|
Name |
Accession |
Description |
Interval |
E-value |
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
71-279 |
5.45e-82 |
|
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.
Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 260.70 E-value: 5.45e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 71 VRKGIPHHFRAIVWQLLCDAQTMP---VKDQYSELLKMTSPCEKL----IRRDIARTYPEHNFFKEKDSLGQEVLFNVMK 143
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDtsaDKDLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 144 AYSLVDREVGYCQGSAFIVGLLLLQMP-EEEAFCVFFKLMQDYRLReLFKPSMAELGLCMYQFECMIQEYLPELFVHFQS 222
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564382509 223 QSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELM 279
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
111-279 |
4.45e-54 |
|
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.
Pssm-ID: 459855 Cd Length: 178 Bit Score: 184.38 E-value: 4.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 111 KLIRRDIARTYPEHNFFKEKDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLLQ-MPEEEAFCVFFKLMQDYRLRE 189
Cdd:pfam00566 10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 190 LFKPSMAELGLCMYQFECMIQEYLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIV-FRVGL 268
Cdd:pfam00566 88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
|
170
....*....|.
gi 564382509 269 ALLQMNQAELM 279
Cdd:pfam00566 168 AILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
42-325 |
8.98e-44 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 165.36 E-value: 8.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 42 EEDSWILWGRIVN-EWDDVRKKKEKQVKELVRKGIPHHFRAIVWQLLcdAQTMPVKDQ----YSELLKM-------TSPC 109
Cdd:COG5210 179 ELAADKLWISYLDpNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFL--LGIGFDLDKnpglYERLLNLhreakipTQEI 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 110 EKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLLQMPEEE-AFCVFFKLMQDYRLR 188
Cdd:COG5210 257 ISQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLP 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 189 ELFKPSMAELGLCMYQFECMIQEYLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGL 268
Cdd:COG5210 337 GYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLAL 416
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 564382509 269 ALLQMNQAELMQLDMEGMLQhfqkVIPHQFDGGPEKLIQSayqvkYNSKKMKKLEKE 325
Cdd:COG5210 417 AILKLLRDKLLKLDSDELLD----LLLKQLFLHSGKEAWS-----SILKFRHGTDRD 464
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
317-643 |
5.37e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 317 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQT 396
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 397 DAARAKLEQAESTIRELQHHRHwhkcsstynedfvlQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFpdENNIA 476
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELA--------------EAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--AAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 477 RLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwqrhvartsgrwKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQ 556
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEE-------------EEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 557 RMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVmAVRLREADSIAAVAELQ 636
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV-EAAYEAALEAALAAALQ 549
|
....*..
gi 564382509 637 QHIAELE 643
Cdd:COG1196 550 NIVVEDD 556
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-673 |
1.52e-11 |
|
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: 68.16 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 350 LKQRIETLEKEsASLADRLiqgqvtRAQEAEENYLikrELATIKQQTDAARAKLEQAESTIRELQHHRHwhkcsstyned 429
Cdd:TIGR02168 198 LERQLKSLERQ-AEKAERY------KELKAELREL---ELALLVLRLEELREELEELQEELKEAEEELE----------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 430 fVLQLEKELVQARLSEAESqcALKEMQDKVLDIEKKNNSFpdENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEH 509
Cdd:TIGR02168 257 -ELTAELQELEEKLEELRL--EVSELEEEIEELQKELYAL--ANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 510 WQRHVARTSgRWKDppkrnAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQ------------NQINS--NQLRRA 575
Cdd:TIGR02168 332 LDELAEELA-ELEE-----KLEELKEELESLEAELEELEAELEELESRLEELEEQletlrskvaqleLQIASlnNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 576 EQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMA-VRLREADSIAAVAELQQHIAELE--IQKEEGKLQ 652
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEeLQEELERLEEALEELREELEEAEqaLDAAERELA 485
|
330 340
....*....|....*....|.
gi 564382509 653 GQLNRSDSKQYIRELKDQIAE 673
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
339-674 |
2.12e-11 |
|
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: 67.77 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 339 EIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQTDAARAKLEQAESTIRELQHHRh 418
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 419 whkcsstynedfvLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKnnsfpdennIARLQEELIAVKLREAEAIMGLKE 498
Cdd:TIGR02168 757 -------------TELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---------IEQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 499 LRQQVRDLEEHWQRHVARTSgrwkdpPKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQE 578
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIA------ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 579 VTSLQEKVCSLSLKNKGLLAQLSEAkrRQAEIECKNKEEVMAVRLREADsiAAVAELQQHIAELEIQKEEGKLQGQLNRS 658
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSEL--RRELEELREKLAQLELRLEGLE--VRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
330 340
....*....|....*....|
gi 564382509 659 DSKQYIRE----LKDQIAEL 674
Cdd:TIGR02168 965 DDEEEARRrlkrLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
341-682 |
3.37e-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: 63.93 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 341 KRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEA-----EENYLIKRELATIKQQTDAARAKLEQAESTIREL 413
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELrrIENRLDELSQElsdasRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 414 QHHRhwhkcssTYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLD--IEKKNNSFPDENNIARLQEEliavKLREAE 491
Cdd:TIGR02169 750 EQEI-------ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsrIPEIQAELSKLEEEVSRIEA----RLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 492 AIMGLKEL-RQQVRDLEEHWQRHVARTSGRWKDppKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSN 570
Cdd:TIGR02169 819 QKLNRLTLeKEYLEKEIQELQEQRIDLKEQIKS--IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 571 QLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKE--EVMAVRLREADSIAAVAELQQHIAELE----- 643
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeEIPEEELSLEDVQAELQRVEEEIRALEpvnml 976
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 564382509 644 -IQKEEGKLQGQLNRSDSKQYIRELKDQIAELTHELRCLK 682
Cdd:TIGR02169 977 aIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
320-635 |
3.26e-09 |
|
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: 60.84 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 320 KKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEAEENYLIKRE-----LATI 392
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrLEQQKQILRERLANLERQLEeleaqLEEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 393 KQQTDAARAKLEQAEstirelqhhrhwhkcsstyNEDFVLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKKNNSFPDE 472
Cdd:TIGR02168 329 ESKLDELAEELAELE-------------------EKLEELKEELESLEAELEELEAE--LEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 473 NNIARLQEELIAVKLREAEAimglkelrqQVRDLEEHWQRHVARTSGRWKDpPKRNAVSELQGELMSIRLREAETQAEMR 552
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEA---------RLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 553 EMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLslknkgllaqlsEAKRRQAEIECKNKEEVMAVRLREADSIAAV 632
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSL------------ERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
...
gi 564382509 633 AEL 635
Cdd:TIGR02168 526 SEL 528
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
341-679 |
2.08e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 341 KRLR-TENRL---------LKQRIETLEKEsaslADRLIQGQVTRAQEAE-ENYLIKRELATIKQQTDAARAKLEQAEST 409
Cdd:COG1196 179 RKLEaTEENLerledilgeLERQLEPLERQ----AEKAERYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 410 IRELQHHRHwhkcsstynedfvlQLEKELVQARLSEAESQCALKEMQDKVLDIEKKnnsfpdennIARLQEELIAVKLRE 489
Cdd:COG1196 255 LEELEAELA--------------ELEAELEELRLELEELELELEEAQAEEYELLAE---------LARLEQDIARLEERR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 490 AEAIMGLKELRQQVRDLEEHWQRHVARTSgrwkdppkrnavsELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINS 569
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELE-------------ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 570 NQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIEcknkeevmavrlreadsIAAVAELQQHIAELEIQKEEG 649
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE-----------------EELEELEEALAELEEEEEEEE 441
|
330 340 350
....*....|....*....|....*....|..
