|
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 |
2.36e-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: 264.94 E-value: 2.36e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 160 VHKGIPHHFRAIVWQLLCSAQSMPI---KDQYSELLKMTSPCEKL----IRRDIARTYPEHNFFKEKDSLGQEVLFNVMK 232
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDTsadKDLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 233 AYSLVDREVGYCQGSAFIVGLLLMQMP-EEEAFCVFVKLMQDYRLReLFKPSMAELGLCMYQFECMIQEHLPELFVHFQS 311
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3093476 312 QSFHTSMYASSWFLTIFLTTFPLPVATRIFDIFMSEGLEIVFRVGLALLQMNQAELM 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 |
1.82e-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: 188.62 E-value: 1.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 200 KLIRRDIARTYPEHNFFKEKDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQ-MPEEEAFCVFVKLMQDYRLRE 278
Cdd:pfam00566 10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 279 LFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPVATRIFDIFMSEGLEIV-FRVGL 357
Cdd:pfam00566 88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
|
170
....*....|.
gi 3093476 358 ALLQMNQAELM 368
Cdd:pfam00566 168 AILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
131-377 |
1.99e-43 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 164.59 E-value: 1.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 131 EEDSWILWGRIVN-EWEDVRKKKEKQVKELVHKGIPHHFRAIVWQLLcsAQSMPIKDQ----YSELLKM-------TSPC 198
Cdd:COG5210 179 ELAADKLWISYLDpNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFL--LGIGFDLDKnpglYERLLNLhreakipTQEI 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 199 EKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEE-AFCVFVKLMQDYRLR 277
Cdd:COG5210 257 ISQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLP 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 278 ELFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPVATRIFDIFMSEGLEIVFRVGL 357
Cdd:COG5210 337 GYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLAL 416
|
250 260
....*....|....*....|
gi 3093476 358 ALLQMNQAELMQLDMEGMLQ 377
Cdd:COG5210 417 AILKLLRDKLLKLDSDELLD 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
400-707 |
2.02e-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: 61.23 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 400 QVQYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETL-----EKHKCSSNYNEDFVlQLEKELVQARLSE 474
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeleELSRQISALRKDLA-RLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 475 AESQCALKEMQDKVLDIEKRNNSLPD-----ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGR 549
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 550 WKD-PPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQ 628
Cdd:TIGR02168 830 ERRiAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3093476 629 LSEAKRKQaeIECKNKEEVMAVRLREADsiAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQyigELKDQIAELNHEL 707
Cdd:TIGR02168 910 RSELRREL--EELREKLAQLELRLEGLE--VRIDNLQERLSEEYSLTLEEAEALENKIEDDEE---EARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
492-707 |
3.44e-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: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 492 EKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwQRHLARTTGRWKDPPKKNAMNELQDELMTIRL 571
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE--ELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 572 RE---AETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIecknKEEVM 648
Cdd:TIGR02168 745 LEeriAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL----NEEAA 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3093476 649 AVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNksdsNQYIGELKDQIAELNHEL 707
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----AAEIEELEELIEELESEL 875
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
361-675 |
2.61e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.82 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 361 QMNQAELMQLDMEGMLQHFQKVIphqfdgvpdkliqaayqVQYNSKKMKKLEKE--YTTIKTKEMEEQVE--IKRLRTEN 436
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSIL-----------------VDFEEASGKKIYEHdsMSTMHFRSLGSAISkiLRELDTEI 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 437 RLLKQRI----ETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKRNNSLPDENNI----ARLQ 508
Cdd:pfam15921 234 SYLKGRIfpveDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEIiqeqARNQ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 509 EELIAVKLREAEAIMG-----LKELRQQVKDLEEHWQRHL---------ARTTGRWKDPPKKNAMNELQDELMTIRLREA 574
Cdd:pfam15921 312 NSMYMRQLSDLESTVSqlrseLREAKRMYEDKIEELEKQLvlanselteARTERDQFSQESGNLDDQLQKLLADLHKREK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 575 ETQAEiREIKQRMMEMETQNQINSNHLRRaeqEVISLQEKVQYLSAQNKGLLTQLS-EAKRKQAEIECKNKEevmavrLR 653
Cdd:pfam15921 392 ELSLE-KEQNKRLWDRDTGNSITIDHLRR---ELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNES------LE 461
|
330 340
....*....|....*....|....*..
