 |
1.45e-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: 177.13 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVP---------SAGKvpkgRRDGLPAHIGSMAQRAYWALLNQRRDQS 697
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTGSILVAVNPY-KELPiytqdivkqYFGK----RMGALPPHIFALAEAAYTNMQEDGKNQS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 698 IVALGRSGAGKTTCCEQVLEHLVgmagSVDGRVS-VE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 775
Cdd:cd14883 76 VIISGESGAGKTETTKLILQYLC----AVTNNHSwVEqQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 776 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAG--LDLDLRTELNLHQMAD------SSSFGMGVWSKPEDkqkaaaaFAQ 847
Cdd:cd14883 152 AIIQDYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDyhylnqSGCIRIDNINDKKD-------FDH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 848 LQGAMEMLGISESEQRAVWRVLAAIYHLG--AAGACKVGRKQFMRFEWANYAAEA--LGCEYEELNTA-TFKHhlRQIIQ 922
Cdd:cd14883 225 LRLAMNVLGIPEEMQEGIFSVLSAILHLGnlTFEDIDGETGALTVEDKEILKIVAklLGVDPDKLKKAlTIRQ--INVRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 923 QMTFGPsrwgledeetssgLKMT-GVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdr 1001
Cdd:cd14883 303 NVTEIP-------------LKVQeARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVN---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1002 aaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQF-------DLPDPSPgttvavvdqnpsqvrlpaggga 1071
Cdd:cd14883 366 --SFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGInwsHIVFtdnqeclDLIEKPP---------------------- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1072 qdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQceifHQLGwdPVRYDLTGWLHRAKPNL 1151
Cdd:cd14883 422 ---LGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVK----HYAG--EVTYTVQGFLDKNKDTQ 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1152 SaLDAPQVLQQSKREELRSLFQARAKLPPVCRAVAGLEGTSQqalqrsrmvRRTfasslaavRRKAP--CSQIKLQMDAL 1229
Cdd:cd14883 493 Q-DDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTS---------RGT--------SKGKPtvGDTFKHQLQSL 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1230 TSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLT 1309
Cdd:cd14883 555 VDVLSATQPWYVRCIKPNSLKE----------------------PNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFK 612
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 2462585723 1310 RFRRQFQVLDapllkKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14883 613 EFVDRYLCLD-----PRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
627-1319 |
2.96e-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: 176.12 E-value: 2.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAG---KVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQwlPELYTEEqhsKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMAGSVDgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 781
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLN-DSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 782 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQ---------------MADSSSFgmgvwskpedkqkaaaafA 846
Cdd:cd14903 160 LLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANecaytganktikiegMSDRKHF------------------A 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 847 QLQGAMEMLGISESEQRAVWRVLAAIYHLGAA-----------GACKVGRkqfmrfEWANYAAEALGCEYEELNTATFKH 915
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLqiqskpnddekSAIAPGD------QGAVYATKLLGLSPEALEKALCSR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 916 HLRQIIQQMTFgpsrwGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPR 995
Cdd:cd14903 296 TMRAAGDVYTV-----PLKKDQAE--------DCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 996 HQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP-VQFDLPDPSpgTTVAVVdqnpsqvrlpagggaQDA 1074
Cdd:cd14903 363 HN------SFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRwAHIDFADNQ--DVLAVI---------------EDR 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1075 RGLFWVLDEEV-HVEGSSDSVVLeRLCAAFEKKGAGTEGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAK----P 1149
Cdd:cd14903 420 LGIISLLNDEVmRPKGNEESFVS-KLSSIHKDEQDVIEFPRTSRT-----QFTIKHYAG--PVTYESLGFLEKHKdallP 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1150 NLSALdapqvLQQSKREELRSLFQARaklppvcravAGLEGTSQQALQRSRMVRRTFASSLAAVRrkapcSQIKLQMDAL 1229
Cdd:cd14903 492 DLSDL-----MRGSSKPFLRMLFKEK----------VESPAAASTSLARGARRRRGGALTTTTVG-----TQFKDSLNEL 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1230 TSMIKRSRLHFIHCLVPNPvvesrsgqesppppqpgrdkpgAGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLT 1309
Cdd:cd14903 552 MTTIRSTNVHYVRCIKPNS----------------------IKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHE 609
|
730
....*....|
gi 2462585723 1310 RFRRQFQVLD 1319
Cdd:cd14903 610 EFLDKFWLFL 619
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
628-1172 |
6.67e-45 |
|
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: 174.49 E-value: 6.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAGKVPKGR------RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKP-LPIFDKKHHEEysnlsvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMAGSVDGRVsVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 781
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSDL-LDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 782 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL-----HQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLG 856
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLedpdcHRILRDDNRNRPVFNDSEELEYYRQMFHDLTNIMKLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 857 ISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRFE---WANYAAEALGCEYEELNTAtfkhhlrqIIQQMTFgpsrwgL 933
Cdd:cd14897 240 FSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVAdeyPLHAVAKLLGIDEVELTEA--------LISNVNT------I 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 934 EDEETSSGLKM-TGVDCVEGMASGLYQELFAAVVSLINRSFSSHHL-----SMASIMVVDSPGFQNPRHQGkdraatFEE 1007
Cdd:cd14897 306 RGERIQSWKSLrQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDfqimtRGPSIGILDMSGFENFKINS------FDQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1008 LCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfDLPDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHV 1087
Cdd:cd14897 380 LCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR-DIEYHDNDDVLELFFKKPL--------------GILPLLDEESTF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1088 EGSSDSVVLERLcaafEKKGagteGSSALRTCEQPLQCE--IFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKR 1165
Cdd:cd14897 445 PQSTDSSLVQKL----NKYC----GESPRYVASPGNRVAfgIRHYAE--QVTYDADGFLEKNRDNLSS-DIVGCLLNSNN 513
|
....*..
gi 2462585723 1166 EELRSLF 1172
Cdd:cd14897 514 EFISDLF 520
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
627-1363 |
9.71e-45 |
|
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: 174.82 E-value: 9.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVP---KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVdmyKGKkRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGS--------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRIT 774
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASShkgkkdtsITGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 775 AAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkAAAAFAQLQGAMEM 854
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQ--DDEMFQETLEAMSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 855 LGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsrwglE 934
Cdd:cd14921 238 MGFSEEEQLSILKVVSSVLQLGNI-VFKKERNTDQASMPDNTAAQKV-CHLMGINVTDFTRSI--LTPRIKVG------R 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 935 DEETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIM-VVDSPGFQnprhqgKDRAATFEELCHNYA 1013
Cdd:cd14921 308 DVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFE------IFEVNSFEQLCINYT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1014 HERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGS 1090
Cdd:cd14921 382 NEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIELIERPNNPP--------------GVLALLDEECWFPKA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1091 SDSVVLERLCaafEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLQQSKREEL 1168
Cdd:cd14921 447 TDKSFVEKLC---TEQGNHPKFQKPKQLKDKTEFS-IIHYAG--KVDYNASAWLTK---NMDPLndNVTSLLNASSDKFV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1169 RSLFQARAKlppvcraVAGLEgtsqqalQRSRMVRRTFASslAAVRRKAPCSQI----KLQMDALTSMIKRSRLHFIHCL 1244
Cdd:cd14921 518 ADLWKDVDR-------IVGLD-------QMAKMTESSLPS--ASKTKKGMFRTVgqlyKEQLGKLMTTLRNTTPNFVRCI 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1245 VPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1324
Cdd:cd14921 582 IPNH--EKRSGK--------------------LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIP 639
|
730 740 750
....*....|....*....|....*....|....*....
gi 2462585723 1325 KLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14921 640 KGF-----MDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
628-1363 |
1.10e-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: 174.57 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvpkgRRDGLPAHIGSMAQRAYWALLNQRRDQSIV 699
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPykrlpiYTEEVIDKykGK----RREEMPPHIFAIADNAYRNMLQDRENQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 700 ALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATF--------TVLRAFGSVSMAHSRSATRFSMVMSLDFNATG 771
Cdd:cd01377 78 ITGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKGTLedqilqanPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 772 RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGM-------GVWSKPEDKqkaaaa 844
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSqgeltidGVDDAEEFK------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 845 faQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRF---EWANYAAEALGCEYEELNTATFKHHL---R 918
Cdd:cd01377 232 --LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELdgtEEADKAAHLLGVNSSDLLKALLKPRIkvgR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 919 QIIQQmtfgpsrwgledeetssGLKMTGVDC-VEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQ----N 993
Cdd:cd01377 310 EWVTK-----------------GQNKEQVVFsVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 994 prhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVD--QNPSQvrlp 1066
Cdd:cd01377 373 ----------SFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfglDLQ--------PTIDliEKPNM---- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1067 agggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtegsSALRTCEQPLQCE----IFHQLGwdPVRYDLTG 1142
Cdd:cd01377 431 ---------GILSILDEECVFPKATDKTFVEKLYSNHLGK-------SKNFKKPKPKKSEahfiLKHYAG--DVEYNIDG 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1143 WLHRAKPNLSAlDAPQVLQQSKREELRSLFqaraklppvcrAVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQI 1222
Cdd:cd01377 493 WLEKNKDPLNE-NVVALLKKSSDPLVASLF-----------KDYEESGGGGGKKKKKGGSFRTVS------------QLH 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1223 KLQMDALTSMIKRSRLHFIHCLVPNpvvESRsgqesppppQPGR-DKpgaggPLALDipalrvQLA--GfhILEALRLHR 1299
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPN---EEK---------KPGKiDA-----PLVLH------QLRcnG--VLEGIRICR 603
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462585723 1300 TGYADHMGLTRFRRQFQVLDAPLLKKlmstseGIDERKAVEELLETLDLEKKAV-AVGHSQVFLK 1363
Cdd:cd01377 604 KGFPNRIIFAEFKQRYSILAPNAIPK------GFDDGKAACEKILKALQLDPELyRIGNTKVFFK 662
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
624-1362 |
1.30e-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: 173.89 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 624 VNESSVLNTLLQRYKAQLLHTCTGPD-LIVLQP--RGPSV--PSAGK-------VPKGRRDGLPAHIGSMAQRAYWALLN 691
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPykYLSSNsdASLGEygseyydTTSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 692 QRRDQSIVALGRSGAGKTTCCEQVLEHLVGM-AGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 770
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 771 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHqmaDSSSFGMGvWS--------KP--EDkqk 840
Cdd:cd14879 161 GRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLD---DPSDYALL-ASygchplplGPgsDD--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 841 aAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVgrkqfmrfewANY-----AAEALGCEY 905
Cdd:cd14879 234 -AEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGnleftydhegGEESAVV----------KNTdvldiVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 906 EELNTA-TFKhhlrqiiqqmtfgpsrwgledeetssgLKMTGVDCVEGM-------------ASGLYQELFAAVVSLINR 971
Cdd:cd14879 303 EDLETSlTYK---------------------------TKLVRKELCTVFldpegaaaqrdelARTLYSLLFAWVVETINQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 972 SFSSHHLSMAS-IMVVDSPGFQNprhQGKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdlPDPSpg 1050
Cdd:cd14879 356 KLCAPEDDFATfISLLDFPGFQN---RSSTGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSV----PATS-- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1051 ttvaVVDqNPSQVRLPAGGGAqdarGLFWVLDEEV-HVEGSSDSVVLERLCAAFEKK-------GAGTEGSSALRTceqp 1122
Cdd:cd14879 427 ----YFD-NSDCVRLLRGKPG----GLLGILDDQTrRMPKKTDEQMLEALRKRFGNHssfiavgNFATRSGSASFT---- 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1123 lqceIFHQLGwdPVRYDLTGWLHRakpNLSALDApqvlqqskreELRSLfqaraklppvcravagLEGTSQqalqrsrmv 1202
Cdd:cd14879 494 ----VNHYAG--EVTYSVEGFLER---NGDVLSP----------DFVNL----------------LRGATQ--------- 529
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1203 rrtFASSLaavrrkapcsqiklqmDALTSMIKRSRLHFIHCLVPNPvvesrsgqeSPPPPQPGRDKpgaggplaldipaL 1282
Cdd:cd14879 530 ---LNAAL----------------SELLDTLDRTRLWSVFCIRPND---------SQLPNSFDKRR-------------V 568
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1283 RVQLAGFHILEALRLHRTGYADHMGLTRFrrqfqvldaplLKKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFL 1362
Cdd:cd14879 569 KAQIRSLGLPELAARLRVEYVVSLEHAEF-----------CERYKSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
674-1363 |
2.90e-43 |
|
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: 170.03 E-value: 2.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 674 LPAHIGSMAQRAYWALLNQRRDQSIVALGRSGAGKTTCCEQVLEHLVgmAGSVDGRVSVEKIR----ATFTVLRAFGSVS 749
Cdd:cd01378 52 VPPHVFALADSAYRNMKSEKENQCVIISGESGAGKTEASKRIMQYIA--AVSGGSESEVERVKdmllASNPLLEAFGNAK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 750 MAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQ--------- 820
Cdd:cd01378 130 TLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRpeqyyyysk 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 821 --------MADSSSFgmgvwskpedkqkaaaafAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGR 885
Cdd:cd01378 210 sgcfdvdgIDDAADF------------------KEVLNAMKVIGFTEEEQDSIFRILAAILHLGniqfaedEEGNAAISD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 886 KQFMRFewanyAAEALGCEYEELNTA-TFkhhlRQIIqqmtfgpSRWGlEDEETSSGLKMTGVDCV-EGMASGLYQELFA 963
Cdd:cd01378 272 TSVLDF-----VAYLLGVDPDQLEKAlTH----RTIE-------TGGG-GRSVYEVPLNVEQAAYArDALAKAIYSRLFD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 964 AVVSLINRSFSSHHLSMASIM-VVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---P 1039
Cdd:cd01378 335 WIVERINKSLAAKSGGKKKVIgVLDIYGFEIFEKNS------FEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIewtP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1040 VQF-------DLpdpspgttvavVDQNPsqvrlpagggaqdaRGLFWVLDEEVHVEG-SSDSVVLERLCAAFEKKGAGTE 1111
Cdd:cd01378 409 IKYfnnkiicDL-----------IEEKP--------------PGIFAILDDACLTAGdATDQTFLQKLNQLFSNHPHFEC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1112 GSSALrtcEQPLQC-EIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKREELRSLFqaraklppvcravagLEG 1190
Cdd:cd01378 464 PSGHF---ELRRGEfRIKHYAG--DVTYNVEGFLDKNKDLLFK-DLKELMQSSSNPFLRSLF---------------PEG 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1191 TSQQALQRSrmvrrTFASslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRSgqesppppqpgrdkpg 1270
Cdd:cd01378 523 VDLDSKKRP-----PTAG-----------TKFKNSANALVETLMKKQPSYIRCIKPN---DNKS---------------- 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1271 aggPLALDIPALRVQLAGFHILEALRLHRTGYAdhmgltrFRRQFqvlDAPLLK-KLMS--TS---EGIDeRKAVEELLE 1344
Cdd:cd01378 568 ---PGEFDEELVLHQVKYLGLLENVRVRRAGFA-------YRQTY---EKFLERyKLLSpkTWpawDGTW-QGGVESILK 633
|
730
....*....|....*....
gi 2462585723 1345 TLDLEKKAVAVGHSQVFLK 1363
Cdd:cd01378 634 DLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
630-1363 |
3.16e-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: 169.94 E-value: 3.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 630 LNTLLQRYKAQLLHTCTGPDLIVLQPRG--------PSVPSAGKVPKGRRDGLPaHIGSMAQRAYWAL----LNQRRDQS 697
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPYKsipllydvPGFDSQRKEEATASSPPP-HVFSIAERAYRAMkgvgKGQGTPQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 698 IVALGRSGAGKTTCCEQVLEHLV-------GMAGSVDGRVSVEKIRATF----TVLRAFGSVSMAHSRSATRFSMVMSLD 766
Cdd:cd14892 83 IVVSGESGAGKTEASKYIMKYLAtasklakGASTSKGAANAHESIEECVllsnLILEAFGNAKTIRNDNSSRFGKYIQIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 767 FNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSFGMGVWSKPEDKQKAAAAFA 846
Cdd:cd14892 163 YNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALEL-TPAESFLFLNQGNCVEVDGVDDATEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 847 QLQGAMEMLGISESEQRAVWRVLAAIYHLGAAgackvgrkqfmRFEwANYAAEALGCEYEELNTATFKHHLRQIIQQMTF 926
Cdd:cd14892 242 QLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNV-----------RFE-ENADDEDVFAQSADGVNVAKAAGLLGVDAAELM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 927 GPSRWgledEETSSG------LKMTGVDCVE---GMASGLYQELFAAVVSLINRSFSSH----HLSMAS------IMVVD 987
Cdd:cd14892 310 FKLVT----QTTSTArgsvleIKLTAREAKNaldALCKYLYGELFDWLISRINACHKQQtsgvTGGAASptfspfIGILD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 988 SPGFQN-PRHqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQFDlpDPSPgtTVAVVDQNPSqv 1063
Cdd:cd14892 386 IFGFEImPTN-------SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIdvsAIEFQ--DNQD--CLDLIQKKPL-- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1064 rlpagggaqdarGLFWVLDEEVHV-EGSSDSVVLERLCAAFEKKGAgtegssalrTCEQP-LQCEIF---HQLGwdPVRY 1138
Cdd:cd14892 453 ------------GLLPLLEEQMLLkRKTTDKQLLTIYHQTHLDKHP---------HYAKPrFECDEFvlrHYAG--DVTY 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1139 DLTGWLHRAKPNLsaldapqvlqqskREELRSLfqaraklppvcravaglegtsqqaLQRSRMVRRtfasslaavrrkap 1218
Cdd:cd14892 510 DVHGFLAKNNDNL-------------HDDLRDL------------------------LRSSSKFRT-------------- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1219 csqiklQMDALTSMIKRSRLHFIHCLVPNPVvesrsgqespppPQPGrdkpGAGGPLALDipalrvQLAGFHILEALRLH 1298
Cdd:cd14892 539 ------QLAELMEVLWSTTPSYIKCIKPNNL------------KFPG----GFSCELVRD------QLIYSGVLEVVRIR 590
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462585723 1299 RTGYADHMGLTRFRRQFQVLDAPLLKKLMS--TSEGIDERKAVeELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14892 591 REGFPIRRQFEEFYEKFWPLARNKAGVAASpdACDATTARKKC-EEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
628-1363 |
2.93e-42 |
|
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: 167.15 E-value: 2.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYkwlpvyNPEVVEGYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMAGSVD-GRVSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 772
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAATGDlAKKKDSKMKGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 773 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqMADSSSFGMGVWSKPE---DKQKAAAAFAQLQ 849
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELL----LITTNPYDYPFISQGEilvASIDDAEELLATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 850 GAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFgpS 929
Cdd:cd14913 236 SAIDILGFTPEEKSGLYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKTAYLMGLNSSDLLKALCF--P 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 930 RWGLEDEETSSGLKMTGVD-CVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 1008
Cdd:cd14913 305 RVKVGNEYVTKGQTVDQVHhAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN------SLEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1009 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLpdpspGTTVAVVdqnpsqVRLpagggAQDARGLFWVLDEEVHV 1087
Cdd:cd14913 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFiDF-----GMDLAAC------IEL-----IEKPMGIFSILEEECMF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1088 EGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKREE 1167
Cdd:cd14913 443 PKATDTSFKNKLYDQHLGKSNNFQKPKVVKG-RAEAHFSLIHYAG--TVDYSVSGWLEKNKDPLNE-TVVGLYQKSSNRL 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1168 LRSLFQ--ARAKLPPVCRAVAGLEGTSQQalqrsrmvrrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLV 1245
Cdd:cd14913 519 LAHLYAtfATADADSGKKKVAKKKGSSFQ--------------TVSALFRE--------NLNKLMSNLRTTHPHFVRCII 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1246 PNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1325
Cdd:cd14913 577 PN---ETKT-------------------PGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPE 634
|
730 740 750
....*....|....*....|....*....|....*...
gi 2462585723 1326 lmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14913 635 ----GQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
628-1247 |
4.60e-42 |
|
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: 165.91 E-value: 4.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSV---PSAGKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGR 703
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGiytEEHSRLYRGAkRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 704 SGAGKTTCCEQVLEHLVGMaGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLL 783
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 784 EKSRVARQPEGESNFLVFSQMLAGLDLDLRTE---LNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISES 860
Cdd:cd01379 161 EKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGFTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 861 EQRAVWRVLAAIYHLG-------AAGACKVGRKQFMRFEWANYAAEALGCEYEElntatfkhhlrqiiqqmtfgpsrwgL 933
Cdd:cd01379 241 EVDSVYSILAAILHIGdieftevESNHQTDKSSRISNPEALNNVAKLLGIEADE-------------------------L 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 934 EDEETSSGLKMTG------------VDCVEGMASGLYQELFAAVVSLINR--SFSSHHLSMA-SIMVVDSPGFQNPRHQg 998
Cdd:cd01379 296 QEALTSHSVVTRGetiirnntveeaTDARDAMAKALYGRLFSWIVNRINSllKPDRSASDEPlSIGILDIFGFENFQKN- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 999 kdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPS-----QVRLpagggaqd 1073
Cdd:cd01379 375 -----SFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVD----------LIEYEDNRPLldmflQKPM-------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1074 arGLFWVLDEEVHVEGSSDSVVLERlcaaFEKkgaGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSA 1153
Cdd:cd01379 432 --GLLALLDEESRFPKATDQTLVEK----FHN---NIKSKYYWRPKSNALSFGIHHYAG--KVLYDASGFLEKNRDTLPP 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1154 lDAPQVLQQSKreelrslfqaraklppvcravaglegtsqqalqrSRMVRRTFAS----SLaavrrkapcsqiklqMDAL 1229
Cdd:cd01379 501 -DVVQLLRSSE----------------------------------NPLVRQTVATyfrySL---------------MDLL 530
|
650
....*....|....*...
gi 2462585723 1230 TSMIKrSRLHFIHCLVPN 1247
Cdd:cd01379 531 SKMVV-GQPHFVRCIKPN 547
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
628-1315 |
1.58e-41 |
|
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: 165.84 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP--SVPSAGKV-----------PKGRRDGLPAHIGSMAQRAYWALL-NQR 693
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPLKPlpDLYSESQLnaykasmtstsPVSQLSELPPHVFAIGGKAFGGLLkPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 694 RDQSIVALGRSGAGKTTCCEQVLEHL--VG-----MAGSVDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSL 765
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLtsVGrdqssTEQEGSDAVEIGKrILQTNPILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 766 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADS---SSFGMGVWSKPEDKQKAA 842
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 843 AAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFM-------RFEWANyAAEALGCEYEELNTATFKH 915
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDAtavtaasRFHLAK-CAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 916 HLRQIIQQMTFGPSRWGLEDEETSsglkmtgvdcvegMASGLYQELFAAVVSLIN---------RSFSSHHLSMASIMVV 986
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGS-------------LAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGIL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 987 DSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfDLPDPSPGTTVAVVDQNPSqvrlp 1066
Cdd:cd14902 388 DIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWK-NISYPSNAACLALFDDKSN----- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1067 agggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGagtegssalrtceqplQCEIFHQLGwdPVRYDLTGWLHR 1146
Cdd:cd14902 456 ---------GLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAG--RVCYNVEQFVEK 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1147 AKPNLSAlDAPQVLQQSKREELRSLFQARAKLPPVCRAVAGLEgtsqqalQRSRMVRrtfASSLAAvrrkapcsQIKLQM 1226
Cdd:cd14902 509 NTDALPA-DASDILSSSSNEVVVAIGADENRDSPGADNGAAGR-------RRYSMLR---APSVSA--------QFKSQL 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1227 DALTSMIKRSRLHFIHCLVPNPVvesrsgqesppppqpgrdkpgaGGPLALDIPALRVQLAGFHILEALRLHRTGYADHM 1306
Cdd:cd14902 570 DRLIVQIGRTEAHYVRCLKPNEV----------------------KKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRL 627
|
....*....
gi 2462585723 1307 GLTRFRRQF 1315
Cdd:cd14902 628 AHASFIELF 636
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
628-1302 |
1.62e-41 |
|
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: 164.73 E-value: 1.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKGRrDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPYKwidnlyGDHLHEQYLKKPR-DKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMAGSVDGRvSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 781
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDK-TIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 782 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESE 861
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 862 QRAVWRVLAAIYHLGAAGACKVGRK--QFMRFEWANYAAEALGCEYEELNTATFKhhlRQIIQQmtfgpsrwgledeETS 939
Cdd:cd14904 240 QRTLFKILSGVLHLGEVMFDKSDENgsRISNGSQLSQVAKMLGLPTTRIEEALCN---RSVVTR-------------NES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 940 SGLKMTGVDCVE---GMASGLYQELFAAVVSLINRSFSS-HHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHE 1015
Cdd:cd14904 304 VTVPLAPVEAEEnrdALAKAIYSKLFDWMVVKINAAISTdDDRIKGQIGVLDIFGFEDFAHNG------FEQFCINYANE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1016 RLQLLFYQRTFVSTLQRYQEEGvpVQFD-LPDPSPGTTVAVVDQNpsqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSV 1094
Cdd:cd14904 378 KLQQKFTTDVFKTVEEEYIREG--LQWDhIEYQDNQGIVEVIDGK---------------MGIIALMNDHLRQPRGTEEA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1095 VLERLCAAFEKKGAGT--EGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKREELRSLF 1172
Cdd:cd14904 441 LVNKIRTNHQTKKDNEsiDFPKVKRT-----QFIINHYAG--PVTYETVGFMEKHRDTLQN-DLLDLVLLSSLDLLTELF 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1173 QAraklppvcravagLEGTSQQALQRSRmvRRTFAsslaavrRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvES 1252
Cdd:cd14904 513 GS-------------SEAPSETKEGKSG--KGTKA-------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPN---AN 567
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1253 RSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGY 1302
Cdd:cd14904 568 KS-------------------PTEFDKRMVVEQLRSAGVIEAIRITRSGY 598
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
627-1247 |
1.64e-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: 164.73 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP-SVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQIlPIYTAEQIRlyRNKKIGeLPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLvgmaGSVDGRVS-VEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQT 780
Cdd:cd01381 81 ESGAGKTESTKLILQYL----AAISGQHSwIEQqILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 781 MLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVwSKPEDKQKAAAAFAQLQGAMEMLGISES 860
Cdd:cd01381 157 YLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGN-CLTCEGRDDAAEFADIRSAMKVLMFTDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 861 EQRAVWRVLAAIYHLGAAG----------ACKVGRKQFmrfewANYAAEALGCEYEELNTATFKHHLrqiiqqMTFGpsr 930
Cdd:cd01381 236 EIWDIFKLLAAILHLGNIKfeatvvdnldASEVRDPPN-----LERAAKLLEVPKQDLVDALTTRTI------FTRG--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 931 wgledEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSF---SSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 1006
Cdd:cd01381 302 -----ETVVSPLSAEQaLDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENFEVN------SFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1007 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDQNPSQVRLpagggAQDARGLFWVLDEEVH 1086
Cdd:cd01381 371 QLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQH----------IEFVDNQDVLDLI-----ALKPMNIMSLIDEESK 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1087 VEGSSDSVVLERLCAAFEKKGAGTEGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKRE 1166
Cdd:cd01381 436 FPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT-----SFGINHFAG--VVFYDTRGFLEKNRDTFSA-DLLQLVQSSKNK 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1167 ELRSLFQAraklppvCRAvAGLEGtsqqalqrsrmvrrtfasslaavRRKAP--CSQIKLQMDALTSMIKRSRLHFIHCL 1244
Cdd:cd01381 508 FLKQLFNE-------DIS-MGSET-----------------------RKKSPtlSSQFRKSLDQLMKTLSACQPFFVRCI 556
|
...
gi 2462585723 1245 VPN 1247
Cdd:cd01381 557 KPN 559
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
627-1363 |
1.98e-41 |
|
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: 164.76 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVA 700
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKwlpvyqKEVMAAYK--GKRRSEAPPHIFAVANNAFQDMLHNRENQSILF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 701 LGRSGAGKTTCCEQVLEHLVGMAGSVDGR----VSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAA 776
Cdd:cd14929 79 TGESGAGKTVNTKHIIQYFATIAAMIESKkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 777 QLQTMLLEKSRVARQPEGESNFLVFSQMLAGldldlrtELNLHQM----ADSSSFGM---GVWSKpeDKQKAAAAFAQLQ 849
Cdd:cd14929 159 DIDIYLLEKSRVIFQQPGERNYHIFYQILSG-------KKELRDLllvsANPSDFHFcscGAVAV--ESLDDAEELLATE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 850 GAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFgpS 929
Cdd:cd14929 230 QAMDILGFLPDEKYGCYKLTGAIMHFG-----NMKFKQKPREE----QLEADGTENADKAAFLMGINSSELVKGLIH--P 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 930 RWGLEDEETSSGLKMTGVDCVEG-MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 1008
Cdd:cd14929 299 RIKVGNEYVTRSQNIEQVTYAVGaLSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYN------SLEQL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1009 CHNYAHERLQLLFYQRTFVSTLQRYQEEG---VPVQFDLpdpspgTTVAVVDQnpsqvrlpagggAQDARGLFWVLDEEV 1085
Cdd:cd14929 373 CINFTNEKLQQFFNQHMFVLEQEEYRKEGidwVSIDFGL------DLQACIDL------------IEKPMGIFSILEEEC 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1086 HVEGSSDSVVLERLC-AAFEKKGAGTEGSSALRTCEqpLQCEIFHQLGWDPvrYDLTGWLHRAKPNLSAlDAPQVLQQSK 1164
Cdd:cd14929 435 MFPKATDLTFKTKLFdNHFGKSVHFQKPKPDKKKFE--AHFELVHYAGVVP--YNISGWLEKNKDLLNE-TVVAVFQKSS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1165 REELRSLFQARAklppvcravaglegTSQQALQRSRMVRRTFASSlaavrrKAPCSQIKLQMDALTSMIKRSRLHFIHCL 1244
Cdd:cd14929 510 NRLLASLFENYI--------------STDSAIQFGEKKRKKGASF------QTVASLHKENLNKLMTNLKSTAPHFVRCI 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1245 VPNPvvesrsgqesppppqpgRDKPGAGGP-LALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDApll 1323
Cdd:cd14929 570 NPNV-----------------NKIPGVLDPyLVLQ------QLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP--- 623
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 2462585723 1324 kKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14929 624 -RTFPKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
627-1363 |
4.61e-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: 163.66 E-value: 4.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKYLPIYSEEIVNmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGSVD------------GRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 770
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKtkkdqssialshGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 771 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKP--EDKqkaaAAFAQL 848
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPgqQDK----ELFAET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 849 QGAMEMLGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKhhlRQIIQ-QMTFG 927
Cdd:cd14932 236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNM-SFKKERNSDQASMPDDTAAQKV-CHLLGMNVTDFT---RAILSpRIKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 928 psRWGLEDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFE 1006
Cdd:cd14932 311 --RDYVQKAQTQEQAEFA----VEALAKASYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFE------IFELNSFE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1007 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPgtTVAVVDQnpsqvrlPAGggaqdARGLFWVLDE 1083
Cdd:cd14932 379 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwsfIDFGL-DLQP--CIELIEK-------PNG-----PPGILALLDE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1084 EVHVEGSSDSVVLERLCaafEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSALD--APQVLQ 1161
Cdd:cd14932 444 ECWFPKATDKSFVEKVV---QEQGNNPKFQKPKKLKDDADFC-IIHYAG--KVDYKANEWLMK---NMDPLNenVATLLN 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1162 QSKREELRSLFQARAKLPPVCRaVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFI 1241
Cdd:cd14932 515 QSTDKFVSELWKDVDRIVGLDK-VAGMGESLHGAFKTRKGMFRTVG------------QLYKEQLMNLMTTLRNTNPNFV 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1242 HCLVPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAP 1321
Cdd:cd14932 582 RCIIPNH--EKKAGKLAH--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 2462585723 1322 LLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14932 640 AIPKGF-----MDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
627-1363 |
5.89e-41 |
|
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: 163.09 E-value: 5.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPS-AGKVPKG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPykRYPVYTNrCAKMYRGkRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK-------IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 775
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSkgsledqVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 776 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL-HQMADSSSFGMGVWSKPedKQKAAAAFAQLQGAMEM 854
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVP--NVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 855 LGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMR---FEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRw 931
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEqdgEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 932 gleDEETSSglkmtgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHN 1011
Cdd:cd14909 318 ---QQVTNS---------IGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG------FEQLCIN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1012 YAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLpdpspgttVAVVDQnpsqvrlpagggAQDARGLFWVLDEEVH 1086
Cdd:cd14909 380 FTNEKLQQFFNHHMFVLEQEEYKREGIDWAFidfgmDL--------LACIDL------------IEKPMGILSILEEESM 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1087 VEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSaldaPQVLQQSKRE 1166
Cdd:cd14909 440 FPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAG--CVSYNITGWLEKNKDPLN----DTVVDQFKKS 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1167 ELRSLFQARAKLPPVCRAVAGLEGTsqqalqrsrmvRRTFASSLAAVRrkapcSQIKLQMDALTSMIKRSRLHFIHCLVP 1246
Cdd:cd14909 514 QNKLLIEIFADHAGQSGGGEQAKGG-----------RGKKGGGFATVS-----SAYKEQLNSLMTTLRSTQPHFVRCIIP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1247 NPVvesrsgqespppPQPGrdkpgaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKL 1326
Cdd:cd14909 578 NEM------------KQPG----------VVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGE 635
|
730 740 750
....*....|....*....|....*....|....*..
