|
Name |
Accession |
Description |
Interval |
E-value |
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
160-368 |
1.46e-83 |
|
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: 265.71 E-value: 1.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 160 VHKGIPHHFRAIVWQLLCSAQSMPI---KDQYSELLKMTSPCEKL----IRRDIARTYPEHNFFKEKDSLGQEVLFNVMK 232
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDTsadKDLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 233 AYSLVDREVGYCQGSAFIVGLLLMQMP-EEEAFCVFVKLMQDYRLReLFKPSMAELGLCMYQFECMIQEHLPELFVHFQS 311
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 815891150 312 QSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELM 368
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 ... |
200-368 |
1.49e-55 |
|
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: 189.00 E-value: 1.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 200 KLIRRDIARTYPEHNFFKEKDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQ-MPEEEAFCVFVKLMQDYRLRE 278
Cdd:pfam00566 10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 279 LFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIV-FRVGL 357
Cdd:pfam00566 88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
|
170
....*....|.
gi 815891150 358 ALLQMNQAELM 368
Cdd:pfam00566 168 AILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
131-377 |
1.64e-43 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 164.98 E-value: 1.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 131 EEDSWILWGRIVN-EWEDVRKKKEKQVKELVHKGIPHHFRAIVWQLLcsAQSMPIKDQ----YSELLKM-------TSPC 198
Cdd:COG5210 179 ELAADKLWISYLDpNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFL--LGIGFDLDKnpglYERLLNLhreakipTQEI 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 199 EKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEE-AFCVFVKLMQDYRLR 277
Cdd:COG5210 257 ISQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLP 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 278 ELFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGL 357
Cdd:COG5210 337 GYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLAL 416
|
250 260
....*....|....*....|
gi 815891150 358 ALLQMNQAELMQLDMEGMLQ 377
Cdd:COG5210 417 AILKLLRDKLLKLDSDELLD 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
403-718 |
1.60e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 403 YNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQHKCSSNYNEDFVLQLEKELVQAR 482
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 483 LSEAESQCALKEMQDKVldIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWK 562
Cdd:TIGR02168 754 KELTELEAEIEELEERL--EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 563 D-PPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLS 641
Cdd:TIGR02168 832 RiAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815891150 642 EAKRKQaeIECKNKEEVMAVRLREADsiAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQyigELKDQIAELNHEL 718
Cdd:TIGR02168 912 ELRREL--EELREKLAQLELRLEGLE--VRIDNLQERLSEEYSLTLEEAEALENKIEDDEE---EARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
406-675 |
7.15e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 406 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQHKCSSNynedfVLQLEKELVQARLSE 485
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD-----ELAEELAELEEKLEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 486 AESQCA-----LKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGR 560
Cdd:TIGR02168 349 LKEELEsleaeLEELEAELEELESRLEEL--EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 561 WKDpPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQnqinsnhLRRAEQEVISLQEKVQYLSAQNKGLLTQL 640
Cdd:TIGR02168 427 LKK-LEEAELKELQAELEELEEELEELQEELERLEEALEELREE-------LEEAEQALDAAERELAQLQARLDSLERLQ 498
|
250 260 270
....*....|....*....|....*....|....*
gi 815891150 641 SEAKRKQAEIecknkEEVMAVRLREADSIAAVAEL 675
Cdd:TIGR02168 499 ENLEGFSEGV-----KALLKNQSGLSGILGVLSEL 528
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
423-644 |
7.31e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 62.73 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 423 MEEQVEIKRLRTENRL--LKQRIETLEKESASLADRLIQHKCSSNY-----NEDFVLQ----LEKELVQARLSEAESQCA 491
Cdd:COG3206 162 LEQNLELRREEARKALefLEEQLPELRKELEEAEAALEEFRQKNGLvdlseEAKLLLQqlseLESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 492 LKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGL-------KELRQQVKDLEEHWQRHLARttgrwkdp 564
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQR-------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 565 pkknAMNELQDELMTIRLREAETQAEIREIKQRMMEmetqnqinsnhLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAK 644
Cdd:COG3206 314 ----ILASLEAELEALQAREASLQAQLAQLEARLAE-----------LPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
402-719 |
2.85e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 402 KYNSKK---MKKLEKeyttikTKEMEEQVEIkrLRTEnrlLKQRIETLEKESA------SLADRLIQHKCSSNYNEDFVL 472
Cdd:COG1196 169 KYKERKeeaERKLEA------TEENLERLED--ILGE---LERQLEPLERQAEkaeryrELKEELKELEAELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 473 QLEKELVQARLSEAESQcaLKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQR 552
Cdd:COG1196 238 EAELEELEAELEELEAE--LEELEAELAELEAELEEL--RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 553 HLARttgrwkdppkknaMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISL----QEKVQY 628
Cdd:COG1196 314 LEER-------------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAeaelAEAEEE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 629 LSAQNKGLLTQLSEAKRKQAEIEckNKEEVMAVRLREADSI-AAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGEL 707
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLE--ELEEAEEALLERLERLeEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
330
....*....|..
gi 815891150 708 KDQIAELNHELR 719
Cdd:COG1196 459 EALLELLAELLE 470
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
503-718 |
4.77e-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: 60.07 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 503 EKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwQRHLARTTGRWKDPPKKNAMNELQDELMTIRL 582
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE--ELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 583 RE---AETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIecknKEEVM 659
Cdd:TIGR02168 745 LEeriAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL----NEEAA 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 815891150 660 AVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNksdsNQYIGELKDQIAELNHEL 718
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----AAEIEELEELIEELESEL 875
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
361-686 |
1.26e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 361 QMNQAELMQLDMEGMLQHFQKVIPhQFDGVPDKLIQAAYQVKYN---------SKKMKKLEKEYTTIKTK--EMEEQVEI 429
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILV-DFEEASGKKIYEHDSMSTMhfrslgsaiSKILRELDTEISYLKGRifPVEDQLEA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 430 KRLRTENR---LLKQ---RIETLEKESASLADRLIQhKCSSNYNEDFVLQLEKELVQ--ARLSEAESQCALKEMQDKV-- 499
Cdd:pfam15921 250 LKSESQNKielLLQQhqdRIEQLISEHEVEITGLTE-KASSARSQANSIQSQLEIIQeqARNQNSMYMRQLSDLESTVsq 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 500 LDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLArttgrwkdppkknamnelqdelmT 579
Cdd:pfam15921 329 LRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA-----------------------D 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 580 IRLREAETQAEiREIKQRMMEMETQNQINSNHLRRaeqEVISLQEKVQYLSAQNKGLLTQLS-EAKRKQAEIECKNKEev 658
Cdd:pfam15921 386 LHKREKELSLE-KEQNKRLWDRDTGNSITIDHLRR---ELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNES-- 459
|
330 340 350
....*....|....*....|....*....|...
