|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-132 |
7.19e-80 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 251.80 E-value: 7.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 530373156 83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKgtVTHGCIVSTIKLFLP 132
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRK--VTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
165-227 |
6.04e-26 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 101.22 E-value: 6.04e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373156 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 227
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.76e-18 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest protein 1 (DMA1), 2 (DMA2) and similar proteins; DMA1 (also known as checkpoint forkhead associated with RING domains-containing protein 1, or CHF1) and DMA2 (also known as checkpoint forkhead associated with RING domains-containing protein 2, or CHF2) are E3 ubiquitin-protein ligases which function in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, two E2 ubiquitin conjugating enzymes. They are involved in nutritional control of the cell cycle and required for proper spindle positioning, likely regulating septin ring deposition at the bud neck. DMA1 targets the degradation of G1 cyclin PCL1. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438744 [Multi-domain] Cd Length: 139 Bit Score: 82.62 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 530373156 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-759 |
3.48e-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: 89.73 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 158 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 235
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 236 DSLRKELIAL------QEDKHNYETTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 307
Cdd:TIGR02168 396 ASLNNEIERLearlerLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 308 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKidemEEKEQELQAKIEALQADNDFTNERLTALQE---KLI 384
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGrlqAVV 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 385 VEGH----------------------LTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSD---------------DTT 427
Cdd:TIGR02168 552 VENLnaakkaiaflkqnelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvvDDL 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 428 DAQMDEQDLNEPLAKVSLLKDDL------------QGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFEL---QALLE 492
Cdd:TIGR02168 632 DNALELAKKLRPGYRIVTLDGDLvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELrkeLEELE 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 493 EERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEkdseITSTRDELLSARDEILLLHQAAAKV---ASERDTDIASL 569
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEEL 787
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 570 QEELKKVRAELERWRKAASEYEKEITSLQNSF---QLRCQQCEDQQREEATRL----------QGELEKLRKEWNALETE 636
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEEL 867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 637 CHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQk 716
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ- 942
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 530373156 717 eyektQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 759
Cdd:TIGR02168 943 -----ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
241-745 |
2.05e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 241 ELIALQEDKHNYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKD 318
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 319 LSDKLKVAEGKQEEIQQKGQAEKK--ELQHKIDEMEEKEQELQAKIEALQ--ADNDFTNERLTALQEKLIVEGHLTKAVE 394
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 395 ETKLSKENQTRAKESDFSDTLSPSKE--KSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRK--EL 470
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaeEA 1521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 471 IEAQELARTSKQKCFELQALLEEERKAYR-NQVEESTKQIQVLQAQLQRlhidtenlREEKDSEITSTRDELLSardeil 549
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEAK--------KAEEDKNMALRKAEEAK------ 1587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 550 llhqaaaKVASERDTDIASLQEELKKVRAE----LERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEK 625
Cdd:PTZ00121 1588 -------KAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 626 LRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLS 705
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 530373156 706 KAENQAKDVQKEYE---KTQTVLSELKLKFEMTEQEKQSITDE 745
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEekkKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-109 |
7.77e-16 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438747 [Multi-domain] Cd Length: 133 Bit Score: 74.65 E-value: 7.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 530373156 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDV 109
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDI 118
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
237-751 |
4.37e-14 |
|
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: 76.21 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 237 SLRKELIALQEDKHNYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLKEMNERTQEELRELANKYNGAVN 314
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 315 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQH---KIDEMEEKEQELQAKIEAL--QADNDFTNERLTALQEKlivEGHL 389
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQ---EKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 390 TKAveETKLSKENQtraKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEA-KQEIQHLRK 468
Cdd:TIGR04523 324 EEI--QNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlESQINDLES 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 469 ELIEAQELArtskqkcfelqALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEI 548
Cdd:TIGR04523 399 KIQNQEKLN-----------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL-TNQDSVKELIIKNLDNTRESL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 549 lllhqaaakvaserDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGElEKLRK 628
Cdd:TIGR04523 467 --------------ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI-EKLES 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 629 EWNALETECHSLKRENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHL---RDSADLKTL 703
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdliKEIEEKEKK 611
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 530373156 704 LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKN 751
Cdd:TIGR04523 612 ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
4.95e-14 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 68.07 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 530373156 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
1.45e-13 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 66.06 E-value: 1.45e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530373156 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-759 |
1.80e-13 |
|
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: 74.71 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 174 LQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsrlevmgnqlqacSKNQTEDSLRKELIALQEDKHNYE 253
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 254 ttakeslrrvlQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 333
Cdd:TIGR02168 302 -----------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 334 QQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQEklIVEGHLTKAVE------ETKLSKENQT 404
Cdd:TIGR02168 371 ESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ--EIEELLKKLEEaelkelQAELEELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 405 RAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIE-------------------------- 458
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvkallknqsglsgilgvlsel 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 459 -----------------------------AKQEIQHLRKE----------------LIEAQELARTSKQKCFELQAL-LE 492
Cdd:TIGR02168 529 isvdegyeaaieaalggrlqavvvenlnaAKKAIAFLKQNelgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKdLV 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 493 EERKAYRNQVE--------------------------------------------ESTKQIQVLQAQLQRLHIDTENLR- 527
Cdd:TIGR02168 609 KFDPKLRKALSyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEe 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 528 -EEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQ 606
Cdd:TIGR02168 689 lEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 607 QCEdQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQV 686
Cdd:TIGR02168 769 RLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530373156 687 GSLKEQHLRDSA---DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 759
Cdd:TIGR02168 848 EELSEDIESLAAeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
235-748 |
3.34e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 235 EDSLRKELIALQEDKhnyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVN 314
Cdd:COG1196 222 LKELEAELLLLKLRE------LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 315 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndfTNERLTALQEKLIVEGHLTKAVE 394
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 395 ETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEplaKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQ 474
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 475 ELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLRE-EKDSEITSTRDELLSARDEILLLHQ 553
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyEGFLEGVKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 554 AAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKE-----------------------ITSLQNSFQLRCQQCED 610
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratflpldkiraraalaaaLARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 611 QQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLK 690
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 530373156 691 EQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 748
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-729 |
4.66e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 163 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 242
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 243 IALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 322
Cdd:COG1196 298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 323 LKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKEN 402
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 403 QTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQ--DLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTs 480
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAAlaELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA- 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 481 kqkCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIdtENLREEKDSEIT------STRDELLSARDEILLLHQA 554
Cdd:COG1196 526 ---VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAI--EYLKAAKAGRATflpldkIRARAALAAALARGAIGAA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 555 AAKVASERDTDIASLQEElkkVRAELERWRKAASEYEKEITSLQNSFQLRcqqcedQQREEATRLQGELEKLRKEWNALE 634
Cdd:COG1196 601 VDLVASDLREADARYYVL---GDTLLGRTLVAARLEAALRRAVTLAGRLR------EVTLEGEGGSAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 635 TECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDV 714
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570
....*....|....*
gi 530373156 715 QKEYEKTQTVLSELK 729
Cdd:COG1196 752 ALEELPEPPDLEELE 766
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
462-759 |
5.44e-13 |
|
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: 72.79 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 462 EIQHLRKELIEAQELARTSKQKCFELQALLEEERKA----YRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITST 537
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYegyeLLKEKEALERQKEAIERQLASL----EEELEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 538 RDELLSARDeilLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsfQLRCQQCE-DQQREEA 616
Cdd:TIGR02169 264 EKRLEEIEQ---LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 617 TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRD 696
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373156 697 SADlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 759
Cdd:TIGR02169 419 SEE----LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
169-206 |
1.78e-12 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409286 [Multi-domain] Cd Length: 38 Bit Score: 62.12 E-value: 1.78e-12
10 20 30
....*....|....*....|....*....|....*...
gi 530373156 169 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 206
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-759 |
2.62e-12 |
|
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: 70.86 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 192 QRLLAITQEASDTSWQALIDedrllsRLEVMGNQLQAcsKNQTEDSLRKELIALQEDKHNYET--TAKESLRRVLQEKIE 269
Cdd:TIGR02168 213 ERYKELKAELRELELALLVL------RLEELREELEE--LQEELKEAEEELEELTAELQELEEklEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 270 --------VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK 341
Cdd:TIGR02168 285 elqkelyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 342 KELQhkidEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVeghLTKAVEETKLSKENQTRAKESDfsdtlspSKEK 421
Cdd:TIGR02168 365 AELE----ELESRLEELEEQLETLRSKVAQLELQIASLNNEIER---LEARLERLEDRRERLQQEIEEL-------LKKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 422 SSDDTTDAQMDEQDLNEPLAKVSLLKDDLQgaQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQ 501
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLE--EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 502 VEESTKQIQ------------------------VLQAQLQRLHIDTEN---------------------LREEKDSEITS 536
Cdd:TIGR02168 509 KALLKNQSGlsgilgvlselisvdegyeaaieaALGGRLQAVVVENLNaakkaiaflkqnelgrvtflpLDSIKGTEIQG 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 537 TRDELLSARDEILLLHQAAAKVASERD-------------TDIASLQEELKKVRAEL-------ERWRKAASEY---EKE 593
Cdd:TIGR02168 589 NDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRPGYrivtldgDLVRPGGVITggsAKT 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 594 ITSLQNSFQ--LRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSD 671
Cdd:TIGR02168 669 NSSILERRReiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 672 LSILQMSRKELENQVGSLKEQ----------HLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 741
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERleeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
650
....*....|....*...
gi 530373156 742 ITDELKQCKNNLKLLREK 759
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQ 846
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
300-758 |
2.97e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 300 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 379
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 380 QEklIVEGH---------LTKAVEETKLSKENQTRAKEsDFSDTLSPSKEKSSD--DTTDAQMDEQDLNEPLAK-VSLLK 447
Cdd:PRK02224 240 DE--VLEEHeerreeletLEAEIEDLRETIAETERERE-ELAEEVRDLRERLEEleEERDDLLAEAGLDDADAEaVEARR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 448 DDLQGAQSEIE------------AKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKA---YRNQVEESTKQIQVL 512
Cdd:PRK02224 317 EELEDRDEELRdrleecrvaaqaHNEEAESLREDADDLEERAEELREEAAELESELEEAREAvedRREEIEELEEEIEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 513 QAQLQRLHIDTEN-------LREEKD---SEITSTRDELLSARDEI-----LLlhqAAAK---------------VASER 562
Cdd:PRK02224 397 RERFGDAPVDLGNaedfleeLREERDelrEREAELEATLRTARERVeeaeaLL---EAGKcpecgqpvegsphveTIEED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 563 DTDIASLQEELKKVRAELERWR------KAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETE 636
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEerleraEDLVEAEDRIERLEERRE-DLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 637 CHSlKRE---NVLLSSELQRQEKELHNSQ----KQSLELTSDLSILQMSRKELENQVGSLKEQ-------------HLRD 696
Cdd:PRK02224 553 AEE-KREaaaEAEEEAEEAREEVAELNSKlaelKERIESLERIRTLLAAIADAEDEIERLREKrealaelnderreRLAE 631
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530373156 697 SADLKTLLSKA--ENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 758
Cdd:PRK02224 632 KRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
1.13e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 61.51 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 530373156 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
1.39e-11 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 62.30 E-value: 1.39e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 530373156 52 SRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
164-684 |
2.70e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 164 SQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQTEDSLRKELI 243
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAE--AEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 244 ALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 323
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 324 KVAEGKQEEIQQ-KGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKEN 402
Cdd:COG1196 470 EEAALLEAALAElLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 403 QTRAKesdfsdtlspskekssDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQ 482
Cdd:COG1196 550 NIVVE----------------DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 483 KCFELQALLEEERKAYRNQvEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASER 562
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARL-EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 563 DTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKE--WNALETECHSL 640
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdLEELERELERL 772
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 530373156 641 KRE-------NVLLSSELQRQEKELHnsqkqslELTSDLSILQMSRKELEN 684
Cdd:COG1196 773 EREiealgpvNLLAIEEYEELEERYD-------FLSEQREDLEEARETLEE 816
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
214-758 |
3.18e-11 |
|
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: 67.38 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 214 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 293
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 294 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQadndftn 373
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 374 eRLTALQEKLI-VEGHLTKAVEETKLSKENQTraKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSlLKDDLQG 452
Cdd:TIGR00606 465 -QLEGSSDRILeLDQELRKAERELSKAEKNSL--TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTT-RTQMEML 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 453 AQSEIEAKQEIQHLRKElieaQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDS 532
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSR----HSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASL----EQNKNHINN 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 533 EITSTRDELLSARDEILllhqaAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQC---- 608
Cdd:TIGR00606 613 ELESKEEQLSSYEDKLF-----DVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvf 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 609 --EDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLL-------SSELQRQEKELHNSQKQSLELTSDLSILQMSR 679
Cdd:TIGR00606 688 qtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 680 KELENQVGSL--KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEKQSITDELKQCKNNLKL 755
Cdd:TIGR00606 768 EEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIEL 847
|
...