gi 2462585723 1327 MstsegiDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14909 636 E------DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
627-1363 |
1.60e-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: 161.73 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAG----KVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPY-KWLPIYGarvaNMYKGKkRTEMPPHLFSISDNAYHDMLMDRENQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMAG----SVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAA 776
Cdd:cd14934 80 GESGAGKTENTKKVIQYFANIGGtgkqSSDGKGSLEdQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 777 QLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqMADSSSF-----GMGVWSKPEDkqkaAAAFAQLQGA 851
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLL--VPNPKEYhwvsqGVTVVDNMDD----GEELQITDVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 852 MEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRF---EWANYAAEALGCEYEELntatfkhhlrqiiqQMTFGP 928
Cdd:cd14934 234 FDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVdttEVADKVAHLMGLNSGEL--------------QKGITR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 929 SRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEE 1007
Cdd:cd14934 300 PRVKVGNEFVQKGQNMEQCnNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN------SFEQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1008 LCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqvrlpagggAQDARGLFWVLD 1082
Cdd:cd14934 374 LCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFidfglDLQ--------ACIDL------------LEKPMGIFSILE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1083 EEVHVEGSSDSVV--------LERLCAAFEKKGAGTEGSSAlrtceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSal 1154
Cdd:cd14934 434 EQCVFPKATDATFkaalydnhLGKSSNFLKPKGGKGKGPEA--------HFELVHYAG--TVGYNITGWLEKNKDPLN-- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1155 dapqvlqqskrEELRSLFQARAKLppVC----RAVAGLEGTSQQALQRSRMVRRTFasslaavrrkapcsqIKLQMDALT 1230
Cdd:cd14934 502 -----------ETVVGLFQKSSLG--LLallfKEEEAPAGSKKQKRGSSFMTVSNF---------------YREQLNKLM 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1231 SMIKRSRLHFIHCLVPNPVVESRsgqesppppqpgrdkpgaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTR 1310
Cdd:cd14934 554 TTLHSTAPHFVRCIVPNEFKQSG----------------------VVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPE 611
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 2462585723 1311 FRRQFQVLDAPLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14934 612 FKQRYQVLNPNVIPQGF-----VDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
629-1363 |
4.46e-40 |
|
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: 160.67 E-value: 4.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 629 VLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpvynPEVVAAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMA----------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 772
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAvtgekkkeesGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 773 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEdkQKAAAAFAQLQGA 851
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFvSQGEITVPS--IDDQEELMATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 852 MEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRW 931
Cdd:cd14918 238 IDILGFTPEEKVSIYKLTGAVMHYGN-----------MKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 932 GLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 1010
Cdd:cd14918 307 KVGNEYVTKGQTVQQVyNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLCI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1011 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEVHVEGS 1090
Cdd:cd14918 381 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---------------PLGIFSILEEECMFPKA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1091 SDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKREELRS 1170
Cdd:cd14918 446 TDTSFKNKLYDQHLGKSANFQKPKVVKG-KAEAHFSLIHYAG--TVDYNITGWLDKNKDPLND-TVVGLYQKSAMKTLAS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1171 LFQ--ARAKLPPVCRAVAGLEGTSQQalqrsrmvrrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVPNp 1248
Cdd:cd14918 522 LFStyASAEADSGAKKGAKKKGSSFQ--------------TVSALFRE--------NLNKLMTNLRSTHPHFVRCIIPN- 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1249 vvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKlms 1328
Cdd:cd14918 579 --ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE--- 634
|
730 740 750
....*....|....*....|....*....|....*
gi 2462585723 1329 tSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14918 635 -GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
628-1247 |
5.42e-40 |
|
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: 160.11 E-value: 5.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP----RGPSVPSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyfdiPKLYSSETIKSYQGKSLGtLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 782
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIE-QRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 783 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLH--QMADSSSFGmgvwskpedkqkaaaafaQLQGAMEMLGISES 860
Cdd:cd01382 161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKdpLLDDVGDFI------------------RMDKAMKKIGLSDE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 861 EQRAVWRVLAAIYHLG----------AAGACKVGRKQFMRFEwanYAAEALGCEYEELntatfKHHLRQIIQQMTFGPS- 929
Cdd:cd01382 222 EKLDIFRVVAAVLHLGniefeengsdSGGGCNVKPKSEQSLE---YAAELLGLDQDEL-----RVSLTTRVMQTTRGGAk 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 930 ----RWGLEDEETSSGLkmtgvdcvEGMASGLYQELFAAVVSLINRS--FSShhlSMASIMVVDSPGFQNPRHQgkdraa 1003
Cdd:cd01382 294 gtviKVPLKVEEANNAR--------DALAKAIYSKLFDHIVNRINQCipFET---SSYFIGVLDIAGFEYFEVN------ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1004 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQnpsqvrlpagggaQD--------AR 1075
Cdd:cd01382 357 SFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVK----------EVEYVDN-------------QDcidlieakLV 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1076 GLFWVLDEEVHVEGSSD----SVVLE------RLCAAFEKKGAGTEgssALRTCEQPLqceIFHQLGwdPVRYDLTGWLH 1145
Cdd:cd01382 414 GILDLLDEESKLPKPSDqhftSAVHQkhknhfRLSIPRKSKLKIHR---NLRDDEGFL---IRHFAG--AVCYETAQFIE 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1146 RakpNLSALDAP--QVLQQSKREELRSLFQARAKLPPVCRAVAGlegtsqqalqrsrmvRRTFASslaaVRRKapcsqIK 1223
Cdd:cd01382 486 K---NNDALHASleSLICESKDKFIRSLFESSTNNNKDSKQKAG---------------KLSFIS----VGNK-----FK 538
|
650 660
....*....|....*....|....
gi 2462585723 1224 LQMDALTSMIKRSRLHFIHCLVPN 1247
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 ... |
628-1363 |
1.15e-39 |
|
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: 159.11 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKwlpvynAEVVAAYRGKK--RSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMAGSVD--------GRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 772
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAIGDrskkdqtpGKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 773 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPEDKQKA---AAAFAQLQ 849
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILS----NKKPELLDMLLITNNPYDYAFISQGETTVASiddAEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 850 GAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPS 929
Cdd:cd14917 236 NAFDVLGFTSEEKNSMYKLTGAIMHFGN-----------MKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 930 RWGLEDEETSSGLKMTGVDCVEG-MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 1008
Cdd:cd14917 305 RVKVGNEYVTKGQNVQQVIYATGaLAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1009 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqvrlpagggAQDARGLFWVLDE 1083
Cdd:cd14917 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgmDLQ--------ACIDL------------IEKPMGIMSILEE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1084 EVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGWdpVRYDLTGWLHRAKPNLSAlDAPQVLQQS 1163
Cdd:cd14917 439 ECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKG-KPEAHFSLIHYAGT--VDYNIIGWLQKNKDPLNE-TVVGLYQKS 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1164 KREELRSLFQARAKlppvcrAVAGLEGTSQQALQRSRMvrrtfaSSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHC 1243
Cdd:cd14917 515 SLKLLSNLFANYAG------ADAPIEKGKGKAKKGSSF------QTVSALHRE--------NLNKLMTNLRSTHPHFVRC 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1244 LVPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLL 1323
Cdd:cd14917 575 IIPN---ETKS-------------------PGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAI 632
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 2462585723 1324 KKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14917 633 PE----GQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
627-1363 |
1.33e-39 |
|
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: 159.10 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKNLPIYSEEIVEmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGSV-----DGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 777
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHkskkdQGELERQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 778 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKP--EDKqkaaAAFAQLQGAMEML 855
Cdd:cd14919 160 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPgqQDK----DMFQETMEAMRIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 856 GISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALGcEYEELNTATFKHHLrqIIQQMTFGpsrwglED 935
Cdd:cd14919 236 GIPEEEQMGLLRVISGVLQLGNI-VFKKERNTDQASMPDNTAAQKVS-HLLGINVTDFTRGI--LTPRIKVG------RD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 936 EETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEELCHNYAH 1014
Cdd:cd14919 306 YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFE------IFDLNSFEQLCINYTN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1015 ERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVavvdqnpsqVRLPAGggaqdARGLFWVLDEEVHVEGSS 1091
Cdd:cd14919 380 EKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIDL---------IEKPAG-----PPGILALLDEECWFPKAT 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1092 DSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLQQSKREELR 1169
Cdd:cd14919 445 DKSFVEKV---VQEQGTHPKFQKPKQLKDKADFC-IIHYAG--KVDYKADEWLMK---NMDPLndNIATLLHQSSDKFVS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1170 SLFQARAKlppvcraVAGLE---GTSQQALQRSRMVRRTFASSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVP 1246
Cdd:cd14919 516 ELWKDVDR-------IIGLDqvaGMSETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFVRCIIP 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1247 NPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKL 1326
Cdd:cd14919 581 NH--EKKAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG 638
|
730 740 750
....*....|....*....|....*....|....*..
gi 2462585723 1327 MstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14919 639 F-----MDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
627-1363 |
1.41e-39 |
|
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: 158.96 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVA 700
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYkwlpvyTAPVVAAYK--GKRRSEAPPHIYAIADNAYNDMLRNRENQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 701 LGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFT-------------VLRAFGSVSMAHSRSATRFSMVMSLDF 767
Cdd:cd14927 79 TGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTggtledqiieanpAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 768 NATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqMADSSSFGMGVWSKPE---DKQKAAAA 844
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML----LVSMNPYDYHFCSQGVttvDNMDDGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 845 FAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAgacKVGRKQfmRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQM 924
Cdd:cd14927 235 LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNM---KFKQKQ--REE----QAEADGTESADKAAYLMGVSSADLLKGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 925 TFGPSRWGleDEETSSGLKMTGVD-CVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraa 1003
Cdd:cd14927 306 LHPRVKVG--NEYVTKGQSVEQVVyAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFN------ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1004 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqvrlpagggAQDARGLF 1078
Cdd:cd14927 378 SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFidfglDLQ--------ACIDL------------IEKPLGIL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1079 WVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGWDPvrYDLTGWLHRAKPNLSALDAPq 1158
Cdd:cd14927 438 SILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKYEAHFEVVHYAGVVP--YNIVGWLDKNKDPLNETVVA- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1159 VLQQSKREELRSLFQARAKLPPVCRAVAGLEGtsqqalqrsrmvRRTFASSLAAVrrkapcSQI-KLQMDALTSMIKRSR 1237
Cdd:cd14927 515 IFQKSQNKLLATLYENYVGSDSTEDPKSGVKE------------KRKKAASFQTV------SQLhKENLNKLMTNLRATQ 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1238 LHFIHCLVPNpvvESRSgqesppppqpgrdkPGAGGPLaLDIPALRVQlagfHILEALRLHRTGYADHMGLTRFRRQFQV 1317
Cdd:cd14927 577 PHFVRCIIPN---ETKT--------------PGVMDPF-LVLHQLRCN----GVLEGIRICRKGFPNRILYADFKQRYRI 634
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 2462585723 1318 LDAPLLKKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14927 635 LNPSAIPD----DKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
627-1363 |
2.66e-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: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSA-GKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPykQLPIYTEAiVEMYRGKkRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGSVDGR----VSVEKIRATFT---VLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 775
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRkepgVPGELERQLLQanpILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 776 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkaAAAFAQLQGAMEML 855
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE---RELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 856 GISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsrwglED 935
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNI-VLKRERNTDQATMPDNTAAQKL-CRLLGLGVTDFSRAL--LTPRIKVG------RD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 936 EETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIM-VVDSPGFQnprhqgKDRAATFEELCHNYAH 1014
Cdd:cd14930 308 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFE------IFQLNSFEQLCINYTN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1015 ERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSS 1091
Cdd:cd14930 382 EKLQQLFNHTMFVLEQEEYQREGIPwtfLDFGL-DLQPCIDLIERPANPP--------------GLLALLDEECWFPKAT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1092 DSVVLERLCaafEKKGAGTEGSSAlRTCEQPLQCEIFHQLG--------W-----DPVRYDLTGWLHRAKPNLSALDAPQ 1158
Cdd:cd14930 447 DKSFVEKVA---QEQGGHPKFQRP-RHLRDQADFSVLHYAGkvdykaneWlmknmDPLNDNVAALLHQSTDRLTAEIWKD 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1159 VLQQSKREELRSLFQAraklPPVCRAVAGLEGTSQQALQRSrmvrrtfasslaavrrkapcsqiklqMDALTSMIKRSRL 1238
Cdd:cd14930 523 VEGIVGLEQVSSLGDG----PPGGRPRRGMFRTVGQLYKES--------------------------LSRLMATLSNTNP 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1239 HFIHCLVPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1318
Cdd:cd14930 573 SFVRCIVPNH--EKRAGKLEP--------------RLVLD------QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 2462585723 1319 DAPLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14930 631 TPNAIPKGF-----MDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
628-1363 |
3.38e-39 |
|
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: 157.65 E-value: 3.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPyqPIAGLYEPATMEqySRRHLGeLPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK-------IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 775
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSLELSLKEKtscveqaILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 776 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL------NLHQMADSssfgmGVWSkpEDKQKAAAAFAQLQ 849
Cdd:cd14873 162 GRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFylstpeNYHYLNQS-----GCVE--DKTISDQESFREVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 850 GAMEMLGISESEQRAVWRVLAAIYHLG-----AAGACKVGRKQFMrfewaNYAAEALGCEYEELNTAtfkhhlrqIIQQM 924
Cdd:cd14873 235 TAMEVMQFSKEEVREVSRLLAGILHLGniefiTAGGAQVSFKTAL-----GRSAELLGLDPTQLTDA--------LTQRS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 925 TFgpsrwgLEDEETSSGLKM-TGVDCVEGMASGLYQELFAAVVSLINRSFSSHHlSMASIMVVDSPGFQNPRHQgkdraa 1003
Cdd:cd14873 302 MF------LRGEEILTPLNVqQAVDSRDSLAMALYARCFEWVIKKINSRIKGKE-DFKSIGILDIFGFENFEVN------ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1004 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpVQFDLPDPSPGTTVAVVDQNpsqvrlpagggaqdaRGLFWVLDE 1083
Cdd:cd14873 369 HFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGL-VWEDIDWIDNGECLDLIEKK---------------LGLLALINE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1084 EVHVEGSSDSVVLERLcaafekKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQS 1163
Cdd:cd14873 433 ESHFPQATDSTLLEKL------HSQHANNHFYVKPRVAVNNFGVKHYAG--EVQYDVRGILEKNRDTFRD-DLLNLLRES 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1164 KREELRSLFQARAKlppvcravAGLEGTSQQALQRsrmvrrtfasslaavRRKAPCSQIKLQMDALTSMIKRSRLHFIHC 1243
Cdd:cd14873 504 RFDFIYDLFEHVSS--------RNNQDTLKCGSKH---------------RRPTVSSQFKDSLHSLMATLSSSNPFFVRC 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1244 LVPNpvVESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYAdhmgltrFRRQFQvldaPLL 1323
Cdd:cd14873 561 IKPN--MQKMPDQFDQ--------------AVVLN------QLRYSGMLETVRIRKAGYA-------VRRPFQ----DFY 607
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 2462585723 1324 KKLMSTSEGI----DERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14873 608 KRYKVLMRNLalpeDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
628-1363 |
6.07e-39 |
|
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: 157.20 E-value: 6.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpvynPEVVTAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMA------------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNA 769
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeitsGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 770 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPEDKQKA---AAAFA 846
Cdd:cd14912 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITS----NKKPELIEMLLITTNPYDYPFVSQGEISVASiddQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 847 QLQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEElnTATFKHHLRQIIQQMTF 926
Cdd:cd14912 235 ATDSAIDILGFTNEEKVSIYKLTGAVMHYG-----NLKFKQKQREE----QAEPDGTEVAD--KAAYLQSLNSADLLKAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 927 GPSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTF 1005
Cdd:cd14912 304 CYPRVKVGNEYVTKGQTVEQVtNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1006 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEV 1085
Cdd:cd14912 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---------------PMGIFSILEEEC 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1086 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKR 1165
Cdd:cd14912 443 MFPKATDTSFKNKLYEQHLGKSANFQKPKVVKG-KAEAHFSLIHYAG--VVDYNITGWLDKNKDPLNE-TVVGLYQKSAM 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1166 EELRSLFQAraklppvcRAVAGLEGTSQQALQRSRMVRRTFASSLAAVRRkapcsqiklQMDALTSMIKRSRLHFIHCLV 1245
Cdd:cd14912 519 KTLAYLFSG--------AQTAEGASAGGGAKKGGKKKGSSFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCII 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1246 PNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1325
Cdd:cd14912 582 PN---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 639
|
730 740 750
....*....|....*....|....*....|....*...
gi 2462585723 1326 lmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14912 640 ----GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
628-1363 |
6.88e-39 |
|
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: 156.81 E-value: 6.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvyNPEVVTAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMA------------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNA 769
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeaasGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 770 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPE---DKQKAAAAFA 846
Cdd:cd14915 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEitvPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 847 QLQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTF 926
Cdd:cd14915 235 ATDSAVDILGFSADEKVAIYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKAAYLTSLNSADLLKALCY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 927 gpSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTF 1005
Cdd:cd14915 306 --PRVKVGNEYVTKGQTVQQVyNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1006 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEV 1085
Cdd:cd14915 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---------------PMGIFSILEEEC 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1086 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKR 1165
Cdd:cd14915 443 MFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKG-KAEAHFSLVHYAG--TVDYNIAGWLDKNKDPLNE-TVVGLYQKSGM 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1166 EELRSLFQAraklppvcRAVAGLEGTSQQALQRSRmvrrtfASSLAAVRrkapcSQIKLQMDALTSMIKRSRLHFIHCLV 1245
Cdd:cd14915 519 KTLAFLFSG--------GQTAEAEGGGGKKGGKKK------GSSFQTVS-----ALFRENLNKLMTNLRSTHPHFVRCLI 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1246 PNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1325
Cdd:cd14915 580 PN---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
|
730 740 750
....*....|....*....|....*....|....*...
gi 2462585723 1326 lmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14915 638 ----GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
629-1058 |
1.20e-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: 155.91 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 629 VLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALGR 703
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIAVNPfkRLPHLYDAHMMEqyKGAPLGeLSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 704 SGAGKTTCCEQVLEHLVGMAG--SVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 781
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 782 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGMGVWSKPEDkqkaaaaFAQLQGAMEML 855
Cdd:cd01384 163 LLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 856 GISESEQRAVWRVLAAIYHLG--------AAGACKVGRKQfMRFEWANyAAEALGCEYEELNTATFKhhlRQIIqqmtfg 927
Cdd:cd01384 236 GISEEEQDAIFRVVAAILHLGniefskgeEDDSSVPKDEK-SEFHLKA-AAELLMCDEKALEDALCK---RVIV------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 928 psrwgLEDEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQnprhQGKDRaaTFE 1006
Cdd:cd01384 305 -----TPDGIITKPLDPDAaTLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE----SFKTN--SFE 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462585723 1007 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQF-------DLPDPSPGTTVAVVDQ 1058
Cdd:cd01384 374 QFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDwsyIEFvdnqdvlDLIEKKPGGIIALLDE 435
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
628-1363 |
1.31e-38 |
|
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: 155.99 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR---RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGR 703
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPyKWLPVYNAEVVAAYRgkkRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 704 SGAGKTTCCEQVLEHLVGMAG-----------SVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 772
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAigdrskkenpnANKGTLEDQIIQAN-PALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 773 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAG-----LDLDLRTElNLHQMADSSSFGMGVWSKPEDKqkaaaAFAQ 847
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNkkpelLDMLLVTN-NPYDYAFVSQGEVSVASIDDSE-----ELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 848 LQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFG 927
Cdd:cd14916 235 TDSAFDVLGFTAEEKAGVYKLTGAIMHYGN-----------MKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 928 PSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 1006
Cdd:cd14916 304 HPRVKVGNEYVTKGQSVQQVyYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1007 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqvrlpagggAQDARGLFWVL 1081
Cdd:cd14916 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFidfgmDLQ--------ACIDL------------IEKPMGIMSIL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1082 DEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQ 1161
Cdd:cd14916 438 EEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKG-KQEAHFSLVHYAG--TVDYNILGWLEKNKDPLNE-TVVGLYQ 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1162 QSKREELRSLFQARAKlppvcrAVAGLEGTSQQALQRSRMVRrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFI 1241
Cdd:cd14916 514 KSSLKLMATLFSTYAS------ADTGDSGKGKGGKKKGSSFQ-----TVSALHRE--------NLNKLMTNLKTTHPHFV 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1242 HCLVPNPvvesrsgqesppppqpgRDKPGaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAP 1321
Cdd:cd14916 575 RCIIPNE-----------------RKAPG-----VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 632
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 2462585723 1322 LLKKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
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 ... |
628-1363 |
2.47e-38 |
|
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: 155.27 E-value: 2.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR---RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGR 703
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPyKWLPVYNAEVVTAYRgkkRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 704 SGAGKTTCCEQVLEHLVGMAGSVDGR---VSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 772
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKkeeATSGKMQGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 773 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEdkQKAAAAFAQLQGA 851
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFvSQGEITVPS--IDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 852 MEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRW 931
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGN-----------MKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 932 GLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 1010
Cdd:cd14910 309 KVGNEYVTKGQTVQQVyNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1011 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEVHVEGS 1090
Cdd:cd14910 383 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---------------PMGIFSILEEECMFPKA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1091 SDSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCE--IFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKREEL 1168
Cdd:cd14910 448 TDTSFKNKL---YEQHLGKSNNFQKPKPAKGKVEAHfsLIHYAG--TVDYNIAGWLDKNKDPLNE-TVVGLYQKSSMKTL 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1169 RSLFQARAKLPpvCRAVAGLEGTSQQAlqrsrmvrRTFASSLAAVRRkapcsqiklQMDALTSMIKRSRLHFIHCLVPNp 1248
Cdd:cd14910 522 ALLFSGAAAAE--AEEGGGKKGGKKKG--------SSFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCIIPN- 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1249 vvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKlms 1328
Cdd:cd14910 582 --ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE--- 637
|
730 740 750
....*....|....*....|....*....|....*
gi 2462585723 1329 tSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14910 638 -GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
629-1318 |
5.67e-38 |
|
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: 153.91 E-value: 5.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 629 VLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAGKVPKGR-----RDGLPAHIGSMAQRAYWALLNQ----RRDQSIV 699
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKY-LHIYEKEVSQKykcekKSSLPPHIFAVADRAYQSMLGRlargPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 700 ALGRSGAGKTTCCEQVLEHLVGMAgsvDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQL 778
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELC---RGNSQLEQqILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGAKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 779 QTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKpEDKQKAAAAFAQLQGAMEMLGIS 858
Cdd:cd14889 158 NEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCK-REVQYWKKKYDEVCNAMDMVGFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 859 ESEQRAVWRVLAAIYHLGA-------AGACKVGRKQfmrFEWANYAAEALGCEYEEL-----NTATF-------KHHLRQ 919
Cdd:cd14889 237 EQEEVDMFTILAGILSLGNitfemddDEALKVENDS---NGWLKAAAGQFGVSEEDLlktltCTVTFtrgeqiqRHHTKQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 920 IIQqmtfgpsrwgledeetssglkmtgvDCVEGMASGLYQELFAAVVSLINRSFS---SHHLSMASIMVVDSPGFQnprH 996
Cdd:cd14889 314 QAE-------------------------DARDSIAKVAYGRVFGWIVSKINQLLApkdDSSVELREIGILDIFGFE---N 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 997 QGKDRaatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPSQVRLPAgggaqDARG 1076
Cdd:cd14889 366 FAVNR---FEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWK----------EITYKDNKPILDLFLN-----KPIG 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1077 LFWVLDEEVHVEGSSDSVVLERLCAAFekKGAGTEGSSALRTceqPLqCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlda 1156
Cdd:cd14889 428 ILSLLDEQSHFPQATDESFVDKLNIHF--KGNSYYGKSRSKS---PK-FTVNHYAG--KVTYNASGFLEKNRDTIPA--- 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1157 pqvlqqSKREE-LRSLFQARAKLPPVCRAVAGLEGTSQQALQRSrmvrrtfASSLAAVRRKAPCSQIKLQMDALTSMIKR 1235
Cdd:cd14889 497 ------SIRTLfINSATPLLSVLFTATRSRTGTLMPRAKLPQAG-------SDNFNSTRKQSVGAQFKHSLGVLMEKMFA 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1236 SRLHFIHCLVPNPVvesrsgqespppPQPGRdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQF 1315
Cdd:cd14889 564 ASPHFVRCIKPNHV------------KVPGQ----------LDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERY 621
|
...
gi 2462585723 1316 QVL 1318
Cdd:cd14889 622 KIL 624
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
628-1036 |
1.13e-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: 152.69 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRY-KAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvPKGRRDglPaHIGSMAQRAYWALLNQRRDQSI 698
Cdd:cd01380 2 AVLHNLKVRFcQRNAIYTYCGIVLVAINPyedlpiYGEDIIQAysGQ-NMGELD--P-HIFAIAEEAYRQMARDEKNQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 699 VALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 777
Cdd:cd01380 78 IVSGESGAGKTVSAKYAMRYFATVGGSSSGETQVEeKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 778 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqmADSSSF---GMGvwSKPE-DKQKAAAAFAQLQGAME 853
Cdd:cd01380 158 MRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHL---GSAEDFfytNQG--GSPViDGVDDAAEFEETRKALT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 854 MLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRFEWA---NYAAEALGCEYEElntatFKHHL-RQIIQQMTfgps 929
Cdd:cd01380 233 LLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDehlQIACELLGIDESQ-----LAKWLcKRKIVTRS---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 930 rwgledEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRSFSSHHLS--MASIMVVDSPGFQ----Nprhqgkdra 1002
Cdd:cd01380 304 ------EVIVKPLTLQqAIVARDALAKHIYAQLFDWIVDRINKALASPVKEkqHSFIGVLDIYGFEtfevN--------- 368
|
410 420 430
....*....|....*....|....*....|....
gi 2462585723 1003 aTFEELCHNYAHERLQLLFYQRTFvstlQRYQEE 1036
Cdd:cd01380 369 -SFEQFCINYANEKLQQQFNQHVF----KLEQEE 397
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
627-1363 |
2.16e-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: 152.53 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKNLPIYSEEIVEmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGS------------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 770
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslalSHGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 771 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkAAAAFAQLQG 850
Cdd:cd15896 160 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQ--DKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 851 AMEMLGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKhhlRQIIQ-QMTFGps 929
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNM-SFKKERHTDQASMPDNTAAQKV-CHLMGMNVTDFT---RAILSpRIKVG-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 930 RWGLEDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEEL 1008
Cdd:cd15896 311 RDYVQKAQTQEQAEFA----VEALAKATYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFE------IFELNSFEQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1009 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEV 1085
Cdd:cd15896 381 CINYTNEKLQQLFNHTMFILEQEEYQREGIEwsfIDFGL-DLQPCIDLIEKPASPP--------------GILALLDEEC 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1086 HVEGSSDSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKR 1165
Cdd:cd15896 446 WFPKATDKSFVEKV---LQEQGTHPKFFKPKKLKDEADFC-IIHYAG--KVDYKADEWLMKNMDPLND-NVATLLNQSTD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1166 EELRSLFQARAKLPPVCRaVAGLEGTSQQALQRSRMVRRTfasslaavrrkapcSQI-KLQMDALTSMIKRSRLHFIHCL 1244
Cdd:cd15896 519 KFVSELWKDVDRIVGLDK-VSGMSEMPGAFKTRKGMFRTV--------------GQLyKEQLSKLMATLRNTNPNFVRCI 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1245 VPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1324
Cdd:cd15896 584 IPNH--EKKAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIP 641
|
730 740 750
....*....|....*....|....*....|....*....
gi 2462585723 1325 KLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd15896 642 KGF-----MDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
628-1363 |
4.07e-37 |
|
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: 151.38 E-value: 4.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvyNPEVVAAYRGKK--RQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMA-----------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 770
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 771 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPE---DKQKAAAAFAQ 847
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMS----NKKPELIDLLLISTNPFDFPFVSQGEvtvASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 848 LQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFg 927
Cdd:cd14923 235 TDNAIDILGFSSEEKVGIYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKAGYLMGLNSAEMLKGLCC- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 928 pSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 1006
Cdd:cd14923 305 -PRVKVGNEYVTKGQNVQQVtNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1007 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEVH 1086
Cdd:cd14923 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---------------PMGIFSILEEECM 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1087 VEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKRE 1166
Cdd:cd14923 443 FPKATDTSFKNKLYDQHLGKSNNFQKPKPAKG-KAEAHFSLVHYAG--TVDYNIAGWLDKNKDPLNE-TVVGLYQKSSLK 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1167 ELRSLFQARAKlppvcrAVAGLEGTSQQALQRsrmvRRTFASSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVP 1246
Cdd:cd14923 519 LLSFLFSNYAG------AEAGDSGGSKKGGKK----KGSSFQTVSAVFRE--------NLNKLMTNLRSTHPHFVRCLIP 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1247 NpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKl 1326
Cdd:cd14923 581 N---ETKT-------------------PGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPE- 637
|
730 740 750
....*....|....*....|....*....|....*..