gi 564382509 650 KLQGQLNRSDSKQY--IRELKDQIAELTHELR 679
Cdd:COG1196 442 EALEEAAEEEAELEeeEEALLELLAELLEEAA 473
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
359-611 |
3.86e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 359 KESASLADRLIQGQVTRAQEAEENYLIKReLATIKQQTDAARAKLEQAEstiRELQHHRHWHKCSSTYNE-DFVLQ---- 433
Cdd:COG3206 148 ELAAAVANALAEAYLEQNLELRREEARKA-LEFLEEQLPELRKELEEAE---AALEEFRQKNGLVDLSEEaKLLLQqlse 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 434 LEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGL-------KELRQQVRDL 506
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 507 EEHWQRHVARtsgrwkdppkrnAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQinsnQLRRAEQEVTSLQEkv 586
Cdd:COG3206 304 RAQLQQEAQR------------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEA----ELRRLEREVEVARE-- 365
|
250 260
....*....|....*....|....*
gi 564382509 587 cslslknkgLLAQLSeAKRRQAEIE 611
Cdd:COG3206 366 ---------LYESLL-QRLEEARLA 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
317-560 |
2.08e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 317 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQT 396
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 397 DAARAKLEQAESTIRELqhHRHWHKCsstynEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENNia 476
Cdd:TIGR02168 354 ESLEAELEELEAELEEL--ESRLEEL-----EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE-- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 477 rlQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSgrwkdpPKRNAVSELQGELMSIRLREAETQAEMrEMKQ 556
Cdd:TIGR02168 425 --ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE------ELREELEEAEQALDAAERELAQLQARL-DSLE 495
|
....
gi 564382509 557 RMME 560
Cdd:TIGR02168 496 RLQE 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
472-686 |
3.10e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 472 ENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwQRHVARTSGRWKDPPKRNAVSELQGELMSIRLRE---AETQ 548
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEE--ELEQLRKELEELSRQISALRKDLARLEAEVEQLEeriAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 549 AEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIecknKEEVMAVRLREADS 628
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL----NEEAANLRERLESL 829
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564382509 629 IAAVAELQQHIAELEIQKEEGKLQGQ---LNRSDSKQYIRELKDQIAELTHELRCLKGQRD 686
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELEALLNERASLEEALA 890
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
303-674 |
4.80e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 303 EKLIQSAYQVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEEN 382
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 383 YLIKRELATIKQQTD---AARAKLEQAESTIRELQHHRHWHKCSSTYNEdfVLQLEKELVQARLSEAESQCALKEMQD-- 457
Cdd:COG1196 480 AELLEELAEAAARLLlllEAEADYEGFLEGVKAALLLAGLRGLAGAVAV--LIGVEAAYEAALEAALAAALQNIVVEDde 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 458 ---KVLDIEKKNN----SFPDENNIARLqeELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKDPPKRNAV 530
Cdd:COG1196 558 vaaAAIEYLKAAKagraTFLPLDKIRAR--AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 531 SELQGELmsiRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEI 610
Cdd:COG1196 636 LRRAVTL---AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564382509 611 E---CKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKQYIRELKDQIAEL 674
Cdd:COG1196 713 EeerLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
311-674 |
5.09e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 311 QVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELA 390
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 391 TIKQQTDAARAKLEQAESTIRELQHHRHWHKCSSTYNEdfvlqLEKELVQARLSEAESQCA-----LKEMQDKVLDIEKK 465
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLEAGKCPECGQP-----VEGSPHVETIEEDRERVEeleaeLEDLEEEVEEVEER 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 466 NNSFPD----ENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGrwkdppKRNAVSELQGELMSIR 541
Cdd:PRK02224 498 LERAEDlveaEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEE------KREAAAEAEEEAEEAR 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 542 LREAETQAEMREMKQRmmeMETQNQINSNQLRRAE--QEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECK-NKEEV 618
Cdd:PRK02224 572 EEVAELNSKLAELKER---IESLERIRTLLAAIADaeDEIERLREKREALAELNDERRERLAEKRERKRELEAEfDEARI 648
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564382509 619 MAVRLREADSIAAVAELQQHIAEL-----EIQKEEGKLQGQLNRsdskqyIRELKDQIAEL 674
Cdd:PRK02224 649 EEAREDKERAEEYLEQVEEKLDELreerdDLQAEIGAVENELEE------LEELRERREAL 703
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
474-685 |
9.32e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 474 NIARLQEELIavKLREAEAIMglKELRQQVRDLE---EHWQRHVArtsgrwkdppKRNAVSELQGELMSIRLREAET--- 547
Cdd:COG4913 226 AADALVEHFD--DLERAHEAL--EDAREQIELLEpirELAERYAA----------ARERLAELEYLRAALRLWFAQRrle 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 548 --QAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEiECKNKEEVMAVRLRE 625
Cdd:COG4913 292 llEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564382509 626 A-----DSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKQYIRELKDQIAELTHELRCLKGQR 685
Cdd:COG4913 371 LglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
317-673 |
1.45e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 317 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTEnrlLKQRIETLEKESASLADRliQGQVTRAQEAEENYLIKRELATIKQQT 396
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADE---AKKKAEEDKKKADELKKA--AAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 397 DAARaKLEQAESTIRELQHHRHWHKCSSTYNEdfVLQLEKELVQARLSEaESQCALKEMQDKVLDIEKKNNSFPDENNIA 476
Cdd:PTZ00121 1441 EEAK-KADEAKKKAEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 477 RLQEELIAVKLREAEAIMGLKELR--QQVRDLEEHWQRHVARTSGRWKDPPKRNAVSELQGelMSIRLREAETQAEMREM 554
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN--MALRKAEEAKKAEEARI 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 555 KQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRlreADSIAAVAE 634
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK---AAEEAKKAE 1671
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 564382509 635 LQQHIAElEIQKEE---GKLQGQLNR-SDSKQYIRELKDQIAE 673
Cdd:PTZ00121 1672 EDKKKAE-EAKKAEedeKKAAEALKKeAEEAKKAEELKKKEAE 1713
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
320-637 |
2.25e-06 |
|
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: 51.36 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 320 KKLE--KEYTTIKTKEMEEQGE-IKRLRTENRLLKQRIETLEkESASLADRLI-----QGQVTRAQEAEENYLIKRELAT 391
Cdd:pfam10174 401 KKIEnlQEQLRDKDKQLAGLKErVKSLQTDSSNTDTALTTLE-EALSEKERIIerlkeQREREDRERLEELESLKKENKD 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 392 IKQQTDAARAKLEQAESTIRELQHHRHWHKCSSTYNEDFVLQLEKELVQAR-------------LSEAESQCALKEMQDK 458
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKeecsklenqlkkaHNAEEAVRTNPEINDR 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 459 VLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGLKElrQQVRDLEEHWQRHVartsgrwKDPPKRNAVSELQGELM 538
Cdd:pfam10174 560 IRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD--KKIAELESLTLRQM-------KEQNKKVANIKHGQQEM 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 539 siRLREAETQAEMREMKQRMMEMETQNQINS--NQLRRAEQEVTSLQEKVCS--LSLKNK-GLLAQLSEAKRRQAEIECK 613
Cdd:pfam10174 631 --KKKGAQLLEEARRREDNLADNSQQLQLEElmGALEKTRQELDATKARLSStqQSLAEKdGHLTNLRAERRKQLEEILE 708
|
330 340
....*....|....*....|....