gi 530373156 756 LRE 758
Cdd:TIGR00606 848 NRK 850
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
252-759 |
6.19e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 252 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsDKLKV 325
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 326 AEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndfTNERLTALQEKLIVEGHLTKAVEETKlSKENQTR 405
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKEKAEEYIKLSEFYEEYL-DELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 406 AKESDFSDTLSPSKEKSSddttDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIE-AQELARTSKQKC 484
Cdd:PRK03918 314 KRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlKKRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 485 FELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRdeLLSARDEILLLHQAAAKVASERDt 564
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGR--ELTEEHRKELLEEYTAELKRIEK- 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 565 DIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRC--QQCEDQQREEATRLQGELEKLRKEWNALETECHSLKR 642
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 643 E---NVLLSSELQRQEKELHNSQKQSLELTSDLSILQM-SRKELENQVGSLKEQH-----LRDSA----DLKTLLSKAEN 709
Cdd:PRK03918 547 ElekLEELKKKLAELEKKLDELEEELAELLKELEELGFeSVEELEERLKELEPFYneyleLKDAEkeleREEKELKKLEE 626
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 530373156 710 QAKDVQKEYEKTQTVLSELK-----LKFEMTEQEKQSITDELKQCKNNLKLLREK 759
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRkeleeLEKKYSEEEYEELREEYLELSRELAGLRAE 681
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
433-758 |
1.38e-10 |
|
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: 65.09 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 433 EQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCfelqalLEEERKAYRNQVEESTKQIQVL 512
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 513 QAQLQ-----------RLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASER---DTDIASLQEELKKVRA 578
Cdd:TIGR02169 257 TEEISelekrleeieqLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELedaEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 579 ELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE------EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQ 652
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 653 RQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADlktlLSKAENQAKDVQKEYEKTQTVLSELKLKF 732
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330 340
....*....|....*....|....*.
gi 530373156 733 EMTEQEKQSITDELKQCKNNLKLLRE 758
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
486-759 |
3.13e-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: 63.92 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 486 ELQALLEEERKAYRNQVEE-----STKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDEILLLHQAAAKVAS 560
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRElelalLVLRLEELREELEELQEELKEAEEELE-ELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 561 ERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSL 640
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE-ELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 641 KRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKA-ENQAKDVQKEYE 719
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELE 443
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 530373156 720 KTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 759
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
240-759 |
4.86e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 240 KELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQE----------ELRELANKY 309
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEElekeleslegSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 310 NGAVNEIKDLSDKLKVAEGKQEEIQQ-KGQAEK-KELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEG 387
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKElKEKAEEyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 388 HLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQ-EIQHL 466
Cdd:PRK03918 342 ELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIgELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 467 RKELIEAQELARTSKQKCFELQALLEEERKAyrNQVEESTKQIQVLQAQLQRLHIDTENLREEKdseitSTRDELLSARD 546
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKEL-----RELEKVLKKES 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 547 EILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcqqcedqqrEEATRLQGELEKL 626
Cdd:PRK03918 494 ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL------------EKLEELKKKLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 627 RKEWNALETECHSLKRENVLLS----SELQRQEKELHNSQKQSLELT---SDLSILQMSRKELENQVGSLKEQHLRDSAD 699
Cdd:PRK03918 562 EKKLDELEEELAELLKELEELGfesvEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKR 641
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530373156 700 LKTLLSK--------AENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 759
Cdd:PRK03918 642 LEELRKEleelekkySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
441-751 |
6.11e-10 |
|
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: 63.16 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 441 AKVSLLKDDLQGAQSEIEA-KQEIQHLRKELIEAQELARTSKQKCFELQA---LLEEERKAYRNQVEESTKQIQVLQAQl 516
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSDASRKIGEIEKeieQLEQEEEKLKERLEELEEDLSSLEQE- 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 517 qrlhidtenlREEKDSEITSTRDELLSARDEILLLHQAAAKV-ASERDTDIASLQEELKKVRAELERWRKAASEYEKEIT 595
Cdd:TIGR02169 753 ----------IENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 596 SLQ----------NSFQLRCQQCEDQQREEATR----------LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQE 655
Cdd:TIGR02169 823 RLTlekeylekeiQELQEQRIDLKEQIKSIEKEienlngkkeeLEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 656 KELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLS----KAENQAKDVQ------------KEYE 719
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYE 982
|
330 340 350
....*....|....*....|....*....|..
gi 530373156 720 KTQTVLSELKLKFEMTEQEKQSITDELKQCKN 751
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
298-626 |
7.08e-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: 62.77 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 298 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQ---KGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNE 374
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 375 RLTALQEKliveghltKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDttdAQMDEQDLNEPLAKVSLLKDDLQGAQ 454
Cdd:TIGR02168 755 ELTELEAE--------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE---LKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 455 SEIEAKQEIQHLRKELIEaqELARTSKQkcfelqalLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEI 534
Cdd:TIGR02168 824 ERLESLERRIAATERRLE--DLEEQIEE--------LSEDIESLAAEIEELEELIEELESELEAL----LNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 535 TSTRDELLSARDEIlllhQAAAKVASERDTDIASLQEELKKVRAELERWR--------KAASEYEKEITSLQNSFQLRCQ 606
Cdd:TIGR02168 890 ALLRSELEELSEEL----RELESKRSELRRELEELREKLAQLELRLEGLEvridnlqeRLSEEYSLTLEEAEALENKIED 965
|
330 340
....*....|....*....|
gi 530373156 607 QcEDQQREEATRLQGELEKL 626
Cdd:TIGR02168 966 D-EEEARRRLKRLENKIKEL 984
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
301-759 |
1.33e-09 |
|
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: 61.57 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 301 ELRELANKYNGAVNEIKDLSDKLKVAEG---KQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERL- 376
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKnlnKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIk 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 377 TALQEKLIVEGHLTKAVEETKLSKENQTRAKESDF--SDTLSPSKEKSSDDTTDAQMDEQDLNeplakvsLLKDDLQGAQ 454
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKkkEKELEKLNNKYNDLKKQKEELENELN-------LLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 455 SEIeAKQEIQHLRKELIEAQELARTSKQKCFELQAL-LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSE 533
Cdd:TIGR04523 187 KNI-DKIKNKLLKLELLLSNLKKKIQKNKSLESQISeLKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 534 -----------------ITSTRDELLSARDEILLL-HQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEIT 595
Cdd:TIGR04523 266 kkqlsekqkeleqnnkkIKELEKQLNQLKSEISDLnNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 596 SL--------------QNSFQLRCQQCEDQQREEATRLQgELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNS 661
Cdd:TIGR04523 346 QLkkeltnsesensekQRELEEKQNEIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 662 QKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 741
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
490
....*....|....*...
gi 530373156 742 ITDELKQCKNNLKLLREK 759
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKK 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
448-667 |
1.87e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 448 DDLQGAQSEIE-AKQEIQHLRkELIEAQELARTSKQKCFELQALLEeerkayRNQVEESTKQIQVLQAQLQRLhidtENL 526
Cdd:COG4913 235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRA------ALRLWFAQRRLELLEAELEEL----RAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 527 REEKDSEITSTRDELLSARDEILLLHQAAAKVASERdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNSfqlrcq 606
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGGDR---LEQLEREIERLERELEERERRRARLEALLAALGLP------ 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530373156 607 qcEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLE 667
Cdd:COG4913 375 --LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA-EIASLE 432
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
258-729 |
2.58e-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: 60.90 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 258 ESLRRVLQEKIEVVRKLSE--VERSLSNTEDECTHLKEMNERTQEELRELANKYN----GAVNEIKDLSDKLKVAEGKQE 331
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQdrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiqeQARNQNSMYMRQLSDLESTVS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 332 EIQQKGQAEKKELQHKIDEMEEKEQELQAKI-EALQADNDFTNE--RLTALQEKLIVEGHltKAVEETKLSKENQTRAKE 408
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQLVLANSELtEARTERDQFSQEsgNLDDQLQKLLADLH--KREKELSLEKEQNKRLWD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 409 SDFSDTLSPskekssdDTTDAQMDEQDLneplaKVSLLKDDLQGAQSEIEAKQEIQhlrkelIEAQELARTSKQKCFELQ 488
Cdd:pfam15921 406 RDTGNSITI-------DHLRRELDDRNM-----EVQRLEALLKAMKSECQGQMERQ------MAAIQGKNESLEKVSSLT 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 489 ALLEEERKAYRNQVEESTKQIQVLQAQlQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtdias 568
Cdd:pfam15921 468 AQLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD----- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 569 lqeELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLK------- 641
Cdd:pfam15921 542 ---HLRNVQTECEALKLQMAEKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkd 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 642 ---RENVLLSSELQRQEKELHNSQKQSLELTSD--------LSILQMSRKELEN---QVGSLKEQHLRDSADLKTLLSKA 707
Cdd:pfam15921 618 akiRELEARVSDLELEKVKLVNAGSERLRAVKDikqerdqlLNEVKTSRNELNSlseDYEVLKRNFRNKSEEMETTTNKL 697
|
490 500
....*....|....*....|..