gi 2462585723 1327 mstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14923 638 ---GQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
627-1247 |
8.39e-37 |
|
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: 150.57 E-value: 8.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKV-----------PKGRRDGLPAHIGSMAQRAYWALLNQR 693
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPykQIDNLFSEEVMqmykeqiiqngEYFDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 694 RDQSIVALGRSGAGKT---TCC--------------EQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRS 755
Cdd:cd14907 81 KKQAIVISGESGAGKTenaKYAmkfltqlsqqeqnsEEVLTLTSSIRATSKSTKSIEqKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 756 ATRFSMVMSLDFN-ATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqMADSSSFGMGVWSK 834
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGL--KNQLSGDRYDYLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 835 PE----DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKQFMRfewanYAAEA 900
Cdd:cd14907 239 SNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGnlqfddstldDNSPCCVKNKETLQ-----IIAKL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 901 LGCEYEELNTA-TFKhhLRQIIQQMTFGPsrwgledeetssglkMTGVDCV---EGMASGLYQELFAAVVSLINRSFSSH 976
Cdd:cd14907 314 LGIDEEELKEAlTTK--IRKVGNQVITSP---------------LSKKECInnrDSLSKELYDRLFNWLVERLNDTIMPK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 977 HLS--------MASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLP 1045
Cdd:cd14907 377 DEKdqqlfqnkYLSIGLLDIFGFEVFQNNS------FEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdylNQLSYT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1046 DPSPgtTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAafekkgagTEGSSALRTCEQPLQC 1125
Cdd:cd14907 451 DNQD--VIDLLDKPPI--------------GIFNLLDDSCKLATGTDEKLLNKIKK--------QHKNNSKLIFPNKINK 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1126 EIF---HQLGwdPVRYDLTGWLHRAKPNLSaLDAPQVLQQSKREELRSLFQAraklppvcravaglEGTSQQALQRSRMV 1202
Cdd:cd14907 507 DTFtirHTAK--EVEYNIEGFREKNKDEIS-QSIINCIQNSKNRIISSIFSG--------------EDGSQQQNQSKQKK 569
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2462585723 1203 RRtfasslaaVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPN 1247
Cdd:cd14907 570 SQ--------KKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPN 606
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
593-1400 |
9.23e-37 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 151.72 E-value: 9.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 593 DKTITEVDEEHVHRANPP-ELDQVEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR 670
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPfKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 671 R----DGLPAHIGSMAQRAYWALLNQRRDQSIVALGRSGAGKTTCCEQVLEHLV-GMAGSVDGRVSvEKIRATFTVLRAF 745
Cdd:PTZ00014 155 DakdsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAsSKSGNMDLKIQ-NAIMAANPVLEAF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 746 GSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMA--- 822
Cdd:PTZ00014 234 GNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEeyk 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 823 -------------DSSSFGMGVWSkpedkqkaaaafaqlqgaMEMLGISESEQRAVWRVLAAIYHLGAA----------- 878
Cdd:PTZ00014 314 yinpkcldvpgidDVKDFEEVMES------------------FDSMGLSESQIEDIFSILSGVLLLGNVeiegkeegglt 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 879 -GACKVGRKQfmrfEWANYAAEALGCEYEELntatfKHHLrqIIQQMTFGP----SRWGLEDEETSsglkmtgvdcVEGM 953
Cdd:PTZ00014 376 dAAAISDESL----EVFNEACELLFLDYESL-----KKEL--TVKVTYAGNqkieGPWSKDESEML----------KDSL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 954 ASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVST 1029
Cdd:PTZ00014 435 SKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEvfknN----------SLEQLFINITNEMLQKNFVDIVFERE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1030 LQRYQEEGVP---VQFdlpdpspgTTvavvdqNPSQVRLPAGGGaqdaRGLFWVLDEEVHVEGSSDsvvlERLCAAFEKK 1106
Cdd:PTZ00014 505 SKLYKDEGISteeLEY--------TS------NESVIDLLCGKG----KSVLSILEDQCLAPGGTD----EKFVSSCNTN 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1107 gagTEGSSALRTCE--QPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKREELRSLFqaraklppvcra 1184
Cdd:PTZ00014 563 ---LKNNPKYKPAKvdSNKNFVIKHTIG--DIQYCASGFLFKNKDVLRP-ELVEVVKASPNPLVRDLF------------ 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1185 vaglEGtsqQALQRSRMVRRTFASslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRSgqesppppqp 1264
Cdd:PTZ00014 625 ----EG---VEVEKGKLAKGQLIG-----------SQFLNQLDSLMSLINSTEPHFIRCIKPN---ENKK---------- 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1265 grdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLlkklmSTSEGIDERKAVEELLE 1344
Cdd:PTZ00014 674 ---------PLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAV-----SNDSSLDPKEKAEKLLE 739
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462585723 1345 TLDLEKKAVAVGHSQVFLKAGVISRL-EKQREKLVS-QSIV-LFQAACKGFLSRQEFKK 1400
Cdd:PTZ00014 740 RSGLPKDSYAIGKTMVFLKKDAAKELtQIQREKLAAwEPLVsVLEALILKIKKKRKVRK 798
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
628-1362 |
2.48e-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: 148.78 E-value: 2.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-----------RGPSVPSAGKVPKGRRDgLPAHIGSMAQRAYWALLNQRR-- 694
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPfrrlplyddetKEAYYEHGERRAAGERK-LPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 695 --DQSIVALGRSGAGKTTCCEQVLEHLVGMA------GSVDGRVSV-EKIRATFTVLRAFGSVSMAHSRSATRFSMVMSL 765
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgQNATERENVrDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 766 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAF 845
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 846 AQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQfMRFEWANYAAEALGCEYEELNTATFKHHL--RQIIQQ 923
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEG-GTFSMSSLANVRAACDLLGLDMDVLEKTLctREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 924 MTFGPSRWGLEDEETSSglkmtgvdcvEGMASGLYQELFAAVVSLINRS--FSSHHLSMASIMVVDSPGF----QNprhq 997
Cdd:cd14901 320 GEYITMPLSVEQALLTR----------DVVAKTLYAQLFDWLVDRINESiaYSESTGASRFIGIVDIFGFeifaTN---- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 998 gkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdLPDPSPGTTVAVVDQNPSqvrlpagggaqdarGL 1077
Cdd:cd14901 386 ------SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTF-VEYPNNDACVAMFEARPT--------------GL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1078 FWVLDEEVHVEGSSDSVVLERLCAAFEKKgagteGSSALRTCEQPLQC-EIFHQLGwdPVRYDLTGWLHRAKPNLSAlDA 1156
Cdd:cd14901 445 FSLLDEQCLLPRGNDEKLANKYYDLLAKH-----ASFSVSKLQQGKRQfVIHHYAG--AVCYATDGFCDKNKDHVHS-EA 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1157 PQVLQQSKREELrslfqaraklppvcravaglegtsqqalqrsrmvrrtfASSLAAvrrkapcsQIKLQMDALTSMIKRS 1236
Cdd:cd14901 517 LALLRTSSNAFL--------------------------------------SSTVVA--------KFKVQLSSLLEVLNAT 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1237 RLHFIHCLVPNPVVESRSgqesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQ 1316
Cdd:cd14901 551 EPHFIRCIKPNDVLSPSE----------------------FDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYS 608
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 2462585723 1317 VLDAPLLKKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFL 1362
Cdd:cd14901 609 CLAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVFL 654
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
628-1363 |
1.55e-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: 146.75 E-value: 1.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSV-PSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALGR 703
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKflPIYnPKYVKMYQNRRLGkLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 704 SGAGKTTCCEQVLEHLVgmAGSVDGRVS-VEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 781
Cdd:cd01385 82 SGSGKTESTNFLLHHLT--ALSQKGYGSgVEQtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 782 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGmgvwskpEDKQKAAAAFAQLQGAMEML 855
Cdd:cd01385 160 LLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLkqpedyHYLNQSDCYT-------LEGEDEKYEFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 856 GISESEQRAVWRVLAAIYHLgaagackvGRKQFMRfeWANYAAEALGCEYEE-LNTATfkhHLRQIIQQMtfgpsrwgLE 934
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHL--------GNIEYKK--KAYHRDESVTVGNPEvLDIIS---ELLRVKEET--------LL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 935 DEETSSGLKMTGVDCV------------EGMASGLYQELFAAVV-----SLINRSFSSHHlSMASIMVVDSPGFQNPRHQ 997
Cdd:cd01385 292 EALTTKKTVTVGETLIlpyklpeaiatrDAMAKCLYSALFDWIVlrinhALLNKKDLEEA-KGLSIGVLDIFGFEDFGNN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 998 gkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFdlpdpspgttvavVDqNPSQVRLPAGggaqDA 1074
Cdd:cd01385 371 ------SFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISwhnIEY-------------TD-NTGCLQLISK----KP 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1075 RGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtegssalRTCEQPLQCE----IFHQLGwdPVRYDLTGWLHRAKPN 1150
Cdd:cd01385 427 TGLLCLLDEESNFPGATNQTLLAKFKQQHKDN----------KYYEKPQVMEpafiIAHYAG--KVKYQIKDFREKNLDL 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1151 LSAlDAPQVLQQSK----RE-------------ELRSLFQARAKLPPVCRA----VAGLEGTSQQALQRSRMVRRTfass 1209
Cdd:cd01385 495 MRP-DIVAVLRSSSsafvREligidpvavfrwaVLRAFFRAMAAFREAGRRraqrTAGHSLTLHDRTTKSLLHLHK---- 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1210 laavRRKAPCSQIKLQ--MDALTSMIKRSRLHFIHCLVPNpvvesrsgqesppppqpgRDKpgagGPLALDIPALRVQLA 1287
Cdd:cd01385 570 ----KKKPPSVSAQFQtsLSKLMETLGQAEPFFIRCIKSN------------------AEK----KPLRFDDELVLRQLR 623
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462585723 1288 GFHILEALRLHRTGYADHMGLTRFRRQFQVLdapLLKKLMSTSEGIderkavEELLETLDLEKKAVAVGHSQVFLK 1363
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, ... |
627-1302 |
2.79e-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: 139.50 E-value: 2.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSV---PSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDiygLEQVQQYSGRALGeLPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAtGRITAAQLQTML 782
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLVT-EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 783 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL---------HQMADSSSFGMGvwskpedkqkAAAAFAQLQGAME 853
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLqeaekyfylNQGGNCEIAGKS----------DADDFRRLLAAMQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 854 MLGISESEQRAVWRVLAAIYHLG-----------AAGACKVGRKQFMRfewanYAAEALGCEYEELNTA-TFKhhLRQII 921
Cdd:cd01387 229 VLGFSSEEQDSIFRILASVLHLGnvyfhkrqlrhGQEGVSVGSDAEIQ-----WVAHLLQISPEGLQKAlTFK--VTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 922 QQMTFGPsrwgLEDEEtssglkmtGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdr 1001
Cdd:cd01387 302 RERIFTP----LTIDQ--------ALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1002 aaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpvqfdlpdpsPGTTVAVVDQNPSQVRLpagggAQDARGLFWVL 1081
Cdd:cd01387 366 --SFEQLCINYANENLQYYFNKHVFKLEQEEYIREQI----------DWTEIAFADNQPVINLI-----SKKPVGILHIL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1082 DEEVHVEGSSDSVVLERlCaafEKKGAGTEGSSALRTCEQPLQceIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQ 1161
Cdd:cd01387 429 DDECNFPQATDHSFLEK-C---HYHHALNELYSKPRMPLPEFT--IKHYAG--QVWYQVHGFLDKNRDQLRQ-DVLELLV 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1162 QSKREELRSLF-----QARAKLPpvcravAGLEGTSQQALQRSRMVRRTFASSLaavrrkapcsqiklqMDALTSMiKRS 1236
Cdd:cd01387 500 SSRTRVVAHLFsshraQTDKAPP------RLGKGRFVTMKPRTPTVAARFQDSL---------------LQLLEKM-ERC 557
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462585723 1237 RLHFIHCLVPNpvvesrsgqesppppqpgRDKpgagGPLALDIPALRVQLAGFHILEALRLHRTGY 1302
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 ... |
627-1318 |
2.85e-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: 136.06 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP----SVPSAGKVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSlplfSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLVGMAGSVDgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQLQTML 782
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQT-EDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASVSHYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 783 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSF----GMGVWSKPEDKqkaaAAFAQLQGAMEMLGIS 858
Cdd:cd14896 159 LETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYlnqgGACRLQGKEDA----QDFEGLLKALQGLGLC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 859 ESEQRAVWRVLAAIYHLGaaGACkvgrkqFMRFEWANYAAEALGCEYEELNTATFKH----HLRQII-QQMTFGPSRWgl 933
Cdd:cd14896 234 AEELTAIWAVLAAILQLG--NIC------FSSSERESQEVAAVSSWAEIHTAARLLQvppeRLEGAVtHRVTETPYGR-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 934 edeeTSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFS--SHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCH 1010
Cdd:cd14896 304 ----VSRPLPVEGaIDARDALAKTLYSRLFTWLLKRINAWLAppGEAESDATIGVVDAYGFEALRVNG------LEQLCI 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1011 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdLPDPSPgttvavvdQNPSQVRLPAGggaqDARGLFWVLDEEVHVEGS 1090
Cdd:cd14896 374 NLASERLQLFSSQTLLAQEEEECQRELLPW---VPIPQP--------PRESCLDLLVD----QPHSLLSILDDQTWLSQA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1091 SDSVVLErlcaafekKGAGTEGSSALRTCEQpLQCEIF---HQLGwdPVRYDLTGWLHRakpNLSALDaPQVLQ---QSK 1164
Cdd:cd14896 439 TDHTFLQ--------KCHYHHGDHPSYAKPQ-LPLPVFtvrHYAG--TVTYQVHKFLNR---NRDQLD-PAVVEmlaQSQ 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1165 REELRSLFQaraklppvcravaglEGTSQQALQRSRmvrrtfaSSLAavrrkapcSQIKLQMDALTSMIKRSRLHFIHCL 1244
Cdd:cd14896 504 LQLVGSLFQ---------------EAEPQYGLGQGK-------PTLA--------SRFQQSLGDLTARLGRSHVYFIHCL 553
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462585723 1245 VPNPVvesrsgqesppppqpgrDKPGaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1318
Cdd:cd14896 554 NPNPG-----------------KLPG-----LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL 605
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
628-1251 |
2.28e-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: 133.95 E-value: 2.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGRRD-----GLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDinqnkSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 702 GRSGAGKTTCCEQVLEHLVGMAGSV--------DGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT-G 771
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNqqqnnnnnNNNNSIEKdILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 772 RITAAQLQTMLLEKSRVARQPEGES-NFLVFSQMLAGLDLDLRTELNLHQMADS-----------SSF---GMGVWSKPE 836
Cdd:cd14906 162 KIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNDPSKyryldarddviSSFksqSSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 837 DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEwanyaAEALGCEYEELnTATFKHH 916
Cdd:cd14906 242 NKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGN-----------IEFE-----EDSDFSKYAYQ-KDKVTAS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 917 LRQIIQQMTFGPSRWglEDEETSSGLKMTGVDCV--------------EGMASGLYQELFAAVVSLINRSF----SSHHL 978
Cdd:cd14906 305 LESVSKLLGYIESVF--KQALLNRNLKAGGRGSVycrpmevaqseqtrDALSKSLYVRLFKYIVEKINRKFnqntQSNDL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 979 SMAS-------IMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpvqfdlpdpsPGT 1051
Cdd:cd14906 383 AGGSnkknnlfIGVLDIFGFENLSSN------SLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGI----------PWS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1052 TVAVVDqNPSQVRLPagggAQDARGLFWVLDEEVHVEGSSDSVVLERlcaaFEKKGAGTEgSSALRTCEQpLQCEIFHQL 1131
Cdd:cd14906 447 NSNFID-NKECIELI----EKKSDGILSLLDDECIMPKGSEQSLLEK----YNKQYHNTN-QYYQRTLAK-GTLGIKHFA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1132 GwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKREELRSLFQARAKLPPvcravaglegTSQQalqrsrmvRRTFASSLA 1211
Cdd:cd14906 516 G--DVTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT----------NTTK--------KQTQSNTVS 574
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2462585723 1212 avrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVE 1251
Cdd:cd14906 575 --------GQFLEQLNQLIQTINSTSVHYIRCIKPNQTMD 606
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
675-1105 |
5.92e-31 |
|
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: 132.09 E-value: 5.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 675 PAHIGSMAQRAYWALLNQRRDQSIVALGRSGAGKTTCCEQVLEHLV--GMAGSVDGRVSVEKIRATFT------------ 740
Cdd:cd14891 55 PYAIAEMAYQQMCLGSGRMQNQSIVISGESGAGKTETSKIILRFLTtrAVGGKKASGQDIEQSSKKRKlsvtslderlmd 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 741 ---VLRAFGSVSMAHSRSATRFSMVMSLDFNATG-RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL 816
Cdd:cd14891 135 tnpILESFGNAKTLRNHNSSRFGKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKEL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 817 NLhqmadsssfgmgvwSKPEDKQKAAAAF-------------AQLQGAMEMLGISESEQRAVWRVLAAIYHLG------- 876
Cdd:cd14891 215 LL--------------LSPEDFIYLNQSGcvsddniddaanfDNVVSALDTVGIDEDLQLQIWRILAGLLHLGniefdee 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 877 --AAGACKVGRKQFMrfEWANYAAEALGCEYEELntatfkhhLRQIIQQ--MTFGPSRWGLEDEETSSGLKmtgvdcvEG 952
Cdd:cd14891 281 dtSEGEAEIASESDK--EALATAAELLGVDEEAL--------EKVITQReiVTRGETFTIKRNAREAVYSR-------DA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 953 MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNprhqgKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQR 1032
Cdd:cd14891 344 IAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFES-----FETKNDFEQLLINYANEALQATFNQQVFIAEQEL 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462585723 1033 YQEEGVPV-QFDLPDpspgttvavvdqNPSQVRLPagggAQDARGLFWVLDEEVHVEGSSDSVVLERLCAAFEK 1105
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 ... |
677-1253 |
8.11e-31 |
|
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: 132.08 E-value: 8.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 677 HIGSMAQRAYWALLNQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSV---EKIRATFTVLRAFGSVSMAHS 753
Cdd:cd14887 63 HPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQgleARLLQSGPVLEAFGNAHTVLN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 754 RSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLdlrtelnlhqmadSSSFGMGVWS 833
Cdd:cd14887 143 ANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVA-------------AATQKSSAGE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 834 K-PEdkqkaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQfmRFEWANYAAEALGC--------- 903
Cdd:cd14887 210 GdPE-----STDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPE--TSKKRKLTSVSVGCeetaadrsh 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 904 --EYEELN-----TATFKHHLRQIIQQMTFGPSRWGLED----------EETSSGLKMTGVDCVEGMAS-GLYQELFAAV 965
Cdd:cd14887 283 ssEVKCLSsglkvTEASRKHLKTVARLLGLPPGVEGEEMlrlalvsrsvRETRSFFDLDGAAAARDAACkNLYSRAFDAV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 966 VSLINRSFSSHHLSMAS--------------IMVVDSPGFQNPRHQGKDRaatFEELCHNYAHERLQLLFYQRTFVSTLQ 1031
Cdd:cd14887 363 VARINAGLQRSAKPSESdsdedtpsttgtqtIGILDLFGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHM 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1032 RYQEEGVPVQFDL-PDPSPGTTVAVVDQNPSQVRLPAGGGAQDARGLFWVLDEEVHVEGSSDSVVLE-------RLCA-- 1101
Cdd:cd14887 440 LYTQEGVFQNQDCsAFPFSFPLASTLTSSPSSTSPFSPTPSFRSSSAFATSPSLPSSLSSLSSSLSSsppvwegRDNSdl 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1102 AFEKKGAGTEGSSALRTCEQPLQCE-----IFHQLGwdPVRYDLTGWLHRAKPNLSaldapqvlqqskrEELRSLFQAra 1176
Cdd:cd14887 520 FYEKLNKNIINSAKYKNITPALSREnleftVSHFAC--DVTYDARDFCRANREATS-------------DELERLFLA-- 582
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462585723 1177 klppvCRAVaglegTSQQALQRSRMVRrtfassLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESR 1253
Cdd:cd14887 583 -----CSTY-----TRLVGSKKNSGVR------AISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAG 643
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
627-1331 |
3.68e-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: 129.55 E-value: 3.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAGKVPKGRR-DGLPAHIGSMAQRAYWALLNQRRDQSIV 699
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPykelpiYSTMVSQLYLSSSGQLcSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 700 ALGRSGAGKTTCCEQVLEHLVGMAGSvdGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDF-NATGRITAAQ 777
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS--SRTTFDsRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 778 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVwskPEDKQKAAAAFAQLQ-----GAM 852
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTM---REDVSTAERSLNREKlavlkQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 853 EMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNtatfkhhlrQIIQQMTFGPsrwg 932
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGD-----------IRFTALTEADSAFVSDLQLLE---------QVAGMLQVST---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 933 ledEETSSGLkMTGVDCVEG------------------MASGLYQELFAAVVSLINRSFSSHH----LSMASIMVVDSPG 990
Cdd:cd14878 292 ---DELASAL-TTDIQYFKGdmiirrhtiqiaefyrdlLAKSLYSRLFSFLVNTVNCCLQSQDeqksMQTLDIGILDIFG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 991 FQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLpdpSPGTTVAVVD---QNPSqvrlpa 1067
Cdd:cd14878 368 FEEFQKN------EFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAY---SPGNQTGVLDfffQKPS------ 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1068 gggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGT------EGSSALRTCEQPLQCEIFHQLGwdPVRYDLT 1141
Cdd:cd14878 433 --------GFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAvyspmkDGNGNVALKDQGTAFTVMHYAG--RVMYEIV 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1142 GWLHRAKPNLSaldapQVLqqskreelrsLFQARaklppvcravaglegTSQQALqrsrmVRRTFASSLAAVrrkapCSQ 1221
Cdd:cd14878 503 GAIEKNKDSLS-----QNL----------LFVMK---------------TSENVV-----INHLFQSKLVTI-----ASQ 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1222 IKLQMDALTSMIKRSRLHFIHCLVPNpvvesrsgqesppppqpgrdkpGAGGPLALDIPALRVQLAGFHILEALRLHRTG 1301
Cdd:cd14878 543 LRKSLADIIGKLQKCTPHFIHCIKPN----------------------NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYG 600
|
730 740 750
....*....|....*....|....*....|..
gi 2462585723 1302 YADHMGLTRFRRQFQVLDAPLL--KKLMSTSE 1331
Cdd:cd14878 601 YPVRLSFSDFLSRYKPLADTLLgeKKKQSAEE 632
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
673-1315 |
3.80e-30 |
|
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: 129.54 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 673 GLPAHIGSMAQRAYWALLNQ-RRDQSIVALGRSGAGKTTCCEQVLEHLVGMA----GSVDGRVSVEKIRATFT----VLR 743
Cdd:cd14875 53 LLPPHIWQVAHKAFNAIFVQgLGNQSVVISGESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDENLKwsnpVME 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 744 AFGSVSMAHSRSATRFSMVMSLDFN-ATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL-NLHQM 821
Cdd:cd14875 133 SFGNARTVRNDNSSRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 822 AD------SSSF-GMGVWSKPEDKqkaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFE-- 892
Cdd:cd14875 213 QDykclngGNTFvRRGVDGKTLDD---AHEFQNVRHALSMIGVELETQNSIFRVLASILHLME-----------VEFEsd 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 893 ------WANYAAEALGCEYEELNTATfkhhLRQIIqqmtfgpsrwgLEDEETSSGLKMTGVDCVEGM----ASGLYQELF 962
Cdd:cd14875 279 qndkaqIADETPFLTACRLLQLDPAK----LRECF-----------LVKSKTSLVTILANKTEAEGFrnafCKAIYVGLF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 963 AAVVSLINRSFSSHH--LSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPV 1040
Cdd:cd14875 344 DRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNS------FEQLCINYANESLQNHYNKYTFINDEEECRREGIQI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1041 -QFDLPDPSpgTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTC 1119
Cdd:cd14875 418 pKIEFPDNS--ECVNMFDQKRT--------------GIFSMLDEECNFKGGTT----ERFTTNLWDQWANKSPYFVLPKS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1120 EQPLQCEIFHQLGWdpVRYDLTGWLHRakpNLSAL--DAPQVLQQSKREELRSLFQARAKLPpvcravaglegtsqqalQ 1197
Cdd:cd14875 478 TIPNQFGVNHYAAF--VNYNTDEWLEK---NTDALkeDMYECVSNSTDEFIRTLLSTEKGLA-----------------R 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1198 RSRMVRRTFASSLAAVRrkapcsqiklqmdaltSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLAL 1277
Cdd:cd14875 536 RKQTVAIRFQRQLTDLR----------------TELESTETQFIRCIKPNMEAS----------------------PSFL 577
|
650 660 670
....*....|....*....|....*....|....*...
gi 2462585723 1278 DIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQF 1315
Cdd:cd14875 578 DNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYF 615
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
627-1247 |
1.04e-28 |
|
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: 124.96 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAgKVPKGRRD--------GLPAHIGSMAQRAYWALLNQRR--DQ 696
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKP-VPQL-YSPELMREyhaapqpqKLKPHIFTVGEQTYRNVKSLIEpvNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 697 SIVALGRSGAGKTTCCEQVLEHLVGMAGSV---DGRVSVEKIRATF----TVLRAFGSVSMAHSRSATRFSMVMSLDFNA 769
Cdd:cd14880 79 SIVVSGESGAGKTWTSRCLMKFYAVVAASPtswESHKIAERIEQRIlnsnPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 770 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSsfgmgvWSKPEDKQKAAAAFAQLQ 849
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFS------WLPNPERNLEEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 850 GAMEMLGISESEQRAVWRVLAAIYHLG---------AAGACKV--GRKQFMRFewanyAAEALGCEYEELNTATFKHHLR 918
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGniqfadsedEAQPCQPmdDTKESVRT-----SALLLKLPEDHLLETLQIRTIR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 919 QIIQQMTF-GPSRWGLEDeetssglkmTGVDCvegMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQNPRH 996
Cdd:cd14880 308 AGKQQQVFkKPCSRAECD---------TRRDC---LAKLIYARLFDWLVSVINSSICADTDSWTTfIGLLDVYGFESFPE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 997 QgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSpgTTVAVVDQNPSQVrlpagggaqdar 1075
Cdd:cd14880 376 N------SLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFiNYQDNQ--TCLDLIEGSPISI------------ 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1076 glFWVLDEEVHVEGSSDSVVLErlcAAFEKKGAGTEGSSALRTCEQPlQCEIFHQLGwdPVRYDLTGWLHRAK----PNL 1151
Cdd:cd14880 436 --CSLINEECRLNRPSSAAQLQ---TRIESALAGNPCLGHNKLSREP-SFIVVHYAG--PVRYHTAGLVEKNKdpvpPEL 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1152 SaldapQVLQQSKREELRSLFQARAKlppvcravaglEGTSQQALQRSRmvrrtfASSLAAVrrkapcSQIKLQMDALTS 1231
Cdd:cd14880 508 T-----RLLQQSQDPLLQKLFPANPE-----------EKTQEEPSGQSR------APVLTVV------SKFKASLEQLLQ 559
|
650
....*....|....*.
gi 2462585723 1232 MIKRSRLHFIHCLVPN 1247
Cdd:cd14880 560 VLHSTTPHYIRCIKPN 575
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
628-1038 |
5.25e-28 |
|
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: 121.93 E-value: 5.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGK--VPKGRRDGLPaHIGSMAQRAYWALLNQRrDQSIVALGRSG 705
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMkaYLKNYSHVEP-HVYDVAEASVQDLLVHG-NQTIVISGESG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 706 AGKTTCCEQVLEHLV-GMAGSVdgrvSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNatGRITAAQLQTMLL 783
Cdd:cd14898 80 SGKTENAKLVIKYLVeRTASTT----SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 784 EKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqmADSSSFGmgvwSKPEDKQKAAAAFAQLQGAMEMLGISESeqR 863
Cdd:cd14898 154 EKSRVTHHEKGERNFHIFYQFCASKRLNIKNDF-----IDTSSTA----GNKESIVQLSEKYKMTCSAMKSLGIANF--K 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 864 AVWRVLAAIYHLGAAGACKVGRKQFMRFEWANYAAEALGCEYEELNTATFKhhlrqiiqqmtfGPSRWGLEDEETSSGLK 943
Cdd:cd14898 223 SIEDCLLGILYLGSIQFVNDGILKLQRNESFTEFCKLHNIQEEDFEESLVK------------FSIQVKGETIEVFNTLK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 944 mTGVDCVEGMASGLYQELFAAVVSLINRSFSSHhlSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQ 1023
Cdd:cd14898 291 -QARTIRNSMARLLYSNVFNYITASINNCLEGS--GERSISVLDIFGFEIFESNG------LDQLCINWTNEKIQNDFIK 361
|
410
....*....|....*
gi 2462585723 1024 RTFVSTLQRYQEEGV 1038
Cdd:cd14898 362 KMFRAKQGMYKEEGI 376
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
628-1247 |
5.91e-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: 122.34 E-value: 5.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVPK--------------GRRDGLPAHIGSMAQRAYWALLN 691
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfqKLPGLYSSDTMAKyllsfearssstrnKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 692 QRR----DQSIVALGRSGAGKTTCCEQVLEHLvGMAGSVDGRVSV----------EKIRATFTVLRAFGSVSMAHSRSAT 757
Cdd:cd14900 82 GLNgvmsDQSILVSGESGSGKTESTKFLMEYL-AQAGDNNLAASVsmgkstsgiaAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 758 RFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSssfgmgvwskped 837
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKRDMYRRVMDA------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 838 kqkaaaafaqlqgaMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQFM--RFEWA-NYAAEALGCEYEE 907
Cdd:cd14900 228 --------------MDIIGFTPHERAGIFDLLAALLHIGnltfehdENSDRLGQLKSDLapSSIWSrDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 908 LNTATfkhHLRQIIQQMTFGPSRWGLEDEETSSglkmtgvdcvEGMASGLYQELFAAVVSLINRSF-----SSHHLSMAS 982
Cdd:cd14900 294 LEKAL---SVRRIRAGTDFVSMKLSAAQANNAR----------DALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 983 IMVVDSPGFQN-PRHqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDqNPS 1061
Cdd:cd14900 361 IGILDIFGFEVfPKN-------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKY----------VEFCD-NQD 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1062 QVRLPagggAQDARGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtEGSSALRTCEQPLQCEIFHQLGwdPVRYDLT 1141
Cdd:cd14900 423 CVNLI----SQRPTGILSLIDEECVMPKGSDTTLASKLYRACGSH----PRFSASRIQRARGLFTIVHYAG--HVEYSTD 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1142 GWLHRAKPNLsaldapqvlqqskREELRSLFQAraklppvcravaglegtsqqalqrsrmvrrtfasslaavrrkapCSQ 1221
Cdd:cd14900 493 GFLEKNKDVL-------------HQEAVDLFVY--------------------------------------------GLQ 515
|
650 660
....*....|....*....|....*.
gi 2462585723 1222 IKLQMDALTSMIKRSRLHFIHCLVPN 1247
Cdd:cd14900 516 FKEQLTTLLETLQQTNPHYVRCLKPN 541
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
629-1363 |
2.30e-27 |
|
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: 120.86 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 629 VLNTLLQRYKAQLLHTCTGPDLIVLQP-------------RGPSVPSAGKvpkgrrdgLPAHIGSMAQRAYWALLNQRRD 695
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirKYRDAPDLTK--------LPPHVFYTARRALENLHGVNKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 696 QSIVALGRSGAGKTTCCEQVLEHL-VGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRIT 774
Cdd:cd14876 75 QTIIVSGESGAGKTEATKQIMRYFaSAKSGNMDLRIQ-TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 775 AAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMAD-----SSSFGMGVWSKPEDkqkaaaaFAQLQ 849
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEykflnPKCLDVPGIDDVAD-------FEEVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 850 GAMEMLGISESEQRAVWRVLAAIYHLGAAgacKVGRKQFMRFEwanYAAEALGCEYEELNTATFKHHL------RQIIQQ 923
Cdd:cd14876 227 ESLKSMGLTEEQIDTVFSIVSGVLLLGNV---KITGKTEQGVD---DAAAISNESLEVFKEACSLLFLdpealkRELTVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 924 MTF-GP----SRWGLEDEETssgLKMTgvdcvegMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQg 998
Cdd:cd14876 301 VTKaGGqeieGRWTKDDAEM---LKLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNN- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 999 kdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPvqfdlpdpspgTTVAVVDQNPSQVRLPAGGGaqdaRGLF 1078
Cdd:cd14876 370 -----SLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIP-----------TAELEYTSNAEVIDVLCGKG----KSVL 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1079 WVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQ 1158
Cdd:cd14876 430 SILEDQCLAPGGSD----EKFVSACVSKLKSNGKFKPAKV-DSNINFIVVHTIG--DIQYNAEGFLFKNKDVLRA-ELVE 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1159 VLQQSKREELRSLFqaraklppvcravaglEGtsqQALQRSRMVRrtfaSSLAAvrrkapcSQIKLQMDALTSMIKRSRL 1238
Cdd:cd14876 502 VVQASTNPVVKALF----------------EG---VVVEKGKIAK----GSLIG-------SQFLKQLESLMGLINSTEP 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1239 HFIHCLVPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1318
Cdd:cd14876 552 HFIRCIKPN---ETKK-------------------PLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL 609
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 2462585723 1319 DAPLlkklmSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1363
Cdd:cd14876 610 DLGI-----ANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
628-1325 |
1.02e-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: 115.78 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAGK--VPKGRRDG------------LPAHIGSMAQRAYWALLN-Q 692
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPF-QRLPLYGKeiLESYRQEGllrsqgiespqaLGPHVFAIADRSYRQMMSeI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 693 RRDQSIVALGRSGAGKTTCCEQVLEHL--VGMAGSV-------DGRVSV-EKIRATFTVLRAFGSVSMAHSRSATRFSMV 762
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLttLGNGEEGapnegeeLGKLSImDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 763 MSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFG------MGVWSKPE 836
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQLpnefhyTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 837 -DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-----------AAGACKVGRKQFMrfewaNYAAEALGCE 904
Cdd:cd14908 241 lREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGqlefeskeedgAAEIAEEGNEKCL-----ARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 905 YEELNTAtfkhhLRQIIQQMTFGPSRWGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLS--MAS 982
Cdd:cd14908 316 VDKLLRA-----LTSKIIVVRGKEITTKLTPHKAY--------DARDALAKTIYGALFLWVVATVNSSINWENDKdiRSS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 983 IMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDpspgttvavvdqNPS 1061
Cdd:cd14908 383 VGVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFiEFPD------------NQD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1062 QVRLPAGggaqDARGLFWVLDEEVHVegssdsvvlerlcaafekkgaGTEGSSAlrtceqplqceifhqlgwdpvrydlt 1141
Cdd:cd14908 445 CLDTIQA----KKKGILTMLDDECRL---------------------GIRGSDA-------------------------- 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1142 GWLHRakpnLSALDAPQVLQQ-SKREELRSLFQARAKLppvCRAVAGLEGTSQQALQRSRMVRRTFASSLAAVRRKAPCS 1220
Cdd:cd14908 474 NYASR----LYETYLPEKNQThSENTRFEATSIQKTKL---IFAVRHFAGQVQYTVETTFCEKNKDEIPLTADSLFESGQ 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1221 QIKLQMDALTSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRT 1300
Cdd:cd14908 547 QFKAQLHSLIEMIEDTDPHYIRCIKPNDAAK----------------------PDLVTRKRVTEQLRYGGVLEAVRVARS 604
|
730 740
....*....|....*....|....*
gi 2462585723 1301 GYADHMGLTRFRRQFQVLdAPLLKK 1325
Cdd:cd14908 605 GYPVRLPHKDFFKRYRML-LPLIPE 628
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
629-1038 |
1.77e-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: 108.44 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 629 VLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVPKGRR--------DGLPAHIGSMAQRAYWALLNQRRDQSI 698
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfkQIRNLYGTEVIGRYRQadtsrgfpSDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 699 VALGRSGAGKTTCCEQVLEHLVgmAGSVDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 777
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFA--YGHSTSSTDVQSlILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 778 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMaDSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLgI 857
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSL-ESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-F 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 858 SESEQRAVWRVLAAIYHLGAAGACKVGRkqfMRFEwaNYAAEALGCEYEEL------NTATFKHHLRQ---IIQQMTFgp 928
Cdd:cd14886 239 SKNEIDSFYKCISGILLAGNIEFSEEGD---MGVI--NAAKISNDEDFGKMcellgiESSKAAQAIITkvvVINNETI-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 929 srwgledeeTSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 1008
Cdd:cd14886 312 ---------ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN------TYEQL 376
|
410 420 430
....*....|....*....|....*....|
gi 2462585723 1009 CHNYAHERLQLLFYQRTFVSTLQRYQEEGV 1038
Cdd:cd14886 377 LINYANERLQQYFINQVFKSEIQEYEIEGI 406
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1443-2127 |
5.30e-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: 108.22 E-value: 5.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1443 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAERLQAFREVQELKSK 1522
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER-------LANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1523 HEQVQKKLGDVNKQLEEAQQKIqlndlernptggDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQ 1602
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEEL------------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1603 SAYDGAKKMAHQLKRKchhltcdledtcvlLENQQSRNHELEKKQKKFDLQLAQALGESVfEKGLREKVTQENT------ 1676
Cdd:TIGR02168 400 NEIERLEARLERLEDR--------------RERLQQEIEELLKKLEEAELKELQAELEEL-EEELEELQEELERleeale 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1677 SVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGspsLGENCVAGLKERLWKlessaleqqkiqSQQENTIKQLE 1756
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG---FSEGVKALLKNQSGL------------SGILGVLSELI 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1757 QLRQRFELEIE-----RMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDqig 1831
Cdd:TIGR02168 530 SVDEGYEAAIEaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD--- 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1832 HRDFDVEKRL------------------RRDLRRTHALLSDVQL---LLG-----TMEDGKTSVS----KEELEKVHSQL 1881
Cdd:TIGR02168 607 LVKFDPKLRKalsyllggvlvvddldnaLELAKKLRPGYRIVTLdgdLVRpggviTGGSAKTNSSilerRREIEELEEKI 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1882 EQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAAD 1961
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1962 IGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDS 2040
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2041 LIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD 2120
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
....*..
gi 2462585723 2121 LQAALEE 2127
Cdd:TIGR02168 927 LELRLEG 933
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
627-1316 |
6.38e-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: 6.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP---SVPSAGKVPKGRRDGL-----------PAHIGSMAQRAYWALLNQ 692
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPlpiYTPDHMQAYNKSREQTplyekdtvndaPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 693 RRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-----------KIRATFTVLRAFGSVSMAHSRSATRFSM 761
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEgasgvlhpigqQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 762 VMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLD--LRTELNLHQMADssSFGMGVWSKPE--D 837
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVN--EFVMLKQADPLatN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 838 KQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQfmrfewANYAAEALGCEYEELNT 910
Cdd:cd14893 239 FALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGnvdfvpdPEGGKSVGGAN------STTVSDAQSCALKDPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 911 ATFKHHLRQ---IIQQMTFGPSRWGLED-EETSSGLKMTGV----DCVEGMASGLYQELFAAVVSLIN-------RSFSS 975
Cdd:cd14893 313 ILLAAKLLEvepVVLDNYFRTRQFFSKDgNKTVSSLKVVTVhqarKARDTFVRSLYESLFNFLVETLNgilggifDRYEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 976 HHLSMAS--IMVVDSPGFQN--PRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDpspGT 1051
Cdd:cd14893 393 SNIVINSqgVHVLDMVGFENltPSQNS------FDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVENRLTV---NS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1052 TVAVVDQNPSQVRLpaggGAQDARGLFWVLDEEVHVEGSSDSVVLERLCAAFEK--------KGAGTEGSSALRTCEQPL 1123
Cdd:cd14893 464 NVDITSEQEKCLQL----FEDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAvgglsrpnMGADTTNEYLAPSKDWRL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1124 QCEIFHQLGwdPVRYDLTGWLHRAKPNLSALDApQVLQQSKREELRSLFQARAklppvcrAVAGLEGTSQQALQRSRmVR 1203
Cdd:cd14893 540 LFIVQHHCG--KVTYNGKGLSSKNMLSISSTCA-AIMQSSKNAVLHAVGAAQM-------AAASSEKAAKQTEERGS-TS 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1204 RTFASSLAAVRR-----KAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESRsgqesppppqpgrdkpgaggplALD 1278
Cdd:cd14893 609 SKFRKSASSAREsknitDSAATDVYNQADALLHALNHTGKNFLVCIKPNETLEEG----------------------VFD 666
|
730 740 750
....*....|....*....|....*....|....*...
gi 2462585723 1279 IPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQ 1316
Cdd:cd14893 667 SAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
627-1318 |
4.13e-22 |
|
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: 103.80 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVPKgrrdglPAHIGSMAQRAYWALL-NQRRDQSIVALGRSG 705
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIK------KCHISGVAENALDRIKsMSSNAESIVFGGESG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 706 AGKTTCCEQVLEHLVGMAGSvdgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQLQ-TMLLE 784
Cdd:cd14874 75 SGKSYNAFQVFKYLTSQPKS---KVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLTGLNLKyTVPLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 785 KSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMadSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQRA 864
Cdd:cd14874 151 VPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDDHCIS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 865 VWRVLAAIYHLGaagackvgrKQFMRFEWANYAAEALGcEYEELNTATFKHHLRQI-IQQMtfgpSRWGLEDEETSSGLK 943
Cdd:cd14874 229 IYKIISTILHIG---------NIYFRTKRNPNVEQDVV-EIGNMSEVKWVAFLLEVdFDQL----VNFLLPKSEDGTTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 944 M-TGVDCVEGMASGLYQELFAAVVSLINRSFSShHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFY 1022
Cdd:cd14874 295 LnAALDNRDSFAMLIYEELFKWVLNRIGLHLKC-PLHTGVISILDHYGFEKYNNNG------VEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1023 QRTFVSTLQRYQEEGVPVQFDLPDP-SPGTTVAVVDQNPsqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCA 1101
Cdd:cd14874 368 KHSFHDQLVDYAKDGISVDYKVPNSiENGKTVELLFKKP--------------YGLLPLLTDECKFPKGSHESYLEHCNL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1102 AFEKKGAGTEGSSALRtceqpLQCEIFHQLG--WdpvrYDLTGWLHRAKPNLSaLDAPQVLQQSKREELRSLFQARAKlp 1179
Cdd:cd14874 434 NHTDRSSYGKARNKER-----LEFGVRHCIGttW----YNVTDFFSRNKRIIS-LSAVQLLRSSKNPIIGLLFESYSS-- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1180 pvcravagleGTSQQALQRSRMVRRTfASSLAavrrkapcsqiklqmdaltSMIKRSRLHFIHCLvpnpvvesRSGQESp 1259
Cdd:cd14874 502 ----------NTSDMIVSQAQFILRG-AQEIA-------------------DKINGSHAHFVRCI--------KSNNER- 542
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462585723 1260 pppQPGRdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1318
Cdd:cd14874 543 ---QPKK----------FDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
628-1095 |
5.15e-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: 100.57 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgpsvpsagkvpkgRRDGLPAHIGSMAQRA-YWALLN-------QRRD---- 695
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY-------------RDVGNPLTLTSTRSSPlAPQLLKvvqeavrQQSEtgyp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 696 QSIVALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATR---FSMVMSLDfnatGR 772
Cdd:cd14881 69 QAIILSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRighFIEVQVTD----GA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 773 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL--HQMADSS--SFGMGVWSKPEDKqkaaAAFAQL 848
Cdd:cd14881 145 LYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLdgYSPANLRylSHGDTRQNEAEDA----ARFQAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 849 QGAMEMLGISESEqraVWRVLAAIYHLG--------AAGACKVGRKQFmrfewaNYAAEALGCE----YEELNTATfkHH 916
Cdd:cd14881 221 KACLGILGIPFLD---VVRVLAAVLLLGnvqfidggGLEVDVKGETEL------KSVAALLGVSgaalFRGLTTRT--HN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 917 LR-QIIQQmtfgpsrwgLEDEETSSGLKmtgvDCvegMASGLYQELFAAVVSLINR-----SFSSHHLSMASIMVVDSPG 990
Cdd:cd14881 290 ARgQLVKS---------VCDANMSNMTR----DA---LAKALYCRTVATIVRRANSlkrlgSTLGTHATDGFIGILDMFG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 991 FQNPrhqgkdRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDlpdpspgttVAVVDQNP-----SQVRL 1065
Cdd:cd14881 354 FEDP------KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVE---------VDYVDNVPcidliSSLRT 418
|
490 500 510
....*....|....*....|....*....|
gi 2462585723 1066 pagggaqdarGLFWVLDEEVHVEGSSDSVV 1095
Cdd:cd14881 419 ----------GLLSMLDVECSPRGTAESYV 438
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1368-2136 |
1.10e-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: 100.53 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1368 SRLEKQREKL--VSQSIVLFQAACKgfLSRQEFKKLKIRRLAAQciqKNVAVFLAVKDWPWWQLLGSLQPLLsatigtEQ 1445
Cdd:TIGR02169 170 RKKEKALEELeeVEENIERLDLIID--EKRQQLERLRREREKAE---RYQALLKEKREYEGYELLKEKEALE------RQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1446 LRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADerfkgdvacqvLESERAERLQafREVQELKSKHEQ 1525
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD-----------LGEEEQLRVK--EKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1526 VQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQmenefLRKRLQQCEERLDSELTARKELEQKLGELQSAY 1605
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE-----ERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1606 DGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEKKQKKFDLQLAQALgesvfeKGLREKVTQ---ENTSVRWEL 1682
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINE----LKRELDRLQEELQRLSEELADLNAAI------AGIEAKINEleeEKEDKALEI 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1683 gqlqqqlKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLES--SALEQQKIQSQQE----------- 1749
Cdd:TIGR02169 451 -------KKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQRelAEAEAQARASEERvrggraveevl 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1750 --------NTIKQLEQLRQRFELEIE-----RMKQMHQKDREDQEEELEDVRQSCQKRLHQL---EMQLEQEYEEkqmVL 1813
Cdd:TIGR02169 517 kasiqgvhGTVAQLGSVGERYATAIEvaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLplnKMRDERRDLS---IL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1814 HEkqdlEGLIGTLCDQIghrDFDVEKR-----------LRRDLRRTHALLSDVQLLL---------GTM------EDGKT 1867
Cdd:TIGR02169 594 SE----DGVIGFAVDLV---EFDPKYEpafkyvfgdtlVVEDIEAARRLMGKYRMVTlegelfeksGAMtggsraPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1868 SVSKEELEKVHS------QLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLvdeQLYRLQFEKADLLKRIDEDQ 1941
Cdd:TIGR02169 667 LFSRSEPAELQRlrerleGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK---EIEQLEQEEEKLKERLEELE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1942 DDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLqvAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKt 2020
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKlEEEVSRIEARLREIEQK- 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2021 efqkvqIKRFEVLVIRLRDsliKMGEELSQAATSESQQREssqyYQRRLEELKADMEELVQREAEASRRCMELEKYVEEL 2100
Cdd:TIGR02169 821 ------LNRLTLEKEYLEK---EIQELQEQRIDLKEQIKS----IEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
810 820 830
....*....|....*....|....*....|....*.