gi 3093476 654 EADSIAAVAE-----LRQHIAELEIQK 675
Cdd:pfam15921 462 KVSSLTAQLEstkemLRKVVEELTAKK 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
406-708 |
3.76e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 406 KKMKKLEKE------YTTIKTKEMEEQVE-----IKRLRTENRLLKQRIETLEKHKCSSNYNEDfvlQLEKELVQARLSE 474
Cdd:COG1196 200 RQLEPLERQaekaerYRELKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELA---ELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 475 AESQCALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwqrhlarttgrwkdpp 554
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARL--EQDIARLEERRRELEERLEELEEELAELEEELEELEE----------------- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 555 kknAMNELQDELMTIRLREAETQAEIREIKQRmmemetqnqinsnhLRRAEQEVISLQEKvqyLSAQNKGLLTQLSEAKR 634
Cdd:COG1196 338 ---ELEELEEELEEAEEELEEAEAELAEAEEA--------------LLEAEAELAEAEEE---LEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3093476 635 KQAEIEckNKEEVMAVRLREADSI-AAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAELNHELR 708
Cdd:COG1196 398 LAAQLE--ELEEAEEALLERLERLeEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
406-664 |
1.48e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 406 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFV------LQLEKELVQARLSEAESQC 479
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskldeLAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 480 A-----LKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKDpP 554
Cdd:TIGR02168 354 EsleaeLEELEAELEELESRLEEL--EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK-L 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 555 KKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQnqinsnhLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKR 634
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREE-------LEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
250 260 270
....*....|....*....|....*....|
gi 3093476 635 KQAEIecknkEEVMAVRLREADSIAAVAEL 664
Cdd:TIGR02168 504 FSEGV-----KALLKNQSGLSGILGVLSEL 528
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
503-714 |
1.51e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 503 NIARLQEELIavKLREAEAIMglKELRQQVKDLE---EHWQRHLArttgrwkdppKKNAMNELQDELMTIRLREAET--- 576
Cdd:COG4913 226 AADALVEHFD--DLERAHEAL--EDAREQIELLEpirELAERYAA----------ARERLAELEYLRAALRLWFAQRrle 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 577 --QAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEiECKNKEEVMAVRLRE 654
Cdd:COG4913 292 llEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3093476 655 -----ADSIAAVAELRQHIAEL--EIQKEEGKLQGQLNKSDSNQYigELKDQIAELNHELRCLKGQK 714
Cdd:COG4913 371 lglplPASAEEFAALRAEAAALleALEEELEALEEALAEAEAALR--DLRRELRELEAEIASLERRK 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
501-708 |
2.05e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 501 ENNIARLQEEliAVKLREAeaimglKELRQQVKDLE-EHWQRHLARTTGRWKDppKKNAMNELQDELMTIRLREAETQAE 579
Cdd:COG1196 199 ERQLEPLERQ--AEKAERY------RELKEELKELEaELLLLKLRELEAELEE--LEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 580 IREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIEckNKEEVMAVRLREADSIA 659
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE--EELEELEEELEELEEEL 346
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 3093476 660 AVAELRQHIAELEIQKEEGKLQGQLNKSDSNQyiGELKDQIAELNHELR 708
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAE--EELEELAEELLEALR 393
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
423-633 |
4.79e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 423 MEEQVEIKRLRTENRL--LKQRIETLE---------------KHKCSS-----NYNEDFVLQLEKELVQARLSEAESQCA 480
Cdd:COG3206 162 LEQNLELRREEARKALefLEEQLPELRkeleeaeaaleefrqKNGLVDlseeaKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 481 LKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGL-------KELRQQVKDLEEHWQRHLARttgrwkdp 553
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQR-------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 554 pkknAMNELQDELMTIRLREAETQAEIREIKQRMMEmetqnqinsnhLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAK 633
Cdd:COG3206 314 ----ILASLEAELEALQAREASLQAQLAQLEARLAE-----------LPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
393-715 |
5.84e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 393 KLIQAAYQVQynsKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKElvqarl 472
Cdd:PRK03918 183 KFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS------ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 473 seaesqcaLKEMQDKVLDIEKRnnslpdennIARLQEEliavklreaeaimgLKELRQQVKDLEE-HWQRHLARTTGRWK 551
Cdd:PRK03918 254 --------KRKLEEKIRELEER---------IEELKKE--------------IEELEEKVKELKElKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 552 DppkknamnELQDELMTIRLREAETQAEIREIKQRMMEMETQNqinsNHLRRAEQEVISLQEKVQYLsaqnKGLLTQLSE 631
Cdd:PRK03918 303 E--------EYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRLEEL----EERHELYEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 632 AKRKQAEIEcknkeevmavRLREADSIAAVAELRQHIAELEIQKEEgkLQGQLNKsdSNQYIGELKDQIAELNHELRCLK 711
Cdd:PRK03918 367 AKAKKEELE----------RLKKRLTGLTPEKLEKELEELEKAKEE--IEEEISK--ITARIGELKKEIKELKKAIEELK 432
|
....