gi 530373156 708 ENQAKDVQKEYEKTQTVLSELK 729
Cdd:pfam15921 698 KMQLKSAQSELEQTRNTLKSME 719
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
98-701 |
3.39e-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: 60.52 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 98 LSGDIIQFGVDVTENTRKGTVTHGCIVSTIKLFLPDGMEARLRSDVIHAPLPSPVDKVAANTPSMYSQELFQLSQYLQEA 177
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 178 LHR-EQMLEQKLATLQRLLAITQEASDTSWQALIDEdrllSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTa 256
Cdd:pfam15921 240 IFPvEDQLEALKSESQNKIELLLQQHQDRIEQLISE----HEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 257 keslrrvlqekieVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 336
Cdd:pfam15921 315 -------------YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 337 GQAEKKELQHKIDEMEEKEQELQAK-------IEALQADNDFTN---ERLTALQEKLIVEGHLTKAVEETKLSKENQTRA 406
Cdd:pfam15921 382 LLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNmevQRLEALLKAMKSECQGQMERQMAAIQGKNESLE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 407 KESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAK---------------QEIQHLRKE-- 469
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATnaeitklrsrvdlklQELQHLKNEgd 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 470 -------LIEAQELARTSKQKCFEL-------------------------QALLEEERKAYRNQVEE-------STKQIQ 510
Cdd:pfam15921 542 hlrnvqtECEALKLQMAEKDKVIEIlrqqienmtqlvgqhgrtagamqveKAQLEKEINDRRLELQEfkilkdkKDAKIR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 511 VLQAQLQRLHID--------TENLREEKD---------SEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEEL 573
Cdd:pfam15921 622 ELEARVSDLELEkvklvnagSERLRAVKDikqerdqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 574 KKVRAELERWR--------------KAASEYEKEITSLQNsfQLRCQQCEDQQREEATR--------LQGELEKLRKEWN 631
Cdd:pfam15921 702 KSAQSELEQTRntlksmegsdghamKVAMGMQKQITAKRG--QIDALQSKIQFLEEAMTnankekhfLKEEKNKLSQELS 779
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530373156 632 ALETECHSLKRENVLLSSELQRQEKELHNSQ----KQSLELTSDLSILQmsRKELENQvgSLKEQHLRDSADLK 701
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEvaldKASLQFAECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
231-693 |
3.52e-09 |
|
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: 60.45 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 231 KNQTEDSLRKELIALQEDKHNyettaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELA---- 306
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQN-----KNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAmlag 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 307 --NKYNGAVNEIKD-------LSDKLKVAEGKQEEIQQKGQA-------EKKELQHKIDEMEEKEQELQAKIEALQADND 370
Cdd:TIGR00606 661 atAVYSQFITQLTDenqsccpVCQRVFQTEAELQEFISDLQSklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 371 FTNERLTALQEKLiveGHLTKAVEETKLSKENQTRAKEsdfsdTLSPSKEKSSDDTTDAQMDEQdLNEPLAKVSLLKDDL 450
Cdd:TIGR00606 741 LKEKEIPELRNKL---QKVNRDIQRLKNDIEEQETLLG-----TIMPEEESAKVCLTDVTIMER-FQMELKDVERKIAQQ 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 451 QGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRN----QVEESTKQIQVLQAQLQRLHIDTENl 526
Cdd:TIGR00606 812 AAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHlkskTNELKSEKLQIGTNLQRRQQFEEQL- 890
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 527 rEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQ 606
Cdd:TIGR00606 891 -VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD 969
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 607 QCEDQQREEATRLQGEL-------EKLRKEWNALETECHSLKRENVLLSSELQRQE-----KELHNSQKQSLELTSDLSI 674
Cdd:TIGR00606 970 DYLKQKETELNTVNAQLeecekhqEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKrenelKEVEEELKQHLKEMGQMQV 1049
|
490 500
....*....|....*....|.
gi 530373156 675 LQMSR--KELENQVGSLKEQH 693
Cdd:TIGR00606 1050 LQMKQehQKLEENIDLIKRNH 1070
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
249-763 |
6.21e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 249 KHNYETTAKESLRRVLQEKIEVVRKLSEVERSlsntEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAE- 327
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKD----AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADe 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 328 -GKQEEIQQKGQAEKKELQHKIDEMEEKEQElQAKIEALQADNDFTNERLTALQEKliveghltkavEETKLSKENQTRA 406
Cdd:PTZ00121 1283 lKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKK-----------AEEAKKAAEAAKA 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 407 KESDFSDTLSPSKEKssddttdAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQElARTSKQKCFE 486
Cdd:PTZ00121 1351 EAEAAADEAEAAEEK-------AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADE 1422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 487 LQALLEEERKA--YRNQVEESTKQIQVLQAQLQRLhiDTENLReeKDSEITSTRDELLSARDEILLLHQAAAKV-ASERD 563
Cdd:PTZ00121 1423 AKKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAK--KAEEAK--KKAEEAKKADEAKKKAEEAKKADEAKKKAeEAKKK 1498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 564 TDIASLQEELKKVRAELERWRKAASEYE-KEITSLQNSFQLRcqQCEDQQREEATRLQGELEKLRKEWNALETECHSLKR 642
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEaKKAEEAKKADEAK--KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 643 ENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLK----EQHLRDSADLKTLLSKAENQAKDVQKEY 718
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 530373156 719 EKTQTVLSELKLKfemtEQEKQSITDELKQCKNNLKLLREKGNNK 763
Cdd:PTZ00121 1657 EENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-748 |
8.41e-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: 59.31 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 199 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELIALQEDKHNYETTAKESLRRVLQEKI---EVVRKLS 275
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 276 EVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqqkgQAEKKELQHKIDEMEEKE 355
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK----ALEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 356 QELQAKIEALQADNDFTNERLTALQEKLIV----------EGHLTKAVEETK---------------------------- 397
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEaeaqaraseeRVRGGRAVEEVLkasiqgvhgtvaqlgsvgeryataieva 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 398 ----------------------LSKENQTRA------KESDFSDTLSPSKEK---------------------------- 421
Cdd:TIGR02169 545 agnrlnnvvveddavakeaielLKRRKAGRAtflplnKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtl 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 422 --SSDDTTDAQMD-------EQDLNEP--------LAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKC 484
Cdd:TIGR02169 625 vvEDIEAARRLMGkyrmvtlEGELFEKsgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRL 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 485 FELQALLEEERKayrnQVEESTKQIQVLQAQLQRLHIDTENLREekdsEITSTRDELLSARDEIlllhQAAAKVASERDT 564
Cdd:TIGR02169 705 DELSQELSDASR----KIGEIEKEIEQLEQEEEKLKERLEELEE----DLSSLEQEIENVKSEL----KELEARIEELEE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 565 DIASLQEELKKVRAEL--ERWRKAASEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKLRKEWNALETECHSLKR 642
Cdd:TIGR02169 773 DLHKLEEALNDLEARLshSRIPEIQAELSKLEEEVS------------RIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 643 ENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKeqhlRDSADLKTLLSKAENQAKDVQKEYEKTQ 722
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK----KERDELEAQLRELERKIEELEAQIEKKR 916
|
650 660
....*....|....*....|....*.
gi 530373156 723 TVLSELKLKFEMTEQEKQSITDELKQ 748
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
169-508 |
9.48e-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: 59.31 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 169 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELI 243
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkselKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 244 ALQEDKHNYETTAKESLRRVLQEKI-EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 322
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 323 LKVAEGKQEEIqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKlivEGHLTKAVEETKLSKEN 402
Cdd:TIGR02169 849 IKSIEKEIENL----NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK---IEELEAQIEKKRKRLSE 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 403 QTRAKESDFSdtlspskEKSSDDTTDAQMDEQDLNEPLAKVslLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQ 482
Cdd:TIGR02169 922 LKAKLEALEE-------ELSEIEDPKGEDEEIPEEELSLED--VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992
|
330 340
....*....|....*....|....*.
gi 530373156 483 kcfELQALLEEERKAYRNQVEESTKQ 508
Cdd:TIGR02169 993 ---EKRAKLEEERKAILERIEEYEKK 1015
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
166-206 |
1.07e-08 |
|
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409288 [Multi-domain] Cd Length: 45 Bit Score: 51.58 E-value: 1.07e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 530373156 166 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 206
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
239-668 |
1.73e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 239 RKELIALQEDKHNYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTqEELRELANKYNGAVNEIKD 318
Cdd:PRK03918 282 VKELKELKEKAEEYIKL-SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 319 LSDKLKVAEGKQEEIQQ----KGQAEKKELQHKIDEMEEKEQELQAKIEALqadndftNERLTALQEKlivEGHLTKAVE 394
Cdd:PRK03918 360 RHELYEEAKAKKEELERlkkrLTGLTPEKLEKELEELEKAKEEIEEEISKI-------TARIGELKKE---IKELKKAIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 395 ETK------------LSKENQTRAKESDFSDTLSPSKEKSS--DDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAK 460
Cdd:PRK03918 430 ELKkakgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEieEKERKLRKELRELEKVLKKESELIKLKELAEQLKELE 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 461 QEIQHLRKELIEAQ-ELARTSKQKCFELQALLE------EERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSE 533
Cdd:PRK03918 510 EKLKKYNLEELEKKaEEYEKLKEKLIKLKGEIKslkkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 534 ITSTRDELLSARDEILLLHQAAAKVASERDtDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlrcqqcedqqR 613
Cdd:PRK03918 590 LEERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS----------E 658
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 530373156 614 EEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLEL 668
Cdd:PRK03918 659 EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-106 |
2.18e-08 |
|
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.
Pssm-ID: 438737 [Multi-domain] Cd Length: 130 Bit Score: 53.19 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
.
gi 530373156 106 G 106
Cdd:cd22685 105 G 105
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
154-635 |
2.24e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 154 KVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswqaliDEDRLLSRLEVMGNQLQACSKNQ 233
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 234 TEDSLRKELIALQEdkhnyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKE-MNERTQEELRELANKYNGA 312
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 313 VNEIKDLSDKLKVAEGKQEEIQQkgQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKA 392
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEE--ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 393 VEETKLSKENQTRAKESdfsdtLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDdlQGAQSEIEAKQEIQHLRKELIE 472
Cdd:COG4717 283 LGLLALLFLLLAREKAS-----LGKEAEELQALPALEELEEEELEELLAALGLPPD--LSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 473 AQELARTSKQKCF--ELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSeitstrdellsardeilL 550
Cdd:COG4717 356 AEELEEELQLEELeqEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE-----------------L 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 551 LHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLrcqqceDQQREEATRLQGELEKLRKEW 630
Cdd:COG4717 419 EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL------AELLQELEELKAELRELAEEW 492
|
....*
gi 530373156 631 NALET 635
Cdd:COG4717 493 AALKL 497
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.65e-08 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438722 [Multi-domain] Cd Length: 105 Bit Score: 52.23 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 530373156 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
329-636 |
3.04e-08 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 57.38 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 329 KQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEALQAD-NDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRAK 407
Cdd:pfam13166 94 IQEKIAKL-KKEIKDHEEKLDAAEANLQKLDKEKEKLEADfLDECWKKIKRKKNSALSEALNGFKYEANFKSRLLREIEK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 408 ESDFSDTLSPSKEKSSDDTT---DAQMDEQDLNEPLA------KVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELAR 478
Cdd:pfam13166 173 DNFNAGVLLSDEDRKAALATvfsDNKPEIAPLTFNVIdfdaleKAEILIQKVIGKSSAIEELIKNPDLADWVEQGLELHK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 479 TSKQKC--------FELQALLEE---------------------------------------ERKAYRNQVEESTKQIQV 511
Cdd:pfam13166 253 AHLDTCpfcgqplpAERKAALEAhfddeftefqnrlqkliekvesaissllaqlpavsdlasLLSAFELDVEDIESEAEV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 512 LQAQLQRLHIDTENLREE--KDSEITSTRDELLSARDEILLLHQAAAKvASERDTDIASLQEELKKvraelERWRKAASE 589
Cdd:pfam13166 333 LNSQLDGLRRALEAKRKDpfKSIELDSVDAKIESINDLVASINELIAK-HNEITDNFEEEKNKAKK-----KLRLHLVEE 406
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 530373156 590 YEKEITSLQNSFQLRCQQCEDQQrEEATRLQGELEKLRKEWNALETE 636
Cdd:pfam13166 407 FKSEIDEYKDKYAGLEKAINSLE-KEIKNLEAEIKKLREEIKELEAQ 452
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
163-758 |
3.05e-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: 57.44 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 163 YSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAITQEASDtswqALIDedrlLSRLEvmgNQLQACSKNQTEDSL 238
Cdd:pfam15921 83 YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEMQMERD----AMAD----IRRRE---SQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 239 RKELIA--LQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHlkEMNERTQEELRELANkyngAVNEI 316
Cdd:pfam15921 152 HELEAAkcLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIY--EHDSMSTMHFRSLGS----AISKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 317 -KDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQElqaKIEALQADNDFtneRLTALQEKliveghltkavee 395
Cdd:pfam15921 226 lRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQD---RIEQLISEHEV---EITGLTEK------------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 396 tklskENQTRAKESDFSDTLSPSKEKSSDDTTdaqMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKqeIQHLRKELIEAQ- 474
Cdd:pfam15921 287 -----ASSARSQANSIQSQLEIIQEQARNQNS---MYMRQLSDLESTVSQLRSELREAKRMYEDK--IEELEKQLVLANs 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 475 EL--ARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRL-------HIDTENLREEKDS---EITSTRDELL 542
Cdd:pfam15921 357 ELteARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnSITIDHLRRELDDrnmEVQRLEALLK 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 543 SARDEI---LLLHQAAAKVASERDTDIASL-------QEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcQQCEDQQ 612
Cdd:pfam15921 437 AMKSECqgqMERQMAAIQGKNESLEKVSSLtaqlestKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-ERAIEAT 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 613 REEATRLQG-------ELEKLRKEWNAL---ETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKEL 682
Cdd:pfam15921 516 NAEITKLRSrvdlklqELQHLKNEGDHLrnvQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 683 ENQVG----SLKE-QHLRDSADLKtlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLR 757
Cdd:pfam15921 596 EKEINdrrlELQEfKILKDKKDAK--IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
.