gi 564382509 614 NKEEVMAVRLREADSIAAVAELQQ 637
Cdd:pfam10174 709 MKQEALLAAISEKDANIALLELSS 732
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
340-686 |
2.47e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 340 IKRLR--TENRLLKQRIETLEKESASLADRLiqgQVTRAQEAEenylIKRELATIKQQTDAARAKLEQAESTIRELQHHR 417
Cdd:PRK02224 178 VERVLsdQRGSLDQLKAQIEEKEEKDLHERL---NGLESELAE----LDEEIERYEEQREQARETRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 418 hwhkcsstyNEDFVLQLEKELVQARLSEAESQC-----ALKEMQDKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEA 492
Cdd:PRK02224 251 ---------EELETLEAEIEDLRETIAETEREReelaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 493 imGLKELRQQVRDleehwqrhvartsgrwkdppKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQL 572
Cdd:PRK02224 322 --RDEELRDRLEE--------------------CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 573 RRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIEcknkEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQ 652
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR----EERDELREREAELEATLRTARERVEEAEALLEAGKCP 455
|
330 340 350
....*....|....*....|....*....|....*..
gi 564382509 653 --GQ-LNRSDSKQYIRELKDQIAELTHELRCLKGQRD 686
Cdd:PRK02224 456 ecGQpVEGSPHVETIEEDRERVEELEAELEDLEEEVE 492
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
476-685 |
1.03e-05 |
|
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: 49.40 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 476 ARLQEEliavKLREAEAIMGLKELRQQVRDLEEHwqrhvartsgrwkdppkrnaVSELQGELMSIRLREAETQAEMREMK 555
Cdd:pfam01576 82 SRLEEE----EERSQQLQNEKKKMQQHIQDLEEQ--------------------LDEEEAARQKLQLEKVTTEAKIKKLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 556 QRMMEMETQNQINSNQLRRAEQEVTSL-------QEKVCSLS-LKNK--GLLAQLS-----EAKRRQAEIECKNKEEVMA 620
Cdd:pfam01576 138 EDILLLEDQNSKLSKERKLLEERISEFtsnlaeeEEKAKSLSkLKNKheAMISDLEerlkkEEKGRQELEKAKRKLEGES 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564382509 621 VRLREAdsiaaVAELQQHIAELEIQ--KEEGKLQGQLNRSDSKQ--------YIRELKDQIAELTHELRCLKGQR 685
Cdd:pfam01576 218 TDLQEQ-----IAELQAQIAELRAQlaKKEEELQAALARLEEETaqknnalkKIRELEAQISELQEDLESERAAR 287
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
350-686 |
2.06e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 350 LKQRIETLEKESASLADRLIQgQVTRAQEAEENylIKRELATIKQQTDAARAKLEQAEstirelqhhrhwhkcsstyned 429
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEE-CRVAAQAHNEE--AESLREDADDLEERAEELREEAA---------------------- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 430 fvlQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPD-----ENNIARLQEELIAVKLREAEAIMGLKELRQQVR 504
Cdd:PRK02224 367 ---ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVdlgnaEDFLEELREERDELREREAELEATLRTARERVE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 505 DLEEHWQRHVARTSGR-WKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMEtqnqinsnQLRRAEQEVTSLQ 583
Cdd:PRK02224 444 EAEALLEAGKCPECGQpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLE 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 584 EKVCSLSlknkGLLAQ---LSEAKRRQAEIECKNKEEVMAvRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDS 660
Cdd:PRK02224 516 ERREDLE----ELIAErreTIEEKRERAEELRERAAELEA-EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
330 340
....*....|....*....|....*.
gi 564382509 661 KQYIRELKDQIAELTHELRCLKGQRD 686
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKRE 616
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
303-685 |
2.15e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 303 EKLIQSAYQVKynsKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKesasLADRLIQGQVTRAQEAEEN 382
Cdd:PRK03918 182 EKFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 383 YLIKRELATIKQQTDAARAKLEQAESTIRELQHHRHWHKCSSTYNEdFVLQLEKEL--VQARLSEAESQcaLKEMQDKVL 460
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE-FYEEYLDELreIEKRLSRLEEE--INGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 461 DIEKKnnsfpdENNIARLQEELIAVKlREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKDppkrnavsELQGELMSI 540
Cdd:PRK03918 332 ELEEK------EERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE--------KLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 541 RLREAETQAEMREMKQRMMEMETQnqinSNQLRRAEQEVTSLQEK--VC----------------SLSLKN-----KGLL 597
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKE----IKELKKAIEELKKAKGKcpVCgrelteehrkelleeyTAELKRiekelKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 598 AQLSEAKRRQAEIECKNKEEVMAVRLRE-ADSIAAVAE---------LQQHIAELEIQKEE-GKLQGQLNR-SDSKQYIR 665
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKElAEQLKELEEklkkynleeLEKKAEEYEKLKEKlIKLKGEIKSlKKELEKLE 552
|
410 420
....*....|....*....|
gi 564382509 666 ELKDQIAELTHELRCLKGQR 685
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEEL 572
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
307-676 |
4.58e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 307 QSAYQVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL--------IQGQVTRAQE 378
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtalrQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 379 AEENYLIKRE-----LATIKQQTDAARAKLEQAESTIRELQhhrhwhKCSSTYNEDFVLQLEKEL-----VQArLSEAES 448
Cdd:PRK04863 356 DLEELEERLEeqnevVEEADEQQEENEARAEAAEEEVDELK------SQLADYQQALDVQQTRAIqyqqaVQA-LERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 449 QCAL-------------------KEMQDKVLDIEKKNNSFPDenniARLQEELIAVKLREAEAIMGLKELRQQVRDLEEH 509
Cdd:PRK04863 429 LCGLpdltadnaedwleefqakeQEATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 510 W--QRHVARTSgrwkdPPKRNAVSELQGelmsiRLREAETQAEM-REMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKV 586
Cdd:PRK04863 505 LreQRHLAEQL-----QQLRMRLSELEQ-----RLRQQQRAERLlAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 587 CSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMA----VRLRE------ADSiAAVAELQQHIAELEIQKeegklqgQLN 656
Cdd:PRK04863 575 SEARERRMALRQQLEQLQARIQRLAARAPAWLAAqdalARLREqsgeefEDS-QDVTEYMQQLLEREREL-------TVE 646
|
410 420
....*....|....*....|
gi 564382509 657 RSDSKQYIRELKDQIAELTH 676
Cdd:PRK04863 647 RDELAARKQALDEEIERLSQ 666
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
385-651 |
5.95e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 385 IKRELATIKQQTDAARAKLEQAESTIRELQHHrhwhkcsstynEDFVLQLEKELVQARLSEAESQcaLKEMQDKVLDIEK 464
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSALNRL-----------LPRLNLLADETLADRVEEIREQ--LDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 465 KNNSFPD-ENNIARLQ---EELIAVKLREAEAIMGLKELRQQVRDLEEHWQRhvaRTSGRWKDPPKR-NAVSELQgELMS 539
Cdd:PRK04863 916 HGNALAQlEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQR---RAHFSYEDAAEMlAKNSDLN-EKLR 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 540 IRLREAEtqAEMREMKQRMmemeTQNQinsNQLRRAEQEVTSLQEkvcSLSLKNKgllaQLSEAKRR----------QAE 609
Cdd:PRK04863 992 QRLEQAE--QERTRAREQL----RQAQ---AQLAQYNQVLASLKS---SYDAKRQ----MLQELKQElqdlgvpadsGAE 1055
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 564382509 610 IECKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKL 651
Cdd:PRK04863 1056 ERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
318-505 |
8.99e-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: 46.21 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 318 KMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRE---LATIKQ 394
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREldrLQEELQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 395 QTDAARAKLEQAESTIRELQhhrhwhkcsstyNEdfvLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKKnnSFPDENN 474
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKI------------NE---LEEEKEDKALEIKKQEWK--LEQLAADLSKYEQE--LYDLKEE 477
|
170 180 190
....*....|....*....|....*....|.