gi 3093476 712 GQKG 715
Cdd:PRK03918 433 KAKG 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
396-671 |
7.26e-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: 53.14 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 396 QAAYQVQYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSsnyNEDFVLQLEKELVQARLSEA 475
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE---LSEDIESLAAEIEELEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 476 ESQCALKEMQDKVldiekrnnslpdenniARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwqrhlarttgrwkdppk 555
Cdd:TIGR02168 870 ELESELEALLNER----------------ASLEEALALLRSELEELSEELRELESKRSELRR------------------ 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 556 knAMNELQDELMTIRLREAETQAEIREIKQR--------MMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLT 627
Cdd:TIGR02168 916 --ELEELREKLAQLELRLEGLEVRIDNLQERlseeysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIE 993
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 3093476 628 QLSEAKRKQAEIEcKNKEevmavrlreaDSIAAVAELRQHIAEL 671
Cdd:TIGR02168 994 EYEELKERYDFLT-AQKE----------DLTEAKETLEEAIEEI 1026
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
396-677 |
1.10e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.43 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 396 QAAYQVQYNSKKMKKLEKEytTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKELVQARLSEA 475
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQE--RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 476 ESQCALKEMQDKVLDIEKRNNslpdennIARLQEEliavKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKDPPK 555
Cdd:pfam17380 359 KRELERIRQEEIAMEISRMRE-------LERLQME----RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 556 KnamnelQDELMTIRLREAETQAEIREIKQRMMEMETQNQI-----NSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLS 630
Cdd:pfam17380 428 E------QEEARQREVRRLEEERAREMERVRLEEQERQQQVerlrqQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEL 501
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 3093476 631 EAkRKQAEIECKNKEEVMAVRLREADSiAAVAELRQHIAELEIQKEE 677
Cdd:pfam17380 502 EE-RKQAMIEEERKRKLLEKEMEERQK-AIYEEERRREAEEERRKQQ 546
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
506-713 |
2.93e-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: 51.21 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 506 RLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHlarttgRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQ 585
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEEL------RLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 586 RM-------MEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNK---EEVMAVRLREA 655
Cdd:TIGR02168 310 RLanlerqlEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLETLRSKVA 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3093476 656 DSIAAVAELRQHIAELEIQKEEGKL--------QGQLNKSDSNQYIGELKDQIAELNHELRCLKGQ 713
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDrrerlqqeIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
504-708 |
1.14e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 504 IARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKD---PPKKNAMNELQDE----------LMTIR 570
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAElerldassddLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 571 LREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIEC--------- 641
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAverelrenl 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 642 ----------KNKEEVMAVRLREA-------------DSIAAVAELRQHIAELE----IQKEEgKLQGQLNKSdSNQYIG 694
Cdd:COG4913 772 eeridalrarLNRAEEELERAMRAfnrewpaetadldADLESLPEYLALLDRLEedglPEYEE-RFKELLNEN-SIEFVA 849
|
250 260
....*....|....*....|....*
gi 3093476 695 EL-----------KDQIAELNHELR 708
Cdd:COG4913 850 DLlsklrraireiKERIDPLNDSLK 874
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
405-647 |
1.82e-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: 48.53 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 405 SKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKhkcssnynedfvlqlEKELVQARLSEAESQcaLKEM 484
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS---------------ELKELEARIEELEED--LHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 485 QDKVLDIEKRnnslPDENNIARLQEELIAVK---------LREAEAIMGLKEL-RQQVKDLEEHWQRHLARTTGRWKDpp 554
Cdd:TIGR02169 778 EEALNDLEAR----LSHSRIPEIQAELSKLEeevsriearLREIEQKLNRLTLeKEYLEKEIQELQEQRIDLKEQIKS-- 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 555 KKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKR 634
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
250
....*....|...