gi 815891150 659 mavrLREADSIAAVAE-----LRQHIAELEIQK 686
Cdd:pfam15921 460 ----LEKVSSLTAQLEstkemLRKVVEELTAKK 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
514-725 |
2.11e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 514 NIARLQEELIavKLREAEAIMglKELRQQVKDLE---EHWQRHLArttgrwkdppKKNAMNELQDELMTIRLREAET--- 587
Cdd:COG4913 226 AADALVEHFD--DLERAHEAL--EDAREQIELLEpirELAERYAA----------ARERLAELEYLRAALRLWFAQRrle 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 588 --QAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEiECKNKEEVMAVRLRE 665
Cdd:COG4913 292 llEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815891150 666 -----ADSIAAVAELRQHIAEL--EIQKEEGKLQGQLNKSDSNQYigELKDQIAELNHELRCLKGQR 725
Cdd:COG4913 371 lglplPASAEEFAALRAEAAALleALEEELEALEEALAEAEAALR--DLRRELRELEAEIASLERRK 435
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
399-688 |
3.10e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.97 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 399 YQVKYNSKKMKKLE------------KEYTTIKTKEMEEQVEIKRLRTEN----RLLKQRIETLEKESASLADRLIQHKC 462
Cdd:pfam17380 256 YTVRYNGQTMTENEflnqllhivqhqKAVSERQQQEKFEKMEQERLRQEKeekaREVERRRKLEEAEKARQAEMDRQAAI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 463 SSNyNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNslpdennIARLQEEliavKLREAEAIMGLKELRQQ 542
Cdd:pfam17380 336 YAE-QERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRE-------LERLQME----RQQKNERVRQELEAARK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 543 VKDLEEHWQRHLARTTGRWKDPPKKnamnelQDELMTIRLREAETQAEIREIKQRMMEMETQNQI-----NSNHLRRAEQ 617
Cdd:pfam17380 404 VKILEEERQRKIQQQKVEMEQIRAE------QEEARQREVRRLEEERAREMERVRLEEQERQQQVerlrqQEEERKRKKL 477
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815891150 618 EVISLQEKVQYLSAQNKGLLTQLSEAkRKQAEIECKNKEEVMAVRLREADSiAAVAELRQHIAELEIQKEE 688
Cdd:pfam17380 478 ELEKEKRDRKRAEEQRRKILEKELEE-RKQAMIEEERKRKLLEKEMEERQK-AIYEEERRREAEEERRKQQ 546
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
396-682 |
3.74e-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: 53.91 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 396 QAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIqhkcssnynedfvlQLE 475
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE--------------SLA 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 476 KELVQARLSEAESQCALKEMQDKVldiekrnnslpdenniARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwqrhla 555
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNER----------------ASLEEALALLRSELEELSEELRELESKRSELRR------- 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 556 rttgrwkdppkknAMNELQDELMTIRLREAETQAEIREIKQR--------MMEMETQNQINSNHLRRAEQEVISLQEKVQ 627
Cdd:TIGR02168 916 -------------ELEELREKLAQLELRLEGLEVRIDNLQERlseeysltLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 815891150 628 YLSAQNKGLLTQLSEAKRKQAEIEcKNKEevmavrlreaDSIAAVAELRQHIAEL 682
Cdd:TIGR02168 983 ELGPVNLAAIEEYEELKERYDFLT-AQKE----------DLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
405-658 |
9.60e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 405 SKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQHKCSSNYNEDFVLQLEKELVQARLS 484
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 485 EAESQCALKEMQDKVLDIEKRNNSL---PDENNIARLQEELIAVK---------LREAEAIMGLKEL-RQQVKDLEEHWQ 551
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLearLSHSRIPEIQAELSKLEeevsriearLREIEQKLNRLTLeKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 552 RHLARTTGRWKDppKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSA 631
Cdd:TIGR02169 840 EQRIDLKEQIKS--IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
250 260
....*....|....*....|....*..
gi 815891150 632 QNKGLLTQLSEAKRKQAEIECKNKEEV 658
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
517-725 |
3.71e-06 |
|
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: 50.83 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 517 RLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHlarttgRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQ 596
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEEL------RLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 597 RM-------MEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNK---EEVMAVRLREA 666
Cdd:TIGR02168 310 RLanlerqlEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLETLRSKVA 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815891150 667 DSIAAVAELRQHIAELEIQKEEGKL--------QGQLNKSDSNQYIGELKDQIAELNHELRCLKGQR 725
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDrrerlqqeIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
515-719 |
1.68e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 515 IARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKD---PPKKNAMNELQDE----------LMTIR 581
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAElerldassddLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 582 LREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIEC--------- 652
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAverelrenl 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 653 ----------KNKEEVMAVRLREA-------------DSIAAVAELRQHIAELE----IQKEEgKLQGQLNKSdSNQYIG 705
Cdd:COG4913 772 eeridalrarLNRAEEELERAMRAfnrewpaetadldADLESLPEYLALLDRLEedglPEYEE-RFKELLNEN-SIEFVA 849
|
250 260
....*....|....*....|....*
gi 815891150 706 EL-----------KDQIAELNHELR 719
Cdd:COG4913 850 DLlsklrraireiKERIDPLNDSLK 874
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
421-597 |
2.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 421 KEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQhkcssnynedfvLQLEKELVQARLSEAESQCA--------- 491
Cdd:COG4913 275 EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER------------LEARLDALREELDELEAQIRgnggdrleq 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 492 -LKEMQDKVLDIEKRnnslpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTgrwkdppkkNAM 570
Cdd:COG4913 343 lEREIERLERELEER------ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---------EAL 407
|
170 180
....*....|....*....|....*..