gi 564382509 475 IARLQEELIAVKLREAEAIMGLKELRQQVRD 505
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
335-557 |
9.30e-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: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 335 EEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEaeenylikrELATIKQQTDAARAKLEQAESTIRELQ 414
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRA---------ELARLEAELERLEARLDALREELDELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 415 HHRHwhkcSSTYNEdfVLQLEKELVQARLSEAESqcalkemqdkvldiekknnsfpdENNIARLQEELIAVKLREAEAIM 494
Cdd:COG4913 330 AQIR----GNGGDR--LEQLEREIERLERELEER-----------------------ERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564382509 495 GLKELRQQVRDLEEHWQRHVARTsgrwkdppkRNAVSELQGELMSIRLREAETQAEMREMKQR 557
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEAL---------EEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
433-648 |
9.42e-05 |
|
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: 45.53 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 433 QLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFpdENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQR 512
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 513 HVARTSGRWKDPPKRNAVSELQGELMSIRLREAETQAE-MREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSL 591
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564382509 592 KNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEE 648
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
317-688 |
9.78e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 317 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKEsASLADRLIQGQVTRAQEAEENYLIKRELATIKQQT 396
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 397 DaARAKLEQAESTIRELQHH-RHWHKCSSTYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENNI 475
Cdd:COG4717 160 E-LEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 476 ARLQEEL--IAVKLREAEAIMGLKELRQQVRDLEEHWQ---------RHVARTSGRWKDPPKRNAVSELQGELMSIRLRE 544
Cdd:COG4717 239 AALEERLkeARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEE 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 545 AETQaemREMKQRMMEMETQNQINSNQLRRAEQEVTSLQE--------KVCSLSLKNKGLLAQLS-------EAKRRQAE 609
Cdd:COG4717 319 EELE---ELLAALGLPPDLSPEELLELLDRIEELQELLREaeeleeelQLEELEQEIAALLAEAGvedeeelRAALEQAE 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564382509 610 IECKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKqyIRELKDQIAELTHELRCLKGQRDFS 688
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEE--LEELREELAELEAELEQLEEDGELA 472
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
477-687 |
1.09e-04 |
|
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: 45.82 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 477 RLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHvartsgRWKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQ 556
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEEL------RLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 557 RMMEMETQNQINSNQLRRAEQ-------EVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNK---EEVMAVRLREA 626
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESkldelaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLETLRSKVA 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564382509 627 DSIAAVAELQQHIAELEIQKEEGKL--------QGQLNRSDSKQYIRELKDQIAELTHELRCLKGQRDF 687
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDrrerlqqeIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
310-673 |
1.25e-04 |
|
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: 45.50 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 310 YQVKYNSKKMKklEKEYTTIKTKEMEEQGEIKRlrtenRLLKQRIETLEKEsasladRLIQGQVTRAQEAEEnylikrel 389
Cdd:pfam17380 256 YTVRYNGQTMT--ENEFLNQLLHIVQHQKAVSE-----RQQQEKFEKMEQE------RLRQEKEEKAREVER-------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 390 atikqqtdaaRAKLEQAEsTIRELQHHRHwhkcSSTY--NEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNN 467
Cdd:pfam17380 315 ----------RRKLEEAE-KARQAEMDRQ----AAIYaeQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 468 sfpdennIARLQEEliavKLREAEAIMGLKELRQQVRDLEEHWQRHVArtsgrwKDPPKRNAVSELQGELMSIRLREAET 547
Cdd:pfam17380 380 -------LERLQME----RQQKNERVRQELEAARKVKILEEERQRKIQ------QQKVEMEQIRAEQEEARQREVRRLEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 548 QAEmREMKQ-RMMEMETQNQI-----NSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAkRRQAEIECKNKEEVMAV 621
Cdd:pfam17380 443 ERA-REMERvRLEEQERQQQVerlrqQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE-RKQAMIEEERKRKLLEK 520
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564382509 622 RLREADSiAAVAELQQHIAELE------------IQKEEGKLQGQLNRSDSKQYIRELKDQIAE 673
Cdd:pfam17380 521 EMEERQK-AIYEEERRREAEEErrkqqemeerrrIQEQMRKATEERSRLEAMEREREMMRQIVE 583
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
316-638 |
1.52e-04 |
|
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: 45.20 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 316 SKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKE----SASLADRLIQGQVTRAQEAEENYLIKRELAT 391
Cdd:pfam10174 446 SEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPEltekESSLIDLKEHASSLASSGLKKDSKLKSLEIA 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 392 IKQQTDAArAKLEQAESTIRELQHhrhwhkcSSTYNEDFVLQ---LEKELVQARLSEAESQCALKEMQDKVLDIEKKNNS 468
Cdd:pfam10174 526 VEQKKEEC-SKLENQLKKAHNAEE-------AVRTNPEINDRirlLEQEVARYKEESGKAQAEVERLLGILREVENEKND 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 469 fpDENNIARLqEELIAVKLREAEAIMGLKELRQQV--RDLEEHWQRHVARTSGRwKDPPKRNAVSELQGELMSIRLREAE 546
Cdd:pfam10174 598 --KDKKIAEL-ESLTLRQMKEQNKKVANIKHGQQEmkKKGAQLLEEARRREDNL-ADNSQQLQLEELMGALEKTRQELDA 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 547 TQAEMREMKQRMMEMETqnQINSNQLRRAEQevtsLQEKvcsLSLKNKGLLAQLSEAKRRQAEIEC------KNKEEVMA 620
Cdd:pfam10174 674 TKARLSSTQQSLAEKDG--HLTNLRAERRKQ----LEEI---LEMKQEALLAAISEKDANIALLELssskkkKTQEEVMA 744
|
330
....*....|....*...