gi 2462585723 2101 AAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTE 2136
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
627-1247 |
1.70e-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: 99.01 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPS--AGKVPKG--------------RRDGLPAHIGSMAQRAYWALL 690
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPF-QDLPQlyGDEILRGyaydhnsqfgdrvtSTDPREPHLFAVARAAYIDIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 691 NQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGS---------------VDGRVSVE-KIRATFTVLRAFGSVSMAHSR 754
Cdd:cd14899 80 QNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTgnnnltnsesisppaSPSRTTIEeQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 755 SATRFSMVMSLDFNATGR-ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELN--LHQMADSSSFGM-- 829
Cdd:cd14899 160 NSSRFGKFIELRFRDERRrLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEQKqvLALSGGPQSFRLln 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 830 -GVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGA---------------AGACKVGRKQFMRFEW 893
Cdd:cd14899 240 qSLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNvdfeqiphkgddtvfADEARVMSSTTGAFDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 894 ANYAAEALGCEYEELNTATFKhhlrqiiqqmtfgpsRWGLEDEETSsglkMTGVDCVEG------MASGLYQELFAAVVS 967
Cdd:cd14899 320 FTKAAELLGVSTEALDHALTK---------------RWLHASNETL----VVGVDVAHArntrnaLTMECYRLLFEWLVA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 968 LINRSFSSH---------------HLSMASIMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQR 1032
Cdd:cd14899 381 RVNNKLQRQasapwgadesdvddeEDATDFIGLLDIFGFEDMAEN------SFEQLCINYANEALQHQFNQYIFEEEQRL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1033 YQEEGVPVQFdLPDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEG 1112
Cdd:cd14899 455 YRDEGIRWSF-VDFPNNRACLELFEHRPI--------------GIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHF 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1113 SSAlRTCEQPLQCEIFHQLGWdpVRYDLTGWLHRAKPNLSAlDAPQVLQQSKREELRSLfqARAKLPPVCRAVAGLEGTS 1192
Cdd:cd14899 520 RSA-PLIQRTTQFVVAHYAGC--VTYTIDGFLAKNKDSFCE-SAAQLLAGSSNPLIQAL--AAGSNDEDANGDSELDGFG 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2462585723 1193 QQALQRSRmvrrtfaSSLAAVrrkAPCSQIKLQMDALTSMIKRSRLHFIHCLVPN 1247
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 ... |
1428-2112 |
3.54e-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: 95.24 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1428 QLLGSLQPLLSATIGTEQLRAK-EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvaCQVLESER 1506
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKlEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK----NIKLSKDV 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1507 AERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQlNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDS 1586
Cdd:pfam01576 464 SSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQ-EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1587 ELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQalgesvfEKG 1666
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAE-------EKA 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1667 LREKVTQENTSVRWElgqlqqqLKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLESS--------- 1737
Cdd:pfam01576 616 ISARYAEERDRAEAE-------AREKETRALSLARALEEALEAKEEL-------ERTNKQLRAEMEDLVSSkddvgknvh 681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1738 -------ALEQQ----KIQSQQ-ENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQE 1805
Cdd:pfam01576 682 elerskrALEQQveemKTQLEElEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDE 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1806 YEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRdLRRTHALLSDVQlllgtmedgktsvskEELEKVHSQLEQSE 1885
Cdd:pfam01576 762 RKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQ-LKKLQAQMKDLQ---------------RELEEARASRDEIL 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1886 AKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMqkhkdliaqsaadiGQI 1965
Cdd:pfam01576 826 AQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLE--------------ARI 891
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1966 QELQLQLEEAKKEKHKLQEQLQVAQMRIEYL------EQSTVDRAIVSRQEAVICDLENKTEFQKV--QIK-RFEVLVIR 2036
Cdd:pfam01576 892 AQLEEELEEEQSNTELLNDRLRKSTLQVEQLttelaaERSTSQKSESARQQLERQNKELKAKLQEMegTVKsKFKSSIAA 971
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2037 LRDSLIKMGEELSQAATSESQQRESSQYYQRRLEEL--------------KADMEELVQREAEASRRCMELEKYVEELAA 2102
Cdd:pfam01576 972 LEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVllqvederrhadqyKDQAEKGNSRMKQLKRQLEEAEEEASRANA 1051
|
730
....*....|
gi 2462585723 2103 VRQTLQTDLE 2112
Cdd:pfam01576 1052 ARRKLQRELD 1061
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1444-2109 |
1.28e-18 |
|
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: 93.58 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1523
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1524 EQVQKKLGDVNKQLEEAqqKIQLNDLERNPTGGDEWQ---------MRFDCAQMENEFLRKRLQQCEERLDSELTARKEL 1594
Cdd:TIGR02168 389 AQLELQIASLNNEIERL--EARLERLEDRRERLQQEIeellkkleeAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1595 EQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLE------DTCVLLENQQSRNH-------ELEKKQKKFDLQLAQALGES 1661
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQEnlegfsEGVKALLKNQSGLSgilgvlsELISVDEGYEAAIEAALGGR 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1662 VfekglrEKVTQENTSVRW---------ELGQLQQQLKQKEQEASQLKQQVEMLQDHKR------ELLGSPSLGENCVAG 1726
Cdd:TIGR02168 547 L------QAVVVENLNAAKkaiaflkqnELGRVTFLPLDSIKGTEIQGNDREILKNIEGflgvakDLVKFDPKLRKALSY 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1727 LKERLWKLES--SALEQQKIQS-------------------------------QQENTIKQLEQLRQRFELEIERMKQ-- 1771
Cdd:TIGR02168 621 LLGGVLVVDDldNALELAKKLRpgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKal 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1772 -MHQKDREDQEEELEDVR---QSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRR 1847
Cdd:TIGR02168 701 aELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAE 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1848 THALLSDVQLLLGTMEDgKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQ 1927
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1928 FEKADLLKRIDEDQDDLNEL----------MQKHKDLIAQSAADI----GQIQELQLQLEEAKKEKHKLQEQLQVAQMRI 1993
Cdd:TIGR02168 859 AEIEELEELIEELESELEALlnerasleeaLALLRSELEELSEELreleSKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1994 EYLEQSTVDRAIVSRQEAVICDLENKTEFQKVQIKrfevlVIRLRDSLIKMGeELSQAATSESQQressqyYQRRLEELK 2073
Cdd:TIGR02168 939 DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR-----LKRLENKIKELG-PVNLAAIEEYEE------LKERYDFLT 1006
|
730 740 750
....*....|....*....|....*....|....*..
gi 2462585723 2074 ADMEELVqrEAEASrrcmeLEKYVEEL-AAVRQTLQT 2109
Cdd:TIGR02168 1007 AQKEDLT--EAKET-----LEEAIEEIdREARERFKD 1036
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
627-1041 |
1.02e-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: 90.07 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALGRSGA 706
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 707 GKTTCCEQVLE-HLVGMagSVDGRVSVEKIRATFtVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEK 785
Cdd:cd14937 81 GKTEASKLVIKyYLSGV--KEDNEISNTLWDSNF-ILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 786 SRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPE-DKQKAAAAFAQLQGAMEMLGISESeqra 864
Cdd:cd14937 158 IRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEiDDAKDFGNLMISFDKMNMHDMKDD---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 865 VWRVLAAIYHLG--------AAGACKVGRKQFMRFEWANYAAEALGCEYEEL-NTATFKHhlRQIIQQMTFGPsrwgLED 935
Cdd:cd14937 234 LFLTLSGLLLLGnveyqeieKGGKTNCSELDKNNLELVNEISNLLGINYENLkDCLVFTE--KTIANQKIEIP----LSV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 936 EETSSGLKMTGVDcvegmasgLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCHNYAHE 1015
Cdd:cd14937 308 EESVSICKSISKD--------LYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKN------SLEQLLINIANE 373
|
410 420
....*....|....*....|....*.
gi 2462585723 1016 RLQLLFYQRTFVSTLQRYQEEGVPVQ 1041
Cdd:cd14937 374 EIHSIYLYIVYEKETELYKAEDILIE 399
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
628-1041 |
1.02e-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: 89.80 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVP-----SAGKVPKGRRDGLPaHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEypqefHAKYRCKSRSDNAP-HIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 703 RSGAGKTTCCEQVLEHLvGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 782
Cdd:cd14882 81 ESYSGKTTNARLLIKHL-CYLGDGNRGAT-GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 783 LEKSRVARQPEGESNFLVFSQMLAGL-------DLDLRTELNLHQM----ADSSSFGMGVWSKPEDKQKAAAAFAQLQGA 851
Cdd:cd14882 159 LEKLRVSTTDGNQSNFHIFYYFYDFIeaqnrlkEYNLKAGRNYRYLrippEVPPSKLKYRRDDPEGNVERYKEFEEILKD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 852 MEMlgiSESEQRAVWRVLAAIYHLGAAGACKV-GRKQFMRFEWANYAAEALGceyeeLNTATFKHHLRQIIQQMTFGPSR 930
Cdd:cd14882 239 LDF---NEEQLETVRKVLAAILNLGEIRFRQNgGYAELENTEIASRVAELLR-----LDEKKFMWALTNYCLIKGGSAER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 931 WGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINrsfssHHLSMA--------SIMVVDSPGFQNPRHQGkdra 1002
Cdd:cd14882 311 RKHTTEEAR--------DARDVLASTLYSRLVDWIINRIN-----MKMSFPravfgdkySISIHDMFGFECFHRNR---- 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 2462585723 1003 atFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQ 1041
Cdd:cd14882 374 --LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTI 410
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
628-1247 |
1.08e-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: 89.97 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP-------------------SVPSAGKVPkgrrdglPAHIGSMAQRAYWA 688
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPlkelydqdvmnvylhkksnSAASAAPFP-------KAHIYDIANMAYKN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 689 LLNQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFN 768
Cdd:cd14884 75 MRGKLKRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 769 A---------TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGL-DLDL---RTELNLH----------QMADSS 825
Cdd:cd14884 155 EventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLsDEDLarrNLVRNCGvygllnpdesHQKRSV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 826 SFGMGVWSK-----PEDKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGackvgrkqfmrfewANYAAEA 900
Cdd:cd14884 235 KGTLRLGSDsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRA--------------YKAAAEC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 901 LGCEYEELNTaTFKHHLRQIIQQMTFGPSRwglEDEETSSglkmtgvdcVEGMASGLYQELFAAVVSLINR--------- 971
Cdd:cd14884 301 LQIEEEDLEN-VIKYKNIRVSHEVIRTERR---KENATST---------RDTLIKFIYKKLFNKIIEDINRnvlkckekd 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 972 SFSSHHLSM---ASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpVQFDLPDPS 1048
Cdd:cd14884 368 ESDNEDIYSineAIISILDIYGFEELSGND------FDQLCINLANEKLNNYYINNEIEKEKRIYARENI-ICCSDVAPS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1049 PGTTVAVVDQNPSQV----RLPAgGGAQDARGLFW---------VLDEEVHVEGSsdsvVLERLCAAFEKKGAGTEGSSA 1115
Cdd:cd14884 441 YSDTLIFIAKIFRRLdditKLKN-QGQKKTDDHFFryllnnerqQQLEGKVSYGF----VLNHDADGTAKKQNIKKNIFF 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1116 LRtceqplqceifHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLQQSKREELRSlfqaraklppvcravAGLEGTSQQA 1195
Cdd:cd14884 516 IR-----------HYAG--LVTYRINNWIDKNSDKIET-SIETLISCSSNRFLRE---------------ANNGGNKGNF 566
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2462585723 1196 LQRSRMVrrtfasslaavrrkapcsqIKlQMDALTSMIKRSRLHFIHCLVPN 1247
Cdd:cd14884 567 LSVSKKY-------------------IK-ELDNLFTQLQSTDMYYIRCFLPN 598
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1445-2131 |
2.79e-17 |
|
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: 89.08 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1445 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVA----------CQVLESERAERLQAFR 1514
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAekqrrdlgeeLEALKTELEDTLDTTA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1515 EVQELKSKHEQvqkKLGDVNKQLEEAQQ--KIQLNDL-ERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEE--------- 1582
Cdd:pfam01576 317 AQQELRSKREQ---EVTELKKALEEETRshEAQLQEMrQKHTQALEELTEQLEQAKRNKANLEKAKQALESenaelqael 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1583 ------RLDSElTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQL-- 1654
Cdd:pfam01576 394 rtlqqaKQDSE-HKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLqd 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1655 AQALG--ESVFEKGLREKVTQ---ENTSVRWELGQLQQQLKQKEQEASQLKQQvemLQDHKREllgspslgencvagLKE 1729
Cdd:pfam01576 473 TQELLqeETRQKLNLSTRLRQledERNSLQEQLEEEEEAKRNVERQLSTLQAQ---LSDMKKK--------------LEE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1730 RLWKLESSALEQQKIQSQQENTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVRQSC------QKRLHQL---EM 1800
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD-KLEKTKNRLQQELDDLLVDLDHQRQLVsnlekkQKKFDQMlaeEK 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1801 QLEQEY-EEKQMVLHEKQDLEGLIGTLCdqighRDFDVEKRLRRDLRRTHALL-SDVQLLLGTMEDGKTSVskEELEKVH 1878
Cdd:pfam01576 615 AISARYaEERDRAEAEAREKETRALSLA-----RALEEALEAKEELERTNKQLrAEMEDLVSSKDDVGKNV--HELERSK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1879 SQLEQSeakcEEALKTQkvltadLESMHSELEnMTRNKSL---VDEQLYRLQFE-------------KADLLKRIDEDQD 1942
Cdd:pfam01576 688 RALEQQ----VEEMKTQ------LEELEDELQ-ATEDAKLrleVNMQALKAQFErdlqardeqgeekRRQLVKQVRELEA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1943 DLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLeQSTVDRAIVSRQEAVICDLENKTef 2022
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-QRELEEARASRDEILAQSKESEK-- 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2023 qkvQIKRFEVLVIRLRDSLI--------------KMGEELSQAATSESQQRESsqyyQRRLEELKADMEELVQREAEAS- 2087
Cdd:pfam01576 834 ---KLKNLEAELLQLQEDLAaserarrqaqqerdELADEIASGASGKSALQDE----KRRLEARIAQLEEELEEEQSNTe 906
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 2462585723 2088 -------RRCMELEKYVEELAAVRQTLQTD---LETSIRRIADLQAALEEVASS 2131
Cdd:pfam01576 907 llndrlrKSTLQVEQLTTELAAERSTSQKSesaRQQLERQNKELKAKLQEMEGT 960
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1444-1998 |
4.03e-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: 88.15 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLAD---ERFKGDVACQVLES--ERAERLQAfrEVQE 1518
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKiknKLLKLELLLSNLKKkiQKNKSLES--QISE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1519 LKSKH-------EQVQKKLGDVNKQLEEAQQKIQ--LNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLdSELT 1589
Cdd:TIGR04523 223 LKKQNnqlkdniEKKQQEINEKTTEISNTQTQLNqlKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI-SDLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1590 ARKE-------------LEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQ-QSRNHELEKKQKKfdLQLA 1655
Cdd:TIGR04523 302 NQKEqdwnkelkselknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN----SESEnSEKQRELEEKQNE--IEKL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1656 QALGESVFEKglREKVTQENTSVRWELgqlqqqlKQKEQEASQLKQQVEMLQDHKRELLGspslgencvaglkerlwkle 1735
Cdd:TIGR04523 376 KKENQSYKQE--IKNLESQINDLESKI-------QNQEKLNQQKDEQIKKLQQEKELLEK-------------------- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1736 ssalEQQKIQSQ---QENTIKQLEQLRQRFELEIERMKQMhqkdREDQEEELEDVRQSCQKRLHQLEmQLEQEYEEKQ-- 1810
Cdd:TIGR04523 427 ----EIERLKETiikNNSEIKDLTNQDSVKELIIKNLDNT----RESLETQLKVLSRSINKIKQNLE-QKQKELKSKEke 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1811 --MVLHEKQDLEGLIGTLCDQIghrdfdvekrlrrdlrrthallsdvqlllgtmedgktSVSKEELEKVHSQLEQSEAKC 1888
Cdd:TIGR04523 498 lkKLNEEKKELEEKVKDLTKKI-------------------------------------SSLKEKIEKLESEKKEKESKI 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1889 EEalktqkvLTADLESMHSEL--ENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQ 1966
Cdd:TIGR04523 541 SD-------LEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
570 580 590
....*....|....*....|....*....|..
gi 2462585723 1967 ELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1998
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
628-1099 |
1.31e-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: 86.30 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAGKVPK-GRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALGRS 704
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRylPFLHSQELVRNyNQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 705 GAGKTTCCEQVLEHLVGMAGSvDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLE 784
Cdd:cd14905 82 GSGKSENTKIIIQYLLTTDLS-RSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 785 KSRVARQPEGESNFLVFSQMLAGLDLDlrtELNLHQMADSSSF-------GMGVWSKPEDKqkaaaAFAQLQGAMEMLGI 857
Cdd:cd14905 161 ENRVTYQNKGERNFHIFYQFLKGITDE---EKAAYQLGDINSYhylnqggSISVESIDDNR-----VFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 858 SESEQRAVWRVLAAIYHLGAAgackvgrkQFMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRWGLEDEE 937
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNV--------TFFQKNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENRD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 938 TssglkmtgvdcvegMASGLYQELFAAVVSLINRSFSSHHLSMaSIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERL 1017
Cdd:cd14905 305 S--------------LARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQESSQLNG------YEQFSINFLEERL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1018 QLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgTTVAVVDQNPSqvrlpagggAQDARGLFWVLDEEVHVEGSSDSVVLE 1097
Cdd:cd14905 364 QQIYLQTVLKQEQREYQTERIPWM---------TPISFKDNEES---------VEMMEKIINLLDQESKNINSSDQIFLE 425
|
..
gi 2462585723 1098 RL 1099
Cdd:cd14905 426 KL 427
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1450-2127 |
1.74e-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: 86.65 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1450 EEELTTLRRKLEKSEKLRnELRQntDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKK 1529
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYK-ELKA--ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1530 LGDVNKQLEEAQQK-----IQLNDLERNPTGGDEwqmRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSA 1604
Cdd:TIGR02168 276 VSELEEEIEELQKElyalaNEISRLEQQKQILRE---RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1605 YDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQalgesvfekgLREKVTQentsvrwelgq 1684
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER----------LEARLER----------- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1685 lqqqlkqkeqeasqLKQQVEMLQDHKRELLGSPSLGEncvagLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFEL 1764
Cdd:TIGR02168 412 --------------LEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1765 EIERMKQmhqkdREDQEEELedvrQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghrdfDVEKRLRRD 1844
Cdd:TIGR02168 473 AEQALDA-----AERELAQL----QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-----SVDEGYEAA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1845 LRRthALLSDVQLLLgtMEDgktsvsKEELEKVHSQLEQSEAK----CEEALKTQKVLTADLESMHSELENMTRNKSLVD 1920
Cdd:TIGR02168 539 IEA--ALGGRLQAVV--VEN------LNAAKKAIAFLKQNELGrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1921 EqlYRLQFEKA--DLLKR--IDEDQDDLNELMQKHK----------DLIA-------QSAADIGQIQELQLQLEEAKKEK 1979
Cdd:TIGR02168 609 K--FDPKLRKAlsYLLGGvlVVDDLDNALELAKKLRpgyrivtldgDLVRpggvitgGSAKTNSSILERRREIEELEEKI 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1980 HKLQEQLQVAQMRIEYLEQSTVDraivsrqeavicdLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQr 2059
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEE-------------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL- 752
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462585723 2060 essqyyQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2127
Cdd:TIGR02168 753 ------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1444-2112 |
1.64e-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: 83.30 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNEL-RQNTDLLESKIA---------DLTSDLADERFKGDVACQVLES---ERAERL 1510
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELeKKHQQLCEEKNAlqeqlqaetELCAEAEEMRARLAARKQELEEilhELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1511 QAFRE-VQELKSKHEQVQKKLGDVNKQLEE---AQQKIQlndLERNPTGGDEWQMRFDCAQME--NEFLRKRLQQCEERL 1584
Cdd:pfam01576 85 EEEEErSQQLQNEKKKMQQHIQDLEEQLDEeeaARQKLQ---LEKVTTEAKIKKLEEDILLLEdqNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1585 DSELTARKELEQKLgelqsaydgakKMAHQLKRKCHHLTCDLEDTcvlLENQQSRNHELEKKQKKFDLQLAQALGESVFE 1664
Cdd:pfam01576 162 SEFTSNLAEEEEKA-----------KSLSKLKNKHEAMISDLEER---LKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1665 KGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELL---------------GSPSLGENCVAgLKE 1729
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQedleseraarnkaekQRRDLGEELEA-LKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1730 RLWKLESSALEQQKIQSQQENTI----KQLEQLRQRFELEIERMKQMHQKDREDQEEELED---VRQSCQKRLHQLEMQL 1802
Cdd:pfam01576 307 ELEDTLDTTAAQQELRSKREQEVtelkKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQakrNKANLEKAKQALESEN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1803 EQEYEEKQMVLHEKQDLEgligtlcdqigHRdfdvEKRLRRDLRRTHALLSDVQLLLGTMEDgKTSVSKEELEKVHSQLE 1882
Cdd:pfam01576 387 AELQAELRTLQQAKQDSE-----------HK----RKKLEGQLQELQARLSESERQRAELAE-KLSKLQSELESVSSLLN 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1883 QSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI 1962
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMK 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1963 GQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEY------------------LEQSTVDraiVSRQEAVICDLENKTefqk 2024
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEkaaaydklektknrlqqeLDDLLVD---LDHQRQLVSNLEKKQ---- 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2025 vqiKRFEVLVIRLRDSLIKMGEELSQA----------ATSESQQRESSQYYQRRLEE----LKADMEELVQREAEASRRC 2090
Cdd:pfam01576 604 ---KKFDQMLAEEKAISARYAEERDRAeaeareketrALSLARALEEALEAKEELERtnkqLRAEMEDLVSSKDDVGKNV 680
|
730 740
....*....|....*....|..
gi 2462585723 2091 MELEKYVEELAAVRQTLQTDLE 2112
Cdd:pfam01576 681 HELERSKRALEQQVEEMKTQLE 702
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1426-2063 |
4.12e-15 |
|
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: 81.94 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1426 WW--QLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQntdllESKIADLTSDLADERFKGDVACQVLE 1503
Cdd:TIGR00618 243 AYltQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK-----AAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1504 SERAERLQAFREVQELKSKHEQVQKKLGDVNKQLeeaQQKIQLNDLERNPTGgdeWQMRFDCAQMENEFLRKRLQQCEER 1583
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH---SQEIHIRDAHEVATS---IREISCQQHTLTQHIHTLQQQKTTL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1584 LDSELTARKELEQKLGEL-QSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQ-LAQALGES 1661
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQeSAQSLKER 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1662 VFEKGLREKVTQENTSVRWELGQLQQQLKQKEQE--ASQLKQQVEMLQDHKRELLGSPSL-GENCVAGLKERLWKLE--- 1735
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRMQrGEQTYAQLETSEEDVYhql 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1736 SSALEQQKIQSQQENTIKQ----LEQLRQRFELEIERMKQMHQKDREDQEEELEDvRQSCQKRLHQLEMQLEQEYEEKQM 1811
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQsfsiLTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA-EDMLACEQHALLRKLQPEQDLQDV 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1812 VLHEKQ----------DLEGLIGTLCDQighrdfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVS--KEELEKVHS 1879
Cdd:TIGR00618 631 RLHLQQcsqelalkltALHALQLTLTQE------RVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywKEMLAQCQT 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1880 QLEQSEAKCEEALKTQKVLTADLESMHSELEnmtRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1959
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENASSSLGSDLA---AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELS 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1960 ADIGQIQELQLQLEEAKKEKHKLQEQLQvaQMRIEYLEQSTV-DRAIVSRQEAVICDLENKTEfqkvqikrfevLVIRLR 2038
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEIG--QEIPSDEDILNLqCETLVQEEEQFLSRLEEKSA-----------TLGEIT 848
|
650 660
....*....|....*....|....*
gi 2462585723 2039 DSLIKMGEELSQAATSESQQRESSQ 2063
Cdd:TIGR00618 849 HQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1514-2143 |
4.60e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 81.65 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1514 REVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENefLRKRLQQCEERLDSELTARKE 1593
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE--LKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1594 LEQKLGELQSAYDGAKKMAHQLKRKCHHLTcdledtcvllenqqsrnhELEKKQKKFdlqlaQALGEsvfekgLREKVTQ 1673
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELK------------------ELKEKAEEY-----IKLSE------FYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1674 ENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgencvAGLKERLWKLESSALEQQKIQSQQENtik 1753
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-----------KELEKRLEELEERHELYEEAKAKKEE--- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1754 qLEQLRQRFE-LEIERMKQMHQKDREDQEEELEDVRQSCQKRlhqleMQLEQEYEEKQMVLHEkqdLEGLIGTlCDQIGh 1832
Cdd:PRK03918 374 -LERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARI-----GELKKEIKELKKAIEE---LKKAKGK-CPVCG- 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1833 RDFDVEKRLRRdLRRTHALLSDVqlllgtmedgktSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTAdLESMHSELENm 1912
Cdd:PRK03918 443 RELTEEHRKEL-LEEYTAELKRI------------EKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLKE- 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1913 trnkslVDEQLYRLQFEKadlLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMR 1992
Cdd:PRK03918 508 ------LEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1993 IEYLEQSTVDraivsrqeavicDLENKTEFQKVQIKRFevlvIRLRDSLIKMGEELSQAATSESQQRESSQYYQR---RL 2069
Cdd:PRK03918 579 LEELGFESVE------------ELEERLKELEPFYNEY----LELKDAEKELEREEKELKKLEEELDKAFEELAEtekRL 642
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462585723 2070 EELKADMEEL-----VQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVD 2143
Cdd:PRK03918 643 EELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1450-2130 |
1.74e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1450 EEELTTLRRKLEKSEKLRNELRQNTDLLE--SKIA----DLTSDLadERFKGDVACQVLESERAERLQAFREVQELKSKH 1523
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLErqAEKAeryrELKEEL--KELEAELLLLKLRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1524 EQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENE--FLRKRLQQCEERLDSELTARKELEQKLGEL 1601
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiaRLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1602 QSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWE 1681
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1682 LGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSpslgencVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQR 1761
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1762 FELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQ---LEMQLEQEYEEkqmvlhekqDLEGLIGTLCDQIGHRDFDVE 1838
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGavaVLIGVEAAYEA---------ALEAALAAALQNIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1839 KRLRRDLRRtHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSL 1918
Cdd:COG1196 560 AAAIEYLKA-AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1919 VDEQLYRLQFEKADLlkridedqddlnelmqkhkDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1998
Cdd:COG1196 639 AVTLAGRLREVTLEG-------------------EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1999 STVDRAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDsLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEE 2078
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE-LLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462585723 2079 L------VQREAEasrrcmELEKYVEELAAVRQTLQ---TDLETSIRRI-----ADLQAALEEVAS 2130
Cdd:COG1196 779 LgpvnllAIEEYE------ELEERYDFLSEQREDLEearETLEEAIEEIdretrERFLETFDAVNE 838
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1871-2139 |
2.55e-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: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1871 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1950
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1951 HKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLENKTEFQKVQIKRF 2030
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA------LLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2031 EVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTD 2110
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260
....*....|....*....|....*....
gi 2462585723 2111 LETSIRRIADLQAALEEVASSDSDTESVQ 2139
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 ... |
1728-2164 |
2.66e-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: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1728 KERLWKLESSALEQQKIQSQ--QENTIKQlEQLRQRFEL--EIERMKQMhqkdREDQEEELEDVrqscqkrLHQLEMQLE 1803
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQlcEEKNALQ-EQLQAETELcaEAEEMRAR----LAARKQELEEI-------LHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1804 QEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEE--LEKVHSQL 1881
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLEEQLDEEE-AARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERklLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1882 EQSEAKCEEALKTQKVLTADLESMHSELENMTRNkslvdEQLYRLQFEKADllKRIDEDQDDLNElmqkhkdliaqsaad 1961
Cdd:pfam01576 165 TSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK-----EEKGRQELEKAK--RKLEGESTDLQE--------------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1962 igQIQELQLQLEEAKKEKHKLQEQLQVAQMRieyLEQSTVDRAIVSRQ----EAVICDLE----------NKTEFQKVQI 2027
Cdd:pfam01576 223 --QIAELQAQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKirelEAQISELQedleseraarNKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2028 -KRFEVLVIRLRDSL----------IKMGEELSQ--------AATSESQQRESSQYYQRRLEELKADMEELVQREAEASR 2088
Cdd:pfam01576 298 gEELEALKTELEDTLdttaaqqelrSKREQEVTElkkaleeeTRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462585723 2089 RCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQT-AVDCGSSGRKEMDNVSILSSQPEG 2164
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAeLAEKLSKLQSELESVSSLLNEAEG 454
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1444-1984 |
1.51e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTSDLADERfkgdvacqvleseraERLQAFRE-VQELKSK 1522
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKLE---------------EKIRELEErIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1523 HEQVQKKLGDVNKQLEEAQQKIQLNDLErnptggDEWQMRFDCAQMENEFLRKRLQQCEERLD--SELTAR-KELEQKLG 1599
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFY------EEYLDELREIEKRLSRLEEEINGIEERIKelEEKEERlEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1600 ELQSAYDGAKKmAHQLkrkchhltcdLEDTCVLLENQQsrnhELEKKQKKFDLQLAQALGESVFEKglREKVTQENTSVR 1679
Cdd:PRK03918 349 ELEKRLEELEE-RHEL----------YEEAKAKKEELE----RLKKRLTGLTPEKLEKELEELEKA--KEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1680 WELGQLQQQLKQKEQEASQLKQ--------QVEMLQDHKRELLGSPSLG----ENCVAGLKERLWKLESSALEQQKIQSQ 1747
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAElkriEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1748 QENTIKQLEQLRQRFELEiERMKQMHQKDREDQEEELEDVRQ---SCQKRLHQLEMQLEQEYE---EKQMVLHEKQDLEG 1821
Cdd:PRK03918 492 ESELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEYEKLKEkliKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1822 LIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGtmedgktsvSKEELEKVHSQLEQSEAKCEEALKTQKVLTAD 1901
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD---------AEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1902 LESMHSELENMTRNKSLVD-EQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKH 1980
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
....
gi 2462585723 1981 KLQE 1984
Cdd:PRK03918 722 RVEE 725
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1475-2139 |
2.19e-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: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1475 DLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREvQELKSKHEQVQKkLGDVNKQLEEAQQKIQLNDlernpt 1554
Cdd:TIGR00618 171 NLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTP-CMPDTYHERKQV-LEKELKHLREALQQTQQSH------ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1555 ggdEWQMRFDCAQMENEFLRKRLQQCEERLDsELTArkeLEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLE 1634
Cdd:TIGR00618 243 ---AYLTQKREAQEEQLKKQQLLKQLRARIE-ELRA---QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1635 nQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEA-----SQLKQQVEMLQDH 1709
Cdd:TIGR00618 316 -LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqhiHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1710 KRELLGSPSLGENCVAGLKERLwkLESSALEQQKI--QSQQENTIKQLEQLRQRFE--LEIERMKQMHQKDREDQEEELE 1785
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRT--SAFRDLQGQLAhaKKQQELQQRYAELCAAAITctAQCEKLEKIHLQESAQSLKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1786 dvrqscqKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDfdvekrlrrdlrrTHALLSDvqlllgtmEDG 1865
Cdd:TIGR00618 473 -------QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN-------------PARQDID--------NPG 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1866 KTSVSKEELEKVHSQLEQSEAK----CEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRID--- 1938
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEEDvyhqLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEkls 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1939 EDQDDLNELMQKHKDLIAQSAADIGQIQEL-QLQLEEAKKEKHKLQEQLQVAQMRI-EYLEQSTVDRA-IVSRQEAVICD 2015
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLqQCSQELALKLTALHALQLTLTQERVrEHALSIRVLPKeLLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2016 LENKTEF---------QKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESS------QYYQRRLEELKADMEELV 2080
Cdd:TIGR00618 685 MQSEKEQltywkemlaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAlnqslkELMHQARTVLKARTEAHF 764
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462585723 2081 QREAEASRRCMELEKYvEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQ 2139
Cdd:TIGR00618 765 NNNEEVTAALQTGAEL-SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1444-2127 |
2.55e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRnELRQNTDLLESKIADLTSDL--ADERFKGDVACQVLESERAERLQAFREVQ--EL 1519
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAE-EARKAEDAKKAEAARKAEEVrkAEELRKAEDARKAEAARKAEEERKAEEARkaED 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1520 KSKHEQVqKKLGDVNKQLEEAQQKiqlnDLERNptggDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLG 1599
Cdd:PTZ00121 1223 AKKAEAV-KKAEEAKKDAEEAKKA----EEERN----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1600 ELQSAYDgaKKMAHQLKRKChhltcdledtcvllenQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQ-ENTSV 1678
Cdd:PTZ00121 1294 EAKKAEE--KKKADEAKKKA----------------EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaEAEAA 1355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1679 RWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLK--ERLWKLESSALEQQKIQSQQENtIKQLE 1756
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkaDELKKAAAAKKKADEAKKKAEE-KKKAD 1434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1757 QLRQRFEleiERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEmqLEQEYEEKQMVLHEKQDLEgligtlcdqighrdfd 1836
Cdd:PTZ00121 1435 EAKKKAE---EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAE---------------- 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1837 vEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSvskEELEKVHSQLEQSEA-KCEEALKTQKVLTADLESMHSELENMTRN 1915
Cdd:PTZ00121 1494 -EAKKKADEAKKAAEAKKKADEAKKAEEAKKA---DEAKKAEEAKKADEAkKAEEKKKADELKKAEELKKAEEKKKAEEA 1569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1916 KSlvDEQLYRLQFEKADLLKRIDEDQddLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKhklQEQLQVAQMRIEY 1995
Cdd:PTZ00121 1570 KK--AEEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKKE 1642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1996 LEQstVDRAIVSRQEavicdlENKTEFQKVQIKRFEvlvirlrDSLIKMGEELSQAatsESQQRESSQYYQRRLEElKAD 2075
Cdd:PTZ00121 1643 AEE--KKKAEELKKA------EEENKIKAAEEAKKA-------EEDKKKAEEAKKA---EEDEKKAAEALKKEAEE-AKK 1703
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2462585723 2076 MEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2127
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1443-1987 |
3.39e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1443 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacQVLESERAERLQAFREVQELKSK 1522
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-------ERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1523 HEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggdewqmrfDCAQMENEFLRKRLQQcEERLDSELTARKELEQKLGELQ 1602
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELA-----------EAEEALLEAEAELAEA-EEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1603 SAYDGAKKMAHQLKRKCHHLTCDLEDtcvLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWEL 1682
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1683 GQLQQQLKQKEQEASQLKQQVEMLQDH------KRELLGSPSLGENCVAGLKERLWKLESSALEQqkiqsqqentikqle 1756
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYegflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE--------------- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1757 qlrqrfELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDF- 1835
Cdd:COG1196 542 ------AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARy 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1836 -----------DVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLES 1904
Cdd:COG1196 616 yvlgdtllgrtLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1905 MHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELqLQLEEAKKEKHKLQE 1984
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELERELERLER 774
|
...