gi 3093476 635 KQAEIECKNKEEV 647
Cdd:TIGR02169 932 ELSEIEDPKGEDE 944
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
406-714 |
3.90e-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: 47.32 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 406 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKcssNYNEDFVLQLEKELVQARLSEAESQCAL---- 481
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL---NLLEKEKLNIQKNIDKIKNKLLKLELLLsnlk 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 482 ------KEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKL---REAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKD 552
Cdd:TIGR04523 208 kkiqknKSLESQISELKKQNNQL--KDNIEKKQQEINEKTTeisNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 553 ppKKNAMNELQDELMTIRLREA-----ETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLT 627
Cdd:TIGR04523 286 --LEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 628 QLSEaKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAELNHEL 707
Cdd:TIGR04523 364 ELEE-KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI 442
|
....*..
gi 3093476 708 RCLKGQK 714
Cdd:TIGR04523 443 KDLTNQD 449
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
504-714 |
4.17e-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: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 504 IARLQEELIAVKLREAEAIMGLKELRQQVKDLEehwqrhlarttgrwKDPPKKNAMNELQDElmtirLREAETQAEIREI 583
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLR--------------REREKAERYQALLKE-----KREYEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 584 KqrmmEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKqaeIECKNKEEVMAVRLREADSIAAVAE 663
Cdd:TIGR02169 233 E----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK---IKDLGEEEQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3093476 664 LRQHIAELEIQKEEgkLQGQLNKSDSNqyIGELKDQIAELNHELRCLKGQK 714
Cdd:TIGR02169 306 LERSIAEKERELED--AEERLAKLEAE--IDKLLAEIEELEREIEEERKRR 352
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
392-711 |
4.47e-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: 46.94 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 392 DKLIQAAYQVQYNSKKMKKLEKEYTTIKT-----KEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYN----EDFVLQ 462
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSeisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIisqlNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 463 LEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDE-----NNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEE 537
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiknleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 538 HWQRHLARTT---GRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRmmEMETQNQINSNHLRRAEQEVISLQEK 614
Cdd:TIGR04523 427 EIERLKETIIknnSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN--KIKQNLEQKQKELKSKEKELKKLNEE 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 615 VQYLSAQNKGLLTQLSEAKRKQAEIECKNKeevmavrlreadsiaavaelrqhiaelEIQKEEGKLQGQLNKSDSNQYIG 694
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKK---------------------------EKESKISDLEDELNKDDFELKKE 557
|
330
....*....|....*..
gi 3093476 695 ELKDQIAELNHELRCLK 711
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELK 574
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
462-689 |
4.50e-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: 46.68 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 462 QLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLeehwQR 541
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--ERRIAALARRIRALEQELAALEAELAELEKEIAEL----RA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 542 HLARTTGRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSnhLRRAEQEVISLQEKVQYLSAQ 621
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE--LRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 622 NKGLLTQLSEAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELE--IQKEEGKLQGQLNKSDS 689
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEalIARLEAEAAAAAERTPA 245
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
475-668 |
6.03e-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: 45.30 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 475 AESQCALKEMQD---KVLDIEKRNNSLPDEnnIARLQEELIAVKLREAEAIMGLKELRQQVKDLE---EHWQRHLARTTG 548
Cdd:COG1579 3 PEDLRALLDLQEldsELDRLEHRLKELPAE--LAELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 549 RWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEvisLQEKVQYLSAQNKGLLTQ 628
Cdd:COG1579 81 QLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 3093476 629 LSEAKRKQAEIECKNKEEVMAV--RLREADSIAAVAELRQHI 668
Cdd:COG1579 158 LEELEAEREELAAKIPPELLALyeRIRKRKNGLAVVPVEGGA 199
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
525-708 |
6.03e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 525 LKELRQQVKDLEEHWQRHlarttgrwkdppkknamNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNH--LR 602
Cdd:COG4717 73 LKELEEELKEAEEKEEEY-----------------AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqeLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 603 RAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEevmAVRLREADSIAAVAELRQHIAELE-IQKEEGKLQ 681
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEeLQQRLAELE 212
|
170 180
....*....|....*....|....*..
gi 3093476 682 GQLNKSDsnQYIGELKDQIAELNHELR 708
Cdd:COG4717 213 EELEEAQ--EELEELEEELEQLENELE 237
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
410-714 |
1.28e-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: 45.88 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 410 KLEKEYTTIKTK-EMEEQVE--IKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQCALKEMQD 486
Cdd:pfam15921 445 QMERQMAAIQGKnESLEKVSslTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 487 KV-LDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHlARTTG--RWKDPPKKNAMNELQ 563
Cdd:pfam15921 525 RVdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQH-GRTAGamQVEKAQLEKEINDRR 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 564 DELMTIRLREAETQAEIREIKQRM--MEMETQNQINSNHLR-RAEQEVisLQEKVQYLS--AQNKGLLTQLSEA------ 632
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELEARVsdLELEKVKLVNAGSERlRAVKDI--KQERDQLLNevKTSRNELNSLSEDyevlkr 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 633 --KRKQAEIECKNKEevMAVRLREADSiaAVAELRQHIAELE------------IQKEEGKLQGQLNKSDSNqyIGELKD 698
Cdd:pfam15921 682 nfRNKSEEMETTTNK--LKMQLKSAQS--ELEQTRNTLKSMEgsdghamkvamgMQKQITAKRGQIDALQSK--IQFLEE 755
|
330
....*....|....*.