gi 530373156 758 E 758
Cdd:pfam15921 674 E 674
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.34e-08 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 49.87 E-value: 4.34e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 530373156 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
291-741 |
6.43e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 291 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEALQADND 370
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 371 F--TNERLTALQEKLIVEGHLTKAVEETKL---SKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPL----A 441
Cdd:COG4717 127 LlpLYQELEALEAELAELPERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELeelqQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 442 KVSLLKDDLQGAQSEIE-AKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLH 520
Cdd:COG4717 207 RLAELEEELEEAQEELEeLEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 521 IDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQ-- 598
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQle 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 599 ------NSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQ--EKELHNSQKQSLELTS 670
Cdd:COG4717 367 eleqeiAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530373156 671 DLSILQMSRKELENQVGSLKEQHlrDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 741
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDG--ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
453-692 |
9.20e-08 |
|
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: 55.16 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 453 AQSEIEAKQEIQHLRKELIEAQELARTSKQKcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREekds 532
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 533 EITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqqcedQQ 612
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 613 REEATRLQGELEKLRKEWNALETEchsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 692
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
312-561 |
9.80e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 312 AVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLiveghlTK 391
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI------EE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 392 AVEETKlskenqTRAKESdfsdtlspSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEakqEIQHLRKELI 471
Cdd:COG3883 84 RREELG------ERARAL--------YRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLE---ELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 472 EAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLL 551
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250
....*....|
gi 530373156 552 HQAAAKVASE 561
Cdd:COG3883 227 AAAAAAAAAA 236
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
247-733 |
1.12e-07 |
|
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: 55.57 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 247 EDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTH-LKEMNERTQEE---LRELANKYNGAVNEIKDLSDK 322
Cdd:pfam01576 32 EKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEiLHELESRLEEEeerSQQLQNEKKKMQQHIQDLEEQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 323 LKvaegKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKE- 401
Cdd:pfam01576 112 LD----EEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEa 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 402 -----NQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLA--KVSLLK--DDLQGAQSEIEAKQ----------- 461
Cdd:pfam01576 188 misdlEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAelRAQLAKkeEELQAALARLEEETaqknnalkkir 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 462 EIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDEL 541
Cdd:pfam01576 268 ELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 542 LSAR-------DEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYE---KEITSLQNSFQLRCQQCEDQ 611
Cdd:pfam01576 348 QEMRqkhtqalEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEhkrKKLEGQLQELQARLSESERQ 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 612 QREEA---TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLsilqmsrKELENQVGS 688
Cdd:pfam01576 428 RAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL-------RQLEDERNS 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 530373156 689 LKEQhlrdsadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 733
Cdd:pfam01576 501 LQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
184-636 |
2.02e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 184 LEQKLATLQRLLAI----TQEASDTSWQALIDEDRllSRLEVMGNQLQACSknQTEDSLRKELIALQEDKHNYETTAKES 259
Cdd:COG4913 267 ARERLAELEYLRAAlrlwFAQRRLELLEAELEELR--AELARLEAELERLE--ARLDALREELDELEAQIRGNGGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 260 LRRVLQEKievVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQA 339
Cdd:COG4913 343 LEREIERL---ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 340 EKKELQHKIDEMEEK----EQELQAKIEALQADNDFTNERL-----------------TALqEK--------LIVEGH-- 388
Cdd:COG4913 420 ELRELEAEIASLERRksniPARLLALRDALAEALGLDEAELpfvgelievrpeeerwrGAI-ERvlggfaltLLVPPEhy 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 389 --LTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSS-------DDTT-----DAQM----------DEQDL-NEPLA-- 441
Cdd:COG4913 499 aaALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSlagkldfKPHPfrawlEAELgrrfdyvcvdSPEELrRHPRAit 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 442 --------KVSLLKDDLQGAQSE----IEAKQEIQHLRKELIEAQELARTSKQKCFELQAL---LEEERKAYRNQVEEST 506
Cdd:COG4913 579 ragqvkgnGTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAEldaLQERREALQRLAEYSW 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 507 KQIQVLQAQLQRlhidtENLREEKDsEITSTRDELLSARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAELERW 583
Cdd:COG4913 659 DEIDVASAEREI-----AELEAELE-RLDASSDDLAALEEQLEELEAELEELEEELDelkGEIGRLEKELEQAEEELDEL 732
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 530373156 584 RKAASEYEKEITSLQNS-FQLRCQQ--CEDQQREEATRLQGELEKLRKEWNALETE 636
Cdd:COG4913 733 QDRLEAAEDLARLELRAlLEERFAAalGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
257-593 |
2.88e-07 |
|
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: 54.30 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 257 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 336
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 337 GQAEKKELQHKIDEMEEKEQ---ELQAKIEALQADNDftNERLTALQEKLiveghltKAVEETKLSKENQTRAKESDFSD 413
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEdlhKLEEALNDLEARLS--HSRIPEIQAEL-------SKLEEEVSRIEARLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 414 tLSPSKEKSSDDTTDAQMDeqdlneplakvsllKDDLQGAQSEIEAKQEIQHLRKELIEAQElartSKQKCFELQalLEE 493
Cdd:TIGR02169 824 -LTLEKEYLEKEIQELQEQ--------------RIDLKEQIKSIEKEIENLNGKKEELEEEL----EELEAALRD--LES 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 494 ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLReEKDSEITSTRDELLSARDEILLLhQAAAKVASERDTDIASLQEEL 573
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKR-KRLSELKAKLEALEEELSEIEDP-KGEDEEIPEEELSLEDVQAEL 960
|
330 340
....*....|....*....|....
gi 530373156 574 KKVRAELERWR----KAASEYEKE 593
Cdd:TIGR02169 961 QRVEEEIRALEpvnmLAIQEYEEV 984
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
3.51e-07 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438753 [Multi-domain] Cd Length: 106 Bit Score: 49.16 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 530373156 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
184-584 |
4.31e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 184 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELIALQEDKHNYETTaKESLRRV 263
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 264 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEE 332
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 333 IQQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLiveghltkaveETKLSKENQTRAKES 409
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-----------EELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 410 DFSDTLS------------------PSKEKSSDDTTDAQMDEQDlNEPLAKVSLLKDDLQGAQSEIEAKQEiqhLRKELI 471
Cdd:PRK02224 430 ELEATLRtarerveeaealleagkcPECGQPVEGSPHVETIEED-RERVEELEAELEDLEEEVEEVEERLE---RAEDLV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 472 EAQELARTSKQKCFELQALLEEErkayRNQVEESTKQIQVLQAQLQRLhiDTENlrEEKDSEITSTRDELLSARDEILLL 551
Cdd:PRK02224 506 EAEDRIERLEERREDLEELIAER----RETIEEKRERAEELRERAAEL--EAEA--EEKREAAAEAEEEAEEAREEVAEL 577
|
410 420 430
....*....|....*....|....*....|....*
gi 530373156 552 HQAAAKVASERDT--DIASLQEELKKVRAELERWR 584
Cdd:PRK02224 578 NSKLAELKERIESleRIRTLLAAIADAEDEIERLR 612
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
231-762 |
6.01e-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: 53.19 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 231 KNQTEDSLRKELIALQEDKHNYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLKEMNERTQEE 301
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 302 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAkiEALQADNDFTNE---RLTA 378
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEE--EYKKEINDKEKQvslLLIQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 379 LQEKLIVEGHLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIE 458
Cdd:pfam05483 249 ITEKENKMKDLTFLLEESR-DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 459 AKQEIQHLRKELIEAQELARTSKQKCFELQAL-LEEERKAYRNQVEESTKQIQVLQAQLQRlhidtenlreeKDSEItst 537
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFEATTCsLEELLRTEQQRLEKNEDQLKIITMELQK-----------KSSEL--- 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 538 rdellsardeilllhQAAAKVASERDTDIaslqEELKKVRAELERWRKAASEYEKEITSLQNSFQlrcqqcedqqreeat 617
Cdd:pfam05483 394 ---------------EEMTKFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEELKGKEQ--------------- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 618 RLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL-------- 689
Cdd:pfam05483 440 ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkhq 519
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373156 690 ------KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 762
Cdd:pfam05483 520 ediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
7.45e-07 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 48.51 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 530373156 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
7.73e-07 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 47.79 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 530373156 106 G 106
Cdd:cd22698 86 G 86
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
239-620 |
9.90e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 239 RKELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEI 316
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQilSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 317 KDLSDKLKVAEGKQE-------EIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL-IVEGH 388
Cdd:PRK01156 373 ESLKKKIEEYSKNIErmsafisEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMeMLNGQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 389 LTKAVEETKLSKENQTRAKEsDFSDTLSPSKEkssdDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSE--IEAKQEIQHL 466
Cdd:PRK01156 453 SVCPVCGTTLGEEKSNHIIN-HYNEKKSRLEE----KIREIEIEVKDIDEKIVDLKKRKEYLESEEINksINEYNKIESA 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 467 RKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEEstKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARD 546
Cdd:PRK01156 528 RADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDS--KRTSWLNALAVISLIDIETNRSRSN-EIKKQLNDLESRLQ 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 547 EILLlhqAAAKVASERDTDIASLQEELKKVR----------AELERWRKAASEYEKEITSL------QNSFQLRCQQCED 610
Cdd:PRK01156 605 EIEI---GFPDDKSYIDKSIREIENEANNLNnkyneiqenkILIEKLRGKIDNYKKQIAEIdsiipdLKEITSRINDIED 681
|
410
....*....|
gi 530373156 611 QQREEATRLQ 620
Cdd:PRK01156 682 NLKKSRKALD 691
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
1.03e-06 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 47.70 E-value: 1.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 530373156 55 HALVWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
330-532 |
1.95e-06 |
|
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: 50.92 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 330 QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL-IVEGHLTKAVEETKLSKENQTRAKE 408
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIrALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 409 S------DFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEakqEIQHLRKELIEAQELARTSKQ 482
Cdd:COG4942 98 EleaqkeELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE---ELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530373156 483 KCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDS 532
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
236-685 |
2.55e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 236 DSLRKELIALQEDKHNYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER--TQEELRELANKYNGAV 313
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 314 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL-IVEGHLTKA 392
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELeELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 393 VEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIE 472
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 473 AQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLH--IDTENLREEKDSEITSTRDELLSARDEILL 550
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEeeLQLEELEQEIAALLAEAGVEDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 551 LHQAAAKVASERDTDIASLQEELKKVRAELERWRKAasEYEKEITSLQnsfqlrcqqcedqqrEEATRLQGELEKLRKEW 630
Cdd:COG4717 393 QAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELE---------------EELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 530373156 631 NALETECHSLKRENVL--LSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQ 685
Cdd:COG4717 456 AELEAELEQLEEDGELaeLLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
259-507 |
3.97e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 50.31 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 259 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 330
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 331 EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQA---------DNDFTNERLTALQEKLIVEGHLTKAVEETKLSKE 401
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQeierlepwgNFDLDLSLLLGFKYVSVFVGTVPEDKLEELKLES 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 402 NQTRAKESDFSDTLSP-----SKEkssddttdaqmDEQDLNEPLAKVSLLKDDLQ--GAQSEI--EAKQEIQHLRKELIE 472
Cdd:PRK05771 165 DVENVEYISTDKGYVYvvvvvLKE-----------LSDEVEEELKKLGFERLELEeeGTPSELirEIKEELEEIEKERES 233
|
250 260 270
....*....|....*....|....*....|....*
gi 530373156 473 AQELARTSKQKCFELQALLEEERKAYRNQVEESTK 507
Cdd:PRK05771 234 LLEELKELAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-106 |
6.48e-06 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 45.43 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
443-580 |
7.82e-06 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 47.30 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 443 VSLLKDDLQGAQSEIEAK-QEIQHLRKELIEAQELARTSKQKCFELQAlleeerkayrnQVEESTKQIQVLQAQLQRLHI 521
Cdd:pfam06818 12 ISLLKQQLKDSQAEVTQKlNEIVALRAQLRELRAKLEEKEEQIQELED-----------SLRSKTLELEVCENELQRKKN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530373156 522 DTENLRE---EKDSEITSTRDEL--LSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL 580
Cdd:pfam06818 81 EAELLREkvgKLEEEVSGLREALsdVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAEL 144
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
291-547 |
8.84e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 291 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadnd 370
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 371 ftNERLTALQEKLI-VEGHLTK-AVEETKLSKENQTRAKESDFSDtlspskeksSDDTTDAQMdeQDLNEPLAKVSLLKD 448
Cdd:PHA02562 240 --TDELLNLVMDIEdPSAALNKlNTAAAKIKSKIEQFQKVIKMYE---------KGGVCPTCT--QQISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 449 DLQGAQSEIEAKQE-IQHLRKELIEAQELARTSKqkcfELQALLEEERKAYRNQVEEStKQIQVLQAQLQRLHID----T 523
Cdd:PHA02562 307 KLKELQHSLEKLDTaIDELEEIMDEFNEQSKKLL----ELKNKISTNKQSLITLVDKA-KKVKAAIEELQAEFVDnaeeL 381
|
250 260
....*....|....*....|....