gi 2462585723 1985 QLQ 1987
Cdd:COG1196 775 EIE 777
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1445-2099 |
1.50e-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: 70.14 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1445 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIAD---LTSDLADERFKGDVACQVLESERAerlQAFREVQELKS 1521
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEeiqENKDLIKENNATRHLCNLLKETCA---RSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1522 KHEQVQKKLGDVNkqleeaqqkiqlNDLERNPTGGDEWQMRFDCAQMENEFLRK----RLQQCEERLDSELTARK----- 1592
Cdd:pfam05483 177 EREETRQVYMDLN------------NNIEKMILAFEELRVQAENARLEMHFKLKedheKIQHLEEEYKKEINDKEkqvsl 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1593 ------ELEQKLGELQSAYDGAKKMAHQLKRKC--------------HHLTCDLEDTCVLLENQQSRNHELEKkqkkfDL 1652
Cdd:pfam05483 245 lliqitEKENKMKDLTFLLEESRDKANQLEEKTklqdenlkeliekkDHLTKELEDIKMSLQRSMSTQKALEE-----DL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1653 QLAQalgESVFEkglrekVTQENTSVRWELGqlqQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLW 1732
Cdd:pfam05483 320 QIAT---KTICQ------LTEEKEAQMEELN---KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQ 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1733 KLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQ--EEELEDVRQSCQKRLHQLEMQLEQEYEEKQ 1810
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgkEQELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1811 MVLHEKQDLEgligTLCDQIGHRDFDVEKRLRRDLRRTHALL---SDVQLLLGTMEDGKTSVSKEElEKVHSQLEQSEak 1887
Cdd:pfam05483 468 HYLKEVEDLK----TELEKEKLKNIELTAHCDKLLLENKELTqeaSDMTLELKKHQEDIINCKKQE-ERMLKQIENLE-- 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1888 ceealKTQKVLTADLESMHSEL---------------ENMTRNKSLV---DEQLYRLQFEKADLLKRIDEDQDDLNELMQ 1949
Cdd:pfam05483 541 -----EKEMNLRDELESVREEFiqkgdevkckldkseENARSIEYEVlkkEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1950 KHKDLIAQSAADIGQ-------IQELQLQLEEAKKekhKLQEQLQVAQMRIEYLEQS------TVDRAIVSRQEAVICDL 2016
Cdd:pfam05483 616 ENKALKKKGSAENKQlnayeikVNKLELELASAKQ---KFEEIIDNYQKEIEDKKISeeklleEVEKAKAIADEAVKLQK 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2017 ENKTEFQKvQIKRFEVLVIRLRDSLIKMGEEL-SQAATSESQQRESSQyyqrrleeLKADME-ELVQREAE--ASRRCME 2092
Cdd:pfam05483 693 EIDKRCQH-KIAEMVALMEKHKHQYDKIIEERdSELGLYKNKEQEQSS--------AKAALEiELSNIKAEllSLKKQLE 763
|
....*..
gi 2462585723 2093 LEKYVEE 2099
Cdd:pfam05483 764 IEKEEKE 770
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1864-2129 |
2.11e-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: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1864 DGKTSVSKEELEKVHSQLEQSEAKCEE-------------------ALKTQK------VLTADLESMHSELENMTRNKSL 1918
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEkrqqlerlrrerekaeryqALLKEKreyegyELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1919 VDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI--------GQIQELQLQLEEAKKEKHKLQEQLQVAQ 1990
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1991 MRIEyleqstvdraivsRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLE 2070
Cdd:TIGR02169 329 AEID-------------KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462585723 2071 ELKADMEELvqrEAEASRRCMELEKYVEELAAVRQtlqtDLETSIRRIADLQAALEEVA 2129
Cdd:TIGR02169 396 KLKREINEL---KRELDRLQEELQRLSEELADLNA----AIAGIEAKINELEEEKEDKA 447
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1444-2127 |
2.48e-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: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTS-DLADERFKGDVACQVLE-----SERAERLQAF--RE 1515
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMK----LDNEIKALKSrKKQMEKDNSELELKMEKvfqgtDEQLNDLYHNhqRT 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1516 VQELKSKHEQVQKKLGDVNKQLEEAQQKIQ--LNDLERNPTGGDEWQ---MRFDCAQMENEfLRKRLQQCEERLDSELTA 1590
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKERRLLNQEKTelLVEQGRLQLQADRHQehiRARDSLIQSLA-TRLELDGFERGPFSERQI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1591 R--------------KELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSrnhelEKKQKKFDLQLAQ 1656
Cdd:TIGR00606 393 KnfhtlvierqedeaKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQE-----ELKFVIKELQQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1657 ALGESVFEKglrekvTQENTSVRWELgqlqqQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGL---KERLWK 1733
Cdd:TIGR00606 468 GSSDRILEL------DQELRKAEREL-----SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhTTTRTQ 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1734 LESSALEQ----QKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQ--EEELEDVRQSCQKrLHQLEMQLEQEYE 1807
Cdd:TIGR00606 537 MEMLTKDKmdkdEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtRDRLAKLNKELAS-LEQNKNHINNELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1808 EKQMVLHEKQDlegligTLCDQIGHRDFDVE-KRLRRDLRRTHALLSdvqlllgtMEDGKTSVSKEELEKVHSQLEQSEA 1886
Cdd:TIGR00606 616 SKEEQLSSYED------KLFDVCGSQDEESDlERLKEEIEKSSKQRA--------MLAGATAVYSQFITQLTDENQSCCP 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1887 KCEEALKTQKVL---TADLESM-------HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIA 1956
Cdd:TIGR00606 682 VCQRVFQTEAELqefISDLQSKlrlapdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1957 QSAADIGQiQELQLQLEEAKKEKHKLQeQLQVAQMRIEYLEQSTVDRAI---VSRQEAVICDLENKTEFQKVQIKRFEVl 2033
Cdd:TIGR00606 762 RLKNDIEE-QETLLGTIMPEEESAKVC-LTDVTIMERFQMELKDVERKIaqqAAKLQGSDLDRTVQQVNQEKQEKQHEL- 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2034 virlrDSLIKMGEELSQAAtseSQQRESSQYYQRRLEELKADMEELvqreAEASRRCMELEKYVEELAAVRQTLQTDLET 2113
Cdd:TIGR00606 839 -----DTVVSKIELNRKLI---QDQQEQIQHLKSKTNELKSEKLQI----GTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
730
....*....|....
gi 2462585723 2114 SIRRIADLQAALEE 2127
Cdd:TIGR00606 907 AKEQDSPLETFLEK 920
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1444-1932 |
3.57e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELttlrRKLEKSEKLRNELRQNTDllESKIADLTSDLADERFKGDVACQVLESER-AERL----QAFREVQE 1518
Cdd:PTZ00121 1401 EEDKKKADEL----KKAAAAKKKADEAKKKAE--EKKKADEAKKKAEEAKKADEAKKKAEEAKkAEEAkkkaEEAKKADE 1474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1519 LKSKHEQvQKKLGDVNKQLEEAQQKI-QLNDLERNPTGGDEWQmrfdcaQMENEFLRKRLQQCEERLDSELTARKELEQK 1597
Cdd:PTZ00121 1475 AKKKAEE-AKKADEAKKKAEEAKKKAdEAKKAAEAKKKADEAK------KAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1598 LGELQSAYDGAK----KMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQ 1673
Cdd:PTZ00121 1548 ADELKKAEELKKaeekKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1674 ENtSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLK----------ERLWKLESSALEQQK 1743
Cdd:PTZ00121 1628 AE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaeedekkaaEALKKEAEEAKKAEE 1706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1744 IQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQE--EEL---EDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQD 1818
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKkaEEAkkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1819 LE-------------------------GLIGTLCDQIGHRDFDVEKR---LRRDLRRTHALLSDVQLLLGTMEDGKTSVS 1870
Cdd:PTZ00121 1787 EEdekrrmevdkkikdifdnfaniiegGKEGNLVINDSKEMEDSAIKevaDSKNMQLEEADAFEKHKFNKNNENGEDGNK 1866
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462585723 1871 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKAD 1932
Cdd:PTZ00121 1867 EADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRD 1928
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1521-2127 |
3.71e-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: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1521 SKHEQVQKKLGDVNKQLEEAQQKIQlnDLERNPTGGDEwqmrfDCAQMENEFlrKRLQQCEERLDSELTARKeleQKLGE 1600
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELK--NLDKNLNKDEE-----KINNSNNKI--KILEQQIKDLNDKLKKNK---DKINK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1601 LQSaydGAKKMAHQLKRKchhltcdlEDTCVLLENQQSRnheLEKKQKKFDLQLAQALGESVFEKGLREKVTQENtsvrw 1680
Cdd:TIGR04523 101 LNS---DLSKINSEIKND--------KEQKNKLEVELNK---LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1681 elgqlqqqlkqkeqeaSQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQ 1760
Cdd:TIGR04523 162 ----------------NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1761 RFElEIERMKQMHQKDREDQEEELEDVRQscqkrlhQLEmQLEQEYEEKQMVLHEKQ-DLE---GLIGTLCDQIghrdfd 1836
Cdd:TIGR04523 226 QNN-QLKDNIEKKQQEINEKTTEISNTQT-------QLN-QLKDEQNKIKKQLSEKQkELEqnnKKIKELEKQL------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1837 vekrlrrdlrrtHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNK 1916
Cdd:TIGR04523 291 ------------NQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1917 SLVDEQLYrlqfEKADLLKRIDEDQDDLNELMQKHKDliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYL 1996
Cdd:TIGR04523 359 SEKQRELE----EKQNEIEKLKKENQSYKQEIKNLES----------QINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1997 EQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEvlviRLRDSLIKMGEELSQAATSESQQRESSqyyQRRLEELKAD 2075
Cdd:TIGR04523 425 EKEIERlKETIIKNNSEIKDLTNQDSVKELIIKNLD----NTRESLETQLKVLSRSINKIKQNLEQK---QKELKSKEKE 497
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2462585723 2076 MEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2127
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1738-2134 |
4.07e-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: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1738 ALEQQKIQSQQENTIKQLEQLRQRFELEIERmkqmHQKDREDQEEELEDVRQSCQ----KRLHQLEMQLEQEYEEKQMVL 1813
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELER----LEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1814 HEKQDLEgligTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVqlllgtmedgktsvsKEELEKVHSQLEQSEAKceealk 1893
Cdd:COG4913 359 RRRARLE----ALLAALGLPLPASAEEFAALRAEAAALLEAL---------------EEELEALEEALAEAEAA------ 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1894 tQKVLTADLESMHSELENMTRNKSLVDEQLYRLqfeKADLLKRIDEDQDDLN---ELMQ-KHKDLIAQSAAdigqiqELQ 1969
Cdd:COG4913 414 -LRDLRRELRELEAEIASLERRKSNIPARLLAL---RDALAEALGLDEAELPfvgELIEvRPEEERWRGAI------ERV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1970 L------------QLEEAKK--EKHKLQEQLQVAQMRIEYLEQSTVD---------------------RAIVSRQEAVIC 2014
Cdd:COG4913 484 LggfaltllvppeHYAAALRwvNRLHLRGRLVYERVRTGLPDPERPRldpdslagkldfkphpfrawlEAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2015 dLENKTEFQKVqikRFEVlvirLRDSLIKMGEELSQAATsesQQRESSQYY-----QRRLEELKADMEELVQREAEASRR 2089
Cdd:COG4913 564 -VDSPEELRRH---PRAI----TRAGQVKGNGTRHEKDD---RRRIRSRYVlgfdnRAKLAALEAELAELEEELAEAEER 632
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2462585723 2090 CMELEKYVEELAAVRQTLQT---------DLETSIRRIADLQAALEEVASSDSD 2134
Cdd:COG4913 633 LEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDASSDD 686
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1724-2144 |
6.07e-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: 65.08 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1724 VAGLKERlwKLESsaleQQKIQSQQENtIKQLEQLRqrFELE-----IERMKQMHQKDRE--DQEEELEdvRQSCQKRLH 1796
Cdd:TIGR02168 167 ISKYKER--RKET----ERKLERTREN-LDRLEDIL--NELErqlksLERQAEKAERYKElkAELRELE--LALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1797 QLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQI-GHRDFDVEkrLRRDLRRTHALLSDVQLLLGTMEdGKTSVSKEELE 1875
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLeELRLEVSE--LEEEIEELQKELYALANEISRLE-QQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1876 KVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLI 1955
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1956 AQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAvicdLENKTEfqkvqikRFEVLVI 2035
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE----LEELQE-------ELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2036 RLrdslikmgEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSi 2115
Cdd:TIGR02168 462 AL--------EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD- 532
|
410 420 430
....*....|....*....|....*....|..
gi 2462585723 2116 rriADLQAALEEVASSDSD---TESVQTAVDC 2144
Cdd:TIGR02168 533 ---EGYEAAIEAALGGRLQavvVENLNAAKKA 561
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1440-1900 |
1.64e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1440 TIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTSDLADERfkgdvacqvlesERAERLQAFREVQEL 1519
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELR------------EELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1520 KSKHEQVQKKLGDVNKQLEEAQQKIQ-LNDLERnptggdewqmrfDCAQMENEFLRKRLQQCEERLDSELTARKELEQ-- 1596
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEeLRELEE------------ELEELEAELAELQEELEELLEQLSLATEEELQDla 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1597 -KLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQEN 1675
Cdd:COG4717 199 eELEELQQRLAELEEELEEAQEELEELEEELEQ----LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1676 -----------TSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK-RELLGSPSLGENcvaGLKERLWKLESSALEQQK 1743
Cdd:COG4717 275 iagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEElEELLAALGLPPD---LSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1744 IQSQQENTIKQLEQlrQRFELEIER-MKQMHQKDREDQEEELEDVRQSCQ--KRLHQLEMQLEQEYEEKQMVL--HEKQD 1818
Cdd:COG4717 352 LLREAEELEEELQL--EELEQEIAAlLAEAGVEDEEELRAALEQAEEYQElkEELEELEEQLEELLGELEELLeaLDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1819 LEGLIGTLCDQIghrdfdveKRLRRDLRRTHALLSDVQLLLGTMEDGktsvskEELEKVHSQLEQSEAKCEEALKTQKVL 1898
Cdd:COG4717 430 LEEELEELEEEL--------EELEEELEELREELAELEAELEQLEED------GELAELLQELEELKAELRELAEEWAAL 495
|
..
gi 2462585723 1899 TA 1900
Cdd:COG4717 496 KL 497
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1696-2138 |
1.77e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1696 ASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLES------SALEQQKIQSQQENtiKQLEQLRQRFELEIERM 1769
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDrdeelrDRLEECRVAAQAHN--EEAESLREDADDLEERA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1770 KQMHQK----------------DREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghr 1833
Cdd:PRK02224 359 EELREEaaeleseleeareaveDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL--- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1834 dfdveKRLRRDLRRTHALLsdvqlllgtmEDGKTSVSKEELEKvhSQLEQSEAKCEEALKTQKVLTADLESMHSELEN-M 1912
Cdd:PRK02224 436 -----RTARERVEEAEALL----------EAGKCPECGQPVEG--SPHVETIEEDRERVEELEAELEDLEEEVEEVEErL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1913 TRNKSLV--DEQLYRLQfEKADLLK--------RIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKL 1982
Cdd:PRK02224 499 ERAEDLVeaEDRIERLE-ERREDLEeliaerreTIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1983 QEQLQVAQMRIEYLEqstvdraivsRQEAVICDLENktefqkvqikrfevlvirLRDSLIKMGEELSQAATSESQQRESS 2062
Cdd:PRK02224 578 NSKLAELKERIESLE----------RIRTLLAAIAD------------------AEDEIERLREKREALAELNDERRERL 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2063 QYYQRRLEELKAD-----MEELVQREAEASRRCMELEKYVEELAAVRQTLQTD---LETSIRRIADLQAALEEVASSDSD 2134
Cdd:PRK02224 630 AEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEA 709
|
....
gi 2462585723 2135 TESV 2138
Cdd:PRK02224 710 LEAL 713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1631-2126 |
1.78e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1631 VLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1710
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1711 R--ELLGSPSLGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR 1788
Cdd:COG4717 126 QllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1789 QSCQkrlhqlemQLEQEYEEKQMVLHE-KQDLEGLigtlcdQIGHRDFDVEKRLRRdLRRTHALLSDVQLLLGTMEDGKT 1867
Cdd:COG4717 206 QRLA--------ELEEELEEAQEELEElEEELEQL------ENELEAAALEERLKE-ARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1868 SVskeelekvhsqleqseakceeaLKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQfekaDLLKRIDEDQDDLNEL 1947
Cdd:COG4717 271 LI----------------------LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ----ALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1948 MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEylEQSTVDRAIVSRQEAVICDLENKTEFQKVQi 2027
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAGVEDEEELRAALEQAEEYQELK- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2028 KRFEVLVIRLRDSLIKMGEELsqAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEK--YVEELAAVRQ 2105
Cdd:COG4717 402 EELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELE 479
|
490 500
....*....|....*....|.
gi 2462585723 2106 TLQTDLETSIRRIADLQAALE 2126
Cdd:COG4717 480 ELKAELRELAEEWAALKLALE 500
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1581-2127 |
2.52e-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: 63.07 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1581 EERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTcdLEDTCVLLENQ--QSRNHELEKKQKKFDLQLAQAL 1658
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELE--EEYLLYLDYLKlnEERIDLLQELLRDEQEEIESSK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1659 GESVFEKglrEKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspSLGENCVAGLKERLWKLESSA 1738
Cdd:pfam02463 258 QEIEKEE---EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK----VDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1739 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEE---ELEDVRQSCQKRLHQLEMQLEQEYEEKQMV--L 1813
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEllaKKKLESERLSSAAKLKEEELELKSEEEKEAqlL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1814 HEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKT-SVSKEELEKVHSQLEQSEAKCEEAL 1892
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDElELKKSEDLLKETQLVKLQEQLELLL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1893 KTQKVLTAD-LESMHSELENMtrNKSLVDEQLYRLQFEKADLLKRIDE-DQDDLNELMQKHKDLIAQSAADIGQIQELQL 1970
Cdd:pfam02463 491 SRQKLEERSqKESKARSGLKV--LLALIKDGVGGRIISAHGRLGDLGVaVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1971 QLEEAKKEKHKLQEQLQVAQMRIeyleqstVDRAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQ 2050
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPL-------KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESA 641
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462585723 2051 AATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2127
Cdd:pfam02463 642 KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1444-2110 |
2.71e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEE--ELTTLRRKLEKSEKlRNELRQNTDLLESKiADLTSDLADERFKGDVACQVLESERAERLQAFREVQEL-K 1520
Cdd:PTZ00121 1293 DEAKKAEEkkKADEAKKKAEEAKK-ADEAKKKAEEAKKK-ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1521 SKHEQVQKKLGDVNKQLEEAQQKIQL-NDLERNPTGGDEWQMRfDCAQMENEFLRKRLQqcEERLDSELTARKELEQKLG 1599
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAkKKAEEDKKKADELKKA-AAAKKKADEAKKKAE--EKKKADEAKKKAEEAKKAD 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1600 ELQSAYDGAKKmAHQLKRKCHhltcdledtcvllenQQSRNHELEKK-QKKFDLQLAQALGESVFEKGLREKVTQENTSV 1678
Cdd:PTZ00121 1448 EAKKKAEEAKK-AEEAKKKAE---------------EAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1679 RWELGQLQQQLKQKEQEASQLKQQVEMLQDhKRELLGSPSLGEncvaglKERLWKLES--SALEQQKIQSQQENTIKQLE 1756
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEEAKKADEAKK-AEEKKKADELKK------AEELKKAEEkkKAEEAKKAEEDKNMALRKAE 1584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1757 QLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKrlhqlEMQLEQEYEEKQMVLHEKQDLEGligtlcdqighrdfd 1836
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-----AEELKKAEEEKKKVEQLKKKEAE--------------- 1644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1837 vEKRLRRDLRRthallsdvqlllgtmEDGKTSVSKEELEKvhsQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNk 1916
Cdd:PTZ00121 1645 -EKKKAEELKK---------------AEEENKIKAAEEAK---KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA- 1704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1917 slvdEQLYRLQFE---KADLLKRIDEDQDDLNELMQKhkdliaQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQmRI 1993
Cdd:PTZ00121 1705 ----EELKKKEAEekkKAEELKKAEEENKIKAEEAKK------EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE-EI 1773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1994 EYLEQSTVDRAIVSRQEAVICDLENKTefqKVQIKRFEVLV-------IRLRDSLIKMGEELSQAATSESQQRESSQYYQ 2066
Cdd:PTZ00121 1774 RKEKEAVIEEELDEEDEKRRMEVDKKI---KDIFDNFANIIeggkegnLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2462585723 2067 RRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTD 2110
Cdd:PTZ00121 1851 KHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1452-2138 |
2.76e-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: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1452 ELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADErfKGDVACQVLESERAE-RLQAFRE--VQELKSKHEQ--- 1525
Cdd:pfam12128 274 IASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAA--DAAVAKDRSELEALEdQHGAFLDadIETAAADQEQlps 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1526 VQKKLGDVNKQ---LEEAQQKIQ-------LNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDSELtaRKELE 1595
Cdd:pfam12128 352 WQSELENLEERlkaLTGKHQDVTakynrrrSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL--REQLE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1596 QKLGELQSAYDGAKKMAHQLKRKCHHLTCDlEDTCVLLENQQSRNHELEKKQKK-----FDLQLAQALGESVFEKGLrEK 1670
Cdd:pfam12128 430 AGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAanaevERLQSELRQARKRRDQAS-EA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1671 VTQENTSVRWELGQLQQQLKQKEQEASQL----KQQVEMLQDH-----KRELLG----SPSLGENCVAG----------- 1726
Cdd:pfam12128 508 LRQASRRLEERQSALDELELQLFPQAGTLlhflRKEAPDWEQSigkviSPELLHrtdlDPEVWDGSVGGelnlygvkldl 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1727 --------------LKERLWKLESSALEQQKIQSQQEntiKQLEQLRQRFE---LEIERMKQMHQKDREDQeEELEDVRQ 1789
Cdd:pfam12128 588 kridvpewaaseeeLRERLDKAEEALQSAREKQAAAE---EQLVQANGELEkasREETFARTALKNARLDL-RRLFDEKQ 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1790 SCQKRLHQlemqleQEYEEKQMVLHEKQDLEGLIGTLcdQIGHRDFDVEKRlRRDLRRTHALLSDVQLLLGTMEDGKTSV 1869
Cdd:pfam12128 664 SEKDKKNK------ALAERKDSANERLNSLEAQLKQL--DKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQLALL 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1870 sKEELEKVHSQLEQSEAKCEEALKT---------QKV--LTADLESMHSELENMTRNKSLVDE--QLYRLQF--EKADLL 1934
Cdd:pfam12128 735 -KAAIAARRSGAKAELKALETWYKRdlaslgvdpDVIakLKREIRTLERKIERIAVRRQEVLRyfDWYQETWlqRRPRLA 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1935 KRIDEDQDDLNELMQkhkDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYL----EQSTVDRAIVSRQE 2010
Cdd:pfam12128 814 TQLSNIERAISELQQ---QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatlkEDANSEQAQGSIGE 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2011 AVIC--DLENKTEFQKVQIKRFevlvIRLRDSLI--KMGEELsqAATSESqQRESSQYYQRRLEELKADMEELVQREAEA 2086
Cdd:pfam12128 891 RLAQleDLKLKRDYLSESVKKY----VEHFKNVIadHSGSGL--AETWES-LREEDHYQNDKGIRLLDYRKLVPYLEQWF 963
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462585723 2087 SRRCMELEKYVEELAAVRQTLQTD----LETSIRRIADLQAALEEVASSDSDTESV 2138
Cdd:pfam12128 964 DVRVPQSIMVLREQVSILGVDLTEfydvLADFDRRIASFSRELQREVGEEAFFEGV 1019
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1444-2328 |
2.94e-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: 62.83 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKS-EKLRNELRQNTDLLESKIADLTSDLAderfkgdVACQVLESERAERLQAFREVQELKsk 1522
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTvSQLRSELREAKRMYEDKIEELEKQLV-------LANSELTEARTERDQFSQESGNLD-- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1523 hEQVQKKLGDVNKQ-----LEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENEflrkRLQQCEERLDSEltARKELEQK 1597
Cdd:pfam15921 377 -DQLQKLLADLHKRekelsLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQ----RLEALLKAMKSE--CQGQMERQ 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1598 LGELQSAYDGAKKMAhqlkrkchHLTCDLEDTCVLL----ENQQSRNHELEKKQKKFDlQLAQALGESvfEKGLrEKVTQ 1673
Cdd:pfam15921 450 MAAIQGKNESLEKVS--------SLTAQLESTKEMLrkvvEELTAKKMTLESSERTVS-DLTASLQEK--ERAI-EATNA 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1674 ENTSVRwelgqlqqqlkqkeqeaSQLKQQVEMLQDHKREllgspslGENcvaglkerlwkLESSALEQQKIQSQQENTIK 1753
Cdd:pfam15921 518 EITKLR-----------------SRVDLKLQELQHLKNE-------GDH-----------LRNVQTECEALKLQMAEKDK 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1754 QLEQLRQrfelEIERMKQM-HQKDREDQEEELEdvrqscqkrlhqlEMQLEQEYEEKQMVLHEKQDLEgligtlcDQIGH 1832
Cdd:pfam15921 563 VIEILRQ----QIENMTQLvGQHGRTAGAMQVE-------------KAQLEKEINDRRLELQEFKILK-------DKKDA 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1833 RDFDVEKRLrRDLRrthalLSDVQLLLGTMEDGKTSVS-KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELEn 1911
Cdd:pfam15921 619 KIRELEARV-SDLE-----LEKVKLVNAGSERLRAVKDiKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEME- 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1912 MTRNKslvdeqlYRLQFEKADllkridedqddlNELMQKHKDLIAQSAADiGQIQELQLQLEEAKKEKhklQEQLQVAQM 1991
Cdd:pfam15921 692 TTTNK-------LKMQLKSAQ------------SELEQTRNTLKSMEGSD-GHAMKVAMGMQKQITAK---RGQIDALQS 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1992 RIEYLEQSTVDraivsrqeavicdlENKTefqkvqiKRFevlvirLRDSLIKMGEELSQAATSESQ---QRESSQYYQRR 2068
Cdd:pfam15921 749 KIQFLEEAMTN--------------ANKE-------KHF------LKEEKNKLSQELSTVATEKNKmagELEVLRSQERR 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2069 LEELKADMEELVQREAEASRRCMELEKYvEELAAVRQTLQTDLETS------IRRIADLQAALEEVASSDSDTESVQTAV 2142
Cdd:pfam15921 802 LKEKVANMEVALDKASLQFAECQDIIQR-QEQESVRLKLQHTLDVKelqgpgYTSNSSMKPRLLQPASFTRTHSNVPSSQ 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2143 DCGSSGRKEMDNVSILSSQPEGSLQSWLSCTLSL-----ATDTMRTPSRQSATSSRILSPRINEEAgdterTQSALALSR 2217
Cdd:pfam15921 881 STASFLSHHSRKTNALKEDPTRDLKQLLQELRSVineepTVQLSKAEDKGRAPSLGALDDRVRDCI-----IESSLRSDI 955
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2218 ARSTNVHSKTSGDKpVSPHFVRRQKYCHFGDGEVLAVQRKSTERLEPASSPLASRSTNTSPlsrEKLPSPSaALSEFVEG 2297
Cdd:pfam15921 956 CHSSSNSLQTEGSK-SSETCSREPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSP---KKSPVHS-LLTSSAEG 1030
|
890 900 910
....*....|....*....|....*....|....*
gi 2462585723 2298 LRRKRAQRGQGSTL----GLEDWPTLPIyQTTGAS 2328
Cdd:pfam15921 1031 SIGSSSQYRSAKTIhspdSVKDSQSLPI-ETTGKT 1064
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1447-1913 |
4.76e-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: 62.11 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1447 RAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDladerfKGDVACQVLESERAERLqAFREVQELKSKHEQV 1526
Cdd:pfam01576 632 REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSS------KDDVGKNVHELERSKRA-LEQQVEEMKTQLEEL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1527 QKKLG---------DVNKQLEEAQqkiqlndLERnptggdEWQMRFDCAQMENEFLRKRLQQCEERLDSE-------LTA 1590
Cdd:pfam01576 705 EDELQatedaklrlEVNMQALKAQ-------FER------DLQARDEQGEEKRRQLVKQVRELEAELEDErkqraqaVAA 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1591 RKELEQKLGELQSAYDGA-----------KKMAHQLKrkchHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALG 1659
Cdd:pfam01576 772 KKKLELDLKELEAQIDAAnkgreeavkqlKKLQAQMK----DLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQE 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1660 ESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLgencvagLKERLWKLESSAL 1739
Cdd:pfam01576 848 DLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTEL-------LNDRLRKSTLQVE 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1740 EQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQkdredqeeELEDVRQSCQK--------RLHQLEMQLEQEYEEKQM 1811
Cdd:pfam01576 921 QLTTELAAERSTSQKSESARQQLERQNKELKAKLQ--------EMEGTVKSKFKssiaaleaKIAQLEEQLEQESRERQA 992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1812 VlhekqdlegligtlcdqighrdfdvekrlRRDLRRTHALLSDVqLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEA 1891
Cdd:pfam01576 993 A-----------------------------NKLVRRTEKKLKEV-LLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
490 500
....*....|....*....|..
gi 2462585723 1892 LKTQKVLTADLESMHSELENMT 1913
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDAT 1064
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1444-2121 |
5.95e-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: 62.01 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1523
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1524 EQVQKKLGDVNKQLEEAQQKiqLNDLERnptggdewqmRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQ------- 1596
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEE--YDRVEK----------ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhg 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1597 ---KLGELQSAYDGAKKMAhqLKRKCHHLTCDLEDTCV-----LLENQQSRNHEL---EKKQKKFDLQLAQALGESVFEK 1665
Cdd:TIGR02169 526 tvaQLGSVGERYATAIEVA--AGNRLNNVVVEDDAVAKeaielLKRRKAGRATFLplnKMRDERRDLSILSEDGVIGFAV 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1666 GLREKVTQENTSVRWELGQLQQqlkqkeqeasqlkqqVEMLqDHKRELLGspslgencvaglKERLWKLESSALEQQKIQ 1745
Cdd:TIGR02169 604 DLVEFDPKYEPAFKYVFGDTLV---------------VEDI-EAARRLMG------------KYRMVTLEGELFEKSGAM 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1746 SQQENTIKQLEQLRQRFELEIERMKqmhqkdreDQEEELEDVRQSCQKRLHQLEMQLEQeyeekqmVLHEKQDLEGLIGT 1825
Cdd:TIGR02169 656 TGGSRAPRGGILFSRSEPAELQRLR--------ERLEGLKRELSSLQSELRRIENRLDE-------LSQELSDASRKIGE 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1826 LCDQIghrdfdveKRLRRDLRRTHALLSDVQLLLGTMEDGKTSV--SKEELEKVHSQLEQSEAKCEEALktqkvltADLE 1903
Cdd:TIGR02169 721 IEKEI--------EQLEQEEEKLKERLEELEEDLSSLEQEIENVksELKELEARIEELEEDLHKLEEAL-------NDLE 785
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1904 SM--HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHK 1981
Cdd:TIGR02169 786 ARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1982 LQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQ------AATS 2054
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkgEDEE 945
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462585723 2055 ESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADL 2121
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1925-2127 |
6.74e-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: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1925 RLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdra 2004
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2005 ivsrqeavicDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREA 2084
Cdd:COG4942 98 ----------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462585723 2085 EASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2127
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1724-2230 |
1.75e-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: 60.52 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1724 VAGLKERLwkLESSAL-EQQKIQSQQenTIKQLEQLRQRFELEIERMKQMHQKDREDQEeeleDVRQSCQKRLHQLEmql 1802
Cdd:pfam15921 87 VKDLQRRL--NESNELhEKQKFYLRQ--SVIDLQTKLQEMQMERDAMADIRRRESQSQE----DLRNQLQNTVHELE--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1803 eqeyEEKQMvlheKQDLEGLIGTLCDQighrdfdvekrLRRDLRRTHALLSDVQLLLGTMEDGKTsvskeelEKVHSQLE 1882
Cdd:pfam15921 156 ----AAKCL----KEDMLEDSNTQIEQ-----------LRKMMLSHEGVLQEIRSILVDFEEASG-------KKIYEHDS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1883 QSeakceealktqkvlTADLESMHSELENMTRNkslVDEQLYRLQ---FEKADLLKRI-DEDQDDLNELMQKHKDLIAQ- 1957
Cdd:pfam15921 210 MS--------------TMHFRSLGSAISKILRE---LDTEISYLKgriFPVEDQLEALkSESQNKIELLLQQHQDRIEQl 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1958 -SAADIgQIQELQLQLEEAKKEKHKLQEQLQVAQmrieylEQSTVDRAIVSRQeavICDLEN-----KTEFQKVQiKRFE 2031
Cdd:pfam15921 273 iSEHEV-EITGLTEKASSARSQANSIQSQLEIIQ------EQARNQNSMYMRQ---LSDLEStvsqlRSELREAK-RMYE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2032 VLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEelvQREAEASrrcmeLEKYVEELAAVRQT----- 2106
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH---KREKELS-----LEKEQNKRLWDRDTgnsit 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2107 ---LQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVDCGSSgrKEMDNVSILSSQPEGSLQSWLSCTLSLATDTMRT 2183
Cdd:pfam15921 414 idhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKN--ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2462585723 2184 PSRQSATSSriLSPRINEEAGDTERTQSALALSRAR-----STNVHSKTSGD 2230
Cdd:pfam15921 492 ESSERTVSD--LTASLQEKERAIEATNAEITKLRSRvdlklQELQHLKNEGD 541
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1871-2127 |
2.12e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1871 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1950
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1951 HKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKTEFQKVQIKR- 2029
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIe 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2030 FEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQT 2109
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250
....*....|....*...
gi 2462585723 2110 DLETSIRRIADLQAALEE 2127
Cdd:COG4372 291 AALELKLLALLLNLAALS 308
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1445-1992 |
4.71e-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: 58.96 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1445 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDL-------LESKIADLTSDLADERfkgdVACQvleseraerlqafREVQ 1517
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLqdenlkeLIEKKDHLTKELEDIK----MSLQ-------------RSMS 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1518 ELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMEnEFLRKRLQQCEERLDSELTARKELEQK 1597
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE-ELLRTEQQRLEKNEDQLKIITMELQKK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1598 LGELQSAydgaKKMAHQLKRKCHHLTCDL-EDTCVLLENQQSRNHELEKKQKKFDLQ-LAQALGESVFEkgLREKVTQEN 1675
Cdd:pfam05483 390 SSELEEM----TKFKNNKEVELEELKKILaEDEKLLDEKKQFEKIAEELKGKEQELIfLLQAREKEIHD--LEIQLTAIK 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1676 TSVRWelgqlqqqlkqkeqeasQLKQQVEMLQDHKRELLGSPSLGENCvaglkeRLWKLESSALEQQ------KIQSQQE 1749
Cdd:pfam05483 464 TSEEH-----------------YLKEVEDLKTELEKEKLKNIELTAHC------DKLLLENKELTQEasdmtlELKKHQE 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1750 NTIKQLEQlRQRFELEIERMKQMHQKDREdqeeELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQ 1829
Cdd:pfam05483 521 DIINCKKQ-EERMLKQIENLEEKEMNLRD----ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1830 IGHRDFDVEKRLR--RDLRRTHALLSDVqlllGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKT-QKVLTADLESMH 1906
Cdd:pfam05483 596 CNNLKKQIENKNKniEELHQENKALKKK----GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNyQKEIEDKKISEE 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1907 SELENMTRNKSLVDEQLyRLQFEkadLLKRIDEDQDDLNELMQKHK---DLIA----------------QSAADIGQIQE 1967
Cdd:pfam05483 672 KLLEEVEKAKAIADEAV-KLQKE---IDKRCQHKIAEMVALMEKHKhqyDKIIeerdselglyknkeqeQSSAKAALEIE 747
|
570 580 590
....*....|....*....|....*....|....*..