gi 3093476 699 QIAELNHELRCLKGQK 714
Cdd:pfam15921 756 AMTNANKEKHFLKEEK 771
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
406-713 |
1.37e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 406 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKcssnynEDFVLQLEKELVQARLSEAESQcaLKEMQ 485
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL------QLLPLYQELEALEAELAELPER--LEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 486 DKVLDIEKRNNSLPD-ENNIARLQEELiaVKLREAEAIMGLKELRQQVKDLEEHWQRhlarttgrwkdppkknaMNELQD 564
Cdd:COG4717 153 ERLEELRELEEELEElEAELAELQEEL--EELLEQLSLATEEELQDLAEELEELQQR-----------------LAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 565 ELMTIRLREAETQAEIREIKQRMMEMETQNQINSN-------------------------------------------HL 601
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallallglggsllsliltiagvlflvlgllallflLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 602 RRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQ 681
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350
....*....|....*....|....*....|....*..
gi 3093476 682 GQLNKSDSN-----QYIGELKDQIAELNHELRCLKGQ 713
Cdd:COG4717 374 ALLAEAGVEdeeelRAALEQAEEYQELKEELEELEEQ 410
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
392-702 |
1.56e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 392 DKLIQAAYQVQYNSKKMKKLEKEYttiKTKEMEEQVEIKRlRTENrlLKQRIEtlEKHKCSsnynedfvlQLEKELVQAR 471
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAK---KADEAKKKAEEAK-KAEE--AKKKAE--EAKKAD---------EAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 472 LSEaESQCALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELR--QQVKDLEEHWQRHLARTTGR 549
Cdd:PTZ00121 1484 KAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEE 1562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 550 WKDPPKKNAMNElqDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQL 629
Cdd:PTZ00121 1563 KKKAEEAKKAEE--DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3093476 630 SEAKRKQAEIECKNKEEVMAVRlreADSIAAVAELRQHIAElEIQKEE----GKLQGQLNKSDSNQYIGELKDQIAE 702
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIK---AAEEAKKAEEDKKKAE-EAKKAEedekKAAEALKKEAEEAKKAEELKKKEAE 1713
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
439-682 |
1.89e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 439 LKQRIETLEKHKcssnynedfVLQLEKELVQARLSEAESQCALKEMQDKVLD-IEKRNNSLPDE-----NNIARLQEELI 512
Cdd:PRK11281 41 VQAQLDALNKQK---------LLEAEDKLVQQDLEQTLALLDKIDRQKEETEqLKQQLAQAPAKlrqaqAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 513 AVkLREAEAIMGLKELRQQVKDLEEHWQRhlarttgrwkdppKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMET 592
Cdd:PRK11281 112 EE-TRETLSTLSLRQLESRLAQTLDQLQN-------------AQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 593 Q---NQINSNHLR-------RAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAeIECKNKEEVMAVRLREADSIAAVA 662
Cdd:PRK11281 178 LlkgGKVGGKALRpsqrvllQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYL-TARIQRLEHQLQLLQEAINSKRLT 256
|
250 260
....*....|....*....|
gi 3093476 663 ELRQHIAELEIQKEEGKLQG 682
Cdd:PRK11281 257 LSEKTVQEAQSQDEAARIQA 276
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
408-610 |
4.25e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 408 MKKLEKEYTTI-KTKEMEEQVEIKRLRTENRLLKQRIETLEKHKcssnynedfvlQLEKELVQARLSEAESQCALKEMQD 486
Cdd:COG4717 48 LERLEKEADELfKPQGRKPELNLKELKELEEELKEAEEKEEEYA-----------ELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 487 KVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLE------EHWQRHLARTTGRWkDPPKKNAMN 560
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeleaelAELQEELEELLEQL-SLATEEELQ 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3093476 561 ELQDELMTIRLREAETQAEIREIKQRMMEMETQ-NQINSNHLRRAEQEVIS 610
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEElEQLENELEAAALEERLK 246
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
407-714 |
4.92e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 407 KMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLK---QRIETLEKHKCSsnynEDFVLQLEKELVQARLSEAESQcaLKE 483
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKlkeQAKKALEYYQLK----EKLELEEEYLLYLDYLKLNEER--IDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 484 MQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRwkdpPKKNAMNELQ 563
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER----RKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 564 DELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQeviSLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKN 643
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE---LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3093476 644 KE-EVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQ-YIGELKDQIAELNHELRCLKGQK 714
Cdd:pfam02463 395 EElELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQgKLTEEKEELEKQELKLLKDELEL 467
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-586 |
6.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 412 EKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHkcssnynedfVLQLEKELVQA---RLSEAEsqcalKEMQDKV 488
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREE----------LDELEAQIRGNggdRLEQLE-----REIERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 489 LDIEKRnnslpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTgrwkdppkkNAMNELQDELMT 568
Cdd:COG4913 352 RELEER------ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---------EALAEAEAALRD 416
|
170
....*....|....*...