gi 564382509 621 VRlREADSIaaVAELQQH 638
Cdd:pfam10174 745 LK-REKDRL--VHQLKQQ 759
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
315-608 |
1.66e-04 |
|
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: 45.44 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 315 NSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESAsladrliQGQVTRAQEAEENYLIKRELATIKQ 394
Cdd:TIGR02169 278 NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-------KLEAEIDKLLAEIEELEREIEEERK 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 395 QTDAARAKLEQAESTIRELQHhrhwhkcsstynedfvlQLEKELVQARLSEAEsqcaLKEMQDKVLDIEKKNNSFpdENN 474
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRA-----------------ELEEVDKEFAETRDE----LKDYREKLEKLKREINEL--KRE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 475 IARLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwqrhvartsgRWKDppKRNAVSELQGELMSIRLREAETQAEMREM 554
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEE-----------EKED--KALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564382509 555 KQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLS----LKNK------GLLAQLSEAKRRQA 608
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRaveeVLKAsiqgvhGTVAQLGSVGERYA 538
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
315-679 |
1.99e-04 |
|
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: 45.11 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 315 NSKKMKKLEKEYTTIKTKEMEeqgeikrLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELatikQ 394
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSE-------LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL----Q 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 395 QTDAARAKLEQAESTIRElQHHRHWHKcsSTYNEDFVLQLEKEL---------VQARLSEAESQCAlKEMQDKVLDIEKK 465
Cdd:pfam15921 381 KLLADLHKREKELSLEKE-QNKRLWDR--DTGNSITIDHLRRELddrnmevqrLEALLKAMKSECQ-GQMERQMAAIQGK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 466 NNSFpdeNNIARLQEELIAVK--LREAeaimgLKELRQQVRDLEEHwQRHVARTSGRWKDppKRNAVSELQGELMSIRLR 543
Cdd:pfam15921 457 NESL---EKVSSLTAQLESTKemLRKV-----VEELTAKKMTLESS-ERTVSDLTASLQE--KERAIEATNAEITKLRSR 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 544 EAETQAEMREMKQRMMEME-TQNQINSNQLRRAEQE--VTSLQEKVCSLS--LKNKGLLAQLSEAKRRQAEIECKNKE-E 617
Cdd:pfam15921 526 VDLKLQELQHLKNEGDHLRnVQTECEALKLQMAEKDkvIEILRQQIENMTqlVGQHGRTAGAMQVEKAQLEKEINDRRlE 605
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564382509 618 VMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGqlnrSDSKQYIRELKDQIAELTHELR 679
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAG----SERLRAVKDIKQERDQLLNEVK 663
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
321-611 |
2.03e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 321 KLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQ--EAEENYLIKR---ELATIKQQ 395
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREltEEHRKELLEEytaELKRIEKE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 396 TDAARAKLEQAESTIRELQHHRHWHKCSSTYNE--DFVLQLEKELVQARLSEAESQCA-LKEMQDKVLDIEKKNNSFPDE 472
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKE 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 473 -NNIARLQEELIAV--KLREAEAimGLKELRQQVRDLEEHWQRHVARTSGRWKDPPKR-----NAVSELQGELMSIRLRE 544
Cdd:PRK03918 548 lEKLEELKKKLAELekKLDELEE--ELAELLKELEELGFESVEELEERLKELEPFYNEylelkDAEKELEREEKELKKLE 625
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 545 AE---TQAEMREMKQRMMEMEtqNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIE 611
Cdd:PRK03918 626 EEldkAFEELAETEKRLEELR--KELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
351-557 |
2.27e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 351 KQRIETLEKESASLADRL--IQGQVTRAQEAEENYLIKRELATIKQQTDAARAKLEQAESTIRELQHHRhwHKCSSTYNE 428
Cdd:COG4913 609 RAKLAALEAELAELEEELaeAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAEL--ERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 429 dfVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKnnsfpdennIARLQEELIAVKLREAEAIMGLKELRQQvrDLEE 508
Cdd:COG4913 687 --LAALEEQLEELEAELEELEEELDELKGEIGRLEKE---------LEQAEEELDELQDRLEAAEDLARLELRA--LLEE 753
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564382509 509 HWQRHVARTSGrwkdppkRNAVSELQGELMSI--RLREAETQAE--MREMKQR 557
Cdd:COG4913 754 RFAAALGDAVE-------RELRENLEERIDALraRLNRAEEELEraMRAFNRE 799
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
332-508 |
2.47e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 332 KEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEAEENylIKRELATIK-QQTDAARAKLEQAES 408
Cdd:COG4913 275 EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELerLEARLDALREELDE--LEAQIRGNGgDRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 409 TIRELQHHRhwhkcsstynedfvLQLEKELVQARLSEAESQCALKEMQDKVLDIekknnsfpdennIARLQEELIAVKLR 488
Cdd:COG4913 353 ELEERERRR--------------ARLEALLAALGLPLPASAEEFAALRAEAAAL------------LEALEEELEALEEA 406
|
170 180
....*....|....*....|
gi 564382509 489 EAEAIMGLKELRQQVRDLEE 508
Cdd:COG4913 407 LAEAEAALRDLRRELRELEA 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
475-675 |
2.60e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 475 IARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKD---PPKRNAVSELQGELMSIRL--------- 542
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDAssddlaale 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 543 -REAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIEckNKEEVMAV 621
Cdd:COG4913 692 eQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD--AVERELRE 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564382509 622 RLREadsiaavaelQQHIAELEIQKEEGKLQGQLNrsdskQYIRELKDQIAELT 675
Cdd:COG4913 770 NLEE----------RIDALRARLNRAEEELERAMR-----AFNREWPAETADLD 808
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
311-564 |
3.63e-04 |
|
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: 44.28 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 311 QVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEAEENYLIKRE 388
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIesLAAEIEELEELIEELESELE 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 389 LAT-----IKQQTDAARAKLEQAESTIRELQHHRHwhkcsstynedfvlQLEKELVQARLSEAESQCALKEMqdkvldie 463
Cdd:TIGR02168 877 ALLnerasLEEALALLRSELEELSEELRELESKRS--------------ELRRELEELREKLAQLELRLEGL-------- 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 464 kknnsfpdENNIARLQEELIAVKLREAEAIMGLKELRQqvrDLEEHWQRHVARTsgrwkdppkRNAVSELqGE--LMSIr 541
Cdd:TIGR02168 935 --------EVRIDNLQERLSEEYSLTLEEAEALENKIE---DDEEEARRRLKRL---------ENKIKEL-GPvnLAAI- 992
|
250 260
....*....|....*....|...
gi 564382509 542 lreaetqAEMREMKQRMMEMETQ 564
Cdd:TIGR02168 993 -------EEYEELKERYDFLTAQ 1008
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
323-414 |
4.12e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 323 EKEYTTIKTKEMEEQ-----GEIKRLRTENRLLKQRIETLEKESASLADRLiqgqVTRAQEAEENYLIKRELATIKQQTD 397
Cdd:COG2433 400 EKEHEERELTEEEEEirrleEQVERLEAEVEELEAELEEKDERIERLEREL----SEARSEERREIRKDREISRLDREIE 475
|
90
....*....|....*..