gi 815891150 571 NELQDELMTIRLREAETQAEIREIKQR 597
Cdd:COG4913 408 AEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
406-724 |
2.48e-05 |
|
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: 48.09 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 406 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRL--IQHKCSSNYNEDFVLQLEKELVQARL 483
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlnIQKNIDKIKNKLLKLELLLSNLKKKI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 484 SEAesqcalKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKL---REAEAIMGLKELRQQVKDLEEHWQRHLARTTGR 560
Cdd:TIGR04523 211 QKN------KSLESQISELKKQNNQL--KDNIEKKQQEINEKTTeisNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 561 WKDppKKNAMNELQDELMTIRLREA-----ETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKG 635
Cdd:TIGR04523 283 IKE--LEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 636 LLTQLSEaKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAELN 715
Cdd:TIGR04523 361 KQRELEE-KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN 439
|
....*....
gi 815891150 716 HELRCLKGQ 724
Cdd:TIGR04523 440 SEIKDLTNQ 448
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
407-731 |
3.27e-05 |
|
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: 47.66 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 407 KMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLK---QRIETLEKESASLADRLIQHKCSSNYNEDFVLQLEKELVQARL 483
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKlkeQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 484 SEAESQCALKEMQDKVLDIEKRNNSLPDENN-IARLQEELIAVK-LREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRW 561
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEkEKKLQEEELKLLaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 562 KDPPK-KNAMNELQDELMTIRLREAETQAEIREIKQRMMEMET-QNQINSNHLRRAEQEVISLQEKVQYLSAQNKG---- 635
Cdd:pfam02463 328 KELKKeKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQlEEELLAKKKLESERLSSAAKLKEEELELKSEEekea 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 636 -LLTQLSEAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAEL 714
Cdd:pfam02463 408 qLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330
....*....|....*..
gi 815891150 715 NHELRCLKGQRGFSGQP 731
Cdd:pfam02463 488 LLLSRQKLEERSQKESK 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
515-725 |
3.94e-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: 47.37 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 515 IARLQEELIAVKLREAEAIMGLKELRQQVKDLEehwqrhlarttgrwKDPPKKNAMNELQDElmtirLREAETQAEIREI 594
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLR--------------REREKAERYQALLKE-----KREYEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 595 KqrmmEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKqaeIECKNKEEVMAVRLREADSIAAVAE 674
Cdd:TIGR02169 233 E----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK---IKDLGEEEQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 815891150 675 LRQHIAELEIQKEEgkLQGQLNKSDSNqyIGELKDQIAELNHELRCLKGQR 725
Cdd:TIGR02169 306 LERSIAEKERELED--AEERLAKLEAE--IDKLLAEIEELEREIEEERKRR 352
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
411-719 |
4.43e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 411 LEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRliqhkcssnynedfVLQLEKELVQARLSEAESQC 490
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE--------------AAELESELEEAREAVEDRRE 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 491 ALKEMQDKVLDIEKRNNSLPD-----ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGR-WKDP 564
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVdlgnaEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQpVEGS 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 565 PKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETqnqinsnhLRRAEQEVISLQEK---VQYLSAQNKGLLTQLS 641
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED--------LVEAEDRIERLEERredLEELIAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 642 EA---KRKQA---EIECKNKEEVMAVRLREADSIA-AVAELRQHIAELEIQKEE-GKLQGQLNK-SDSNQYIGELKD--- 709
Cdd:PRK02224 537 ERaeeLRERAaelEAEAEEKREAAAEAEEEAEEAReEVAELNSKLAELKERIESlERIRTLLAAiADAEDEIERLREkre 616
|
330
....*....|
gi 815891150 710 QIAELNHELR 719
Cdd:PRK02224 617 ALAELNDERR 626
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
473-700 |
5.70e-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: 46.30 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 473 QLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLeehwQR 552
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--ERRIAALARRIRALEQELAALEAELAELEKEIAEL----RA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 553 HLARTTGRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSnhLRRAEQEVISLQEKVQYLSAQ 632
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE--LRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 633 NKGLLTQLSEAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELE--IQKEEGKLQGQLNKSDS 700
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEalIARLEAEAAAAAERTPA 245
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
486-679 |
8.12e-05 |
|
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: 44.92 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 486 AESQCALKEMQD---KVLDIEKRNNSLPDEnnIARLQEELIAVKLREAEAIMGLKELRQQVKDLE---EHWQRHLARTTG 559
Cdd:COG1579 3 PEDLRALLDLQEldsELDRLEHRLKELPAE--LAELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 560 RWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEvisLQEKVQYLSAQNKGLLTQ 639
Cdd:COG1579 81 QLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 815891150 640 LSEAKRKQAEIECKNKEEVMAV--RLREADSIAAVAELRQHI 679
Cdd:COG1579 158 LEELEAEREELAAKIPPELLALyeRIRKRKNGLAVVPVEGGA 199
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
536-719 |
8.28e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 536 LKELRQQVKDLEEHWQRHlarttgrwkdppkknamNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNH--LR 613
Cdd:COG4717 73 LKELEEELKEAEEKEEEY-----------------AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqeLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 614 RAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEevmAVRLREADSIAAVAELRQHIAELE-IQKEEGKLQ 692
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEeLQQRLAELE 212
|
170 180
....*....|....*....|....*..