gi 2462585723 1968 L------------QLQLEEAKKEKHKLQEQLQVAQMR 1992
Cdd:pfam05483 748 LsnikaellslkkQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1838-2128 |
1.30e-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: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1838 EKRLRRDLRRTHALlsdvqlllgtmedGKTSVSK-EELEKVHSQLEQSEAKCEEALKTQKVLTADLE---SMHSELENMT 1913
Cdd:COG4913 591 EKDDRRRIRSRYVL-------------GFDNRAKlAALEAELAELEEELAEAEERLEALEAELDALQerrEALQRLAEYS 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1914 RNKSLVDEQLYRLQfEKADLLKRIDEDQDDLNELMQKHKDLIAQsaadigqIQELQLQLEEAKKEKHKLQEQLQVAQMRI 1993
Cdd:COG4913 658 WDEIDVASAEREIA-ELEAELERLDASSDDLAALEEQLEELEAE-------LEELEEELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1994 EYLeQSTVDRAIVSRQEAVICDLENKteFQKVQI-KRFEVLVIRLRDSLIKMGEELSQAATS-ESQQR------------ 2059
Cdd:COG4913 730 DEL-QDRLEAAEDLARLELRALLEER--FAAALGdAVERELRENLEERIDALRARLNRAEEElERAMRafnrewpaetad 806
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462585723 2060 -----ESSQYYQRRLEELKADmeELVQREAEASRRCMELEKyvEELAAVRQTLQTDLETSIRRIADLQAALEEV 2128
Cdd:COG4913 807 ldadlESLPEYLALLDRLEED--GLPEYEERFKELLNENSI--EFVADLLSKLRRAIREIKERIDPLNDSLKRI 876
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1444-1950 |
1.33e-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: 57.34 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSD---LADERFKGDVACQVLESERAERLQafrEVQELK 1520
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEnseKQRELEEKQNEIEKLKKENQSYKQ---EIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1521 SKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggdewqmrfdcaQMENEFlrKRLQQCEERLDSELtarKELEQKLGE 1600
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKE--------------LLEKEI--ERLKETIIKNNSEI---KDLTNQDSV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1601 LQSAYDGAKKMAHQLKRKchhltcdLEDtcvlLENQ-QSRNHELEKKQKKFDLQlaqalgesvfekglrekvtqentsvr 1679
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQ-------LKV----LSRSiNKIKQNLEQKQKELKSK-------------------------- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1680 welgqlqqqlkqkeqeasqlKQQVEMLQDHKRELlgspslgENCVAGLKErlwKLESSALEQQKIqsqqENTIKQLEQLR 1759
Cdd:TIGR04523 495 --------------------EKELKKLNEEKKEL-------EEKVKDLTK---KISSLKEKIEKL----ESEKKEKESKI 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1760 QRFELEIERMKQMHQKdredqeEELEDVRQSCQKRLHQLEMQ---LEQEYEEKQMVLHEKQDlegLIGTLCDQIGHRDFD 1836
Cdd:TIGR04523 541 SDLEDELNKDDFELKK------ENLEKEIDEKNKEIEELKQTqksLKKKQEEKQELIDQKEK---EKKDLIKEIEEKEKK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1837 VEKrLRRDLRRTHALLSDVQLLLGTMEDGKTSVsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLE------------- 1903
Cdd:TIGR04523 612 ISS-LEKELEKAKKENEKLSSIIKNIKSKKNKL-KQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDdiielmkdwlkel 689
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2462585723 1904 SMHSE--LENMTRNKSLvdEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1950
Cdd:TIGR04523 690 SLHYKkyITRMIRIKDL--PKLEEKYKEIEKELKKLDEFSKELENIIKN 736
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1428-2101 |
1.94e-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: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1428 QLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEKSEKlrnelRQNTDLLESKIADLTSDLADerfkgdvacqVLESERA 1507
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-----NSLTETLKKEVKSLQNEKAD----------LDRKLRK 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1508 ErlqafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNdlernptggdEWQMRFDCAQMENEFLRKRlqQCEERLDSE 1587
Cdd:TIGR00606 520 L-----DQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI----------KSRHSDELTSLLGYFPNKK--QLEDWLHSK 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1588 LTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLE-------DTCVlLENQQSRNHELEKKQKKFDLQLAQALGE 1660
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklfDVCG-SQDEESDLERLKEEIEKSSKQRAMLAGA 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1661 SVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLESSALE 1740
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST-------ESELKKKEKRRDEMLGLAPG 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1741 QQKIQSQQENTIKQLEQLRQRFELEIERMKQmhqkDREDQEEELEDVR------QSCQKRLHQLEMQLEQEYEEKQMVLH 1814
Cdd:TIGR00606 735 RQSIIDLKEKEIPELRNKLQKVNRDIQRLKN----DIEEQETLLGTIMpeeesaKVCLTDVTIMERFQMELKDVERKIAQ 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1815 EKQDLEGLIGTLCDQighrdfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVskEELEKVHSQLEQSEAKCEEALKT 1894
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQ------QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI--QHLKSKTNELKSEKLQIGTNLQR 882
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1895 QKVLTADLESMHSELENM------TRNKSLVDEQ-LYRLQFEKADLLKRIDED----QDDLNELMQKHKDLIAQSAADIG 1963
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLireikdAKEQDSPLETfLEKDQQEKEELISSKETSnkkaQDKVNDIKEKVKNIHGYMKDIEN 962
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1964 QIQE---------------LQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTV---DRAIVSRQEAVICDLENKTEFQKV 2025
Cdd:TIGR00606 963 KIQDgkddylkqketelntVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERwlqDNLTLRKRENELKEVEEELKQHLK 1042
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462585723 2026 QIKRFEVLviRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELA 2101
Cdd:TIGR00606 1043 EMGQMQVL--QMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELV 1116
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1753-2132 |
2.30e-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: 56.65 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1753 KQLEQLRqRFELEIE-RMKQMHQKDREDQE--EELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEK---QDLEGLIGTL 1826
Cdd:pfam05483 85 KEAEKIK-KWKVSIEaELKQKENKLQENRKiiEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnatRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1827 CDQIGHRDFDVEKRlRRDLRRTHA-LLSDVQLLLGTMEDGKTSVSKEELEkVHSQLEQSEAKCEEALktqkvltadlESM 1905
Cdd:pfam05483 164 CARSAEKTKKYEYE-REETRQVYMdLNNNIEKMILAFEELRVQAENARLE-MHFKLKEDHEKIQHLE----------EEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1906 HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHK-------DLIAQSAADIGQIQELQLQLEEAKKE 1978
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1979 KHKLQEQLQVAQMRIEYL--------EQSTVDRA----IVSRQEAVICDLEnktEFQKVQIKRFEvlviRLRDSLIKMGE 2046
Cdd:pfam05483 312 QKALEEDLQIATKTICQLteekeaqmEELNKAKAahsfVVTEFEATTCSLE---ELLRTEQQRLE----KNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2047 ELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALE 2126
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK----QFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
....*.
gi 2462585723 2127 EVASSD 2132
Cdd:pfam05483 461 AIKTSE 466
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1869-2128 |
2.96e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1869 VSKEELEKVHSQLEQSEaKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNEL- 1947
Cdd:PRK03918 142 ESDESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELr 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1948 --MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraivsrqeavICDLENKTEFQKv 2025
Cdd:PRK03918 221 eeLEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE-------------IEELEEKVKELK- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2026 QIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEEL---KADMEELVQREAEASRRCMELEKYVEELAA 2102
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELeekEERLEELKKKLKELEKRLEELEERHELYEE 366
|
250 260 270
....*....|....*....|....*....|.
gi 2462585723 2103 VRQtLQTDLET-----SIRRIADLQAALEEV 2128
Cdd:PRK03918 367 AKA-KKEELERlkkrlTGLTPEKLEKELEEL 396
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1744-2125 |
3.42e-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: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1744 IQSQQENTIKQLEQLRQRFEL---EIERMKQMHQKDREDQEEELEDVRQSCQkRLHQLEMQLEQEYEEKQMVLHEKQDLE 1820
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAanrQREKEKERYKRDREQWERQRRELESRVA-ELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1821 GLIGTLCDQIGHRDFDVEKRLRRdlrrthaLLSDVQLLLGTMEDGKTSVS--KEELEKVHSQLEQSEAKCEEALKTQKVL 1898
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRE-------LEEDIKTLTQRVLERETELErmKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1899 TADLESMHSELENMTRNKSLVDEQLYRLQfekadllkridedqDDLNELMQKhkdliaqsaadIGQIQELQLQLEEAKKE 1978
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQ--------------DTITTLTQK-----------LTTAHRKEAENEALLEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1979 KHKLQEQLQVAQMRIEYLEQSTvdRAIVSRQEAVICDLeNKTEFQKVQikrfevLVIRLRDSLIKMGEELSQAATSESQQ 2058
Cdd:pfam07888 239 LRSLQERLNASERKVEGLGEEL--SSMAAQRDRTQAEL-HQARLQAAQ------LTLQLADASLALREGRARWAQERETL 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2059 RESSQYYQRRLEELKAD---MEELVQREAeasrrcMELEKYVEELAAVRQTLQTDLETSIRRIADLQAAL 2125
Cdd:pfam07888 310 QQSAEADKDRIEKLSAElqrLEERLQEER------MEREKLEVELGREKDCNRVQLSESRRELQELKASL 373
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1965-2219 |
4.20e-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: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1965 IQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIV----------SRQEAVICDLEN-KTEFQKVQiKRFEVL 2033
Cdd:pfam05701 79 IEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEASVaakaqlevakARHAAAVAELKSvKEELESLR-KEYASL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2034 VIRlRDSLIKMGEElsqaATSESQQREssqyyqRRLEELKAD----MEEL-----VQREAEASRRC-------------- 2090
Cdd:pfam05701 158 VSE-RDIAIKRAEE----AVSASKEIE------KTVEELTIEliatKESLesahaAHLEAEEHRIGaalareqdklnwek 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2091 ------MELEKYVEELAAVRQtLQTDLETSIRRIADLQA--------ALEEVASSDSDTE----SVQTAVDcgsSGRKEM 2152
Cdd:pfam05701 227 elkqaeEELQRLNQQLLSAKD-LKSKLETASALLLDLKAelaaymesKLKEEADGEGNEKktstSIQAALA---SAKKEL 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462585723 2153 DNV--SILSSQPE--------GSLQSWLSCTLS-LATdtmrtpSRQSATSSRILSPRINEEagdTERTQSALALSRAR 2219
Cdd:pfam05701 303 EEVkaNIEKAKDEvnclrvaaASLRSELEKEKAeLAS------LRQREGMASIAVSSLEAE---LNRTKSEIALVQAK 371
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1872-2141 |
4.40e-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: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1872 EELEKvhsQLEQSEAKCEEALKTQKvLTADLEsmhselenmtrnksLVDEQLYRLQFEKADllKRIDEDQDDLNELMQKH 1951
Cdd:COG1196 196 GELER---QLEPLERQAEKAERYRE-LKEELK--------------ELEAELLLLKLRELE--AELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1952 KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdraivsrqeavicdlenktefqkvQIKRFE 2031
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ---------------------------DIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2032 VLVIRLRDSLIKMGEELSQAATSESQQREssqyyqrRLEELKADMEELvqrEAEASRRCMELEKYVEELAAVRQTLQTDL 2111
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEE-------ELEELEEELEEA---EEELEEAEAELAEAEEALLEAEAELAEAE 378
|
250 260 270
....*....|....*....|....*....|
gi 2462585723 2112 ETSIRRIADLQAALEEVASSDSDTESVQTA 2141
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEA 408
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1724-2213 |
4.45e-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: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1724 VAGLKERLWKLESSaLEQQKIQSQQentikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLE 1803
Cdd:pfam15921 233 ISYLKGRIFPVEDQ-LEALKSESQN-----KIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1804 QEYEEKQMVLHEKQDLEGLIgtlcdqighrdfdveKRLRRDLRRTHALLSDvqlllgtmedgktsvSKEELEK--VHSQL 1881
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTV---------------SQLRSELREAKRMYED---------------KIEELEKqlVLANS 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1882 EQSEAKCEEALKTQKV--LTADLESMHSELENMTRNKSLVDEQLYRLQFEKA------DLLKRideDQDDLNELMQKHKD 1953
Cdd:pfam15921 357 ELTEARTERDQFSQESgnLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitiDHLRR---ELDDRNMEVQRLEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1954 LIA------------QSAADIG------QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQsTVDRAIVSRQEAvicd 2015
Cdd:pfam15921 434 LLKamksecqgqmerQMAAIQGknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER-TVSDLTASLQEK---- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2016 lENKTEFQKVQIKRFEVLV-IRLRD--SLIKMGEELSQAATSESQQRESSQYYQRRLEELKADME--------------- 2077
Cdd:pfam15921 509 -ERAIEATNAEITKLRSRVdLKLQElqHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgrtaga 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2078 ---ELVQREAEASRRCMELEKYveelaavrQTLQTDLETSIR----RIADLQaaLEEVASSDSDTESVQTAVDCgssgRK 2150
Cdd:pfam15921 588 mqvEKAQLEKEINDRRLELQEF--------KILKDKKDAKIReleaRVSDLE--LEKVKLVNAGSERLRAVKDI----KQ 653
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462585723 2151 EMDNVSILSSQPEGSLQSwLSCTLSLATDTMRTPSRQSATSSRILSPRINEEAGDTERTQSAL 2213
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNS-LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1941-2129 |
5.09e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1941 QDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ--STVDRAIVSRQEAvicdLEN 2018
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeiAEAEAEIEERREE----LGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2019 KTEFQKVQIKRFEVLvirlrdSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVE 2098
Cdd:COG3883 91 RARALYRSGGSVSYL------DVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190
....*....|....*....|....*....|.
gi 2462585723 2099 ELAAVRQTLQTDLETSIRRIADLQAALEEVA 2129
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1889-2124 |
8.23e-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: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1889 EEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAqsaadigQIQEL 1968
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1969 QLQLEEAKKEkhkLQEQLQVAQM--RIEYLE----QSTVDRAIVSRQ--EAVICDLENKTEFQKVQIKRfevlVIRLRDS 2040
Cdd:COG4942 96 RAELEAQKEE---LAELLRALYRlgRQPPLAlllsPEDFLDAVRRLQylKYLAPARREQAEELRADLAE----LAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2041 LIKMGEELSQAATSESQQRessqyyqRRLEELKADMEELVqreAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD 2120
Cdd:COG4942 169 LEAERAELEALLAELEEER-------AALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
....
gi 2462585723 2121 LQAA 2124
Cdd:COG4942 239 AAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1853-2127 |
1.04e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1853 SDVQLLLGTMEDGKtsvsKEELEKVHSQLEQSEAKceEALKTQKVLTADLESMHSELENMTRNKSLVDEQLyrlqfEKAD 1932
Cdd:PRK02224 172 SDARLGVERVLSDQ----RGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETR-----DEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1933 L-LKRIDEDQDDLNELMQkhkdliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLE--------QSTVDR 2003
Cdd:PRK02224 241 EvLEEHEERREELETLEA--------------EIEDLRETIAETEREREELAEEVRDLRERLEELEeerddllaEAGLDD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2004 AIVSRQEAVICDLENKTEF-------QKVQIKRFEVLVIRLRDSLIKMGEEL----SQAATSESQ---QRESSQYYQRRL 2069
Cdd:PRK02224 307 ADAEAVEARREELEDRDEElrdrleeCRVAAQAHNEEAESLREDADDLEERAeelrEEAAELESEleeAREAVEDRREEI 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462585723 2070 EELKADMEELVQREAEASRRCMELEKYVEELAAVRQ-------TLQTDLETSIRRIADLQAALEE 2127
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDelrereaELEATLRTARERVEEAEALLEA 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1910-2139 |
1.18e-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: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1910 ENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHK--DLIAQSAADIGQIQELQLQLEEAkkekhklQEQLQ 1987
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA-------RAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1988 VAQMRIEYLEQ---STVDRAIVSRQEAVICDLenKTEFQKVQIKRFEvLVIRLRDSLIKMGEELSQAATSESQQRESSqy 2064
Cdd:COG3206 237 EAEARLAALRAqlgSGPDALPELLQSPVIQQL--RAQLAELEAELAE-LSARYTPNHPDVIALRAQIAALRAQLQQEA-- 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462585723 2065 yQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQT---LQTDLETSIRRIADLQAALEEV-ASSDSDTESVQ 2139
Cdd:COG3206 312 -QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARELYESLLQRLEEArLAEALTVGNVR 389
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1506-2156 |
1.95e-06 |
|
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: 53.69 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1506 RAERLQAfrEVQELKSKHEQVQK-KLGDVNKQLEEA-QQKIQ---LNDLE-RNPTGGDEWQMRFDCAQMENEFLRKRLQQ 1579
Cdd:pfam12128 242 EFTKLQQ--EFNTLESAELRLSHlHFGYKSDETLIAsRQEERqetSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1580 CEERLDSeLTARKELEQKLGELQSAYDgaKKMAHQLKRKCHHLTCDLEdtcVLLENQQSRNHELEKKQKKFDLQLAQALg 1659
Cdd:pfam12128 320 DRSELEA-LEDQHGAFLDADIETAAAD--QEQLPSWQSELENLEERLK---ALTGKHQDVTAKYNRRRSKIKEQNNRDI- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1660 eSVFEKGLREkvtQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKREL---LGSPSLGENCVAGLKERLWKLES 1736
Cdd:pfam12128 393 -AGIKDKLAK---IREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLksrLGELKLRLNQATATPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1737 SALEQQKIQSQQENTIKQLE-------QLRQRFELEIERMKQMHQKdredqeeeLEDVRQSCQKRLHQLEMQleqeyeeK 1809
Cdd:pfam12128 469 FDERIERAREEQEAANAEVErlqselrQARKRRDQASEALRQASRR--------LEERQSALDELELQLFPQ-------A 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1810 QMVLH----EKQDLEGLIGTLCD--QIGHRDFDVEKrlrrdlrrTHALLSDVQLLLGTMEDGKtSVSKEELEKVHSQLEQ 1883
Cdd:pfam12128 534 GTLLHflrkEAPDWEQSIGKVISpeLLHRTDLDPEV--------WDGSVGGELNLYGVKLDLK-RIDVPEWAASEEELRE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1884 SEAKCEEALKTQKVLTADLESMHSELenmtrNKSLvDEQLYRLQFEKADlLKRIDEDQDDLNELMQKHKDLIAQSAADIG 1963
Cdd:pfam12128 605 RLDKAEEALQSAREKQAAAEEQLVQA-----NGEL-EKASREETFARTA-LKNARLDLRRLFDEKQSEKDKKNKALAERK 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1964 QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQST-------------------VDRAIVSRQEAV-----ICDLENK 2019
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTekqaywqvvegaldaqlalLKAAIAARRSGAkaelkALETWYK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2020 TEFQKVQIKrfEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQR-----------RLEELKADMEEL------VQR 2082
Cdd:pfam12128 758 RDLASLGVD--PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQEtwlqrrprlatQLSNIERAISELqqqlarLIA 835
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462585723 2083 EAEASRRCMELEKYVEELAAVRQT-LQTDLETSIRRIADLQaaleEVASSDSDTESVQTAVDCGSSGRKEMDNVS 2156
Cdd:pfam12128 836 DTKLRRAKLEMERKASEKQQVRLSeNLRGLRCEMSKLATLK----EDANSEQAQGSIGERLAQLEDLKLKRDYLS 906
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1638-1919 |
2.99e-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: 52.82 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1638 SRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQ--DHKRELlg 1715
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRqeERKREL-- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1716 sPSLGENCVAGLKERLWKLESSALEQQ----KIQSQQENTIKQ--LEQLRQR------FELEIERMKQMHQKDR------ 1777
Cdd:pfam17380 363 -ERIRQEEIAMEISRMRELERLQMERQqkneRVRQELEAARKVkiLEEERQRkiqqqkVEMEQIRAEQEEARQRevrrle 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1778 EDQEEELEDVRQSCQKRLHQLEM--QLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDv 1855
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK- 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462585723 1856 qlllgTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESmHSELENMTRNKSLV 1919
Cdd:pfam17380 521 -----EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE-RSRLEAMEREREMM 578
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1733-1998 |
3.18e-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: 52.76 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1733 KLESSALEQQKIQSQQENTIKQLEQLRQR----------FELEIERMKQM--HQKDREDQEE--ELEDVRQSCQKRLHQL 1798
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARieeleedlhkLEEALNDLEARlsHSRIPEIQAElsKLEEEVSRIEARLREI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1799 EMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKE------ 1872
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKErdelea 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1873 ELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELenmtrnkSLVDEQLYRLQFEKADLLKrIDEDQDDLNELMQKHK 1952
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-------SEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIR 968
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462585723 1953 DLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1998
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1444-1877 |
3.65e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLeSKIADLTSDLADERfkgdvacQVLESERAERLQAFREVQELKSKH 1523
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEI-------NGIEERIKELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1524 EQVQKKLGDVN---KQLEEAQQKI-QLNDLERNPTGgdewqMRFDCAQMENEFLRKRLQQCEERLdSELTARK-ELEQKL 1598
Cdd:PRK03918 348 KELEKRLEELEerhELYEEAKAKKeELERLKKRLTG-----LTPEKLEKELEELEKAKEEIEEEI-SKITARIgELKKEI 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1599 GELQSAYDGAKKMahqlKRKC---------HH-------LTCDLED-----------------------TCVLLENQQSR 1639
Cdd:PRK03918 422 KELKKAIEELKKA----KGKCpvcgrelteEHrkelleeYTAELKRiekelkeieekerklrkelreleKVLKKESELIK 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1640 NH-------ELEKKQKKFDLQLAQALGESvFEKGLRE--KVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1710
Cdd:PRK03918 498 LKelaeqlkELEEKLKKYNLEELEKKAEE-YEKLKEKliKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1711 RELLgspSLGENCVAGLKERLWKLES------------SALE-----QQKIQSQQENTIKQLEQLRQRFELEIERMKQMH 1773
Cdd:PRK03918 577 KELE---ELGFESVEELEERLKELEPfyneylelkdaeKELEreekeLKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1774 QKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVlheKQDLEGLigtlcdqigHRDFDVEKRLRRDLRRTHALLS 1853
Cdd:PRK03918 654 KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEI---KKTLEKL---------KEELEEREKAKKELEKLEKALE 721
|
490 500
....*....|....*....|....
gi 2462585723 1854 DVQLLLGTMEDGKTSVSKEELEKV 1877
Cdd:PRK03918 722 RVEELREKVKKYKALLKERALSKV 745
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1727-2133 |
6.14e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1727 LKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFEL---EIERMKQMHQKDREDQE-EELEDVRQSCQKRLHQLEMQL 1802
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1803 eQEYEEKQmvlHEKQDLEGLIGTLCDQI----GHRDFDVEKRLRRDLRRTHALLSDVQLLLGTMEDgktsvSKEELEKVH 1878
Cdd:COG4717 156 -EELRELE---EELEELEAELAELQEELeellEQLSLATEEELQDLAEELEELQQRLAELEEELEE-----AQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1879 SQLEQSEAKCEEALKTQK---------------------------------VLTADLESMHSELENMTRNKSLVDEQLYR 1925
Cdd:COG4717 227 EELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1926 LQfekaDLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQvaqmrIEYLEQstvdrai 2005
Cdd:COG4717 307 LQ----ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-----LEELEQ------- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2006 vsrqeavicdlENKTEFQKVQIKrfevlvirLRDSLIKMGEELSQAAtsesQQRESSQYYQRRLEELKADMEELVQREAE 2085
Cdd:COG4717 371 -----------EIAALLAEAGVE--------DEEELRAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLEALDE 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2462585723 2086 AsrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDS 2133
Cdd:COG4717 428 E-----ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1515-2003 |
7.38e-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: 51.39 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1515 EVQELKSK-HEQVQKKLGDVNKQLEEAQQkiqLNDlernptggdewQMRFDCAQMENEFLRKRLQQCEERLDSELTARKE 1593
Cdd:pfam06160 46 KFEEWRKKwDDIVTKSLPDIEELLFEAEE---LND-----------KYRFKKAKKALDEIEELLDDIEEDIKQILEELDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1594 LEQKLGELQSAYDGAKKMAHQLKRKchhltcdledtcvLLENqqsrNHELEKKQKKFDLQLAQAlgESVFEKglrekVTQ 1673
Cdd:pfam06160 112 LLESEEKNREEVEELKDKYRELRKT-------------LLAN----RFSYGPAIDELEKQLAEI--EEEFSQ-----FEE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1674 ENTSvrwelgqlqqqlkQKEQEASQLKQQVEMLQDHKRELLGS-PSLGENCVAGLKERLWKLES--SALEQQKIQSQQEN 1750
Cdd:pfam06160 168 LTES-------------GDYLEAREVLEKLEEETDALEELMEDiPPLYEELKTELPDQLEELKEgyREMEEEGYALEHLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1751 TIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDvrqscqkRLHQLEMQLEQEYEEKQMVLHEKQDLEgligtlcDQI 1830
Cdd:pfam06160 235 VDKEIQQLEEQLEENLALLENLELDEAEEALEEIEE-------RIDQLYDLLEKEVDAKKYVEKNLPEIE-------DYL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1831 GHRDfDVEKRLRRDLRRT---------------------HALLSDVQLLLGTMEDGKTSVS--KEELEKVHSQLEQSEAK 1887
Cdd:pfam06160 301 EHAE-EQNKELKEELERVqqsytlnenelervrglekqlEELEKRYDEIVERLEEKEVAYSelQEELEEILEQLEEIEEE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1888 CEEALKTQKVLTAD-------LESMHSELENM-----TRNKSLVDEQlYRLQFEKA-DLLKRIDED-------------- 1940
Cdd:pfam06160 380 QEEFKESLQSLRKDelearekLDEFKLELREIkrlveKSNLPGLPES-YLDYFFDVsDEIEDLADElnevplnmdevnrl 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1941 ----QDDLNELMQKHKDLIaQSAADIGQ-IQ----------ELQLQLEEAKK--EKHKLQEQLQVAQMRIEYLEQSTVDR 2003
Cdd:pfam06160 459 ldeaQDDVDTLYEKTEELI-DNATLAEQlIQyanryrssnpEVAEALTEAELlfRNYDYEKALEIAATALEKVEPGAYER 537
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1430-1801 |
8.04e-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: 51.66 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1430 LGSLQPLLSATigTEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAER 1509
Cdd:pfam15921 463 VSSLTAQLEST--KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1510 lqafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERL--DSE 1587
Cdd:pfam15921 541 ----DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIlkDKK 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1588 LTARKELEQKLGELQ--------------SAYDGAKKMAHQLKRKCHHLTCDL----EDTCVLLENQQSRNHELEKKQKK 1649
Cdd:pfam15921 617 DAKIRELEARVSDLElekvklvnagserlRAVKDIKQERDQLLNEVKTSRNELnslsEDYEVLKRNFRNKSEEMETTTNK 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1650 FDLQLAQALGEsvfekglREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDhKRELLGSPSLGENcvaglKE 1729
Cdd:pfam15921 697 LKMQLKSAQSE-------LEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQS-KIQFLEEAMTNAN-----KE 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1730 R-LWKLESSALEQQ--KIQSQQENTIKQLEQLR---QRFELEIERMK--------QMHQKDREDQEEELEDVRQSCQKRL 1795
Cdd:pfam15921 764 KhFLKEEKNKLSQElsTVATEKNKMAGELEVLRsqeRRLKEKVANMEvaldkaslQFAECQDIIQRQEQESVRLKLQHTL 843
|
....*.
gi 2462585723 1796 HQLEMQ 1801
Cdd:pfam15921 844 DVKELQ 849
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1736-2128 |
8.15e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 51.76 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1736 SSALEQQKIQSQQENTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVRQSCQKRL-----HQLEMQLEQ--EYEE 1808
Cdd:PTZ00440 891 RSNSNKQLVEHLLNNKIDLKNKLEQHMK-IINTDNIIQKNEKLNLLNNLNKEKEKIEKQLsdtkiNNLKMQIEKtlEYYD 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1809 KQmvlheKQDLEGLIGTLCDQighrdFDVEKRLRRDLRRT-HALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAK 1887
Cdd:PTZ00440 970 KS-----KENINGNDGTHLEK-----LDKEKDEWEHFKSEiDKLNVNYNILNKKIDDLIKKQHDDIIELIDKLIKEKGKE 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1888 CEEalKTQKVLTAdLESMHSELENMTRNK-------SLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS-- 1958
Cdd:PTZ00440 1040 IEE--KVDQYISL-LEKMKTKLSSFHFNIdikkyknPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNAdk 1116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1959 ------------AADIG----QIQELQLQLEEAKKEKHKLQEqlqVAQMRIEYleqstvDRAIVSRQEAVICDLENKTEF 2022
Cdd:PTZ00440 1117 eknkqtehynkkKKSLEkiykQMEKTLKELENMNLEDITLNE---VNEIEIEY------ERILIDHIVEQINNEAKKSKT 1187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2023 QKVQIKRFEVLVIRLRDSLIKmgEELSQAATSESQQressqyYQRRLEELKADMEELVQrEAEASRRCMELEKYVEELAA 2102
Cdd:PTZ00440 1188 IMEEIESYKKDIDQVKKNMSK--ERNDHLTTFEYNA------YYDKATASYENIEELTT-EAKGLKGEANRSTNVDELKE 1258
|
410 420
....*....|....*....|....*.
gi 2462585723 2103 VRQTLQTDLETSIRRIADLQAALEEV 2128
Cdd:PTZ00440 1259 IKLQVFSYLQQVIKENNKMENALHEI 1284
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1744-2069 |
1.31e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.06 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1744 IQSQQENTIKQLEQLrqrfeleiERMKQMHQKDrEDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLI 1823
Cdd:PLN02939 102 MQRDEAIAAIDNEQQ--------TNSKDGEQLS-DFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1824 GTLcdqighrdfdvEKRLRRdlrrthallSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQ---SEAKCEEA-------LK 1893
Cdd:PLN02939 173 NIL-----------EMRLSE---------TDARIKLAAQEKIHVEILEEQLEKLRNELLIrgaTEGLCVHSlskeldvLK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1894 TQKV-LTADLESMHSELENMT----------RNKSLVDEQLYRLQFE----KADLLK----RID---EDQDDLNELMQKH 1951
Cdd:PLN02939 233 EENMlLKDDIQFLKAELIEVAeteervfkleKERSLLDASLRELESKfivaQEDVSKlsplQYDcwwEKVENLQDLLDRA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1952 KDLIAQSAADIGQ-------IQELQLQLEEAKKEKHKLqEQLQVAQMRIEYLEqstvdraivSRQEAviCDLENKTefqk 2024
Cdd:PLN02939 313 TNQVEKAALVLDQnqdlrdkVDKLEASLKEANVSKFSS-YKVELLQQKLKLLE---------ERLQA--SDHEIHS---- 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2462585723 2025 vQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRL 2069
Cdd:PLN02939 377 -YIQLYQESIKEFQDTLSKLKEESKKRSLEHPADDMPSEFWSRIL 420
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1739-2143 |
1.67e-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: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1739 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDRE-DQEEELEDVRQSCQKRLH--------QLEM--------- 1800
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDREsDRNQELQKRIRLLEKREAeaeealreQAELnrlkkkyle 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1801 ---QLEQEYEEKQMVLHEKQD-LEGLIGTLCDQIGHRDFDVE------KRLRRDLRRTHALLSDVQLLLGTMEdGKTSVS 1870
Cdd:pfam05557 87 alnKKLNEKESQLADAREVIScLKNELSELRRQIQRAELELQstnselEELQERLDLLKAKASEAEQLRQNLE-KQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1871 KEELEKVhSQLE---QSEAKCEEALKTQKVLTADLESMHSELE----------NMTRNKSLVDEQLYRLQ-----FEK-- 1930
Cdd:pfam05557 166 AEAEQRI-KELEfeiQSQEQDSEIVKNSKSELARIPELEKELErlrehnkhlnENIENKLLLKEEVEDLKrklerEEKyr 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1931 ---ADLLKRIDEDQDDLNE---LMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdra 2004
Cdd:pfam05557 245 eeaATLELEKEKLEQELQSwvkLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQE----- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2005 iVSRQEAVICDLENKTEFQKVQIKRFE---VLVIRLRDSLIKMGEELSqaatSESQQRESSQYYQRRLEELkADMEELVQ 2081
Cdd:pfam05557 320 -LAQYLKKIEDLNKKLKRHKALVRRLQrrvLLLTKERDGYRAILESYD----KELTMSNYSPQLLERIEEA-EDMTQKMQ 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462585723 2082 REAEASRrcMELEKYVEELAAVRQTLQTD-LETSIRRiadLQAALEEVASSDSDTESVQTAVD 2143
Cdd:pfam05557 394 AHNEEME--AQLSVAEEELGGYKQQAQTLeRELQALR---QQESLADPSYSKEEVDSLRRKLE 451
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1444-1804 |
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 2462585723 1444 EQLRAKEEELTTLRRKL-EKSEKLRNELRQNT-------DLLESKIADLTSDLadERFkgdvacqVLESERAERLQAFRE 1515
Cdd:PRK04778 129 QELLESEEKNREEVEQLkDLYRELRKSLLANRfsfgpalDELEKQLENLEEEF--SQF-------VELTESGDYVEAREI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1516 VQELKSKHEQVQKKLGDVNKQLEEAQQKI--QLNDLErnpTGGDEWQM---RFDCAQMENEF--LRKRLQQC-------- 1580
Cdd:PRK04778 200 LDQLEEELAALEQIMEEIPELLKELQTELpdQLQELK---AGYRELVEegyHLDHLDIEKEIqdLKEQIDENlalleeld 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1581 -----------EERLDS-------ELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLtcdledtcvllenQQSR--N 1640
Cdd:PRK04778 277 ldeaeekneeiQERIDQlydilerEVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRV-------------KQSYtlN 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1641 HELEKKQKKFDLQLAQAlgESVFEKgLREKVTQENTSvrwelgqlqqqlkqkeqeASQLKQQVEMLQDHkrellgspslg 1720
Cdd:PRK04778 344 ESELESVRQLEKQLESL--EKQYDE-ITERIAEQEIA------------------YSELQEELEEILKQ----------- 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1721 encvaglkerlwklessaLEQqkIQSQQENTIKQLEQLR----------QRFELEIERMKQMHQKDR-----EDQEEELE 1785
Cdd:PRK04778 392 ------------------LEE--IEKEQEKLSEMLQGLRkdeleareklERYRNKLHEIKRYLEKSNlpglpEDYLEMFF 451
|
410
....*....|....*....