gi 564382509 398 AARAKLEQAESTIRELQ 414
Cdd:COG2433 476 RLERELEEERERIEELK 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
475-686 |
4.15e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 475 IARLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwqrhvartsgrwkdppKRNAVSELQGelMSIRLREAETQAEMREM 554
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRR-----------------EREKAERYQA--LLKEKREYEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 555 KqrmmEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRqaeIECKNKEEVMAVRLREADSIAAVAE 634
Cdd:TIGR02169 233 E----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK---IKDLGEEEQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564382509 635 LQQHIAELEIQKEEgkLQGQLNRSDSKqyIRELKDQIAELTHELRCLKGQRD 686
Cdd:TIGR02169 306 LERSIAEKERELED--AEERLAKLEAE--IDKLLAEIEELEREIEEERKRRD 353
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
433-670 |
5.09e-04 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 43.31 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 433 QLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSfpdeNNIARLQEE--------LIAVKLREAEAIMGLKELRQQVR 504
Cdd:pfam08017 25 QSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQG----NVLERRQRDaenrsqgnVLERRQRDAENRSQGNVLERRQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 505 DLEEHWQRHVA---------RTSGRWKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRA 575
Cdd:pfam08017 101 DAENRSQGNVLerrqrdaenKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 576 EQEVTSlQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREAD--SIAAVAELQQHIAE-------LEIQK 646
Cdd:pfam08017 181 DAENKS-QGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEnrSQGNVLERRQRDAEnksqgnvLERRQ 259
|
250 260
....*....|....*....|....
gi 564382509 647 EEGKLQGQLNRSDSKQYIRELKDQ 670
Cdd:pfam08017 260 RDAENRSQGNVLERRQRDAENRSQ 283
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
318-673 |
5.24e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 318 KMKKLEKEYTTI------KTKEMEE-QGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELA 390
Cdd:TIGR04523 343 QISQLKKELTNSesenseKQRELEEkQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 391 TIKQQTDAARAKLEQAESTIRELQhhrhwhkcsstyNEDFVLQLE-KELVQARLSEaesqcalkEMQDKVLDIEKKNNsf 469
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLT------------NQDSVKELIiKNLDNTRESL--------ETQLKVLSRSINKI-- 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 470 pdENNIARLQEELiavKLREAEaimgLKELRQQVRDLEEhwqrhvartsgRWKDPPKRNAVSELQGELMSIRLREAETqa 549
Cdd:TIGR04523 481 --KQNLEQKQKEL---KSKEKE----LKKLNEEKKELEE-----------KVKDLTKKISSLKEKIEKLESEKKEKES-- 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 550 EMREMKQRMMEMETQNqiNSNQLrraEQEVTSLQEKVCSLSLKNKGLlaqlsEAKRRQAEIECKNKE-EVMAVRLREADS 628
Cdd:TIGR04523 539 KISDLEDELNKDDFEL--KKENL---EKEIDEKNKEIEELKQTQKSL-----KKKQEEKQELIDQKEkEKKDLIKEIEEK 608
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 564382509 629 IAAVAELQQHIAelEIQKEEGKLQGQLNRSDSK-----QYIRELKDQIAE 673
Cdd:TIGR04523 609 EKKISSLEKELE--KAKKENEKLSSIIKNIKSKknklkQEVKQIKETIKE 656
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
477-654 |
6.00e-04 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 42.93 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 477 RLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwqrhvaRTSGRWKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQ 556
Cdd:pfam08017 137 RSQGNVLERRQRDAENRSQGNVLERRQRDAEN-------RSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNVLER 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 557 RMMEMETQNQINSNQLRRAEQEVTSlQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAVAELQ 636
Cdd:pfam08017 210 RQRDAENRSQGNVLERRQRDAENRS-QGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLE 288
|
170
....*....|....*...
gi 564382509 637 QHIAELEIQKEEGKLQGQ 654
Cdd:pfam08017 289 RRQRDAENKSQVGQLIGK 306
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
303-677 |
7.69e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 303 EKLIQSAYQVKYNSKKMKKLEKEYTtiKTKEMEEQGEIKRLRTEnrlLKQRIETLEK--------ESASLADRLIQG--Q 372
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKK--KADEAKKKAEEKKKADE---AKKKAEEAKKadeakkkaEEAKKAEEAKKKaeE 1468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 373 VTRAQEAEENYLIKRELATIKQQTDAARAKLEQAESTIRELQHHRHWHKCSSTYNEDFVLQLEKELVQARLSEAESQCAL 452
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 453 KEMQ--------DKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGLKELR-----QQVRDLEEHwqrhvartsg 519
Cdd:PTZ00121 1549 DELKkaeelkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEkkmkaEEAKKAEEA---------- 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 520 RWKDPPKRNAvSELQGELMSIRLREAETQAEMREMKQRmmemETQNQINSNQL-RRAEQEVTSLQEkvcslslknkglLA 598
Cdd:PTZ00121 1619 KIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKA----EEENKIKAAEEaKKAEEDKKKAEE------------AK 1681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 599 QLSEAKRRQAEIECKNKEE---VMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKQYIRE--LKDQIAE 673
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeEKKKIAH 1761
|
....
gi 564382509 674 LTHE 677
Cdd:PTZ00121 1762 LKKE 1765
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
496-679 |
8.38e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 496 LKELRQQVRDLEEHWQRHVArtsgrwkdppKRNAVSELQGELMSIRLREAETQAEMREMKQrmmemETQNQINSNQLRRA 575
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAE----------LQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 576 EQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEevmAVRLREADSIAAVAELQQHIAELE-IQKEEGKLQGQ 654
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEeLQQRLAELEEE 214
|
170 180
....*....|....*....|....*
gi 564382509 655 LNRsdSKQYIRELKDQIAELTHELR 679
Cdd:COG4717 215 LEE--AQEELEELEEELEQLENELE 237
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
315-686 |
8.90e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 315 NSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQvtraqeaEENYLIKRELATIKQ 394
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE-------KEKLNIQKNIDKIKN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 395 QtdaaRAKLEQAESTIREL-QHHR-------HWHKCSSTYNEDFV-LQLEKELVQARLSEAESQC---------ALKEMQ 456
Cdd:TIGR04523 195 K----LLKLELLLSNLKKKiQKNKslesqisELKKQNNQLKDNIEkKQQEINEKTTEISNTQTQLnqlkdeqnkIKKQLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 457 DKVLDIEKKNNSFPD-ENNIARLQEELIAVKLREAEAIMglKELRQQVRDleehwqrhvartsgrwkdppKRNAVSELQG 535
Cdd:TIGR04523 271 EKQKELEQNNKKIKElEKQLNQLKSEISDLNNQKEQDWN--KELKSELKN--------------------QEKKLEEIQN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 536 ELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNK 615
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564382509 616 eevmavrlreadsiaavaELQQHIAELEIQKEEGKLQGQL---NRSDSKQYIRELKDQIAELTHELRCLKGQRD 686
Cdd:TIGR04523 409 ------------------QKDEQIKKLQQEKELLEKEIERlkeTIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
337-686 |
9.00e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 337 QGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQ---EAEENylIKRELATIKQQTDAARAKLEQAESTIREL 413
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggDRLEQ--LEREIERLERELEERERRRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 414 QH------------HRHWHKCSSTYNEDFVlQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDE--NNIARLQ 479
Cdd:COG4913 372 GLplpasaeefaalRAEAAALLEALEEELE-ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARllALRDALA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 480 E-------------ELIAVKLREAE---AIMGLkeLRQQVRDL---EEHWQ---RHVARTSGR----------------- 520
Cdd:COG4913 451 EalgldeaelpfvgELIEVRPEEERwrgAIERV--LGGFALTLlvpPEHYAaalRWVNRLHLRgrlvyervrtglpdper 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 521 -------------WKDPPKRNAVSELQGELMSI----------RLREAETQAEMREMKQRMMEMETQNQINSN------- 570
Cdd:COG4913 529 prldpdslagkldFKPHPFRAWLEAELGRRFDYvcvdspeelrRHPRAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfdn 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 571 --QLRRAEQEVTSLQEKVcslslknKGLLAQLSEAKRRQAEIEckNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEe 648
Cdd:COG4913 609 raKLAALEAELAELEEEL-------AEAEERLEALEAELDALQ--ERREALQRLAEYSWDEIDVASAEREIAELEAELE- 678
|
410 420 430
....*....|....*....|....*....|....*...