gi 815891150 693 GQLNKSDsnQYIGELKDQIAELNHELR 719
Cdd:COG4717 213 EELEEAQ--EELEELEEELEQLENELE 237
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
392-713 |
1.01e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 392 DKLIQAAYQVKYNSKKMKKLEKEYTtiKTKEMEEQVEIKRLRTEnrlLKQRIETLEK--------ESASLADRLIQHKCS 463
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKK--KADEAKKKAEEKKKADE---AKKKAEEAKKadeakkkaEEAKKAEEAKKKAEE 1468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 464 SNYNEdfvlQLEKELVQARLSEaESQCALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELR--Q 541
Cdd:PTZ00121 1469 AKKAD----EAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaE 1543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 542 QVKDLEEHWQRHLARTTGRWKDPPKKNAMNElqDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVIS 621
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEE--DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 622 LQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEEVMAVRlreADSIAAVAELRQHIAElEIQKEE----GKLQGQLNK 697
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK---AAEEAKKAEEDKKKAE-EAKKAEedekKAAEALKKE 1697
|
330
....*....|....*.
gi 815891150 698 SDSNQYIGELKDQIAE 713
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAE 1713
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
401-726 |
1.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 401 VKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQHKCSSNYNEDFvLQLEKELVQ 480
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY-IKLSEFYEE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 481 ARLSEAESQCALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGR 560
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 561 WKDPPKK------NAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQE-----VISLQEKVQYL 629
Cdd:PRK03918 385 TPEKLEKeleeleKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRI 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 630 SAQNKGLLTQLSEAKRKQAEIECKNKEEVMAVRLRE-ADSIAAVAE---------LRQHIAELEIQKEE-GKLQGQL-NK 697
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKElAEQLKELEEklkkynleeLEKKAEEYEKLKEKlIKLKGEIkSL 544
|
330 340
....*....|....*....|....*....
gi 815891150 698 SDSNQYIGELKDQIAELNHELRCLKGQRG 726
Cdd:PRK03918 545 KKELEKLEELKKKLAELEKKLDELEEELA 573
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
392-722 |
1.11e-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: 45.78 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 392 DKLIQAAYQVKYNSKKMKKLEKEYTTIKT-----KEMEEQVEIKRLRTENRLLKQRIETLEKEsasladrLIQHKCSSNY 466
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSeisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQ-------ISQNNKIISQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 467 NEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDE-----NNIARLQEELIAVKLREAEAIMGLKELRQ 541
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiknleSQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 542 QVKDLEEHWQRHLARTT---GRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRmmEMETQNQINSNHLRRAEQE 618
Cdd:TIGR04523 420 EKELLEKEIERLKETIIknnSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN--KIKQNLEQKQKELKSKEKE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 619 VISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKeevmavrlreadsiaavaelrqhiaelEIQKEEGKLQGQLNKS 698
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK---------------------------EKESKISDLEDELNKD 550
|
330 340
....*....|....*....|....
gi 815891150 699 DSNQYIGELKDQIAELNHELRCLK 722
Cdd:TIGR04523 551 DFELKKENLEKEIDEKNKEIEELK 574
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
393-726 |
1.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 393 KLIQAAYQVKynsKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADrliqhkcssnynedfvL 472
Cdd:PRK03918 183 KFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----------------L 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 473 QLEKELVQARlseaesqcaLKEMQDKVLDIEKRnnslpdennIARLQEEliavklreaeaimgLKELRQQVKDLEE-HWQ 551
Cdd:PRK03918 244 EKELESLEGS---------KRKLEEKIRELEER---------IEELKKE--------------IEELEEKVKELKElKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 552 RHLARTTGRWKDppkknamnELQDELMTIRLREAETQAEIREIKQRMMEMETQNqinsNHLRRAEQEVISLQEKVQYLsa 631
Cdd:PRK03918 292 AEEYIKLSEFYE--------EYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRLEEL-- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 632 qnKGLLTQLSEAKRKQAEIEcknkeevmavRLREADSIAAVAELRQHIAELEIQKEEgkLQGQLNKsdSNQYIGELKDQI 711
Cdd:PRK03918 358 --EERHELYEEAKAKKEELE----------RLKKRLTGLTPEKLEKELEELEKAKEE--IEEEISK--ITARIGELKKEI 421
|
330
....*....|....*
gi 815891150 712 AELNHELRCLKGQRG 726
Cdd:PRK03918 422 KELKKAIEELKKAKG 436
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
429-725 |
4.42e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 429 IKRLR--TENRLLKQRIETLEKESASLADRLIQHKCSSNYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKRn 506
Cdd:PRK02224 178 VERVLsdQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 507 nslpdENNIARLQEElIAVKLREAEAIMG-LKELRQQVKDLEEHwQRHLARTTGRwkDPPKKNAMNELQDELMTirlREA 585
Cdd:PRK02224 257 -----EAEIEDLRET-IAETEREREELAEeVRDLRERLEELEEE-RDDLLAEAGL--DDADAEAVEARREELED---RDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 586 ETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIEcKNKEEVMA----- 660
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE-EEIEELRErfgda 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 661 --------------------VRLREADSIAAVAELRQHIAELEIQKEEGKLQ--GQ-LNKSDSNQYIGELKDQIAELNHE 717
Cdd:PRK02224 404 pvdlgnaedfleelreerdeLREREAELEATLRTARERVEEAEALLEAGKCPecGQpVEGSPHVETIEEDRERVEELEAE 483
|
....*...
gi 815891150 718 LRCLKGQR 725
Cdd:PRK02224 484 LEDLEEEV 491
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
411-722 |
4.91e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 411 LEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQHKCSSNYNEDFVLQLEKELVQ--ARLSEA-- 486
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEkkSRLEEKir 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 487 ESQCALKEMQDKVLDIEKR---------NNSLPDENNIARLQEELIAVKLREAEaimgLKELRQQVKDLEEHWQR-HLAR 556
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRkeyleseeiNKSINEYNKIESARADLEDIKIKINE----LKDKHDKYEEIKNRYKSlKLED 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 557 TTGRWKDPPKKNAMNELQDeLMTIRLREAETQAEIREIKQRMMEMETQ----NQINSNHLRRAEQEVISLQEKVqylsaq 632
Cdd:PRK01156 563 LDSKRTSWLNALAVISLID-IETNRSRSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNKY------ 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 633 nkglltQLSEAKRKQAEiECKNKEEVMAVRLREADSIA-AVAELRQHIaeLEIQKEEGKLQGQLNKSDSNQY-------- 703
Cdd:PRK01156 636 ------NEIQENKILIE-KLRGKIDNYKKQIAEIDSIIpDLKEITSRI--NDIEDNLKKSRKALDDAKANRArlestiei 706
|
330 340
....*....|....*....|...