gi 530373156 524 ENLREEKDsEITSTRDELLSARDE 547
Cdd:PHA02562 382 AKLQDELD-KIVKTKSELVKEKYH 404
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
1.03e-05 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 44.85 E-value: 1.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373156 51 LSRNHALVWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
253-763 |
1.06e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 253 ETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR-ELANKYNGA--VNEIKDLSDKLKVAE- 327
Cdd:PTZ00121 1114 ARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaEEARKAEDAkkAEAARKAEEVRKAEEl 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 328 GKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKI------------EALQADNDFTNERLTALQEKLIVEGHLTKAVE- 394
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkkaeeakkdaeEAKKAEEERNNEEIRKFEEARMAHFARRQAAIk 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 395 -ETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDE--------QDLNEPLAKVSLLKDDLQGAQSEIEA-KQEIQ 464
Cdd:PTZ00121 1274 aEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakkadeakKKAEEAKKKADAAKKKAEEAKKAAEAaKAEAE 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 465 HLRKELIEAQELART-------SKQKCFELQALLEEERKA--YRNQVEESTKQIQVL------QAQLQRLHIDTENLRE- 528
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAaekkkeeAKKKADAAKKKAEEKKKAdeAKKKAEEDKKKADELkkaaaaKKKADEAKKKAEEKKKa 1433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 529 ---EKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL----ERWRKAASEYEKEITSLQNSF 601
Cdd:PTZ00121 1434 deaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKKADEAKKAAEAKKKAD 1513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 602 QLR----CQQCEDQQREEATRLQGELEKLRKEWNALEtechsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQM 677
Cdd:PTZ00121 1514 EAKkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADE-----LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 678 SRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKlkfemTEQEKQSITDELKQCKNNLKLLR 757
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-----KEAEEKKKAEELKKAEEENKIKA 1663
|
....*.
gi 530373156 758 EKGNNK 763
Cdd:PTZ00121 1664 AEEAKK 1669
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
264-753 |
1.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 264 LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERT------------QEELRELANKYNGAVNEIKDLSDKLKVAEGK-- 329
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALrlwfaqrrlellEAELEELRAELARLEAELERLEARLDALREEld 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 330 --QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQadndftnERLTALqeklivegHLTKAVEETKLsKENQTRAK 407
Cdd:COG4913 327 elEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE-------ALLAAL--------GLPLPASAEEF-AALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 408 EsdFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQeiQHLRKELieAQELARTSKQKCF-- 485
Cdd:COG4913 391 A--LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LALRDAL--AEALGLDEAELPFvg 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 486 ELQALLEEER-------KAYRNQ-----VEESTKQiQVLQA--QLQ-RLHIDTENLREEKDSEITSTRDEllsardeill 550
Cdd:COG4913 465 ELIEVRPEEErwrgaieRVLGGFaltllVPPEHYA-AALRWvnRLHlRGRLVYERVRTGLPDPERPRLDP---------- 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 551 lHQAAAKVASERDTDIASLQEELKKVRA--------ELERWRKAaseyekeITS---LQNSFQLRcqQCEDQQREEATRL 619
Cdd:COG4913 534 -DSLAGKLDFKPHPFRAWLEAELGRRFDyvcvdspeELRRHPRA-------ITRagqVKGNGTRH--EKDDRRRIRSRYV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 620 QGE-----LEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRK--ELENQVGSLkeq 692
Cdd:COG4913 604 LGFdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELERL--- 680
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530373156 693 hLRDSADLKTLlskaENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNL 753
Cdd:COG4913 681 -DASSDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
1.21e-05 |
|
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438726 [Multi-domain] Cd Length: 108 Bit Score: 44.95 E-value: 1.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 530373156 52 SRNH-ALVWfdHK-TGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
255-632 |
1.36e-05 |
|
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: 48.66 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 255 TAKESLRRVLQEKIEVVR-KLSEVERSLSNTedecthlkemnertQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 333
Cdd:pfam10174 334 TAKEQRAAILQTEVDALRlRLEEKESFLNKK--------------TKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 334 QQKGQaekkELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRAKESDFSD 413
Cdd:pfam10174 400 QKKIE----NLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKK 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 414 TLSPSKEKSSDDTTDAQMDEQDLNEPLAKVS-----LLKDDLQGAQSEIEAKQ---EIQHLRKELIEAQELARTSkQKCF 485
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLKEHASslassGLKKDSKLKSLEIAVEQkkeECSKLENQLKKAHNAEEAV-RTNP 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 486 ELQ---ALLEEERKAYRnqvEESTKQiqvlQAQLQRLH---IDTENLREEKDSEItstrdellsARDEILLLHQaaAKVA 559
Cdd:pfam10174 555 EINdriRLLEQEVARYK---EESGKA----QAEVERLLgilREVENEKNDKDKKI---------AELESLTLRQ--MKEQ 616
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373156 560 SERDTDIASLQEELKKVRAELerwrkaaseyekeitsLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNA 632
Cdd:pfam10174 617 NKKVANIKHGQQEMKKKGAQL----------------LEEARRREDNLADNSQQLQLEELMGALEKTRQELDA 673
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
1.52e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 44.25 E-value: 1.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373156 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
338-719 |
1.65e-05 |
|
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: 48.15 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 338 QAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALqEKLIVEG--------HLTKAVEETKlskENQTRAKES 409
Cdd:pfam05622 6 QEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQL-ESGDDSGtpggkkylLLQKQLEQLQ---EENFRLETA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 410 dfSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDL----QGAQSEIEAKQEIQHLRKELIEAQELARTSKQ--- 482
Cdd:pfam05622 82 --RDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMdilrESSDKVKKLEATVETYKKKLEDLGDLRRQVKLlee 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 483 ---KCFELQALLEEERKAY---RNQVEESTKQIQVLQAQLQRLHIDTENLR------EEKDSEITSTRDELLSARD---- 546
Cdd:pfam05622 160 rnaEYMQRTLQLEEELKKAnalRGQLETYKRQVQELHGKLSEESKKADKLEfeykklEEKLEALQKEKERLIIERDtlre 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 547 --EILLLHQAAAKVASERDTDIASLQEELKKVRAELerwrkAASEYEKEITSLQNSFQ-LRCQQcEDQQREEATRLQGEL 623
Cdd:pfam05622 240 tnEELRCAQLQQAELSQADALLSPSSDPGDNLAAEI-----MPAEIREKLIRLQHENKmLRLGQ-EGSYRERLTELQQLL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 624 EKLRKEWNALETEcHSLKRENVLLSS----ELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ--HLRDS 697
Cdd:pfam05622 314 EDANRRKNELETQ-NRLANQRILELQqqveELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQieELEPK 392
|
410 420
....*....|....*....|..
gi 530373156 698 ADLKTLLSKAENQAKDVQKEYE 719
Cdd:pfam05622 393 QDSNLAQKIDELQEALRKKDED 414
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
164-737 |
1.67e-05 |
|
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: 48.28 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 164 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 239
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 240 KELIALQEDKH-NYETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRElankyngavnEIK 317
Cdd:pfam10174 206 KENIHLREELHrRNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREE----------EIK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 318 dlsdKLKVAEGKQEEIQQKGQAEKKELQHKIDEMeekeQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETK 397
Cdd:pfam10174 276 ----QMEVYKSHSKFMKNKIDQLKQELSKKESEL----LALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 398 LSKENQTRAKES---DFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAK-QEIQHLRKELIEA 473
Cdd:pfam10174 348 DALRLRLEEKESflnKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKdKQLAGLKERVKSL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 474 QELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREekdsEITSTRDELLSARDEILLLHQ 553
Cdd:pfam10174 428 QTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKE----KVSALQPELTEKESSLIDLKE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 554 AAAKVAS---ERDTDIASLQEELKKVRAELERW----RKAASEYEKEITSLQNSFQLRCQQCEDQQ-REEATRLQGELEK 625
Cdd:pfam10174 504 HASSLASsglKKDSKLKSLEIAVEQKKEECSKLenqlKKAHNAEEAVRTNPEINDRIRLLEQEVARyKEESGKAQAEVER 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 626 LRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQsleltsdlsiLQMSRKELENQVGSLKEQHLRDSADLKTllS 705
Cdd:pfam10174 584 LLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN----------IKHGQQEMKKKGAQLLEEARRREDNLAD--N 651
|
570 580 590
....*....|....*....|....*....|..