gi 3093476 569 IRLREAETQAEIREIKQR 586
Cdd:COG4913 417 LRRELRELEAEIASLERR 434
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
502-708 |
9.60e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 502 NNIARL-QEELIAVKLREAEAIMG-----LKELRQQVKDLEEHWQRHLARTTGRwkDPPKK-----NAMNELQDELMTIR 570
Cdd:COG3206 155 NALAEAyLEQNLELRREEARKALEfleeqLPELRKELEEAEAALEEFRQKNGLV--DLSEEaklllQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 571 LREAETQAEIREIKQRmmemetqnqinsnhLRRAEQEVISLQEkvqylSAQNKGLLTQLSEAKRKQAEiecknkeevMAV 650
Cdd:COG3206 233 AELAEAEARLAALRAQ--------------LGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAE---------LSA 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3093476 651 RLREADSiaAVAELRQHIAELE--IQKEEGKLQGQL--NKSDSNQYIGELKDQIAELNHELR 708
Cdd:COG3206 285 RYTPNHP--DVIALRAQIAALRaqLQQEAQRILASLeaELEALQAREASLQAQLAQLEARLA 344
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
556-713 |
1.15e-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: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 556 KNAMNELQDELMTIR--LREAEtqAEIREIKQR--MMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSE 631
Cdd:COG3206 174 RKALEFLEEQLPELRkeLEEAE--AALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 632 AKRKQAEIecKNKEEVMAVRLREADSIAAVAELRQ-----HIAELEIQKEEGKLQGQLnKSDSNQYIGELKDQIAELNHE 706
Cdd:COG3206 252 GPDALPEL--LQSPVIQQLRAQLAELEAELAELSArytpnHPDVIALRAQIAALRAQL-QQEAQRILASLEAELEALQAR 328
|
....*..
gi 3093476 707 LRCLKGQ 713
Cdd:COG3206 329 EASLQAQ 335
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
501-714 |
1.37e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 501 ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGrwkdppKKNAMNELQDELmtirlreAETQAEI 580
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA------LQAEIDKLQAEI-------AEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 581 REIKQRMMEMETQNQINSNHLRRAE--------QEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEiecknkeevmavrl 652
Cdd:COG3883 82 EERREELGERARALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA-------------- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3093476 653 READSIAAVAELRQHIAELEIQKEEgkLQGQlnKSDSNQYIGELKDQIAELNHELRCLKGQK 714
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAE--LEAQ--QAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
405-717 |
1.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 405 SKKMKKLEKEYTTIKTKEMEEQvEIKRLRTENRLLKQRIETLEKHKcssnynedfvlqLEKELvqarlSEAESqcALKEM 484
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEK------------LEKEL-----EELEK--AKEEI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 485 QDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRqqvkdlEEHwqrhlarttgrwkdppKKNAMNELQD 564
Cdd:PRK03918 404 EEEISKITARIGEL--KKEIKELKKAIEELKKAKGKCPVCGRELT------EEH----------------RKELLEEYTA 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 565 ELMTIRLREAETQAEIREIKQRMMEMETqnqinsnhLRRAEQEVISLQEKVQYL-SAQNKGLLTQLSEAKRKQAEIEcKN 643
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEK--------VLKKESELIKLKELAEQLkELEEKLKKYNLEELEKKAEEYE-KL 530
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3093476 644 KEEVMAVR---LREADSIAAVAELRQHIAELEIQkeegklqgqlnksdsnqyIGELKDQIAELNHELRclkgQKGFS 717
Cdd:PRK03918 531 KEKLIKLKgeiKSLKKELEKLEELKKKLAELEKK------------------LDELEEELAELLKELE----ELGFE 585
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-640 |
1.99e-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: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 391 PDKLIQAAYQVQYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHkcssnynedfVLQLEKELVQA 470
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----------LAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 471 RLSEAESQCALKEMQDkvlDIEKRNNSLPDENNIARLQEELIAVKLREAE-AIMGLKELRQQVKDLEEHWQRHLArttgr 549
Cdd:COG4942 89 EKEIAELRAELEAQKE---ELAELLRALYRLGRQPPLALLLSPEDFLDAVrRLQYLKYLAPARREQAEELRADLA----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 550 wkdppkknamnELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQL 629
Cdd:COG4942 161 -----------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|.