gi 815891150 704 ----IGELKDQIAELNHELRCLK 722
Cdd:PRK01156 707 lrtrINELSDRINDINETLESMK 729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
437-621 |
6.85e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 437 RLLKQRIETLEKESASLADRLIQHKcssnynedfvlQLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDENNIA 516
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYA-----------ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 517 RLQEELIAVKLREAEAIMGLKELRQQVKDLE------EHWQRHLARTTGRWkDPPKKNAMNELQDELMTIRLREAETQAE 590
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEeleaelAELQEELEELLEQL-SLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190
....*....|....*....|....*....|..
gi 815891150 591 IREIKQRMMEMETQ-NQINSNHLRRAEQEVIS 621
Cdd:COG4717 215 LEEAQEELEELEEElEQLENELEAAALEERLK 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
405-692 |
1.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 405 SKKMKKLEKEYTTIKTKEMEEQVEIKRLrtENRLLKQRIETLEKESAsladrliqhkcssnyneDFVLQLEKELVQARLS 484
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKELA-----------------EQLKELEEKLKKYNLE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 485 EAESQCA-LKEMQDKVLDIEKRNNSLPDE-NNIARLQEELIAV--KLREAEAIMG-------------LKELRQQVKDLE 547
Cdd:PRK03918 519 ELEKKAEeYEKLKEKLIKLKGEIKSLKKElEKLEELKKKLAELekKLDELEEELAellkeleelgfesVEELEERLKELE 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 548 EHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETqnqinsnhlRRAEQEVISLQEKVQ 627
Cdd:PRK03918 599 PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK---------KYSEEEYEELREEYL 669
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 815891150 628 YLSAQNKGLLTQLSEAKRKQAEIEC------KNKEEVMAVRLREAD---SIAAVAELRQHIAELEIQKEEGKLQ 692
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKtleklkEELEEREKAKKELEKlekALERVEELREKVKKYKALLKERALS 743
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
419-678 |
1.12e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 419 KTKEMEEQVEIKR---LRTENRLLK-QRIETLEKESASLADRL--IQHKCSSNYNEDFVLQLEKELVQARLSEAESQCAL 492
Cdd:pfam10174 518 KLKSLEIAVEQKKeecSKLENQLKKaHNAEEAVRTNPEINDRIrlLEQEVARYKEESGKAQAEVERLLGILREVENEKND 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 493 KEmqDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTgrwkdppkkNAMNE 572
Cdd:pfam10174 598 KD--KKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELM---------GALEK 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 573 LQDELMTIRLREAETQAEIREiKQRMMEmetqnqiNSNHLRRAEQEVIsLQEKVQYLSA------QNKGLLtQLSEAKRK 646
Cdd:pfam10174 667 TRQELDATKARLSSTQQSLAE-KDGHLT-------NLRAERRKQLEEI-LEMKQEALLAaisekdANIALL-ELSSSKKK 736
|
250 260 270
....*....|....*....|....*....|..
gi 815891150 647 qaeiecKNKEEVMAVRlREADSIaaVAELRQH 678
Cdd:pfam10174 737 ------KTQEEVMALK-REKDRL--VHQLKQQ 759
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
412-697 |
1.19e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 412 EKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLeKESASLADRLIqhkcssnyneDFVLQLEKELVQARLSEAESQca 491
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQA-KEGLSALNRLL----------PRLNLLADETLADRVEEIREQ-- 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 492 LKEMQDKVLDIEKRNNSLPD-ENNIARLQ---EELIAVKLREAEAIMGLKELRQQVKDLEEHWQR--HLArttgrWKDPP 565
Cdd:PRK04863 903 LDEAEEAKRFVQQHGNALAQlEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRraHFS-----YEDAA 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 566 KK-NAMNELQDELMTiRLREAETQAeiREIKQRMMEMETQnqinsnhLRRAEQEVISLQEkvqylSAQNKglLTQLSEAK 644
Cdd:PRK04863 978 EMlAKNSDLNEKLRQ-RLEQAEQER--TRAREQLRQAQAQ-------LAQYNQVLASLKS-----SYDAK--RQMLQELK 1040
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 815891150 645 RKQAEI---ECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNK 697
Cdd:PRK04863 1041 QELQDLgvpADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKK 1096
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
513-719 |
1.46e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 513 NNIARL-QEELIAVKLREAEAIMG-----LKELRQQVKDLEEHWQRHLARTTGRwkDPPKK-----NAMNELQDELMTIR 581
Cdd:COG3206 155 NALAEAyLEQNLELRREEARKALEfleeqLPELRKELEEAEAALEEFRQKNGLV--DLSEEaklllQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 582 LREAETQAEIREIKQRmmemetqnqinsnhLRRAEQEVISLQEkvqylSAQNKGLLTQLSEAKRKQAEiecknkeevMAV 661
Cdd:COG3206 233 AELAEAEARLAALRAQ--------------LGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAE---------LSA 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815891150 662 RLREADSiaAVAELRQHIAELE--IQKEEGKLQGQL--NKSDSNQYIGELKDQIAELNHELR 719
Cdd:COG3206 285 RYTPNHP--DVIALRAQIAALRaqLQQEAQRILASLeaELEALQAREASLQAQLAQLEARLA 344
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-648 |
1.48e-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: 41.67 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 391 PDKLIQAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIqhkcssnynedf 470
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 471 vlQLEKELVQARLSEAESQCALKEMqDKVLDIEKRNNSLP------DENNIARLQEELIAVKLREAEAIMGLKELRQQVK 544
Cdd:COG4942 87 --ELEKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 545 DLEEHWQRHLARttgrwkdppKKNAMNELQDELMTIRLREAETQAEIREIKQRmmemetqnqinsnhLRRAEQEVISLQE 624
Cdd:COG4942 164 ALRAELEAERAE---------LEALLAELEEERAALEALKAERQKLLARLEKE--------------LAELAAELAELQQ 220
|
250 260
....*....|....*....|....