gi 2462585723 1786 DVrqscQKRLHQLEMQLEQ 1804
Cdd:PRK04778 452 EV----SDEIEALAEELEE 466
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1871-2087 |
3.06e-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: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1871 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESmHSELENMTRnkslVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1950
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA-KLLLQQLSE----LESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1951 HKDLIAQSAAD--IGQIQELQLQLEEAKK---EKH----KLQEQLQVAQmrieyleqstvdRAIVSRQEAVICDLENKTE 2021
Cdd:COG3206 256 LPELLQSPVIQqlRAQLAELEAELAELSArytPNHpdviALRAQIAALR------------AQLQQEAQRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462585723 2022 FQKVQIKrfevlviRLRDSLIKMGEELSQAATSESQQREssqyYQRRLEELKADMEELVQREAEAS 2087
Cdd:COG3206 324 ALQAREA-------SLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRLEEAR 378
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1872-2100 |
3.92e-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: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1872 EELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKH 1951
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1952 KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStVDRAI--VSRQEAVICDLENKTEFQKVQIKR 2029
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGD-LERAEerAELAESKIVELEEELKVVGNNLKS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462585723 2030 FEVlvirlrdslikmgeelsqaATSESQQRESSqyYQRRLEELKADMEELVQREAEASRRCMELEKYVEEL 2100
Cdd:pfam00261 160 LEA-------------------SEEKASEREDK--YEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRL 209
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1443-1610 |
4.74e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1443 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAERLQAFREVQELKSK 1522
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE-------AQELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1523 HEQVQKKLGDVNKQLEEAQQKIQlndlERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERldsELTAR-KELEQKLGEL 1601
Cdd:COG1340 80 RDELNEKLNELREELDELRKELA----ELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK---ELVEKiKELEKELEKA 152
|
....*....
gi 2462585723 1602 QSAYDGAKK 1610
Cdd:COG1340 153 KKALEKNEK 161
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1450-2058 |
5.57e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1450 EEELTTLRRKLEKSEKLRNELRQNTDLLES---KIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQV 1526
Cdd:PRK01156 172 KDVIDMLRAEISNIDYLEEKLKSSNLELENikkQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1527 QKklgdVNKQLEEAQQKIQLNDLERNP-TGGDEWQMRF--DCAQMENEFLRK---------RLQQCEERLDSELTARKEL 1594
Cdd:PRK01156 252 NR----YESEIKTAESDLSMELEKNNYyKELEERHMKIinDPVYKNRNYINDyfkykndieNKKQILSNIDAEINKYHAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1595 EQKLGELQSAYDGAKKMAHQ---LKRKCHHLTCDLEDTCVLLENQQSRN---HELEKKQKKFDLQLAQALGESVFE---- 1664
Cdd:PRK01156 328 IKKLSVLQKDYNDYIKKKSRyddLNNQILELEGYEMDYNSYLKSIESLKkkiEEYSKNIERMSAFISEILKIQEIDpdai 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1665 KGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGE----NCVAGLKERLWKLESSALE 1740
Cdd:PRK01156 408 KKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEeksnHIINHYNEKKSRLEEKIRE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1741 QQKIQSQQENTIKQLEQLRQRFEL-EIERMKQMHQKdREDQEEELEDVRQScQKRLHQLEMQLEQEYEE-KQMVLhekQD 1818
Cdd:PRK01156 488 IEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNK-IESARADLEDIKIK-INELKDKHDKYEEIKNRyKSLKL---ED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1819 LEGLIGTLCDQIGHRD-FDVEK-RLRRDlrrthallsDVQLLLGTMEDGKTSVsKEELEKVHSQLEQSEAKCEEALKTqk 1896
Cdd:PRK01156 563 LDSKRTSWLNALAVISlIDIETnRSRSN---------EIKKQLNDLESRLQEI-EIGFPDDKSYIDKSIREIENEANN-- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1897 vltadLESMHSELENmtrNKSLVDEqlyrLQFEKADLLKRI---DEDQDDLNELMQKhkdlIAQSAADIGQIQElqlQLE 1973
Cdd:PRK01156 631 -----LNNKYNEIQE---NKILIEK----LRGKIDNYKKQIaeiDSIIPDLKEITSR----INDIEDNLKKSRK---ALD 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1974 EAKKEKHKLQEQLQVAQMRIEYLEQSTVDRaivsrqeavicdleNKTEFQKVQIKRFEVLVIRLRDSLIKMG------EE 2047
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDI--------------NETLESMKKIKKAIGDLKRLREAFDKSGvpamirKS 757
|
650
....*....|.
gi 2462585723 2048 LSQAATSESQQ 2058
Cdd:PRK01156 758 ASQAMTSLTRK 768
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1788-2127 |
6.50e-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: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1788 RQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQlllGTMEDGKT 1867
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR---EQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1868 SvsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMtrnkslvDEQLYRLQFEKADLLKRIDEDQDDLNEL 1947
Cdd:pfam05557 81 K--KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA-------ELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1948 MQKHKDLIAQ---SAADIGQIQEL--QLQLEEAKKE--KHKLQEQLQVAQMRIEyLEQSTVDRAIVSRQEAVICDLENKT 2020
Cdd:pfam05557 152 EQLRQNLEKQqssLAEAEQRIKELefEIQSQEQDSEivKNSKSELARIPELEKE-LERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2021 EFQKVQIKRFEvlviRLRDSLIKMGEELSQAATSESQQRESSQYYQ---RRLEELKADMEELVQREAEASRRCMELEKYV 2097
Cdd:pfam05557 231 EDLKRKLEREE----KYREEAATLELEKEKLEQELQSWVKLAQDTGlnlRSPEDLSRRIEQLQQREIVLKEENSSLTSSA 306
|
330 340 350
....*....|....*....|....*....|
gi 2462585723 2098 EELAAVRQTLQTDLETSIRRIADLQAALEE 2127
Cdd:pfam05557 307 RQLEKARRELEQELAQYLKKIEDLNKKLKR 336
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1900-2133 |
6.61e-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: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1900 ADLESMHSELENMTRnkslvdeqlyrlqfeKADLLKRIDEDQDDLNELMQKHKDLiaQSAADIGQIQELQLQLEEAKKEK 1979
Cdd:COG4913 235 DDLERAHEALEDARE---------------QIELLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1980 HKLQEQLQVAQMRIEYLEQsTVDRAIVSRQEAVICDLENKTEfqkvQIKRFEvlvirlrdslikmgEELSQAATSESQQR 2059
Cdd:COG4913 298 EELRAELARLEAELERLEA-RLDALREELDELEAQIRGNGGD----RLEQLE--------------REIERLERELEERE 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462585723 2060 ESSQYYQRRLEELK----ADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDS 2133
Cdd:COG4913 359 RRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1444-1603 |
9.91e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADerfkgdvacqvLESERAERLQafREVQELKSKH 1523
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-----------NGGDRLEQLE--REIERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1524 EQVQKKLGDVNKQLEEAQQKIqlndlernPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQS 1603
Cdd:COG4913 355 EERERRRARLEALLAALGLPL--------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1664-2156 |
1.07e-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: 48.04 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1664 EKGLREKVTQENTSvRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLESSALEQQK 1743
Cdd:TIGR00618 228 LKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1744 IQSQQENTIKQleqlRQRFELEIERMK-QMHQKDREDQEE----------ELEDVRQSCQKRLHQLEmQLEQEYEEKQMV 1812
Cdd:TIGR00618 307 QQAQRIHTELQ----SKMRSRAKLLMKrAAHVKQQSSIEEqrrllqtlhsQEIHIRDAHEVATSIRE-ISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1813 LHEKQDLEGLIGTLcdQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGTME-DGKTSVSKEELEKVHSQLEQSEAKCEE- 1890
Cdd:TIGR00618 382 HTLQQQKTTLTQKL--QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKi 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1891 -------ALKTQKVLTADLESMHselENMTRNKSLVDEQLYRLQFEKADLLKRIDEdqddLNELMQKHKDLIAQSAADIG 1963
Cdd:TIGR00618 460 hlqesaqSLKEREQQLQTKEQIH---LQETRKKAVVLARLLELQEEPCPLCGSCIH----PNPARQDIDNPGPLTRRMQR 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1964 QIQELQLQLEEAKKEKHKLQEQLQVAQmriEYLEQSTvdRAIVSRQEAVICDLENKTEFQKVQIKRFEVL-VIRLRDSLI 2042
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRA---SLKEQMQ--EIQQSFSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2043 KMGEELSQAATSESQ-----------QRESSQYYQRRLEELKADMEELVQ-REAEASRRCMELEkyvEELAAVRQTLQTD 2110
Cdd:TIGR00618 608 DMLACEQHALLRKLQpeqdlqdvrlhLQQCSQELALKLTALHALQLTLTQeRVREHALSIRVLP---KELLASRQLALQK 684
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2462585723 2111 LETSIRRIADLqaaLEEVASSDSDTESVQTAVDCGSSGRKEMDNVS 2156
Cdd:TIGR00618 685 MQSEKEQLTYW---KEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1698-2128 |
1.14e-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: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1698 QLKQQVEMLQDHKREllgspslGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIE-RMKQMHQKD 1776
Cdd:TIGR04523 51 NKEKELKNLDKNLNK-------DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKnDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1777 RE--DQEEELEDVRQSCQK---RLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRRTHAL 1851
Cdd:TIGR04523 124 VElnKLEKQKKENKKNIDKfltEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK-IKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1852 LSDVQLLlgtMEDGKTSVSK-EELEKVHSQLEQSEAKceealKTQKV--LTADLESMHSELENMTRNKSLVDEQLYRLQF 1928
Cdd:TIGR04523 203 LSNLKKK---IQKNKSLESQiSELKKQNNQLKDNIEK-----KQQEIneKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1929 EKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIgqIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ---------- 1998
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEqisqlkkelt 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1999 ------STVDRAIVSRQEAVIcDLENKTEFQKVQIKRFEVLVIRLRdSLIKMGEELSQAATSESQQRESS-QYYQRRLEE 2071
Cdd:TIGR04523 353 nsesenSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLESQINDLE-SKIQNQEKLNQQKDEQIKKLQQEkELLEKEIER 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462585723 2072 LKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEV 2128
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1921-2112 |
1.72e-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: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1921 EQLYRLQfekaDLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQst 2000
Cdd:COG1579 7 RALLDLQ----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2001 vdraivsRQEAV-----ICDLENKTEFQKVQIKRFEvlvirlrDSLIKMGEELSQAATSESQQREssqyyqrRLEELKAD 2075
Cdd:COG1579 81 -------QLGNVrnnkeYEALQKEIESLKRRISDLE-------DEILELMERIEELEEELAELEA-------ELAELEAE 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462585723 2076 MEELvqrEAEASRRCMELEKYVEELAAVRQTLQTDLE 2112
Cdd:COG1579 140 LEEK---KAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1457-1929 |
1.86e-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: 46.77 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1457 RRKLEKSEKLRNELRQNTDLLESKIADLTSDLAderfkgdvacQVLESERAERLqafrEVQELKSKHEQVQKKLGDVNKQ 1536
Cdd:pfam06160 78 KYRFKKAKKALDEIEELLDDIEEDIKQILEELD----------ELLESEEKNRE----EVEELKDKYRELRKTLLANRFS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1537 LEEAQQKI--QLNDLERNPTGGDEW--QMRFDCAQMENEFLRKRLQQCEERLDS--EL--TARKELEQKLGELQSAYDga 1608
Cdd:pfam06160 144 YGPAIDELekQLAEIEEEFSQFEELteSGDYLEAREVLEKLEEETDALEELMEDipPLyeELKTELPDQLEELKEGYR-- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1609 kkmahQLKRKCHHLT-CDLEDTCVLLENQQSRNHELEKKqkkfdLQLAQAlgesvfEKGLREkvtqentsvrwelgqlqq 1687
Cdd:pfam06160 222 -----EMEEEGYALEhLNVDKEIQQLEEQLEENLALLEN-----LELDEA------EEALEE------------------ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1688 qlkqkeqEASQLKQQVEMLQdhkRELLGSPSLGENcVAGLKERLwklessaleqQKIQSQQENTIKQLEQLRQRFELeie 1767
Cdd:pfam06160 268 -------IEERIDQLYDLLE---KEVDAKKYVEKN-LPEIEDYL----------EHAEEQNKELKEELERVQQSYTL--- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1768 rmkqmhqkdredQEEELEDVRQScQKRLHQLE---MQLEQEYEEKQMVLHEKQD-LEGLIGTLcDQI--GHRDFDVE-KR 1840
Cdd:pfam06160 324 ------------NENELERVRGL-EKQLEELEkryDEIVERLEEKEVAYSELQEeLEEILEQL-EEIeeEQEEFKESlQS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1841 LRRDLRRTHALLSDVQLLLGTMedgKTSVSK------------------EELEKVHSQLEQS-------EAKCEEAlktq 1895
Cdd:pfam06160 390 LRKDELEAREKLDEFKLELREI---KRLVEKsnlpglpesyldyffdvsDEIEDLADELNEVplnmdevNRLLDEA---- 462
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2462585723 1896 kvlTADLESMHSELENMTRNKSLVdEQL------YRLQFE 1929
Cdd:pfam06160 463 ---QDDVDTLYEKTEELIDNATLA-EQLiqyanrYRSSNP 498
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1733-1983 |
1.86e-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: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1733 KLESSALEQQKiqsqQENTIKqlEQLRQRFELEIERMKQMHQKDredqeeeledvrqscQKRLHQLEMQLEQEYEEKQMV 1812
Cdd:pfam09728 71 KLEKLCRELQK----QNKKLK--EESKKLAKEEEEKRKELSEKF---------------QSTLKDIQDKMEEKSEKNNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1813 LHEKQDLEGLIGTLCDQIGHRDFDVEKRLR-RDLrrthallsDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEA 1891
Cdd:pfam09728 130 REENEELREKLKSLIEQYELRELHFEKLLKtKEL--------EVQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1892 LKTQKVLTADLeSMHS----ELENmTRNKSLVDEQLYRLQFEK-ADLLKRIDEDqddlNELMQKHKDLIAQSAADIGQ-I 1965
Cdd:pfam09728 202 SETEKELREQL-NLYVekfeEFQD-TLNKSNEVFTTFKKEMEKmSKKIKKLEKE----NLTWKRKWEKSNKALLEMAEeR 275
|
250
....*....|....*...
gi 2462585723 1966 QELQLQLEEAKKEKHKLQ 1983
Cdd:pfam09728 276 QKLKEELEKLQKKLEKLE 293
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1749-2086 |
1.96e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1749 ENTIKQLEQLRQRFELEIERMKQMHQKDREdQEEELEDVRQSCQKRL----HQ-------LEMQLEQ------------- 1804
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLESEEKNRE-EVEQLKDLYRELRKSLlanrFSfgpaldeLEKQLENleeefsqfvelte 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1805 --EYEEKQMVLHEKQDLEGLIGTLCDQI--------------------GHRD----------FDVEKRLRR---DLRRTH 1849
Cdd:PRK04778 190 sgDYVEAREILDQLEEELAALEQIMEEIpellkelqtelpdqlqelkaGYRElveegyhldhLDIEKEIQDlkeQIDENL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1850 ALLSdvQLLLGTMEDGKTSVSkEELEKVHSQLEQS-EAKcEEALKTQKVLTADLEsmHSElenmTRNKSLVDE-----QL 1923
Cdd:PRK04778 270 ALLE--ELDLDEAEEKNEEIQ-ERIDQLYDILEREvKAR-KYVEKNSDTLPDFLE--HAK----EQNKELKEEidrvkQS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1924 YRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQ--VAQMRIEylEQSTV 2001
Cdd:PRK04778 340 YTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSemLQGLRKD--ELEAR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2002 DRAIVSRQEavicdLENktefqkvqIKRfevLVIRLR---------DSLIKMGEELSQAATSESQQRESSQYYQRRLEEL 2072
Cdd:PRK04778 418 EKLERYRNK-----LHE--------IKR---YLEKSNlpglpedylEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEA 481
|
410
....*....|....
gi 2462585723 2073 KADMEELvQREAEA 2086
Cdd:PRK04778 482 TEDVETL-EEETEE 494
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1644-2016 |
2.10e-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: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1644 EKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLgENC 1723
Cdd:COG5185 232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI-KKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1724 VAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMhqKDREDQEEELEDVRQScQKRLHQLEMQLE 1803
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAI--KEEIENIVGEVELSKS-SEELDSFKDTIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1804 ---QEYEEKQMVLhEKQDLEGLIgTLCDQIGHRDFDVEkRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQ 1880
Cdd:COG5185 388 stkESLDEIPQNQ-RGYAQEILA-TLEDTLKAADRQIE-ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSR 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1881 LEQSEAKCEEALKTQK-VLTADLESMHSELENMTRNkslVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1959
Cdd:COG5185 465 LEEAYDEINRSVRSKKeDLNEELTQIESRVSTLKAT---LEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462585723 1960 ADIGQIQELQLQLEEakkekHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDL 2016
Cdd:COG5185 542 ENLIPASELIQASNA-----KTDGQAANLRTAVIDELTQYLSTIESQQAREDPIPDQ 593
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1842-2142 |
2.30e-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: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1842 RRDLRRTHALLSDVQLLLGTME----------DGKTSVSKEELEKVHSQLEQSEAKCEealKTQKVLTADLESMHSELEn 1911
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMElehkrarielEKKASALKRQLDRESDRNQELQKRIR---LLEKREAEAEEALREQAE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1912 MTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDL-NELMQKHKdliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQ 1990
Cdd:pfam05557 77 LNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSELRR-----------QIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1991 MRIEYLEQstvdraivsrqeaVICDLENKTEFQKVQIKRFEVLVIRLR----DSLI--KMGEELSQAATSESQQR----- 2059
Cdd:pfam05557 146 AKASEAEQ-------------LRQNLEKQQSSLAEAEQRIKELEFEIQsqeqDSEIvkNSKSELARIPELEKELErlreh 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2060 ---------------ESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSiRRIADLQ-- 2122
Cdd:pfam05557 213 nkhlnenienklllkEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLS-RRIEQLQqr 291
|
330 340
....*....|....*....|..
gi 2462585723 2123 --AALEEVASSDSDTESVQTAV 2142
Cdd:pfam05557 292 eiVLKEENSSLTSSARQLEKAR 313
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1698-2107 |
3.48e-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: 45.84 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1698 QLKQQVEMLQDHKRELLGspslgENcvAGLKERLWKLES------------SALEQQKIQSQQENTikQLEQLRQRFELE 1765
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQ-----EN--KKLQERLDQLESgddsgtpggkkyLLLQKQLEQLQEENF--RLETARDDYRIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1766 IERMK------QMHQKDREDQEEELE------DVRQSCQKRLHQLEMQLE------QEYEE--KQMVLHEKQDLEGLIGT 1825
Cdd:pfam05622 89 CEELEkevlelQHRNEELTSLAEEAQalkdemDILRESSDKVKKLEATVEtykkklEDLGDlrRQVKLLEERNAEYMQRT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1826 LcdqighrdfdvekRLRRDLRRTHALLSDVQLLlgtmedgktsvsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESM 1905
Cdd:pfam05622 169 L-------------QLEEELKKANALRGQLETY------------KRQVQELHGKLSEESKKADKLEFEYKKLEEKLEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1906 HSELENMTRN----KSLVDE----QLYRLQFEKAD-LLKRIDEDQDDLN-ELM------------QKHKDL-IAQSAADI 1962
Cdd:pfam05622 224 QKEKERLIIErdtlRETNEElrcaQLQQAELSQADaLLSPSSDPGDNLAaEIMpaeireklirlqHENKMLrLGQEGSYR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1963 GQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStVDRAIVSRQEAvicdlENKTEFQKVQIKRFEVLVIRLRdsli 2042
Cdd:pfam05622 304 ERLTELQQLLEDANRRKNELETQNRLANQRILELQQQ-VEELQKALQEQ-----GSKAEDSSLLKQKLEEHLEKLH---- 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462585723 2043 KMGEELS--QAATSESQQRESSQyYQRRLEELkadMEELVQREAEAsrRCME--LEKYVEELAAVRQTL 2107
Cdd:pfam05622 374 EAQSELQkkKEQIEELEPKQDSN-LAQKIDEL---QEALRKKDEDM--KAMEerYKKYVEKAKSVIKTL 436
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
263-555 |
4.63e-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: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 263 LGDPGQGTVAlkkgeEGQSivgKGLGTPKTTEL-KEAEPQGKDRQGTrpQAQGPGEGVRPGKAEKEGAEPTNtvEKGNVS 341
Cdd:TIGR00927 627 LGDLSKGDVA-----EAEH---TGERTGEEGERpTEAEGENGEESGG--EAEQEGETETKGENESEGEIPAE--RKGEQE 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 342 KDVGSEGKhvRPQIPGRKWGGFLGRRSKWDGPQNKKDKEGVLLSKAEKTG-EPQTQMEKTSQVQGElGDDLRMGEKAGEL 420
Cdd:TIGR00927 695 GEGEIEAK--EADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEdEGEGEAEGKHEVETE-GDRKETEHEGETE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 421 RSTTGKAGESWDKKEKMGQPQGKSG--NAGEARSQTEKGCEAPKEVSTMVESPAAPGKGGwPGSRGQEAEEPCSRAGDGA 498
Cdd:TIGR00927 772 AEGKEDEDEGEIQAGEDGEMKGDEGaeGKVEHEGETEAGEKDEHEGQSETQADDTEVKDE-TGEQELNAENQGEAKQDEK 850
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462585723 499 GAlETELEGPSQPALEKDAERPRIRKENQDGPAPQEEGKGGQSRDSDQAPEDRWYEA 555
Cdd:TIGR00927 851 GV-DGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQKQA 906
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1450-1836 |
4.90e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1450 EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvleseraERLQAFREVQELKSKHEQVQKK 1529
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAS---------------DHLNLVQTALRQQEKIERYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1530 LGDVNKQLEEAQQKIQLndlernptggdewqmrfdcAQMENEFLRKRLQQCEERLDseltarkELEQKLGELQSAYDGAK 1609
Cdd:PRK04863 357 LEELEERLEEQNEVVEE-------------------ADEQQEENEARAEAAEEEVD-------ELKSQLADYQQALDVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1610 KMAHQ------LKRKCHHLtCDLEDtcVLLENQQSRNHELEKKQKKFD---LQLAQALGESVFEKGLREKVTQENTSVRW 1680
Cdd:PRK04863 411 TRAIQyqqavqALERAKQL-CGLPD--LTADNAEDWLEEFQAKEQEATeelLSLEQKLSVAQAAHSQFEQAYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1681 ELgqlqqqlkqkeqEASQLKQQ-VEMLQDHKRELLGSPSLGencvaGLKERLWKLESSALEQQkiqsQQENTIKQLEQlR 1759
Cdd:PRK04863 488 EV------------SRSEAWDVaRELLRRLREQRHLAEQLQ-----QLRMRLSELEQRLRQQQ----RAERLLAEFCK-R 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1760 QRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQ------EYEEKQMVLHEKQD-LEgligTLCDQIGH 1832
Cdd:PRK04863 546 LGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQlqariqRLAARAPAWLAAQDaLA----RLREQSGE 621
|
....
gi 2462585723 1833 RDFD 1836
Cdd:PRK04863 622 EFED 625
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1721-2130 |
5.74e-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: 45.42 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1721 ENCVAGLKERLWKLE---SSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQ 1797
Cdd:TIGR00606 244 ENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1798 LEMQLEQEYEEKQMVLHEKQDLEGLIGTLC-------DQIGHRDFD-----------------------------VEKRL 1841
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKTELLVEQGRLQlqadrhqEHIRARDSLiqslatrleldgfergpfserqiknfhtlVIERQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1842 RRDLRRTHALLSDVQ------------------LLLGTMEDGKTSVSKE--ELEKVHSQLEQSEAKCEEALKTQKVLTAD 1901
Cdd:TIGR00606 404 EDEAKTAAQLCADLQskerlkqeqadeirdekkGLGRTIELKKEILEKKqeELKFVIKELQQLEGSSDRILELDQELRKA 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1902 LESMhSELENMTRNKSLVDEQLYrLQFEKADLLK---RIDEDQDDLN------------------------ELMQKHKDL 1954
Cdd:TIGR00606 484 EREL-SKAEKNSLTETLKKEVKS-LQNEKADLDRklrKLDQEMEQLNhhtttrtqmemltkdkmdkdeqirKIKSRHSDE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1955 IAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTeFQKVQIKRFEVL 2033
Cdd:TIGR00606 562 LTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHiNNELESKEEQLSSYEDKL-FDVCGSQDEESD 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2034 VIRLRDSLIKMGEELSQAATsesqqreSSQYYQRRLEELkadmeelvqreAEASRRCMELEKYVEELAAVRQTLQTDLET 2113
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAG-------ATAVYSQFITQL-----------TDENQSCCPVCQRVFQTEAELQEFISDLQS 702
|
490
....*....|....*..
gi 2462585723 2114 SIRRIADLQAALEEVAS 2130
Cdd:TIGR00606 703 KLRLAPDKLKSTESELK 719
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1915-2137 |
6.68e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1915 NKSLVDEQlyrlqfekADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQ-IQELQLQLEEAKKEKHKLQEQLQVAQMRI 1993
Cdd:PHA02562 172 NKDKIREL--------NQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1994 EYLEQSTVDRAivsrqeAVICDLENKTEFQKVQIKRFevlvirlrDSLIKMGEE----------LSQAATSESQQRESSQ 2063
Cdd:PHA02562 244 LNLVMDIEDPS------AALNKLNTAAAKIKSKIEQF--------QKVIKMYEKggvcptctqqISEGPDRITKIKDKLK 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462585723 2064 YYQRRLEELKADMEELVQREAEASrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTES 2137
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFN----EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1733-1987 |
7.22e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1733 KLESSALEQQKIQSQQENTIKQLEQLRQRFELEIermkqmhqKDREDQEEELEDVRQSCQK----RLhQLEMQLE--QEY 1806
Cdd:pfam00038 62 QLDTLTVERARLQLELDNLRLAAEDFRQKYEDEL--------NLRTSAENDLVGLRKDLDEatlaRV-DLEAKIEslKEE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1807 EEKQMVLHEKQdleglIGTLCDQIGHRDFDVEKRLRRDLRRTHALlSDVQlllgTMEDGKTSVSKEELEkvhsqlEQSEA 1886
Cdd:pfam00038 133 LAFLKKNHEEE-----VRELQAQVSDTQVNVEMDAARKLDLTSAL-AEIR----AQYEEIAAKNREEAE------EWYQS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1887 KCEEALKTQKVLTADLESMHSELENMTRnkslvdeQLYRLQFEKADLLKRIDEDQDDLNELMQKHkdliaqsAADIGQIQ 1966
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEEITELRR-------TIQSLEIELQSLKKQKASLERQLAETEERY-------ELQLADYQ 262
|
250 260
....*....|....*....|..
gi 2462585723 1967 ELQLQLEEAKKE-KHKLQEQLQ 1987
Cdd:pfam00038 263 ELISELEAELQEtRQEMARQLR 284
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1921-2127 |
8.23e-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: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1921 EQLYRL---QFEKA-DLLKRIdedQ-----DDLNELMQKH-------KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQE 1984
Cdd:COG4913 180 ARLRRRlgiGSEKAlRLLHKT---QsfkpiGDLDDFVREYmleepdtFEAADALVEHFDDLERAHEALEDAREQIELLEP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1985 QLQVAQMRIEYLEQSTVDRAIVSRQEAvicdlenktEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRES--- 2061
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRL---------WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREElde 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462585723 2062 --SQYYQ---RRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2127
Cdd:COG4913 328 leAQIRGnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1870-1979 |
9.02e-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: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1870 SKEELEKVHSQ---LEQSEAKCEEALKTQKVLTADLE----SMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQD 1942
Cdd:pfam05911 686 LKEEFEQLKSEkenLEVELASCTENLESTKSQLQESEqliaELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEA 765
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462585723 1943 DLNELMQK--------------HKDLIAQSaadigqiQELQLQLEEAKKEK 1979
Cdd:pfam05911 766 ELNELRQKfealeveleeekncHEELEAKC-------LELQEQLERNEKKE 809
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1444-1823 |
9.77e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdlleskiadltsdladerfkgdvacqvlESERA-ERLQAFREVQELKSK 1522
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQ------------------------------DYQAAsDHLNLVQTALRQQEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1523 HEQVQKKLGDVNKQLEEAQQKIQLNDLERnptggDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQ 1602
Cdd:PRK04863 350 IERYQADLEELEERLEEQNEVVEEADEQQ-----EENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1603 SA----------YDGAKKMAHQLKRKCHHLTCDLEDtcvlLEnQQSRNHELEKKQKKFDLQLAQALGESV--------FE 1664
Cdd:PRK04863 425 RAkqlcglpdltADNAEDWLEEFQAKEQEATEELLS----LE-QKLSVAQAAHSQFEQAYQLVRKIAGEVsrseawdvAR 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1665 KGLREKVTQENTSVRweLGQLQQQLKQKEQEASQLKQQVEMLQDHKREL---LGSPSLGENCVAGLKERLWKLESSALEQ 1741
Cdd:PRK04863 500 ELLRRLREQRHLAEQ--LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgknLDDEDELEQLQEELEARLESLSESVSEA 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1742 QKIQSQQENTIKQLEQLRQRFEleiERMKQMHQKD------REDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQmVLHE 1815
Cdd:PRK04863 578 RERRMALRQQLEQLQARIQRLA---ARAPAWLAAQdalarlREQSGEEFEDSQDVTEYMQQLLERERELTVERDE-LAAR 653
|
....*...
gi 2462585723 1816 KQDLEGLI 1823
Cdd:PRK04863 654 KQALDEEI 661
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1444-1706 |
1.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1523
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1524 EQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQS 1603
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1604 AYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELG 1683
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
250 260
....*....|....*....|...
gi 2462585723 1684 QLQQQLKQKEQEASQLKQQVEML 1706
Cdd:COG4372 285 LEALEEAALELKLLALLLNLAAL 307
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1745-1960 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1745 QSQQENTIKQLEQLRQRFELEIERMKQMhQKDREDQEEELEDVRQSCQKRLHQLEmQLEQEYEEKQMVLhekQDLEGLIG 1824
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAEL---AELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1825 TLCDQIGHRDFDVEKRLRRDLRrtHALLSDVQLLLGTmEDGKTSVSK---------------EELEKVHSQLEQSEAKCE 1889
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYR--LGRQPPLALLLSP-EDFLDAVRRlqylkylaparreqaEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462585723 1890 EALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAA 1960
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1742-2139 |
1.20e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1742 QKIQSQQENTIKQlEQLRQRFELEIERmKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEG 1821
Cdd:PTZ00440 546 KYYLQSIETLIKD-EKLKRSMKNDIKN-KIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQE 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1822 LIGTLCDQIGHRDFDvekrlrrdlrrthALLSDvqlLLGTMEDGKTSV----SKEELEKVHSQLEQSEAKCEEalKTQKV 1897
Cdd:PTZ00440 624 KVKYILNKFYKGDLQ-------------ELLDE---LSHFLDDHKYLYheakSKEDLQTLLNTSKNEYEKLEF--MKSDN 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1898 LTADLESMHSELENM-TRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKdliaqsaADIGQIQELQLQLEEAK 1976
Cdd:PTZ00440 686 IDNIIKNLKKELQNLlSLKENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYK-------EEEEKLEVYKHQIINRK 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1977 KE--------KHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQeAVICDlENKTEFQKvQIKRFEVLVIRLRDSLIKMGEEL 2048
Cdd:PTZ00440 759 NEfilhlyenDKDLPDGKNTYEEFLQYKDTILNKENKISND-INILK-ENKKNNQD-LLNSYNILIQKLEAHTEKNDEEL 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2049 SQaatsesqqreSSQYYQRRLEELKADmeelvqreaeasrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEV 2128
Cdd:PTZ00440 836 KQ----------LLQKFPTEDENLNLK----------------ELEKEFNENNQIVDNIIKDIENMNKNINIIKTLNIAI 889
|
410
....*....|.
gi 2462585723 2129 ASSDSDTESVQ 2139
Cdd:PTZ00440 890 NRSNSNKQLVE 900
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1879-2149 |
1.26e-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: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1879 SQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS 1958
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1959 AADIGQIQELQLQLEeakkekhklQEQLQVAQMRIEYLEQ-STVDRAIVSRQEAVICDLENKTEFQKVQIKrfevlviRL 2037
Cdd:COG3883 96 YRSGGSVSYLDVLLG---------SESFSDFLDRLSALSKiADADADLLEELKADKAELEAKKAELEAKLA-------EL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2038 RDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRR 2117
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270
....*....|....*....|....*....|..
gi 2462585723 2118 IADLQAALEEVASSDSDTESVQTAVDCGSSGR 2149
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1444-1656 |
1.28e-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: 43.60 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLaderfkgdvacQVLESERAErlqAFREVQELKSKH 1523
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----------RALEQELAA---LEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1524 EQVQKKLGDVNKQLEE---AQQKIQLNDLER---NPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQK 1597
Cdd:COG4942 93 AELRAELEAQKEELAEllrALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462585723 1598 LGELQSAYDGAKKMAHQLKRkchhltcdledtcvLLENQQSRNHELEKKQKKFDLQLAQ 1656
Cdd:COG4942 173 RAELEALLAELEEERAALEA--------------LKAERQKLLARLEKELAELAAELAE 217
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1444-1617 |
1.36e-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: 43.60 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkGDVACQVLESERAER-------------L 1510
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK--EELAELLRALYRLGRqpplalllspedfL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1511 QAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggdewqmrfdcaqmENEFLRKRLQQCEERLDSELTA 1590
Cdd:COG4942 133 DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA----------------ELEALLAELEEERAALEALKAE 196
|
170 180 190
....*....|....*....|....*....|.
gi 2462585723 1591 RK----ELEQKLGELQSAYDGAKKMAHQLKR 1617
Cdd:COG4942 197 RQkllaRLEKELAELAAELAELQQEAEELEA 227
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1748-2127 |
1.48e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1748 QENTIKQLEQLRQRFElEIERMkqmhqkdreDQEEELEDVRQscqkrLHqLEMQLEQEYEEKqmvlheKQDLEGLIGTLC 1827
Cdd:PRK04778 24 RKRNYKRIDELEERKQ-ELENL---------PVNDELEKVKK-----LN-LTGQSEEKFEEW------RQKWDEIVTNSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1828 DQIGHRDFDVEKRLRR-DLRRTHALLSDVQLLLGTMEDGKTSVSKE-----ELEKVHSQL-EQSEAKCEEALKT------ 1894
Cdd:PRK04778 82 PDIEEQLFEAEELNDKfRFRKAKHEINEIESLLDLIEEDIEQILEElqellESEEKNREEvEQLKDLYRELRKSllanrf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1895 -----QKVLTADLESMHSELENMTRNKSLVDEQlyrlqfEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI-GQIQEL 1968
Cdd:PRK04778 162 sfgpaLDELEKQLENLEEEFSQFVELTESGDYV------EAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1969 QL---QLEEAK---------KEKHKLQEQLQVAQMRIEYLEqstVDRAivsrqEAVICDLENKTE-----FQK-VQIKRF 2030
Cdd:PRK04778 236 KAgyrELVEEGyhldhldieKEIQDLKEQIDENLALLEELD---LDEA-----EEKNEEIQERIDqlydiLEReVKARKY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2031 -EVLVIRLRDSLIKMGEELSQ--AATSESQQR--------ESSQYYQRRLEELKADMEELVQREAEASRRCMELEkyvEE 2099
Cdd:PRK04778 308 vEKNSDTLPDFLEHAKEQNKElkEEIDRVKQSytlneselESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQ---EE 384
|
410 420
....*....|....*....|....*...
gi 2462585723 2100 LAAVRQTLqTDLETSIRRIADLQAALEE 2127
Cdd:PRK04778 385 LEEILKQL-EEIEKEQEKLSEMLQGLRK 411
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1503-1820 |
1.48e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1503 ESERAERLQAFREVQELKSKHEQvQKKLGDVNKQLEEAQQKIQLNDLERNPTGG---DEWQMRFDCAQMENEFLRKRLQQ 1579
Cdd:pfam02029 3 DEEEAARERRRRAREERRRQKEE-EEPSGQVTESVEPNEHNSYEEDSELKPSGQgglDEEEAFLDRTAKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1580 CEER---LDSELTARKE---LEQKLGELQSAYDGAKkmahQLKRKCHHLTCDLEDTcvllenqqsrnHELEKKQKKFDLQ 1653
Cdd:pfam02029 82 ALERqkeFDPTIADEKEsvaERKENNEEEENSSWEK----EEKRDSRLGRYKEEET-----------EIREKEYQENKWS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1654 LAQALGESVFEKglREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELL-GSPSLGENCVAGLK---E 1729
Cdd:pfam02029 147 TEVRQAEEEGEE--EEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPeVKSQNGEEEVTKLKvttK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1730 RLWKLESSALEQQKIQSQQENTIKQLEQLRQRF-ELEIERMKQMHQKDRE-DQE-EELEDVRQSCQKRLHQLEMQLEQEY 1806
Cdd:pfam02029 225 RRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRqEKESEEFEKLRQKQQEaELElEELKKKREERRKLLEEEEQRRKQEE 304
|
330
....*....|....*....