gi 3093476 630 SEAKRKQAEIE 640
Cdd:COG4942 230 ARLEAEAAAAA 240
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
433-695 |
2.19e-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: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 433 RTENRLLKQRIETLEkHKCSSNYNE----DFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKRN--NSLPDENNIAR 506
Cdd:pfam08017 41 RSQGNVLERRQRDAE-NRSQGNVLErrqrDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSqgNVLERRQRDAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 507 LQEELIAVKLREAEAimglkELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAE--TQAEIREIK 584
Cdd:pfam08017 120 NKSQGNVLERRQRDA-----ENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEnkSQGNVLERR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 585 QRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKgllTQLSEAKRKQAEIECKNKEEVMAVRLREAD--SIAAVA 662
Cdd:pfam08017 195 QRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENR---SQGNVLERRQRDAENKSQGNVLERRQRDAEnrSQGNVL 271
|
250 260 270
....*....|....*....|....*....|....*
gi 3093476 663 ELRQHIAELEIQKE--EGKLQGQLNKSDSNQYIGE 695
Cdd:pfam08017 272 ERRQRDAENRSQGNvlERRQRDAENKSQVGQLIGK 306
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
408-686 |
2.20e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 408 MKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQCA-LKEMQD 486
Cdd:PRK04863 839 LRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRfVQQHGN 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 487 KVLDIEKRNNSL-PDENNIARLQEELiavklreAEAIMGLKELRQQVKDLEEHWQR--HLArttgrWKDPPKK-NAMNEL 562
Cdd:PRK04863 919 ALAQLEPIVSVLqSDPEQFEQLKQDY-------QQAQQTQRDAKQQAFALTEVVQRraHFS-----YEDAAEMlAKNSDL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 563 QDELMTiRLREAETQAeiREIKQRMMEMETQnqinsnhLRRAEQEVISLQEkvqylSAQNKglLTQLSEAKRKQAEI--- 639
Cdd:PRK04863 987 NEKLRQ-RLEQAEQER--TRAREQLRQAQAQ-------LAQYNQVLASLKS-----SYDAK--RQMLQELKQELQDLgvp 1049
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 3093476 640 ECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNK 686
Cdd:PRK04863 1050 ADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKK 1096
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
392-707 |
2.45e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 392 DKLIQAAYQVQYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLE----KEL 467
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelkeKAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 468 VQARLSEaesqcALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTT 547
Cdd:PRK03918 294 EYIKLSE-----FYEEYLDELREIEKRLSRL--EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 548 GRwkdpPKKNAMNELQDELMTIRLREAEtqAEIREIKQRMMEMETQnqinsnhLRRAEQEVISLQEKVqylsAQNKGLLT 627
Cdd:PRK03918 367 AK----AKKEELERLKKRLTGLTPEKLE--KELEELEKAKEEIEEE-------ISKITARIGELKKEI----KELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 628 QLSEAKRK----QAEIECKNKEEVMAVRLREADSIAA-VAELRQHIAELEiqKEEGKLQGQLNKSDSNQYIGELKDQIAE 702
Cdd:PRK03918 430 ELKKAKGKcpvcGRELTEEHRKELLEEYTAELKRIEKeLKEIEEKERKLR--KELRELEKVLKKESELIKLKELAEQLKE 507
|
....*
gi 3093476 703 LNHEL 707
Cdd:PRK03918 508 LEEKL 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
419-621 |
2.65e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 419 KTKEMEEQVEIKRLRTENRLLKQRI-ETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQCALKEMQdkVLDIEKRNNS 497
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELeELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 498 LPDENNIArlQEELIAVKLREAEAimgLKELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAET- 576
Cdd:COG4717 375 LLAEAGVE--DEEELRAALEQAEE---YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELe 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 3093476 577 --QAEIREIKQRMMEMETQNQinsnhLRRAEQEVISLQEKVQYLSAQ 621
Cdd:COG4717 450 elREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEE 491
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
402-666 |
3.71e-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: 40.96 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 402 QYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIEtLEKHKcssnyneDFVLQLEKELVQARLSEAESQcAL 481