gi 815891150 625 KVQYLSAQNKGLLTQLSEAKRKQA 648
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTP 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
406-724 |
1.52e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 406 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQHKCSSNYNE-----DFVLQLEKELVQ 480
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElperlEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 481 ARLSEAESQCALKEMQDKvLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwQRHLARTTGR 560
Cdd:COG4717 161 LEEELEELEAELAELQEE-LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE--ELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 561 WKDPPKKNAMNE----LQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGL 636
Cdd:COG4717 238 AAALEERLKEARllllIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 637 LTQLSEAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSN-----QYIGELKDQI 711
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEdeeelRAALEQAEEY 397
|
330
....*....|...
gi 815891150 712 AELNHELRCLKGQ 724
Cdd:COG4717 398 QELKEELEELEEQ 410
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
567-724 |
1.54e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 567 KNAMNELQDELMTIR--LREAEtqAEIREIKQR--MMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSE 642
Cdd:COG3206 174 RKALEFLEEQLPELRkeLEEAE--AALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 643 AKRKQAEIecKNKEEVMAVRLREADSIAAVAELRQ-----HIAELEIQKEEGKLQGQLnKSDSNQYIGELKDQIAELNHE 717
Cdd:COG3206 252 GPDALPEL--LQSPVIQQLRAQLAELEAELAELSArytpnHPDVIALRAQIAALRAQL-QQEAQRILASLEAELEALQAR 328
|
....*..
gi 815891150 718 LRCLKGQ 724
Cdd:COG3206 329 EASLQAQ 335
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
392-718 |
1.74e-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: 41.93 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 392 DKLIQAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLL-------KQRIETLEKESASLADRLIQHKCSS 464
Cdd:TIGR04523 61 KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKInseikndKEQKNKLEVELNKLEKQKKENKKNI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 465 NYNEDFVLQLEKELvqarlseAESQCALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLReaeaimgLKELRQQVK 544
Cdd:TIGR04523 141 DKFLTEIKKKEKEL-------EKLNNKYNDLKKQKEELENELNLL--EKEKLNIQKNIDKIKNK-------LLKLELLLS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 545 DLEEHWQRHLARTTgrwKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQE 624
Cdd:TIGR04523 205 NLKKKIQKNKSLES---QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 625 KVQYLSAQNKGLLTQLSEAKR-KQAEIECKNKEEvmavrlreadsiaavaelrqhIAELEIQKEEgkLQGQLNKsdSNQY 703
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNqKEQDWNKELKSE---------------------LKNQEKKLEE--IQNQISQ--NNKI 336
|
330
....*....|....*
gi 815891150 704 IGELKDQIAELNHEL 718
Cdd:TIGR04523 337 ISQLNEQISQLKKEL 351
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
433-706 |
1.76e-03 |
|
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: 41.39 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 433 RTENRLLKQRIETLEKES-ASLADRliQHKCSSNYNEDFVLQLEKelvqaRLSEAESQCALKEMQDKVLDIEKRNNSLPD 511
Cdd:pfam08017 41 RSQGNVLERRQRDAENRSqGNVLER--RQRDAENRSQGNVLERRQ-----RDAENRSQGNVLERRQRDAENRSQGNVLER 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 512 ENNIARLQEELIAVKLREAEAimglkELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAE--TQA 589
Cdd:pfam08017 114 RQRDAENKSQGNVLERRQRDA-----ENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEnkSQG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 590 EIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKgllTQLSEAKRKQAEIECKNKEEVMAVRLREAD-- 667
Cdd:pfam08017 189 NVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENR---SQGNVLERRQRDAENKSQGNVLERRQRDAEnr 265
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 815891150 668 SIAAVAELRQHIAELEIQKE--EGKLQGQLNKSDSNQYIGE 706
Cdd:pfam08017 266 SQGNVLERRQRDAENRSQGNvlERRQRDAENKSQVGQLIGK 306
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
413-726 |
1.78e-03 |
|
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: 42.08 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 413 KEYTTIKTKEMEEQVEikrlrTENRLLKQRIETLEKESASLADRLiqhkcssnyNEDFVLQLEKELVQARLS--EAESQC 490
Cdd:pfam01576 10 KEEELQKVKERQQKAE-----SELKELEKKHQQLCEEKNALQEQL---------QAETELCAEAEEMRARLAarKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 491 ALKEMQDKVLDIEKRNNSLPDENniarlqeeliavklreaeaimglKELRQQVKDLEEHW-QRHLARTTGRWKDPPKKNA 569
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEK-----------------------KKMQQHIQDLEEQLdEEEAARQKLQLEKVTTEAK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 570 MNELQDELMTIRLREAETQAEIREIKQRMMEMETQnqinsnhLRRAEQEVISLQEkvqyLSAQNKGLLTQLS-----EAK 644
Cdd:pfam01576 133 IKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN-------LAEEEEKAKSLSK----LKNKHEAMISDLEerlkkEEK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 645 RKQAEIECKNKEEVMAVRLREAdsiaaVAELRQHIAELEIQ--KEEGKLQGQLNKSDSNQ--------YIGELKDQIAEL 714
Cdd:pfam01576 202 GRQELEKAKRKLEGESTDLQEQ-----IAELQAQIAELRAQlaKKEEELQAALARLEEETaqknnalkKIRELEAQISEL 276
|
330
....*....|..