gi 530373156 706 KAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 737
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
218-759 |
2.44e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 218 RLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECthlkemnER 297
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYL-EEKLKSSNLELENIKKQIADDEKSHSITLKEI-------ER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 298 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqQKGQAEKKELQHKIDEMEEKEQELqakiealqadNDFTNERLT 377
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-KTAESDLSMELEKNNYYKELEERH----------MKIINDPVY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 378 ALQEKLIVEGHLTKAVEETKLSKENqTRAKESDFSDTLSPSK--EKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQS 455
Cdd:PRK01156 292 KNRNYINDYFKYKNDIENKKQILSN-IDAEINKYHAIIKKLSvlQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 456 EIEA-KQEIQHLRKElieaQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIqvlQAQLQRLHIDTENLREEKDSei 534
Cdd:PRK01156 371 SIESlKKKIEEYSKN----IERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI---SSKVSSLNQRIRALRENLDE-- 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 535 tstrdelLSARDEILLLHQAAAKVASERDTDiaslqeelkKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE 614
Cdd:PRK01156 442 -------LSRNMEMLNGQSVCPVCGTTLGEE---------KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 615 EATRLQGELEKLRKEWNALETECHSLKRenvLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELenqvgsLKEQHL 694
Cdd:PRK01156 506 KEYLESEEINKSINEYNKIESARADLED---IKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSW------LNALAV 576
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530373156 695 RDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 759
Cdd:PRK01156 577 ISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEN 641
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
2.96e-05 |
|
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438742 [Multi-domain] Cd Length: 105 Bit Score: 43.82 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 530373156 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
2.98e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 43.29 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 530373156 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
3.08e-05 |
|
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438724 [Multi-domain] Cd Length: 108 Bit Score: 43.82 E-value: 3.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 530373156 49 KVLSRNHALVWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
168-759 |
3.78e-05 |
|
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: 47.41 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 168 FQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDslRKELIalqe 247
Cdd:pfam05483 215 FKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN--LKELI---- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 248 DKHNYETTAKESLRRVLQEKIEVVRKLsevERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLkvae 327
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKAL---EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSL---- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 328 gkqeeiQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKE--NQTR 405
Cdd:pfam05483 362 ------EELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKiaEELK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 406 AKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQgaQSEIEAKQEIQHLRKELIEAQELARTSKQKCF 485
Cdd:pfam05483 436 GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE--KEKLKNIELTAHCDKLLLENKELTQEASDMTL 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 486 ELqalleeerKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEkdseITSTRDELLSARDEILLLHQAAAKVASERDTD 565
Cdd:pfam05483 514 EL--------KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDE----LESVREEFIQKGDEVKCKLDKSEENARSIEYE 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 566 IASLQEELKKVRAELERWRKAASEYEKEITSLqnsfqlrcqqcedQQREEATRLQGELEKlrKEWNALETECHSLKREnv 645
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEEL-------------HQENKALKKKGSAEN--KQLNAYEIKVNKLELE-- 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 646 lLSSELQRQEKELHNSQKQ----SLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKT 721
Cdd:pfam05483 645 -LASAKQKFEEIIDNYQKEiedkKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER 723
|
570 580 590
....*....|....*....|....*....|....*...
gi 530373156 722 QTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 759
Cdd:pfam05483 724 DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
4.15e-05 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 43.57 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 530373156 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
514-729 |
4.37e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 514 AQLQRLHIDTENLREEKD--SEITSTRDELLSARDEILLLHQAAAKVASERD-TDIASLQEELKKVRAELERWRKAASEY 590
Cdd:COG4913 235 DDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 591 EKEITSLQNsfqlRCQQCEDQQREEATRlqgELEKLRKEWNALETECHSLKREnvllSSELQRQEKELHnsqkqsLELTS 670
Cdd:COG4913 315 EARLDALRE----ELDELEAQIRGNGGD---RLEQLEREIERLERELEERERR----RARLEALLAALG------LPLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530373156 671 DLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 729
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEEL----EALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
212-513 |
4.89e-05 |
|
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: 46.98 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 212 EDRLLSRLEVMGNQLQacsKNQTEDSLRKELIALQEDKHNYETTAK--------ESLRRVLQEKIEVVRKLSEVERSLSN 283
Cdd:TIGR02169 186 IERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekealeRQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 284 TEDECTH----LKEMNER----TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ---QKGQAEKKELQHKIDEME 352
Cdd:TIGR02169 263 LEKRLEEieqlLEELNKKikdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEerlAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 353 EKEQELQAKIEALQADNDFTNERLTALQEKLiveGHLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMD 432
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAEL---EEVDKEFAETR-DELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 433 EQDLNEPLAKVSLLKDDLQGAQSEIEAKQ-EIQHLRKELIEAQELARTSKQKCFELQA---LLEEERKAYRNQVEESTKQ 508
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEDKAlEIKKQEWKLEQLAADLSKYEQELYDLKEeydRVEKELSKLQRELAEAEAQ 498
|
....*
gi 530373156 509 IQVLQ 513
Cdd:TIGR02169 499 ARASE 503
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
4.99e-05 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 42.70 E-value: 4.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373156 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
324-741 |
5.79e-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: 46.66 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 324 KVAEGKQEEIQQKGQAEKKELQHK----------------IDEMEEKEQELQAKIEALQADNdftNERLTALQEKlIVEG 387
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKrarielekkasalkrqLDRESDRNQELQKRIRLLEKRE---AEAEEALREQ-AELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 388 HLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIeakQEIQHLR 467
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKA---SEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 468 KELIEAQELARTSKQKCFELqalleEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDe 547
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKEL-----EFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEE- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 548 illLHQAAAKVASERDT--DIASLQEELKKVRAELERWRKAASEYEKEITS--LQNSFQLRCQQCEDQQREEATRLQGEL 623
Cdd:pfam05557 230 ---VEDLKRKLEREEKYreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 624 EKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDL----SILQMSRKELENQVGSlkEQHLRDSAD 699
Cdd:pfam05557 307 RQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELTMSNYS--PQLLERIEE 384
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 530373156 700 LKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 741
Cdd:pfam05557 385 AEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.66e-05 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 42.22 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 530373156 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
506-718 |
9.73e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 506 TKQIQVLQAQLQRLhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVA--SERDTDIASLQEELKKVRAELERW 583
Cdd:COG4913 609 RAKLAALEAELAEL--------EEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 584 RKAASEYEkeitslqnsfqlrcqqcedqqreeatRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 663
Cdd:COG4913 681 DASSDDLA--------------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530373156 664 QSLELTSDLSILQmsRKELENQVGSLKEQHLRDS---------ADLKTLLSKAENQAKDVQKEY 718
Cdd:COG4913 735 RLEAAEDLARLEL--RALLEERFAAALGDAVERElrenleeriDALRARLNRAEEELERAMRAF 796
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
548-767 |
1.31e-04 |
|
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: 45.14 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 548 ILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQcEDQQREEATRLQGELEKLR 627
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 628 KEWNALETECHSLKRE-----------------NVLLSSE--------LQRQEKELHNSQKQSLELTSDLSILQMSRKEL 682
Cdd:COG4942 90 KEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 683 ENQVGSLKE---QHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 759
Cdd:COG4942 170 EAERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*...
gi 530373156 760 GNNKPWPW 767
Cdd:COG4942 250 ALKGKLPW 257
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
257-582 |
1.41e-04 |
|
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: 45.73 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 257 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQE-----------ELRELANKYNGAVNEIKDLSDKLKV 325
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkekleleEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 326 AEGKQEEIQQKGQ---AEKKELQHKIDEMEEKEQELQ-------AKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEE 395
Cdd:pfam02463 248 DEQEEIESSKQEIekeEEKLAQVLKENKEEEKEKKLQeeelkllAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 396 TKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQE 475
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 476 LARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEiTSTRDELLSARDEILLLHQAA 555
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL-ELKKSEDLLKETQLVKLQEQL 486
|
330 340
....*....|....*....|....*..
gi 530373156 556 AKVASERDTDIASLQEELKKVRAELER 582
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLL 513
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
255-576 |
1.72e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 255 TAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ 334
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 335 ---QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRAKESDF 411
Cdd:COG4372 115 eelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 412 SDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALL 491
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 492 EEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQE 571
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
....*
gi 530373156 572 ELKKV 576
Cdd:COG4372 355 VLELL 359
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
2.33e-04 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 41.16 E-value: 2.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530373156 52 SRNHALVWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
324-691 |
2.52e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.36 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 324 KVAEGKQEEIQQKGQAeKKELQHKIDEMEEKEQELQAKIEALQADNDFT-NERLTALQEKLIVE-GHLTKAVEETKLSKE 401
Cdd:pfam09731 78 ESKEPKEEKKQVKIPR-QSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEkEKALEEVLKEAISKaESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 402 NQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLkddlqGAQSEIEAKqeiqhlrKELIEAQELArtsk 481
Cdd:pfam09731 157 QAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINL-----AKQSEEEAA-------PPLLDAAPET---- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 482 qkcfeLQALLEEErkayrNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDEL----------LSARDEILLL 551
Cdd:pfam09731 221 -----PPKLPEHL-----DNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIipvlkednllSNDDLNSLIA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 552 H------QAAAKVASERDTDIASLQEELKKVRAELERWRkaaseyEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEK 625
Cdd:pfam09731 291 HahreidQLSKKLAELKKREEKHIERALEKQKEELDKLA------EELSARLEEVRAADEAQLRLEFEREREEIRESYEE 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 626 LRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLE----LTSDLSILQMSRKELENQVGSLKE 691
Cdd:pfam09731 365 KLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEeragRLLKLNELLANLKGLEKATSSHSE 434
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
247-543 |
2.61e-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: 44.57 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 247 EDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmnertqeELRELANKYNGAVNEIKDLSDKLKVA 326
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDN-------RSKEDIPNLQNITVRLQDLTEKLSEA 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 327 EGKQEEIQQkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRA 406
Cdd:TIGR00618 607 EDMLACEQH---ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQ 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 407 KESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAK--------QEIQHLRKELIEAQEL-- 476
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARedalnqslKELMHQARTVLKARTEah 763
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530373156 477 ARTSKQKCFELQAL-----LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLS 543
Cdd:TIGR00618 764 FNNNEEVTAALQTGaelshLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLS 835
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
3.08e-04 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 40.32 E-value: 3.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 530373156 53 RNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
155-383 |
4.94e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 155 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcSKNQT 234
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-ELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 235 EDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEdectHLKEMNERTQEELRELANKyngaVN 314
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEELRAD----LA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373156 315 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL 383
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
5.17e-04 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 43.21 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 530373156 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
5.82e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 40.50 E-value: 5.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373156 49 KVLSRNHALVWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
615-761 |
6.69e-04 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.38 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 615 EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmsrkELENQVGSLKeqhl 694
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530373156 695 rdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 761
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAYRNMKEMLTKKNE 265
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
6.77e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 39.21 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 530373156 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
368-667 |
7.95e-04 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 42.86 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 368 DNDFTNERLTALQEKL-IVEGHLtkavEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQ-------MDEQDLNEP 439
Cdd:COG5391 216 SDEFIEERRQSLQNFLrRVSTHP----LLSNYKNSKSWESHSTLLSSFIENRKSVPTPLSLDLTsttqeldMERKELNES 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 440 LAKV--SLLKDD---------LQGAQSEIEAKQEIQH--LRKELIEAQELARTSKQKCFELQALLE----------EERK 496
Cdd:COG5391 292 TSKAihNILSIFslfekiliqLESEEESLTRLLESLNnlLLLVLNFSGVFAKRLEQNQNSILNEGVvqaetlrsslKELL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 497 AYRNQVEESTKQIQVLQAQLQRLHIDTENLREE----------KDSEITSTRDELLSARDEILLLHqaAAKVASERDTDI 566
Cdd:COG5391 372 TQLQDEIKSRESLILTDSNLEKLTDQNLEDVEElsrslrknssQRAVVSQQPEGLTSFSKLSYKLR--DFVQEKSRSKSI 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 567 ASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQcedqqreeatrlqgELEKLRKEWNaletECHslkrenvl 646
Cdd:COG5391 450 ESLQQDKEKLEEQLAIAEKDAQEINEELKNELKFFFSVRNS--------------DLEKILKSVA----DSH-------- 503
|
330 340
....*....|....*....|.