gi 564382509 649 gklqgQLNRSDSKqyIRELKDQIAELTHELRCLKGQRD 686
Cdd:COG4913 679 -----RLDASSDD--LAALEEQLEELEAELEELEEELD 709
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
477-674 |
9.10e-04 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 42.54 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 477 RLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVA---------RTSGRWKDPPKRNAVSELQGELMSIRLREAET 547
Cdd:pfam08017 105 RSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNVLerrqrdaenRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 548 QAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSlQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREAD 627
Cdd:pfam08017 185 KSQGNVLERRQRDAENRSQGNVLERRQRDAENRS-QGNVLERRQRDAENRSQGNVLERRQRDAENKSQGNVLERRQRDAE 263
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564382509 628 SIAavaelQQHIAELEIQKEEGKLQGqlNRSDSKQYIRELKDQIAEL 674
Cdd:pfam08017 264 NRS-----QGNVLERRQRDAENRSQG--NVLERRQRDAENKSQVGQL 303
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
332-670 |
1.11e-03 |
|
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: 42.65 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 332 KEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKREL--ATIKQQTDAARAKLEQAEST 409
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLneERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 410 IRELQHH----RHWHKCSSTYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENN----------- 474
Cdd:pfam02463 257 KQEIEKEeeklAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKaekelkkekee 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 475 IARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKDPPKRNAVSELQGELMSIRLREAETQAEMREM 554
Cdd:pfam02463 337 IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 555 KQ--RMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAV 632
Cdd:pfam02463 417 LEdlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
330 340 350
....*....|....*....|....*....|....*...
gi 564382509 633 AELQQHIAELEIQKEEGKLQGQLNRSDSKQYIRELKDQ 670
Cdd:pfam02463 497 ERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
315-449 |
1.89e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 315 NSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL----IQGQVTRAQEAEENY------- 383
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeaaeDLARLELRALLEERFaaalgda 762
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564382509 384 LIKRELATIKQQTDAARAKLEQAESTIREL--QHHRHWHKCSST------YNEDFVLQLEKeLVQARLSEAESQ 449
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERAmrAFNREWPAETADldadleSLPEYLALLDR-LEEDGLPEYEER 835
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
322-661 |
1.99e-03 |
|
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: 41.65 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 322 LEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQTD---- 397
Cdd:pfam05557 109 LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQdsei 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 398 --AARAKLEQAESTIRELQHHRHWHKCSSTYNED-FVLQLEKELVQARLSEAEsqcalkEMQDKVLDIEKKNNSFPDE-- 472
Cdd:pfam05557 189 vkNSKSELARIPELEKELERLREHNKHLNENIENkLLLKEEVEDLKRKLEREE------KYREEAATLELEKEKLEQElq 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 473 --------------------NNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVAR-TSGRWKDPPKRNAVS 531
Cdd:pfam05557 263 swvklaqdtglnlrspedlsRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKiEDLNKKLKRHKALVR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 532 ELQGELMSI----------------RLREAETQAE----MREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSL 591
Cdd:pfam05557 343 RLQRRVLLLtkerdgyrailesydkELTMSNYSPQllerIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLER 422
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 592 KNKGLLAQLSEAKRRQAeiecknKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSK 661
Cdd:pfam05557 423 ELQALRQQESLADPSYS------KEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTK 486
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
302-537 |
2.02e-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: 41.29 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 302 PEKLIQSAYQVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL----IQGQVTRAQ 377
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 378 EAEENYLIKRELATIKQQTDAARAKLEQAESTIRELQHHRHWHKCSSTYNEDFVLQLEKELVQARLSEAESQCALKEMQD 457
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 458 KVLDIEKKNNSFpdENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKDPPKRNaVSELQGEL 537
Cdd:COG4942 179 LLAELEEERAAL--EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG-FAALKGKL 255
|
|
| DUF1129 |
pfam06570 |
Protein of unknown function (DUF1129); This family consists of several hypothetical bacterial ... |
427-465 |
2.75e-03 |
|
Protein of unknown function (DUF1129); This family consists of several hypothetical bacterial proteins of unknown function.
Pssm-ID: 429008 Cd Length: 200 Bit Score: 39.95 E-value: 2.75e-03
10 20 30
....*....|....*....|....*....|....*....
gi 564382509 427 NEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKK 465
Cdd:pfam06570 6 NQDYIFRLTKQLIKDGKSDEEIKEILDEMLPEILEGQKK 44
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
472-681 |
3.87e-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: 40.52 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 472 ENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHvartsgrwkdppkRNAVSELQGELMSIRLREAETQAEM 551
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-------------EQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 552 REMKQRMMEMETQNQINSNQlrraEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIA- 630
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQ----PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAe 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564382509 631 ---AVAELQQHIAELEIQKEE-GKLQGQLNR--SDSKQYIRELKDQIAELTHELRCL 681
Cdd:COG4942 176 leaLLAELEEERAALEALKAErQKLLARLEKelAELAAELAELQQEAEELEALIARL 232
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
303-679 |
4.53e-03 |
|
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: 40.80 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 303 EKLIQSAYQVKYNSKKMKKLEKEYTTIKTKEmeeQGEIKRLRTENRLLKQR-IETLEKESASLADRLIQGQVTRAQEAEE 381
Cdd:TIGR00606 447 EILEKKQEELKFVIKELQQLEGSSDRILELD---QELRKAERELSKAEKNSlTETLKKEVKSLQNEKADLDRKLRKLDQE 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 382 NYLIKRELATIKQQTDAARAKLEQAESTIRELQHHRH------------------WHKCSSTYN--EDFVLQLEKELVQA 441
Cdd:TIGR00606 524 MEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDeltsllgyfpnkkqledwLHSKSKEINqtRDRLAKLNKELASL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 442 RLSEAESQCALKEMQDKVLDIEKK----NNSFPDENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVART 517
Cdd:TIGR00606 604 EQNKNHINNELESKEEQLSSYEDKlfdvCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVC 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 518 SGRWKDPPKRNAV-SELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGL 596
Cdd:TIGR00606 684 QRVFQTEAELQEFiSDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 597 LAQLSEakrRQAEIECKNKEEVMAvrlreADSIAAVAELQQHIAEL-EIQKEEGKLQGQLNRSDSKQYIRELKDQIAELT 675
Cdd:TIGR00606 764 KNDIEE---QETLLGTIMPEEESA-----KVCLTDVTIMERFQMELkDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
....