gi 815891150 715 NHELRCLKGQRG 726
Cdd:pfam01576 277 QEDLESERAARN 288
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
474-692 |
2.07e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 474 LEKEL--VQARLSEAESqcALKEMQDK--VLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEeh 549
Cdd:COG3206 180 LEEQLpeLRKELEEAEA--ALEEFRQKngLVDLSEEAKLL--LQQLSELESQLAEARAELAEAEARLAALRAQLGSGP-- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 550 wqrhlarttgrwkdppkkNAMNELQD--ELMTIRLREAETQAEIREIKQRMMEmetqnqinsNHlrraeQEVISLQEKVQ 627
Cdd:COG3206 254 ------------------DALPELLQspVIQQLRAQLAELEAELAELSARYTP---------NH-----PDVIALRAQIA 301
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815891150 628 YLSAQNKglltqlSEAKRKQAEIEcknkEEVMAVRLREADSIAAVAELRQHIAEL-EIQKEEGKLQ 692
Cdd:COG3206 302 ALRAQLQ------QEAQRILASLE----AELEALQAREASLQAQLAQLEARLAELpELEAELRRLE 357
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
406-725 |
2.23e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 406 KKMKKLEKEYTTIKTK--EMEEQV-EIKRLRTENRLLKQRIETLEKESASLADRLiqhkcsSNYNEDFVLQLEKELVQAR 482
Cdd:COG4717 132 QELEALEAELAELPERleELEERLeELRELEEELEELEAELAELQEELEELLEQL------SLATEEELQDLAEELEELQ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 483 LSEAESQCALKEMQDKVLDIEKRNNSLPDENNIARLQEEL--IAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTG- 559
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLkeARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGl 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 560 ----RWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKV--------- 626
Cdd:COG4717 286 lallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAeeleeelql 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 627 QYLSAQNKGLLTQLS-------EAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNKSD 699
Cdd:COG4717 366 EELEQEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
330 340
....*....|....*....|....*.
gi 815891150 700 SNqyIGELKDQIAELNHELRCLKGQR 725
Cdd:COG4717 446 EE--LEELREELAELEAELEQLEEDG 469
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
475-693 |
2.28e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 475 EKELVQARLSEAESQCALKEMQDKVLD-IEKRNNSLPDE-----NNIARLQEELIAVkLREAEAIMGLKELRQQVKDLEE 548
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEETEqLKQQLAQAPAKlrqaqAELEALKDDNDEE-TRETLSTLSLRQLESRLAQTLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 549 HWQRhlarttgrwkdppKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQ---NQINSNHLR-------RAEQE 618
Cdd:PRK11281 136 QLQN-------------AQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLlkgGKVGGKALRpsqrvllQAEQA 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815891150 619 VISLQEKVQYLSAQNKGLLTQLSEAKRKQAeIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQG 693
Cdd:PRK11281 203 LLNAQNDLQRKSLEGNTQLQDLLQKQRDYL-TARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQA 276
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
512-725 |
2.35e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 512 ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGrwkdppKKNAMNELQDELmtirlreAETQAEI 591
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA------LQAEIDKLQAEI-------AEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 592 REIKQRMMEMETQNQINSNHLRRAE--------QEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEiecknkeevmavrl 663
Cdd:COG3883 82 EERREELGERARALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA-------------- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815891150 664 READSIAAVAELRQHIAELEIQKEEgkLQGQlnKSDSNQYIGELKDQIAELNHELRCLKGQR 725
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAE--LEAQ--QAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
424-692 |
4.01e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 424 EEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQHKcssnyneDFVLQLEKElvqarLSEAESQCALKEMQDKvlDIE 503
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETEREREELAEEVRDLR-------ERLEELEEE-----RDDLLAEAGLDDADAE--AVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 504 KRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRhlarttgrwkdppKKNAMNELQDELMTIR-- 581
Cdd:PRK02224 314 ARREEL--EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE-------------LREEAAELESELEEARea 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 582 LREAETQ-----AEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKE 656
Cdd:PRK02224 379 VEDRREEieeleEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECG 458
|
250 260 270
....*....|....*....|....*....|....*.
gi 815891150 657 EvmavRLREADSIAAVAELRQHIAELEIQKEEGKLQ 692
Cdd:PRK02224 459 Q----PVEGSPHVETIEEDRERVEELEAELEDLEEE 490
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
406-548 |
4.14e-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: 39.52 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 406 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQHKCSSNYNEdfvLQLEKELVQARLSE 485
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA---LQKEIESLKRRISD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815891150 486 AESQcaLKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKlREAEAImgLKELRQQVKDLEE 548
Cdd:COG1579 108 LEDE--ILELMERIEELEEELAEL--EAELAELEAELEEKK-AELDEE--LAELEAELEELEA 163
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
421-677 |
4.58e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 421 KEMEEQV---EIKRLRTENRLLKQRIETL-----EKES---------ASLADRLIQHKCSSNYNE-------DFVLQLEK 476
Cdd:pfam10174 459 REREDRErleELESLKKENKDLKEKVSALqpeltEKESslidlkehaSSLASSGLKKDSKLKSLEiaveqkkEECSKLEN 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 477 ELVQARLSEAESQcALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKElrQQVKDLEEHWQRHLar 556
Cdd:pfam10174 539 QLKKAHNAEEAVR-TNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD--KKIAELESLTLRQM-- 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 557 ttgrwKDPPKKNAMNELQDELMtiRLREAETQAEIREIKQRMMEMETQNQINS--NHLRRAEQEVISLQEKV---QYLSA 631
Cdd:pfam10174 614 -----KEQNKKVANIKHGQQEM--KKKGAQLLEEARRREDNLADNSQQLQLEElmGALEKTRQELDATKARLsstQQSLA 686
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 815891150 632 QNKGLLTQLSEAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQ 677
Cdd:pfam10174 687 EKDGHLTNLRAERRKQLEEILEMKQEALLAAISEKDANIALLELSS 732
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
424-646 |