gi 530373156 647 lsSELQRQEKELHNSQKQSLE 667
Cdd:COG5391 504 --IEWAEENLEIWKSVKEQLD 522
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
488-728 |
9.00e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 488 QALLEEERKAYRNQVEESTKQIQVLQAQLQrlhiDTENLREEkdseITSTRDELLSARDEILLLHQAAAKVASER--DTD 565
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKE----ETEQLKQQ----LAQAPAKLRQAQAELEALKDDNDEETRETlsTLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 566 IASLQEELKKVRAELERWRKAASEYEKEITSLQNsfqlrcqQCEDQQREEATRLQgELEKLRKEWNALETECHSLKREN- 644
Cdd:PRK11281 123 LRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQT-------QPERAQAALYANSQ-RLQQIRNLLKGGKVGGKALRPSQr 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 645 VLLSSELQRQekELHNS-QKQSLELTSDLSILQMSRKELENQVGSLKEQHLrdsADLKTL-----LSKAENQAKDVQKEY 718
Cdd:PRK11281 195 VLLQAEQALL--NAQNDlQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQL---QLLQEAinskrLTLSEKTVQEAQSQD 269
|
250
....*....|
gi 530373156 719 EKTQTVLSEL 728
Cdd:PRK11281 270 EAARIQANPL 279
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
314-690 |
1.15e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 314 NEIKDLSDKLKvaEGKQEEiqqkgqAEKKELQHKIdemeEKEQELQAKIEALQADNDFTNERLTALQEKLiveghlTKAV 393
Cdd:PRK11281 39 ADVQAQLDALN--KQKLLE------AEDKLVQQDL----EQTLALLDKIDRQKEETEQLKQQLAQAPAKL------RQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 394 EE-TKLSKENQTRAKEsDFSDTLSPSKEKSSDDTTDAQMDEQ-DLNEPLAKVSLLKDDLQGAQSEI-EAKQEIQHLRKEL 470
Cdd:PRK11281 101 AElEALKDDNDEETRE-TLSTLSLRQLESRLAQTLDQLQNAQnDLAEYNSQLVSLQTQPERAQAALyANSQRLQQIRNLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 471 IEAQElartskqkcfelqalleeerkayrNQVEESTKQIQVLQAQLQRLhiDTENLREEKDSEITSTRDELLSARDEILL 550
Cdd:PRK11281 180 KGGKV------------------------GGKALRPSQRVLLQAEQALL--NAQNDLQRKSLEGNTQLQDLLQKQRDYLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 551 LHqaaakvaserdtdIASLQEELKKVRAELERWRKAASEYEKEitslqnsfqlrcqqcEDQQREEATRLQGeleklrkew 630
Cdd:PRK11281 234 AR-------------IQRLEHQLQLLQEAINSKRLTLSEKTVQ---------------EAQSQDEAARIQA--------- 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373156 631 NALetechsLKRE---NVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLK 690
Cdd:PRK11281 277 NPL------VAQEleiNLQLSQRLLKATEKLNTLTQQNLRVKNWLDRLTQSERNIKEQISVLK 333
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
461-681 |
1.17e-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: 42.19 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 461 QEIQHLRKELIEAQELARTSKQKCFELQallEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDE 540
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERY---KRDREQWERQRRELESRVAELKEELRQSREKHEEL-EEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 541 LLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWR---KAASEYEKEITSLQNSFQLRCQQCEDQQREEAT 617
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKeraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 618 RLQG----------------------------------ELEKLRKEWNALETECHSLKRENVLLSSELQ-------RQEK 656
Cdd:pfam07888 193 EFQElrnslaqrdtqvlqlqdtittltqklttahrkeaENEALLEELRSLQERLNASERKVEGLGEELSsmaaqrdRTQA 272
|
250 260
....*....|....*....|....*
gi 530373156 657 ELHNSQKQSLELTSDLSILQMSRKE 681
Cdd:pfam07888 273 ELHQARLQAAQLTLQLADASLALRE 297
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
555-780 |
1.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 555 AAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWN--- 631
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-ALQAEIDKLQAEIAEAEAEIEERREELGera 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 632 -ALETECHSLKRENVLLSSE-----LQRQE--KELHNSQKQSLELTSDLsilqmsRKELENQVGSLKEQhlrdSADLKTL 703
Cdd:COG3883 93 rALYRSGGSVSYLDVLLGSEsfsdfLDRLSalSKIADADADLLEELKAD------KAELEAKKAELEAK----LAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530373156 704 LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNKPWPWMPMLAALVAVTAI 780
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
276-383 |
1.60e-03 |
|
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: 41.76 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 276 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 342
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 530373156 343 ELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL 383
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.82e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 38.22 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
265-593 |
1.95e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 265 QEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgqaeKKEL 344
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEK----VKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 345 QHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEkliveghLTKAVEetKLSKENQTRakesdfsdTLSPSKEKssd 424
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDK-------LRKEIE--RLEWRQQTE--------VLSPEEEK--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 425 dttdaqmdeqdlnEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTskqkcfelqalleeerkaYRNQVEE 504
Cdd:COG1340 137 -------------ELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEE------------------IHKKIKE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 505 STKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDEILLLHQAAAKvaserdtDIASLQEELKKVRAELERWR 584
Cdd:COG1340 186 LAEEAQELHEEMIELYKEADELRKEAD-ELHKEIVEAQEKADELHEEIIELQK-------ELRELRKELKKLRKKQRALK 257
|
....*....
gi 530373156 585 KAASEYEKE 593
Cdd:COG1340 258 REKEKEELE 266
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
304-664 |
1.98e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 304 ELANKYNG-AVNEIKDLSDKLKVAEGKQ--EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIE------ALQADNDfTNE 374
Cdd:pfam17380 255 EYTVRYNGqTMTENEFLNQLLHIVQHQKavSERQQQEKFEKMEQERLRQEKEEKAREVERRRKleeaekARQAEMD-RQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 375 RLTALQEKLIVEghltKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSdDTTDAQMDEQDLNEPL-------AKVSLLK 447
Cdd:pfam17380 334 AIYAEQERMAME----RERELERIRQEERKRELERIRQEEIAMEISRMR-ELERLQMERQQKNERVrqeleaaRKVKILE 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 448 DDLQgaQSEIEAKQEIQHLRKELIEAQELartskqkcfELQALLEE-ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENL 526
Cdd:pfam17380 409 EERQ--RKIQQQKVEMEQIRAEQEEARQR---------EVRRLEEErAREMERVRLEEQERQQQVERLRQQEEERKRKKL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 527 REEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQ-EELKKVRAELERWRKAASEYEKEitslqnsfqlrc 605
Cdd:pfam17380 478 ELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEmEERQKAIYEEERRREAEEERRKQ------------ 545
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 530373156 606 qqcedQQREEATRLQGELEKLRKEWNALEtechSLKRENvllssELQRQEKELHNSQKQ 664
Cdd:pfam17380 546 -----QEMEERRRIQEQMRKATEERSRLE----AMERER-----EMMRQIVESEKARAE 590
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
610-732 |
2.33e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 610 DQQREEATR----LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQekelhNSQKQSLELTSDLSILQMSRKELENQ 685
Cdd:COG3206 167 ELRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAK-----LLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 530373156 686 VGSLKEQHLRDSADLKTLLSKAENQakDVQKEYEKTQTVLSELKLKF 732
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSARY 286
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
417-600 |
2.52e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 417 PSKEKSSDDTTDAQMDEQDLNeplAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEE- 494
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQ---AELDALQAELEELNEEYnELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 495 RKAYRNQVEEST--------------------KQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQA 554
Cdd:COG3883 93 RALYRSGGSVSYldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530373156 555 AAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNS 600
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
165-364 |
2.60e-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: 40.90 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALID--------EDRLLSRLEVMGNQLQACSKNQTED 236
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 237 SLrkELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLKEMNERTQEELRELANkyngAV 313
Cdd:COG4942 121 PL--ALLLSPEDFLDAVRRLQylKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALEA----LK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530373156 314 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEA 364
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
491-650 |
3.01e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 491 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseitstrdELlsaRDEILllhqaaakvasERDTDIASLQ 570
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE--------EL---EAELE-----------EKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 571 EELKKVRAElerwRKAASEYEKEITSLQNsfqlrcqqcedqqreEATRLQGELEKLRKEWNALETECHSLKRENVLLSSE 650
Cdd:COG2433 448 RELSEARSE----ERREIRKDREISRLDR---------------EIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
571-762 |
3.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 571 EELKKVRAELERWRKAASEYEKEITSLQnsfQLRcqqcedQQREEATRLQGELEKLRKEWNALETECHSLKREnvLLSSE 650
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLE---PIR------ELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 651 LQRQEKELHNSQKQSLELTSDLSILQMSRKELENQvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 730
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190
....*....|....*....|....*....|..
gi 530373156 731 KFEMTEQEKQSITDELKQCKNNLKLLREKGNN 762
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
312-587 |
4.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 312 AVNEIKDLSDKLKVAEGKQEEIQQKGQAEkkELQHKIDEMEEKEQELQAKIEALQAdndFTNERLTALQEKLIVEghLTK 391
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQIELLEPIR--ELAERYAAARERLAELEYLRAALRL---WFAQRRLELLEAELEE--LRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 392 AVEETKLSKENQTRAKEsdfsdtlspskekssddttDAQMDEQDLNEPLAKvsllkddlQGAQSEIEAKQEIQHLRKELI 471
Cdd:COG4913 303 ELARLEAELERLEARLD-------------------ALREELDELEAQIRG--------NGGDRLEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 472 EAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLH----------IDTENLREEKDSEITSTR--- 538
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaeaeaalRDLRRELRELEAEIASLErrk 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 530373156 539 ----DELLSARDEIlllhqAAAKVASERDTDIASlqeELKKVRAELERWRKAA 587
Cdd:COG4913 436 snipARLLALRDAL-----AEALGLDEAELPFVG---ELIEVRPEEERWRGAI 480
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
258-367 |
4.22e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 258 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNE--------IKDLSD--KLKVA 326
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEakkeadeiIKELRQlqKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 530373156 327 EGKQEEIQQKgqaeKKELQHKIDEMEEKEQELQAKIEALQA 367
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
215-659 |
4.70e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 215 LLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKEslrrvlqeKIEVVRKLSEVERSlsntedecthlKEM 294
Cdd:TIGR01612 1455 LFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGC--------KDEADKNAKAIEKN-----------KEL 1515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 295 NERTQEELRELANKY----------------NGAVNEIKDLSDKLKVAEGKQEeiqQKGQAEKKElqhkidemeekeqel 358
Cdd:TIGR01612 1516 FEQYKKDVTELLNKYsalaiknkfaktkkdsEIIIKEIKDAHKKFILEAEKSE---QKIKEIKKE--------------- 1577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 359 QAKIEALQADNDFTNerltalqeKLIVEGHLTKAVEETKLSKENQTRAKESD-FSDTLSPSKEKS--SDDTTDAQMDEQD 435
Cdd:TIGR01612 1578 KFRIEDDAAKNDKSN--------KAAIDIQLSLENFENKFLKISDIKKKINDcLKETESIEKKISsfSIDSQDTELKENG 1649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 436 LNepLAKVSLLKDDLQGAQSEIE-AKQEIQHLRKElIEAQELARTSKQKCFELQAL--LEEERKAYRNQVeESTKQIqvL 512
Cdd:TIGR01612 1650 DN--LNSLQEFLESLKDQKKNIEdKKKELDELDSE-IEKIEIDVDQHKKNYEIGIIekIKEIAIANKEEI-ESIKEL--I 1723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 513 QAQLQRL----------HIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASE----RDTDIASLQEELKKVRA 578
Cdd:TIGR01612 1724 EPTIENLissfntndleGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITydeiKNTRINAQNEFLKIIEI 1803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 579 ELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHslkrENVLLssELQRQEKEL 658
Cdd:TIGR01612 1804 EKKSKSYLDDIEAKEFDRIINHFKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNSTD----ENLLF--DILNKTKDA 1877
|
.