gi 564382509 676 HELR 679
Cdd:TIGR00606 836 HELD 839
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
298-585 |
5.16e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 298 FDGGPEKLIQSAYQvkynskKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQ---RIETLEKESasLADRL--IQGQ 372
Cdd:PRK04863 831 FEADPEAELRQLNR------RRVELERALADHESQEQQQRSQLEQAKEGLSALNRllpRLNLLADET--LADRVeeIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 373 VTRAQEAEeNYL---------IKRELATIK---QQTDAARAKLEQAESTIRELQhhrhwhkcsstyNEDFVLqleKELVQ 440
Cdd:PRK04863 903 LDEAEEAK-RFVqqhgnalaqLEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAK------------QQAFAL---TEVVQ 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 441 AR--LSEAESQCALKEMQDkvldiekknnsfpdenniarLQEELIAvKLREAEAiMGLK---ELRQQVRDLEEHWQRHVA 515
Cdd:PRK04863 967 RRahFSYEDAAEMLAKNSD--------------------LNEKLRQ-RLEQAEQ-ERTRareQLRQAQAQLAQYNQVLAS 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 516 RTSGRwkdPPKRNAVSELQGELMSI------------RLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQ 583
Cdd:PRK04863 1025 LKSSY---DAKRQMLQELKQELQDLgvpadsgaeeraRARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
|
..
gi 564382509 584 EK 585
Cdd:PRK04863 1102 RD 1103
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
433-690 |
5.30e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 433 QLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFpdENNIARLQ---------EELIAVKLREAEAimGLKELRQQV 503
Cdd:pfam12128 217 RLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTL--ESAELRLShlhfgyksdETLIASRQEERQE--TSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 504 RDLEEHWQRHVARTSGRWKdpPKRNAVSELQGELMsiRLREAETQAEMREMKQRMMEMETQNQInSNQLRRAEQEVTSLQ 583
Cdd:pfam12128 293 RTLDDQWKEKRDELNGELS--AADAAVAKDRSELE--ALEDQHGAFLDADIETAAADQEQLPSW-QSELENLEERLKALT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 584 EKVCSLSLKNKGLLAQLSEakRRQAEIEcKNKEEVMAVRlREADSIAAVAE--LQQHIAELEIQKEEGKLQGQLNRSDSK 661
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKE--QNNRDIA-GIKDKLAKIR-EARDRQLAVAEddLQALESELREQLEAGKLEFNEEEYRLK 443
|
250 260
....*....|....*....|....*....
gi 564382509 662 QYIRELKDQIAELTHELRCLKGQRDFSSR 690
Cdd:pfam12128 444 SRLGELKLRLNQATATPELLLQLENFDER 472
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
339-516 |
5.85e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 339 EIKRLRTENRLLKQRIETLEKESASLADRLiqgqVTRAQEAEEnylIKRELATIKQQTDAARAKLEQAE------STIRE 412
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARL----EAAKTELED---LEKEIKRLELEIEEVEARIKKYEeqlgnvRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 413 LQHhrhwhkcsstynedfvLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKKNNSFpdENNIARLQEELIAVKlREAEA 492
Cdd:COG1579 91 YEA----------------LQKEIESLKRRISDLEDE--ILELMERIEELEEELAEL--EAELAELEAELEEKK-AELDE 149
|
170 180
....*....|....*....|....
gi 564382509 493 ImgLKELRQQVRDLEEHWQRHVAR 516
Cdd:COG1579 150 E--LAELEAELEELEAEREELAAK 171
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
527-684 |
6.00e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 527 RNAVSELQGELMSIRLREAETQAEMREMKQR--MMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAK 604
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 605 RRQAEIecKNKEEVMAVRLREADSIAAVAELQQH-------IAEL--EIQKEEGKLQGQLNR--SDSKQYIRELKDQIAE 673
Cdd:COG3206 254 DALPEL--LQSPVIQQLRAQLAELEAELAELSARytpnhpdVIALraQIAALRAQLQQEAQRilASLEAELEALQAREAS 331
|
170
....*....|.
gi 564382509 674 LTHELRCLKGQ 684
Cdd:COG3206 332 LQAQLAQLEAR 342
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
401-594 |
6.21e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 401 AKLEQAESTIRELQ-HHRHWHKcsstynedfvLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKKNNSFPDENNIARLQ 479
Cdd:COG4717 71 KELKELEEELKEAEeKEEEYAE----------LQEELEELEEELEELEAE--LEELREELEKLEKLLQLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 480 EELIAVKLREAEAIMGLKELRQQVRDLEEhWQRHVARTsgrwkdppKRNAVSELQGELMSIRLREAETQAEMREMKQRMM 559
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEE-LEAELAEL--------QEELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190
....*....|....*....|....*....|....*
gi 564382509 560 EMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNK 594
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
303-682 |
7.91e-03 |
|
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: 39.62 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 303 EKLIQSAYQVKYNSKKMKKLEKEYTTIKTKemeeqgeikrlrtenrllkqrIETLEKEsasladrliqgqvtraQEAEEN 382
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSE---------------------ISDLNNQ----------------KEQDWN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 383 YLIKRELATIKQQTDAARAKLEQAESTIRELqhhrhwhkcsstynEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDI 462
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQL--------------NEQISQLKKELTNSESENSEKQRELEEKQNEIEKL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 463 EKKNNSFPDE-----NNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQR---HVARTSGRWKDPPKRNAVSELQ 534
Cdd:TIGR04523 376 KKENQSYKQEiknleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlkeTIIKNNSEIKDLTNQDSVKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 535 GELMSIRLREAETQAEmrEMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKN 614
Cdd:TIGR04523 456 IKNLDNTRESLETQLK--VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564382509 615 KeevmavrlreadsiaavaELQQHIAELEiqKEEGKLQGQLNRSDSKQYIRELKDQIAELTHELRCLK 682
Cdd:TIGR04523 534 K------------------EKESKISDLE--DELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLK 581
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
380-648 |
8.52e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.13 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 380 EENYLIKRELATIKQQTDAARAKLEQA-ESTIRELqhhRHWHKCSSTYN--------------EDFVLQLEKELVQARLS 444
Cdd:pfam00038 25 QQNKLLETKISELRQKKGAEPSRLYSLyEKEIEDL---RRQLDTLTVERarlqleldnlrlaaEDFRQKYEDELNLRTSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 445 EAESQCALKEMQDKVL---DIEKKnnsfpdennIARLQEELIAVK-LREAEaimgLKELRQQVRDLeehwQRHVARTSGR 520
Cdd:pfam00038 102 ENDLVGLRKDLDEATLarvDLEAK---------IESLKEELAFLKkNHEEE----VRELQAQVSDT----QVNVEMDAAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 521 WKDPPKrnAVSEL--QGELMSIR-LREAETQaemreMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLL 597
Cdd:pfam00038 165 KLDLTS--ALAEIraQYEEIAAKnREEAEEW-----YQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564382509 598 AQLSEAKRRQAEIECKNKEEVMAVRlreaDSIAAV-AELQQHIAELEIQKEE 648
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQ----ELISELeAELQETRQEMARQLRE 285
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
546-684 |
9.47e-03 |
|
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: 39.65 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382509 546 ETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIEcknkEEVMAVRLRE 625
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----AEVEQLEERI 749
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564382509 626 ADSIAAVAELQQHIAEL--EIQKEEGKLQGQL-NRSDSKQYIRELKDQIAELTHELRCLKGQ 684
Cdd:TIGR02168 750 AQLSKELTELEAEIEELeeRLEEAEEELAEAEaEIEELEAQIEQLKEELKALREALDELRAE 811
|
|
| |