4.83e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 424 EEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQHKCSSNYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIE 503
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 504 KRnnslpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwqrhlarttgrwkdppkknaMNELQDELMTIRLR 583
Cdd:COG1196 709 LA------EAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL---------------------LEEEALEELPEPPD 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815891150 584 EAETQAEIREIKQRMMEMETQNQinsnhlrRAEQEVISLQEKVQYLSAQnkglLTQLSEAKRK 646
Cdd:COG1196 762 LEELERELERLEREIEALGPVNL-------LAIEEYEELEERYDFLSEQ----REDLEEARET 813
|
|
| DUF1129 |
pfam06570 |
Protein of unknown function (DUF1129); This family consists of several hypothetical bacterial ... |
464-504 |
5.16e-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: 39.18 E-value: 5.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 815891150 464 SNYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEK 504
Cdd:pfam06570 3 TKKNQDYIFRLTKQLIKDGKSDEEIKEILDEMLPEILEGQK 43
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
435-719 |
6.00e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 435 ENRLlkqrieTLE--KESASLAD---RLI---QHKCSSNY----NE-----DFVLQLEKELVQARLSEAESQCALKEMQD 497
Cdd:COG3096 240 ENRM------TLEaiRVTQSDRDlfkHLIteaTNYVAADYmrhaNErrelsERALELRRELFGARRQLAEEQYRLVEMAR 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 498 KVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAImglkELRQQvkDLEEHWQRhLARTTGrwkdppkknAMNELQDEL 577
Cdd:COG3096 314 ELEELSARESDLEQDYQAASDHLNLVQTALRQQEKI----ERYQE--DLEELTER-LEEQEE---------VVEEAAEQL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 578 MTIRLREAETQAEIREIK------------------------QRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQN 633
Cdd:COG3096 378 AEAEARLEAAEEEVDSLKsqladyqqaldvqqtraiqyqqavQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEV 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 634 KGLLTQLSEAKRKQAEIE------CKNKEEVMAVR--------LREADSIAAVAE----LRQHIAELE----IQKEEGKL 691
Cdd:COG3096 458 LELEQKLSVADAARRQFEkayelvCKIAGEVERSQawqtarelLRRYRSQQALAQrlqqLRAQLAELEqrlrQQQNAERL 537
|
330 340 350
....*....|....*....|....*....|....*..
gi 815891150 692 QGQLNKSDSNQY---------IGELKDQIAELNHELR 719
Cdd:COG3096 538 LEEFCQRIGQQLdaaeeleelLAELEAQLEELEEQAA 574
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
407-725 |
6.24e-03 |
|
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: 40.10 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 407 KMKKLEKEYTTIKTK---EMEEQVEIKRLRTEN----RLLKQRIETLEKESASLADRLIQHKCSSNYNEDFVLQLEKELV 479
Cdd:pfam15921 427 EVQRLEALLKAMKSEcqgQMERQMAAIQGKNESlekvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 480 QARLSEAESQCALKEMQDKV-LDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHlARTT 558
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQH-GRTA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 559 G--RWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRM--MEMETQNQINSNHLR-RAEQEVisLQEKVQYLS--A 631
Cdd:pfam15921 586 GamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVsdLELEKVKLVNAGSERlRAVKDI--KQERDQLLNevK 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 632 QNKGLLTQLSEA--------KRKQAEIECKNKEevMAVRLREADSiaAVAELRQHIAELE------------IQKEEGKL 691
Cdd:pfam15921 664 TSRNELNSLSEDyevlkrnfRNKSEEMETTTNK--LKMQLKSAQS--ELEQTRNTLKSMEgsdghamkvamgMQKQITAK 739
|
330 340 350
....*....|....*....|....*....|....
gi 815891150 692 QGQLNKSDSNqyIGELKDQIAELNHELRCLKGQR 725
Cdd:pfam15921 740 RGQIDALQSK--IQFLEEAMTNANKEKHFLKEEK 771
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
400-719 |
6.79e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 400 QVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQHKCSSNYNEDFVLQLEKELV 479
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 480 QARLSEAESQCALKEMQDKVL----------------------------DIEKRNNSLPDENNIARLQEELIAVKLREAE 531
Cdd:PRK02224 423 ELREREAELEATLRTARERVEeaealleagkcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEERLERAE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 532 AIM----GLKELRQQVKDLEEHWQRHLARTTG-RWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQ 606
Cdd:PRK02224 503 DLVeaedRIERLEERREDLEELIAERRETIEEkRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 607 INSNHLRR-------------AEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEevmavrlreadsiAAVA 673
Cdd:PRK02224 583 ELKERIESlerirtllaaiadAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE-------------ARIE 649
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 815891150 674 ELRQHIAELE--IQKEEGKLQGQLNKSDSNQ-YIGELKDQIAELNhELR 719
Cdd:PRK02224 650 EAREDKERAEeyLEQVEEKLDELREERDDLQaEIGAVENELEELE-ELR 697
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
473-715 |
8.19e-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: 39.82 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 473 QLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLpdENNIARLQ---------EELIAVKLREAEAimGLKELRQQV 543
Cdd:pfam12128 217 RLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTL--ESAELRLShlhfgyksdETLIASRQEERQE--TSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 544 KDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLReaetQAEIREIKQRMMEMETQNQINSNhlrraeqevISLQ 623
Cdd:pfam12128 293 RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG----AFLDADIETAAADQEQLPSWQSE---------LENL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 624 EKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEEVMAVRLreaDSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQY 703
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL---AKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
|
250
....*....|....
gi 815891150 704 IGE--LKDQIAELN 715
Cdd:pfam12128 437 EEEyrLKSRLGELK 450
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
583-696 |
9.12e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 38.01 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891150 583 REAETQAEIREIKQRMMEMETQnqinsnhLRRAEQEVISLQEKVQYLSAQNKglltqlSEAKRKQAEIECKNKEEVMAVR 662
Cdd:PRK07352 51 RREAILQALKEAEERLRQAAQA-------LAEAQQKLAQAQQEAERIRADAK------ARAEAIRAEIEKQAIEDMARLK 117
|
90 100 110
....*....|....*....|....*....|....*....
gi 815891150 663 ---LREADSIA--AVAELRQHIAELEIQKEEGKLQGQLN 696
Cdd:PRK07352 118 qtaAADLSAEQerVIAQLRREAAELAIAKAESQLPGRLD 156
|
|
| |