gi 530373156 659 H 659
Cdd:TIGR01612 1878 Y 1878
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
258-763 |
5.03e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 258 ESLRRVLQEKIEVVRK--LSEVERSLSNTEDECTHLKEMN--ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 333
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 334 QQKGQAEKKELQHKID----------------EMEEKEQELQAKIEALQADNDFTNERLTALQEkliVEGHLTkAVEETK 397
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINdledvadkaisnddpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAE---IEKDKT-SLEEVK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 398 LSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEpLAKVSLLKDDLQGAQSEIEAKQEIQHLRKEliEAQELA 477
Cdd:TIGR01612 1214 GINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHD--DDKDHH 1290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 478 RTSKQKCFELQALLEEERKAYRNQVEEStkQIQVLQAQLQRLHIDTEnlreEKDSEITSTRDELLSARDeILLLHQAAaK 557
Cdd:TIGR01612 1291 IISKKHDENISDIREKSLKIIEDFSEES--DINDIKKELQKNLLDAQ----KHNSDINLYLNEIANIYN-ILKLNKIK-K 1362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 558 VASERDTDIASLQEELKKVRAELerwrkaaSEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETEC 637
Cdd:TIGR01612 1363 IIDEVKEYTKEIEENNKNIKDEL-------DKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 638 HSLK---------RENVLL--SSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENqvgslKEQHLRDSADLKtllSK 706
Cdd:TIGR01612 1436 SNIDtyfknadenNENVLLlfKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHID-----KSKGCKDEADKN---AK 1507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373156 707 AENQAKDVQKEYEKTQTVL------SELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNK 763
Cdd:TIGR01612 1508 AIEKNKELFEQYKKDVTELlnkysaLAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQK 1570
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
165-395 |
5.19e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 238
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 239 RKELIALQEDKHnYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEIKD 318
Cdd:COG0497 247 GQALRALERLAE-YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEELLA 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530373156 319 LSDKLkvaegkqeeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQAdndfTNERLTALQEKLIVEghLTKAVEE 395
Cdd:COG0497 325 YAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE----AAEKLSAARKKAAKK--LEKAVTA 381
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
458-696 |
5.62e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 458 EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITST 537
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 538 RDellsardeillLHQAAAKVASErdtdIASLQEELKKVR--AELERWRKAASEYEKEITSLQNS---FQLRCQQCEDQQ 612
Cdd:PHA02562 258 NK-----------LNTAAAKIKSK----IEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKlkeLQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 613 REEATRLQgELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL-KE 691
Cdd:PHA02562 323 DELEEIMD-EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELvKE 401
|
....*
gi 530373156 692 QHLRD 696
Cdd:PHA02562 402 KYHRG 406
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
468-763 |
5.72e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 468 KELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDE 547
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 548 ILLLHQAAAKVaserDTDIASLQEELKKVRAELERWRkaasEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKLR 627
Cdd:PRK03918 247 LESLEGSKRKL----EEKIRELEERIEELKKEIEELE----EKVKELKELK------------EKAEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 628 KEWNALETECHSLKREnvllSSELQRQEKELHNSQKQSLELTSDLsilqmsrKELENQVGSLKEQHlRDSADLKTLLSKA 707
Cdd:PRK03918 307 DELREIEKRLSRLEEE----INGIEERIKELEEKEERLEELKKKL-------KELEKRLEELEERH-ELYEEAKAKKEEL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 530373156 708 ENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNK 763
Cdd:PRK03918 375 ERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
302-430 |
5.74e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 302 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQE 381
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 530373156 382 KLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQ 430
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
165-672 |
5.87e-03 |
|
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: 40.34 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 165 QELFQLSQYLQEALHREQMLEQKLATLQRL----LAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLR- 239
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDILQREqatiDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEk 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 240 ----------KELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMnERTQEELRELANKY 309
Cdd:TIGR00618 459 ihlqesaqslKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP-GPLTRRMQRGEQTY 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 310 NGAVNEIKDLSDKLkVAEGKQeeiQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHL 389
Cdd:TIGR00618 538 AQLETSEEDVYHQL-TSERKQ---RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 390 TKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKddLQGAQSEIEAKQEIQHLRKE 469
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLP--KELLASRQLALQKMQSEKEQ 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 470 LIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEkdseitstRDELLSARDEIL 549
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ--------ARTVLKARTEAH 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 550 LLHQAAAKVASERDTdiaslqeELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKE 629
Cdd:TIGR00618 764 FNNNEEVTAALQTGA-------ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSR 836
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 530373156 630 WNALETECHSLKRENVLLSSELQRQEkELHNSQKQSLELTSDL 672
Cdd:TIGR00618 837 LEEKSATLGEITHQLLKYEECSKQLA-QLTQEQAKIIQLSDKL 878
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
6.04e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 36.70 E-value: 6.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530373156 52 SRNHALVWFDHKTGKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
265-602 |
6.97e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.89 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 265 QEKIEVVRKLSEVERS----LSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAE 340
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSsnskLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 341 KKELQHK-----IDEMEEKEQEL-QAKIEALQADNDFTNERlTALQEKL-IVEGHLTKAVEETKLSKENQTRAkesdfsD 413
Cdd:PLN02939 125 LSDFQLEdlvgmIQNAEKNILLLnQARLQALEDLEKILTEK-EALQGKInILEMRLSETDARIKLAAQEKIHV------E 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 414 TLSPSKEKSSDDTTDAQMDEQDLNEPLAK-VSLLKDDlqgaqsEIEAKQEIQHLRKELIEAQE----LARTSKQKCFELQ 488
Cdd:PLN02939 198 ILEEQLEKLRNELLIRGATEGLCVHSLSKeLDVLKEE------NMLLKDDIQFLKAELIEVAEteerVFKLEKERSLLDA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 489 ALLEEERKAYRNQ---VEESTKQIQVLQAQLQRLH--IDTENLREEKDSEITSTRDELlsaRDEILLLHQ--AAAKVASE 561
Cdd:PLN02939 272 SLRELESKFIVAQedvSKLSPLQYDCWWEKVENLQdlLDRATNQVEKAALVLDQNQDL---RDKVDKLEAslKEANVSKF 348
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 530373156 562 RDTDIASLQEELKKVRaelERWRKAASEYEKEITSLQNSFQ 602
Cdd:PLN02939 349 SSYKVELLQQKLKLLE---ERLQASDHEIHSYIQLYQESIK 386
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
210-383 |
7.26e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.82 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 210 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHNYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 285
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 286 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKG----------QAEKKELQHKIDEME 352
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIaeqeiayselQEELEEILKQLEEIE 396
|
170 180 190
....*....|....*....|....*....|.
gi 530373156 353 EKEQELQAKIEALQADNDFTNERLTALQEKL 383
Cdd:PRK04778 397 KEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
331-636 |
8.39e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 331 EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQadndftnERLTALQE-----KLIVEGHLTKAVEETKlskenqtr 405
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAK-------EGLSALNRllprlNLLADETLADRVEEIR-------- 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 406 akesdfsdtlspskekssDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEieaKQEIQHLRKELIEAQELARTSKQKCF 485
Cdd:PRK04863 901 ------------------EQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSD---PEQFEQLKQDYQQAQQTQRDAKQQAF 959
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 486 ELQALLE-EERKAYRNQVEESTKQiQVLQAQLQRLHIDTENLREEkdseitsTRDELLSARDEILLLHQAAAKVASERDT 564
Cdd:PRK04863 960 ALTEVVQrRAHFSYEDAAEMLAKN-SDLNEKLRQRLEQAEQERTR-------AREQLRQAQAQLAQYNQVLASLKSSYDA 1031
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 565 ---DIASLQEELKK--VRAELERWRKAASEYEKEITSLQNSfQLRCQQCEDQ---QREEATRLQGELEKLRKEWNALETE 636
Cdd:PRK04863 1032 krqMLQELKQELQDlgVPADSGAEERARARRDELHARLSAN-RSRRNQLEKQltfCEAEMDNLTKKLRKLERDYHEMREQ 1110
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
460-679 |
8.53e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 460 KQEIQHLRKELIEAQELARTSKQKcfELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreekdseitstRD 539
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQK--NGLVDLSEEAKLLLQQLSELESQLAEARAELAEA------------------EA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 540 ELLSARDEILLLHQAAAKVASerDTDIASLQEELKKVRAELERWRKAASE-------YEKEITSLQNSFQLRCQQCEDQQ 612
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQLQQEAQRILASL 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530373156 613 REEATRLQGELEKLRKEWNALETECHSLKRenvlLSSELQRQEKELHNSQKQSLELTSDLSILQMSR 679
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
553-745 |
8.68e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 553 QAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcedQQREEATRLQGELEKLRKEWNa 632
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL------PLYQELEALEAELAELPERLE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 633 letechslkrenvllssELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDsadLKTLLSKAENQAK 712
Cdd:COG4717 150 -----------------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLA 209
|
170 180 190
....*....|....*....|....*....|...
gi 530373156 713 DVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 745
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
165-344 |
9.11e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 243
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 244 ALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIKDL 319
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|....*
gi 530373156 320 SDKLKVAEGKQEEIQQKGQAEKKEL 344
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEEL 789
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
232-758 |
9.41e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 39.65 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 232 NQTEDSLRKELIALQEDKHNYETTAKESLRRVlqEKIevvrklseVERSLSNTEDECTHLKEMNERTQ-EELRELANKYN 310
Cdd:TIGR01612 1124 DQKIDHHIKALEEIKKKSENYIDEIKAQINDL--EDV--------ADKAISNDDPEEIEKKIENIVTKiDKKKNIYDEIK 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 311 GAVNEIKDLS-DKLKVAEGKQEEIQQkGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHL 389
Cdd:TIGR01612 1194 KLLNEIAEIEkDKTSLEEVKGINLSY-GKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 390 TKAVEETKLS----KENQTRAKESDfsDTLSPSKEKS--------------------SDDTTDAQMDEQDLNEPLAKVS- 444
Cdd:TIGR01612 1273 KAEMETFNIShdddKDHHIISKKHD--ENISDIREKSlkiiedfseesdindikkelQKNLLDAQKHNSDINLYLNEIAn 1350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 445 ---LLK--------DDLQGAQSEIEAKQeiQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQ 513
Cdd:TIGR01612 1351 iynILKlnkikkiiDEVKEYTKEIEENN--KNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELK 1428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 514 AQL--QRLHIDT--ENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEEL---KKVRAELERWRKA 586
Cdd:TIGR01612 1429 NHIlsEESNIDTyfKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIdksKGCKDEADKNAKA 1508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 587 AS-------EYEKEITSLQNSF-QLRCQQCEDQQREEATRLQGELEKLRK----EWNALETECHSLKRENVLLSSELQRQ 654
Cdd:TIGR01612 1509 IEknkelfeQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEKSEQKIKEIKKEKFRIEDDAAKN 1588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 655 EKE----------LHNSQKQSLELTSDLSILQMSRKE---LENQVGSL----KEQHLRDSAD----LKTLLSKAENQAKD 713
Cdd:TIGR01612 1589 DKSnkaaidiqlsLENFENKFLKISDIKKKINDCLKEtesIEKKISSFsidsQDTELKENGDnlnsLQEFLESLKDQKKN 1668
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 530373156 714 VQKEYEKTQTVLSELK-LKFEMTEQEK-------QSITDELKQCKNNLKLLRE 758
Cdd:TIGR01612 1669 IEDKKKELDELDSEIEkIEIDVDQHKKnyeigiiEKIKEIAIANKEEIESIKE 1721
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
174-363 |
9.42e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 37.96 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 174 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHNYE 253
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373156 254 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 323
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530373156 324 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIE 363
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| |