gi 2462585723 1807 EEKQMVLHE-----KQDLE 1820
Cdd:pfam02029 305 AERKLREEEekrrmKEEIE 323
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1420-1622 |
1.49e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1420 AVKDWPWWQLLGSLQplLSATIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQNtDLLESKIADLTSDLADErfkgdvac 1499
Cdd:COG4717 315 ELEEEELEELLAALG--LPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED-------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1500 qvlESERAERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLErnptggdewqmrfdcAQMENefLRKRLQQ 1579
Cdd:COG4717 384 ---EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE---------------EELEE--LEEELEE 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462585723 1580 CEERLDSELTARKELEQKLGELQS--AYDGAKKMAHQLKRKCHHL 1622
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELREL 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1443-1771 |
1.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1443 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLEskiadltsdladerfkgdvacqvlesERAERLQAFREVQELKSK 1522
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ--------------------------ERREALQRLAEYSWDEID 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1523 HEQVQKKLGDVNKQLEEaqqkiqlndLERNPTGGDEwqmrfdcaqmenefLRKRLQQCEERLDseltarkELEQKLGELQ 1602
Cdd:COG4913 663 VASAEREIAELEAELER---------LDASSDDLAA--------------LEEQLEELEAELE-------ELEEELDELK 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1603 SAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEkkqkkFDLQLAQALGESVfEKGLREKVTQENTSVRwel 1682
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEA----AEDLARLELRAL-----LEERFAAALGDAV-ERELRENLEERIDALR--- 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1683 gqlqqqlkqkeQEASQLKQQVE-MLQDHKRE-----LLGSPSLGENcvAGLKERLWKLESSAL---EQQKIQSQQENTIK 1753
Cdd:COG4913 780 -----------ARLNRAEEELErAMRAFNREwpaetADLDADLESL--PEYLALLDRLEEDGLpeyEERFKELLNENSIE 846
|
330
....*....|....*...
gi 2462585723 1754 QLEQLRQRFELEIERMKQ 1771
Cdd:COG4913 847 FVADLLSKLRRAIREIKE 864
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1926-2143 |
1.62e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1926 LQFEKADLLKRIDEDQDDLnelmqkHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQvaqmRIEYLEQStvdrai 2005
Cdd:COG4717 40 LAFIRAMLLERLEKEADEL------FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEE------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2006 VSRQEAVICDLENKTEFQKVQIKRFEVLvirlrdslikmgEELSQAatsesqqRESSQYYQRRLEELKADMEELVQREAE 2085
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLY------------QELEAL-------EAELAELPERLEELEERLEELRELEEE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462585723 2086 ASRRCMELEKYVEELAAVRQTLQTDLETSIRRIA-DLQAALEEVASSDSDTESVQTAVD 2143
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELE 223
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
675-765 |
1.63e-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: 41.56 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 675 PAHIGSMAQRAYWALLNQRRDQSIVALGRSGAGKTTCCEQVLEHLVGMAGSVDGR--------------VSVEKIRATFT 740
Cdd:cd01363 32 QPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgetegwvylteitvTLEDQILQANP 111
|
90 100
....*....|....*....|....*
gi 2462585723 741 VLRAFGSVSMAHSRSATRFSMVMSL 765
Cdd:cd01363 112 ILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
366-548 |
1.68e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.42 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 366 RRSKWDGPQNKKDKEGVLLSKAEKTGEPQTQMEKTSQVQGELGDDLRMGEKAGElrsttGKAGESWDKKEKMGQPQGKSG 445
Cdd:PHA03169 34 GRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEER-----GQGGPSGSGSESVGSPTPSPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 446 NAGEAR----SQTEKGCEAPKEVSTMVESPAAPGKGGwPGSRGQEAEEPCSRAGDGAGALETELEGPSQPALEKDAERPR 521
Cdd:PHA03169 109 GSAEELasglSPENTSGSSPESPASHSPPPSPPSHPG-PHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEP 187
|
170 180
....*....|....*....|....*..
gi 2462585723 522 IRKENQDGPAPQEEGKGGQSRDSDQAP 548
Cdd:PHA03169 188 DSPGPPQSETPTSSPPPQSPPDEPGEP 214
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1644-1994 |
1.74e-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: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1644 EKKQKKFDLQLAQALGESVfEKGLR---EKVT----------QENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1710
Cdd:pfam15742 14 EVQQLRQNLQRLQILCTSA-EKELRyerGKNLdlkqhnsllqEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1711 REllgspslgencvaglkerlwkLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQS 1790
Cdd:pfam15742 93 RE---------------------LELEVLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKVCLTDTCIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1791 CQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghrdfdveKRLRRDLRRTHALLsdvqlllgTMEDGKTSVS 1870
Cdd:pfam15742 152 EKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNEL--------QQQVRSLQDKEAQL--------EMTNSQQQLR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1871 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELEnmtrnkslvdeqlyRLQFEKADLLKRIDEDQDDLNELMQK 1950
Cdd:pfam15742 216 IQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEKE--------------ALQEELQQVLKQLDVHVRKYNEKHHH 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2462585723 1951 HKdliaqsaADIGQIQELQLQLEEAKKEKHK-LQEQLQVAQMRIE 1994
Cdd:pfam15742 282 HK-------AKLRRAKDRLVHEVEQRDERIKqLENEIGILQQQSE 319
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1420-1877 |
1.76e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1420 AVKDWPWWQLLGSLQpllsatigtEQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTSDLADERfkgdvac 1499
Cdd:COG4717 124 LLQLLPLYQELEALE---------AELAELPERLEELEERLEELRELEEELEE----LEAELAELQEELEELL------- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1500 qvleseRAERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQlnDLERnptggdewqmrfDCAQMENEFLRKRLQQ 1579
Cdd:COG4717 184 ------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE--ELEE------------ELEQLENELEAAALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1580 CEERLDSELTARKELEQKLGELQSAYDGAKKMAhqlkrkchhltcdlEDTCVLLENQQSRNHELEKKQKKFDLQLAQALG 1659
Cdd:COG4717 244 RLKEARLLLLIAAALLALLGLGGSLLSLILTIA--------------GVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1660 ESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSpSLGENCVAGLKERLWKLESSAL 1739
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1740 EQQKIQSQQENTIKQLEQLRQRFELEIERMKQ-MHQKDREDQEEELEDVRQscqkRLHQLEMQLEQEYEEKQMVLHEKQD 1818
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEElLEALDEEELEEELEELEE----ELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462585723 1819 LEGliGTLCDQIGHRDFDVEKRLRRDLRRTHALlsdvQLLLGTMEDGKTSVSKEELEKV 1877
Cdd:COG4717 465 LEE--DGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYREERLPPV 517
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1872-2123 |
1.78e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1872 EELEKVHSQLEQSEAKCEEAlktqkvltadlesmHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQ---------- 1941
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEA--------------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQtraiqyqqav 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1942 ---DDLNELMQKhKDLIAQSAADIgqIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ--STVDRAI--VSRQEA--V 2012
Cdd:PRK04863 421 qalERAKQLCGL-PDLTADNAEDW--LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayQLVRKIAgeVSRSEAwdV 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2013 ICDLENKTEFQKVQIKRFEVLVIRLRDslikMGEELSQAATSESQQRESSQYYQRRLEElkADMEELVQREAEASRRcmE 2092
Cdd:PRK04863 498 ARELLRRLREQRHLAEQLQQLRMRLSE----LEQRLRQQQRAERLLAEFCKRLGKNLDD--EDELEQLQEELEARLE--S 569
|
250 260 270
....*....|....*....|....*....|.
gi 2462585723 2093 LEKYVEELAAVRQTLQTDLETSIRRIADLQA 2123
Cdd:PRK04863 570 LSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1929-2121 |
1.80e-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: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1929 EKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQlqvaqmrieyleqstvdRAIVSR 2008
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNL-----------------KARLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2009 QEAVICDLEnktEFQKVQIKRFEVLViRLRDSLIKMGEElsqaATSESQQRES--SQYYQRRLEELKADMEelvQREAea 2086
Cdd:pfam13851 97 LEKELKDLK---WEHEVLEQRFEKVE-RERDELYDKFEA----AIQDVQQKTGlkNLLLEKKLQALGETLE---KKEA-- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462585723 2087 srrcmELEKYV-------EELAAVRQTLQTDLETSIRRIADL 2121
Cdd:pfam13851 164 -----QLNEVLaaanldpDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1443-1628 |
1.88e-03 |
|
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: 43.90 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1443 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSK 1522
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1523 HEQVQKKLGDVNKQLEEAQQKIQlndlernptggdEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQ 1602
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLR------------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
170 180
....*....|....*....|....*.
gi 2462585723 1603 SaYDGAKKMAHQLKRKCHHLTCDLED 1628
Cdd:TIGR02169 945 E-IPEEELSLEDVQAELQRVEEEIRA 969
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1698-2143 |
2.16e-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: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1698 QLKQQVEMLQDHKR-----------ELLGSPSLGENCVaglkerlWKLESSALEQQKIQSQQENTIKQLEQLR---QRFE 1763
Cdd:pfam10174 71 HLQLTIQALQDELRaqrdlnqllqqDFTTSPVDGEDKF-------STPELTEENFRRLQSEHERQAKELFLLRktlEEME 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1764 LEIERMKQ--------------MHQKD---REDQEEELEDVRQ--SCQKRLHQLEMQLEQEYEEKQMV---LHEK---QD 1818
Cdd:pfam10174 144 LRIETQKQtlgardesikklleMLQSKglpKKSGEEDWERTRRiaEAEMQLGHLEVLLDQKEKENIHLreeLHRRnqlQP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1819 LEGLIGTLCDQIGHRDFDVEKrLRRDLRRthaLLSDVQLL----LGTMEDGKTSVSKEELEKVHS--------QLEQSEA 1886
Cdd:pfam10174 224 DPAKTKALQTVIEMKDTKISS-LERNIRD---LEDEVQMLktngLLHTEDREEEIKQMEVYKSHSkfmknkidQLKQELS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1887 KCEEALKTqkvLTADLESMHSELENMTRNKSLVDEQLYR-------LQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1959
Cdd:pfam10174 300 KKESELLA---LQTKLETLTNQNSDCKQHIEVLKESLTAkeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1960 ADIGQIQELQ--LQLEEAK-----KEKHKLQEQL-----QVAQM--RIEYLEQ--STVDRAIVSRQEAvICDLENKTEFQ 2023
Cdd:pfam10174 377 TLAGEIRDLKdmLDVKERKinvlqKKIENLQEQLrdkdkQLAGLkeRVKSLQTdsSNTDTALTTLEEA-LSEKERIIERL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2024 KVQIKRFEVLVIRLRDSLIKMGEELSQAATS---ESQQRESSqyyqrrLEELKADMEELVQREAEASRRC----MELEKY 2096
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEKVSAlqpELTEKESS------LIDLKEHASSLASSGLKKDSKLksleIAVEQK 529
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2462585723 2097 VEELAAVRQTLQT-----DLETSIRRIADLQAALE-EVASSDSDTESVQTAVD 2143
Cdd:pfam10174 530 KEECSKLENQLKKahnaeEAVRTNPEINDRIRLLEqEVARYKEESGKAQAEVE 582
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1964-2128 |
2.27e-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: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1964 QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdrAIVSRQEAVicdlenktEFQKVQIKRFEVLVIRLRDSLIK 2043
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEA-----RLEAAKTEL--------EDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2044 MGEELSQAATsesqQRESsQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRR----IA 2119
Cdd:COG1579 78 YEEQLGNVRN----NKEY-EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEldeeLA 152
|
....*....
gi 2462585723 2120 DLQAALEEV 2128
Cdd:COG1579 153 ELEAELEEL 161
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1885-2142 |
2.33e-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: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1885 EAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRlqfEKADLLKRIDEDQDDLNELMQKHKDLIAQSaadigq 1964
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWER---QRRELESRVAELKEELRQSREKHEELEEKY------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1965 iQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdraivsrqeavicdlENKTEFQKVQIKrfEVLVIRLRDSLIKM 2044
Cdd:pfam07888 104 -KELSASSEELSEEKDALLAQRAAHEARIRELEE------------------DIKTLTQRVLER--ETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2045 GEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVeelaavrQTLQTDLETSIRRIADLQAA 2124
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTI-------TTLTQKLTTAHRKEAENEAL 235
|
250
....*....|....*...
gi 2462585723 2125 LEEVASSDSDTESVQTAV 2142
Cdd:pfam07888 236 LEELRSLQERLNASERKV 253
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1591-2167 |
2.34e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1591 RKELEQKLGELQSAYDGAKKmahqLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKkfdlQLAQAlgESVFEKGLREK 1670
Cdd:PRK01156 151 RKKILDEILEINSLERNYDK----LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKK----QIADD--EKSHSITLKEI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1671 vtqENTSVrwELGQLQQQLKQKEQEASQLKQQVEMLQDHKREL------LGSPSLGENCVAGLKERLWKLESSALeqqki 1744
Cdd:PRK01156 221 ---ERLSI--EYNNAMDDYNNLKSALNELSSLEDMKNRYESEIktaesdLSMELEKNNYYKELEERHMKIINDPV----- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1745 qsqqentIKQLEQLRQRFELeiermkqmhQKDREDQEEELEDVRQSCQK--RLHQLEMQLEQEYEEKQMVLHEKQDLegl 1822
Cdd:PRK01156 291 -------YKNRNYINDYFKY---------KNDIENKKQILSNIDAEINKyhAIIKKLSVLQKDYNDYIKKKSRYDDL--- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1823 igtlcdqighrdfdveKRLRRDLRRTHallSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEakceealkTQKVLTADL 1902
Cdd:PRK01156 352 ----------------NNQILELEGYE---MDYNSYLKSIESLKKKIEEYSKNIERMSAFISE--------ILKIQEIDP 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1903 ESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNEL--------------MQKHKDLIAQSAADIGQIQEl 1968
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEE- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1969 qlQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSrqeavicdlENKTEFQKVQIKRFEVLVIRLRDSLIKmgeel 2048
Cdd:PRK01156 484 --KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINE---------YNKIESARADLEDIKIKINELKDKHDK----- 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2049 SQAATSESQQRESSQYYQRRLEELKA-------DMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD- 2120
Cdd:PRK01156 548 YEEIKNRYKSLKLEDLDSKRTSWLNAlavisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENe 627
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2121 ---LQAALEEVASSDSDTESVQTAVDCGSSGRKEMDnvSILSSQPEGSLQ 2167
Cdd:PRK01156 628 annLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID--SIIPDLKEITSR 675
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1721-1816 |
2.72e-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: 42.18 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1721 ENCVAGLKERLWKLESSALEQQKIQSQQentikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKrlhQLEM 1800
Cdd:cd16269 199 EIEAERAKAEAAEQERKLLEEQQRELEQ-----KLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLK---EQEA 270
|
90
....*....|....*.
gi 2462585723 1801 QLEQEYEEKQMVLHEK 1816
Cdd:cd16269 271 LLEEGFKEQAELLQEE 286
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1445-1584 |
3.00e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1445 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDL--------LESKIADLTSDLADerfkgdvacqvLESERAERLQAFREV 1516
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEasferlaeLRDELAELEEELEA-----------LKARWEAEKELIEEI 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1517 QELKSKHEQVQKKLGDVNKQLEEAQQKI-QLNDLERNPTGGDE-------W------QMrfdcaqMENEflRKRLQQCEE 1582
Cdd:COG0542 474 QELKEELEQRYGKIPELEKELAELEEELaELAPLLREEVTEEDiaevvsrWtgipvgKL------LEGE--REKLLNLEE 545
|
..
gi 2462585723 1583 RL 1584
Cdd:COG0542 546 EL 547
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1871-2013 |
3.03e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1871 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELE-NMTRNKSLVDEQLYRLQFEKADLLKR----IDEDQDDLN 1945
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEeKKEKLQEEEDKLLEEAEKEAQQAIKEakkeADEIIKELR 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462585723 1946 ELMQ-KHKDLIAQSAADI-GQIQELQLQLEEAKKEKHKLQEQLQVAQ-MRIEYLEQSTVDRAIVSRQEAVI 2013
Cdd:PRK00409 595 QLQKgGYASVKAHELIEArKRLNKANEKKEKKKKKQKEKQEELKVGDeVKYLSLGQKGEVLSIPDDKEAIV 665
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1458-1669 |
3.47e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1458 RKLEKSEKLRNELRQNTDLLeskIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKKLGDVNKQL 1537
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1538 EEAQQKIQLNDLERNPTggdewQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKR 1617
Cdd:COG4372 83 EELNEQLQAAQAELAQA-----QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462585723 1618 KCHHLTCDLEDTcvlleNQQSRNHELEKKQKKFDLQLAQALGESVFEKGLRE 1669
Cdd:COG4372 158 QLESLQEELAAL-----EQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1733-1975 |
3.50e-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: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1733 KLESSALEQQKIQSQQENTIKQLEQLRQrfelEIERMkqmhQKDREDQEEELEDVRQscqkrlhQLEmQLEQEYEEKQMV 1812
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA----ELEEL----NEEYNELQAELEALQA-------EID-KLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1813 LHEKQDlegligtlcdqighrdfDVEKRLRrDLRRTHALLSDVQLLLG-----TMEDGKTSVSK---------EELEKVH 1878
Cdd:COG3883 81 IEERRE-----------------ELGERAR-ALYRSGGSVSYLDVLLGsesfsDFLDRLSALSKiadadadllEELKADK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1879 SQLEQSEAKCEEALKTQKVLTADLESMHSELEnmtRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS 1958
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELE---AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
250
....*....|....*..
gi 2462585723 1959 AADIGQIQELQLQLEEA 1975
Cdd:COG3883 220 AAAAAAAAAAAAAAAAA 236
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
1871-2004 |
4.08e-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: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1871 KEELEKvhSQLEQSEAK-CEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQ 1949
Cdd:pfam06785 62 KEKFEK--SFLEEKEAKlTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRL 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462585723 1950 KHKDLIAQSAAdigQIQELQLQLEEAKKEKHKLQEQlqvaqmrIEYLEQSTVDRA 2004
Cdd:pfam06785 140 ESEEQLAEKQL---LINEYQQTIEEQRSVLEKRQDQ-------IENLESKVRDLN 184
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
1847-1955 |
4.09e-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: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1847 RTHALLSDVQLLLGTMEDGKTsvskeELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELEnmTRNKSLVDEQLYRL 1926
Cdd:pfam09744 44 RNQEHNVELEELREDNEQLET-----QYEREKALRKRAEEELEEIEDQWEQETKDLLSQVESLE--EENRRLEADHVSRL 116
|
90 100
....*....|....*....|....*....
gi 2462585723 1927 QFEKADLLKRIDEDQDDLNELMQKHKDLI 1955
Cdd:pfam09744 117 EEKEAELKKEYSKLHERETEVLRKLKEVV 145
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1641-2150 |
4.27e-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: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1641 HELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLG 1720
Cdd:pfam12128 241 PEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1721 ENCVAGLKERLWKLESSALEQQKIQSQQENTIK-QLEQLRQRFELEIERmkqmHQKDREDQEEELEDVRQSCQKRLHQLE 1799
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQLPSWQsELENLEERLKALTGK----HQDVTAKYNRRRSKIKEQNNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1800 MQLEQEYEEKQMVLH-EKQDLEGLIGTLCDQI--GHRDF-DVEKRLRRDLRRTHALLSDVQlllgtmedgktsVSKEELE 1875
Cdd:pfam12128 397 DKLAKIREARDRQLAvAEDDLQALESELREQLeaGKLEFnEEEYRLKSRLGELKLRLNQAT------------ATPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1876 kvhsQLEQSEAKCEEALKTQKVLTADLESMHSELenmTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLI 1955
Cdd:pfam12128 465 ----QLENFDERIERAREEQEAANAEVERLQSEL---RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1956 A---QSAAD----IGQI----QELQLQLEEAKKEKHKLQEQ----LQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKT 2020
Cdd:pfam12128 538 HflrKEAPDweqsIGKVispeLLHRTDLDPEVWDGSVGGELnlygVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAR 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2021 EfqkvQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELV---QREAEASRRCMELEKYV 2097
Cdd:pfam12128 618 E----KQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALaerKDSANERLNSLEAQLKQ 693
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2462585723 2098 EELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVDCGSSGRK 2150
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAK 746
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1458-1819 |
4.30e-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: 42.59 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1458 RKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgDVACQVLESERAERLQAF----REVQELKSKHEQVQKKLGDV 1533
Cdd:pfam15964 353 KALIQCEQLKSELERQKERLEKELASQQEKRAQEK---EALRKEMKKEREELGATMlalsQNVAQLEAQVEKVTREKNSL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1534 NKQLEEAQQKIQLNDLERNPTGGdewQMRF--DCAQMENEFLRKRLQQCEERLDSELTARkelEQKLGELQSAYDGAKKM 1611
Cdd:pfam15964 430 VSQLEEAQKQLASQEMDVTKVCG---EMRYqlNQTKMKKDEAEKEHREYRTKTGRQLEIK---DQEIEKLGLELSESKQR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1612 AHQLKRKCHHLTCDLEDTCVLLENQQSRNH----ELEKKQKKFDLQL-AQALGESVFEKGLREKVTQENTSVRWELGQLQ 1686
Cdd:pfam15964 504 LEQAQQDAARAREECLKLTELLGESEHQLHltrlEKESIQQSFSNEAkAQALQAQQREQELTQKMQQMEAQHDKTVNEQY 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1687 QQLKQKEQEASQLKQQVEMLQDHKRELlgspslgencvaglkerlwkLESSALEQQKIQSQQENTIKQLEQLRQRFElEI 1766
Cdd:pfam15964 584 SLLTSQNTFIAKLKEECCTLAKKLEEI--------------------TQKSRSEVEQLSQEKEYLQDRLEKLQKRNE-EL 642
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462585723 1767 ERMKQMHQKDREDQEEELEDVRQSCQ---KRLHQLEMQLEQEYEEKQMVLHEKQDL 1819
Cdd:pfam15964 643 EEQCVQHGRMHERMKQRLRQLDKHCQataQQLVQLLSKQNQLFKERQNLTEEVQSL 698
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1724-2127 |
4.42e-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: 42.63 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1724 VAGLKERLWKLESsALEQQKIQSQQENTikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR-------------QS 1790
Cdd:COG3096 838 LAALRQRRSELER-ELAQHRAQEQQLRQ--QLDQLKEQLQLLNKLLPQANLLADETLADRLEELReeldaaqeaqafiQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1791 CQKRLHQLEM-------------QLEQEYEEKQmvlHEKQDLEGLIGTLCDQIGhrdfdvekrlrrdlRRTHALLSDVQL 1857
Cdd:COG3096 915 HGKALAQLEPlvavlqsdpeqfeQLQADYLQAK---EQQRRLKQQIFALSEVVQ--------------RRPHFSYEDAVG 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1858 LLGTmedgktsvSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELenmtrnkslvdeqlyrlqfekADLLKRI 1937
Cdd:COG3096 978 LLGE--------NSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVL---------------------ASLKSSR 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1938 DEDQDDLNELMQKHKDLIAQSAADIgqiqelqlqLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLE 2017
Cdd:COG3096 1029 DAKQQTLQELEQELEELGVQADAEA---------EERARIRRDELHEELSQNRSRRSQLEKQ------LTRCEAEMDSLQ 1093
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2018 N---KTEfQKVQIKRFEV--------LVIRL-RDSLIKMG---EELsqAATSESQQRESSQYYQRRLEELKADMEEL--V 2080
Cdd:COG3096 1094 KrlrKAE-RDYKQEREQVvqakagwcAVLRLaRDNDVERRlhrREL--AYLSADELRSMSDKALGALRLAVADNEHLrdA 1170
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2462585723 2081 QREAEASRRCmelEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2127
Cdd:COG3096 1171 LRLSEDPRRP---ERKVQFYIAVYQHLRERIRQDIIRTDDPVEAIEQ 1214
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1457-1831 |
4.57e-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: 42.63 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1457 RRKLEKSEKLRNELRQNTDLLESKIADLTsDLADERFKGDVACQVLESE---RAERLQAFREVQELKSKHEQVQKKLGDV 1533
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLV-EMARELEELSARESDLEQDyqaASDHLNLVQTALRQQEKIERYQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1534 NKQLEEAQQKIQLndlernptggdewqmrfdcAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAyDGAKKMAH 1613
Cdd:COG3096 360 TERLEEQEEVVEE-------------------AAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTR-AIQYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1614 QLKRKCHHLtCDLEDtcVLLENQQSRNHELEKKQKKFD---LQLAQALGESVFEKGLREKVtqentsvrWELGQLQQQLK 1690
Cdd:COG3096 420 QALEKARAL-CGLPD--LTPENAEDYLAAFRAKEQQATeevLELEQKLSVADAARRQFEKA--------YELVCKIAGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1691 QKEQEASQLKQQVEMLQDHKrellgspSLGENcVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFElEIERMK 1770
Cdd:COG3096 489 ERSQAWQTARELLRRYRSQQ-------ALAQR-LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-ELEELL 559
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462585723 1771 QMHQKDREDQEEELEDvrqsCQKRLHQLEMQLEQ------EYEEKQMVLHEKQD-LEgligTLCDQIG 1831
Cdd:COG3096 560 AELEAQLEELEEQAAE----AVEQRSELRQQLEQlrarikELAARAPAWLAAQDaLE----RLREQSG 619
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1444-2118 |
4.93e-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: 42.63 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDL-------------LESKIADLTSDLADERFKGDVACQVLE------S 1504
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLEELTERLEEQEEVVEeaaeqlA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1505 ERAERLQAFR-EVQELKSKHEQVQKKLgDVN-----------KQLEEAQQKIQLNDLErnPTGGDEWQMRFDcAQmENEF 1572
Cdd:COG3096 379 EAEARLEAAEeEVDSLKSQLADYQQAL-DVQqtraiqyqqavQALEKARALCGLPDLT--PENAEDYLAAFR-AK-EQQA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1573 LRKRLQQcEERLDSELTARKELEQKLGELQSAYDG-AKKMAHQLKRKchhLTCDLEDTCVLLENQQS---RNHELEKK-- 1646
Cdd:COG3096 454 TEEVLEL-EQKLSVADAARRQFEKAYELVCKIAGEvERSQAWQTARE---LLRRYRSQQALAQRLQQlraQLAELEQRlr 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1647 --QKKFDL--QLAQALGESVFEKGLREKVTQENTSVRWELgqlQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgen 1722
Cdd:COG3096 530 qqQNAERLleEFCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARIKEL--------- 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1723 cvaGLKERLWKLESSALEQ------------QKIQSQQENTIK----------QLEQLRQRFELEIERmkqMHQKD-RED 1779
Cdd:COG3096 598 ---AARAPAWLAAQDALERlreqsgealadsQEVTAAMQQLLErereatverdELAARKQALESQIER---LSQPGgAED 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1780 QE--------------EELEDV---------------RQ--------SCQKRLHQLEMQLEQEYeekqMVLHEKQ----- 1817
Cdd:COG3096 672 PRllalaerlggvllsEIYDDVtledapyfsalygpaRHaivvpdlsAVKEQLAGLEDCPEDLY----LIEGDPDsfdds 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1818 --DLEGLIGTLCDQIGHRDFDVEK-----RLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQ------- 1883
Cdd:COG3096 748 vfDAEELEDAVVVKLSDRQWRYSRfpevpLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghla 827
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1884 --SEAKCEEALKTQKVLTADLESMHSELE-NMTRNKSLVD------EQLYRLQ-----FEKADLLKRIDEDQDDLNEL-- 1947
Cdd:COG3096 828 vaFAPDPEAELAALRQRRSELERELAQHRaQEQQLRQQLDqlkeqlQLLNKLLpqanlLADETLADRLEELREELDAAqe 907
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1948 ----MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKTefq 2023
Cdd:COG3096 908 aqafIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSD--- 984
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2024 kvqikrfevLVIRLRDSLIKMGEELSQAATS-ESQQRESSQYYQRR-------------LEELKADMEEL-VQREAEASR 2088
Cdd:COG3096 985 ---------LNEKLRARLEQAEEARREAREQlRQAQAQYSQYNQVLaslkssrdakqqtLQELEQELEELgVQADAEAEE 1055
|
810 820 830
....*....|....*....|....*....|
gi 2462585723 2089 RCMELEKYVEELAAVRQTLQTDLETSIRRI 2118
Cdd:COG3096 1056 RARIRRDELHEELSQNRSRRSQLEKQLTRC 1085
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1934-2141 |
5.00e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1934 LKRIDEDQDDLNELmqkhKDLIAQSAAdigQIQELQLQLEEAKKeKHKLQEQLQVAQMRIEYLEqstvDRAIVSRQEAvi 2013
Cdd:COG1196 178 ERKLEATEENLERL----EDILGELER---QLEPLERQAEKAER-YRELKEELKELEAELLLLK----LRELEAELEE-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2014 cdLENKTEFQKVQIKRFEvlvirlrdslikmgEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMEL 2093
Cdd:COG1196 244 --LEAELEELEAELEELE--------------AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462585723 2094 EKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTA 2141
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1445-1610 |
5.59e-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: 41.06 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1445 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvLESERAErlqafREVQELKSKHE 1524
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---------KEIKRLE-----LEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1525 QVQKKLGDV--NKQLEEAQQKIQLndlernptggdewqmrfdcAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQ 1602
Cdd:COG1579 77 KYEEQLGNVrnNKEYEALQKEIES-------------------LKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
....*...
gi 2462585723 1603 SAYDGAKK 1610
Cdd:COG1579 138 AELEEKKA 145
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
303-556 |
6.75e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.49 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 303 KDRQGTRPQAQGPGEGVRPGKAEKeGAEPTNTVEKGNVSKDVGSEGKHVRPQIPGRKWGGFLGRRSKwDGPQNKKDKEGV 382
Cdd:PHA03169 24 KRHGGTREQAGRRRGTAARAAKPA-PPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQ-GGPSGSGSESVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 383 LLSKAEKTGEPQTQMEKTSQVQGELGDDLRMGEkaGELRSTTGKAGESWDKKEKMGQPQGKSGNAGEARSQTEKGCEAPK 462
Cdd:PHA03169 102 SPTPSPSGSAEELASGLSPENTSGSSPESPASH--SPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 463 EVSTMVESPAA-------PGKGGWPGSRGQEAEEPCSRAGDGA--------GALETELEGPSQPALEKDAERPRIRKENQ 527
Cdd:PHA03169 180 PPTSEPEPDSPgppqsetPTSSPPPQSPPDEPGEPQSPTPQQApspntqqaVEHEDEPTEPEREGPPFPGHRSHSYTVVG 259
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462585723 528 DGPAPQEEG-------KGGQSRDSDQAPEDRWYEAE 556
Cdd:PHA03169 260 WKPSTRPGGvpklclrCTSHPSHRSRLPEGQQSEDK 295
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1696-2000 |
7.92e-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: 41.42 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1696 ASQLKQQV-EMLQDHKRELLGSPSLGEncvaglkERLWKLESSALEQQKIQsQQENTIKQLEQLRQRFELEIERMKQ--- 1771
Cdd:pfam07888 89 LRQSREKHeELEEKYKELSASSEELSE-------EKDALLAQRAAHEARIR-ELEEDIKTLTQRVLERETELERMKErak 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1772 ---MHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIG--HRDFDVEKRLRRDLR 1846
Cdd:pfam07888 161 kagAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtaHRKEAENEALLEELR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1847 RTHALLSdvqlllgtMEDGKTSVSKEELEKV-----HSQLEQSEAKCEEALKTQKVLTADLE------SMHSELENMTRN 1915
Cdd:pfam07888 241 SLQERLN--------ASERKVEGLGEELSSMaaqrdRTQAELHQARLQAAQLTLQLADASLAlregraRWAQERETLQQS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1916 KSLVDEQLYRLQFEKADLLKRIDEDQDDLN----ELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQM 1991
Cdd:pfam07888 313 AEADKDRIEKLSAELQRLEERLQEERMEREklevELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
....*....
gi 2462585723 1992 RIEYLEQST 2000
Cdd:pfam07888 393 YIRQLEQRL 401
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1738-2127 |
7.94e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1738 ALEQQKIQSQQENtiKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR-------------QSCQKRLHQLEMQL-- 1802
Cdd:PRK04863 852 ALADHESQEQQQR--SQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIReqldeaeeakrfvQQHGNALAQLEPIVsv 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1803 ----EQEYEE-KQMVLHEKQDLegligtlcdqighRDFDVEKRLRRDL--RRTHALLSDVQLLLGtmedgKTSVSKEELE 1875
Cdd:PRK04863 930 lqsdPEQFEQlKQDYQQAQQTQ-------------RDAKQQAFALTEVvqRRAHFSYEDAAEMLA-----KNSDLNEKLR 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1876 KVHSQLEQSEAKCEEALKTQKvltadlesmhselENMTRNKslvdeQLYrlqfekADLLKRIDEDQDDLNELMQKHKDLI 1955
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQAQ-------------AQLAQYN-----QVL------ASLKSSYDAKRQMLQELKQELQDLG 1047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1956 AQsaADIGQIQELQLQLEEakkekhkLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLENK-TEFQK--VQIKRFEV 2032
Cdd:PRK04863 1048 VP--ADSGAEERARARRDE-------LHARLSANRSRRNQLEKQ------LTFCEAEMDNLTKKlRKLERdyHEMREQVV 1112
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 2033 -------LVIRL-RDSLIK---MGEELsqAATSESQQRESSQYYQRRLEELKADMEEL--VQREAEASRRcmeLEKYVEE 2099
Cdd:PRK04863 1113 nakagwcAVLRLvKDNGVErrlHRREL--AYLSADELRSMSDKALGALRLAVADNEHLrdVLRLSEDPKR---PERKVQF 1187
|
410 420
....*....|....*....|....*...
gi 2462585723 2100 LAAVRQTLQTDLETSIRRIADLQAALEE 2127
Cdd:PRK04863 1188 YIAVYQHLRERIRQDIIRTDDPVEAIEQ 1215
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1444-1610 |
8.17e-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: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAER-LQAF-REVQELKS 1521
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-------LGNVRNNKeYEALqKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1522 KHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggdewQMRFDCAQMENEfLRKRLQQCEERLDSELTARKELEQKLGE- 1600
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELA-------ELEAELEEKKAE-LDEELAELEAELEELEAEREELAAKIPPe 175
|
170
....*....|
gi 2462585723 1601 LQSAYDGAKK 1610
Cdd:COG1579 176 LLALYERIRK 185
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1444-1545 |
8.64e-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: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1444 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvleSERAERLQAFREVQELKSKH 1523
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKDREISRLDREI 474
|
90 100
....*....|....*....|..
gi 2462585723 1524 EQVQKKLGDVNKQLEEAQQKIQ 1545
Cdd:COG2433 475 ERLERELEEERERIEELKRKLE 496
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1413-1549 |
8.68e-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: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462585723 1413 KNVAVFLAVKDW-PW-WQLLGSLQPLLSATIGT-----EQLRAKEEELTTLRRKLEKS-----EKLRNELRQNTDLLESK 1480
Cdd:smart00787 123 KTFARLEAKKMWyEWrMKLLEGLKEGLDENLEGlkedyKLLMKELELLNSIKPKLRDRkdaleEELRQLKQLEDELEDCD 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462585723 1481 IADLtsDLADERFKGDVACQVLESERAERLQafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDL 1549
Cdd:smart00787 203 PTEL--DRAKEKLKKLLQEIMIKVKKLEELE--EELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| |