Cdd:pfam10174 483 KVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIA-VEQKK-------EECSKLENQLKKAHNAEEAVR-TN 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 482 KEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKElrQQVKDLEEHWQRHLarttgrwKDPPKKNAMNE 561
Cdd:pfam10174 554 PEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD--KKIAELESLTLRQM-------KEQNKKVANIK 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 562 LQDELMtiRLREAETQAEIREIKQRMMEMETQNQINS--NHLRRAEQEVISLQEKV---QYLSAQNKGLLTQLSEAKRKQ 636
Cdd:pfam10174 625 HGQQEM--KKKGAQLLEEARRREDNLADNSQQLQLEElmGALEKTRQELDATKARLsstQQSLAEKDGHLTNLRAERRKQ 702
|
250 260 270
....*....|....*....|....*....|
gi 3093476 637 AEIECKNKEEVMAVRLREADSIAAVAELRQ 666
Cdd:pfam10174 703 LEEILEMKQEALLAAISEKDANIALLELSS 732
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
405-714 |
4.60e-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: 40.39 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 405 SKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLekhkcsSNYNEDFVLQLE---KELVQA--RLSEAESQC 479
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL------KDEQNKIKKQLSekqKELEQNnkKIKELEKQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 480 ALKEMQDKVLDIEKRNNSLPD-ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHwqrhlaRTTGRWKDPPKKNA 558
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE------LTNSESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 559 MNELQDELMTIRLREAETQAEIREIKQRMMEMETQ-------NQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSE 631
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiqnqeklNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 632 AKRKQAEIECKNK---------EEVMAVRLREADSIAAvaELRQHIAELEIQKEEGKlqgQLN--KSDSNQYIGELKDQI 700
Cdd:TIGR04523 445 LTNQDSVKELIIKnldntreslETQLKVLSRSINKIKQ--NLEQKQKELKSKEKELK---KLNeeKKELEEKVKDLTKKI 519
|
330
....*....|....
gi 3093476 701 AELNHELRCLKGQK 714
Cdd:TIGR04523 520 SSLKEKIEKLESEK 533
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
402-713 |
4.71e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 402 QYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIE----TLEKHKcsSNYNEDFVLQLEKELVQARLSEAES 477
Cdd:PRK02224 195 QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDeadeVLEEHE--ERREELETLEAEIEDLRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 478 QC-----ALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAimGLKELRQQVKDLEEHWQRHlarttgrwkd 552
Cdd:PRK02224 273 EReelaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAH---------- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 553 ppkknamnELQDELMTIRLREAETQAEirEIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEA 632
Cdd:PRK02224 341 --------NEEAESLREDADDLEERAE--ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 633 KRKQAEIEcknkEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQ--GQ-LNKSDSNQYIGELKDQIAELNHELRC 709
Cdd:PRK02224 411 EDFLEELR----EERDELREREAELEATLRTARERVEEAEALLEAGKCPecGQpVEGSPHVETIEEDRERVEELEAELED 486
|
....
gi 3093476 710 LKGQ 713
Cdd:PRK02224 487 LEEE 490
|
|
| DUF1129 |
pfam06570 |
Protein of unknown function (DUF1129); This family consists of several hypothetical bacterial ... |
453-493 |
5.22e-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: 5.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 3093476 453 SNYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEK 493
Cdd:pfam06570 3 TKKNQDYIFRLTKQLIKDGKSDEEIKEILDEMLPEILEGQK 43
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
462-704 |
6.25e-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: 40.21 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 462 QLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLpdENNIARLQ---------EELIAVKLREAEAimGLKELRQQV 532
Cdd:pfam12128 217 RLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTL--ESAELRLShlhfgyksdETLIASRQEERQE--TSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 533 KDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLReaetQAEIREIKQRMMEMETQNQINSNhlrraeqevISLQ 612
Cdd:pfam12128 293 RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG----AFLDADIETAAADQEQLPSWQSE---------LENL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 613 EKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEEVMAVRLreaDSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQY 692
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL---AKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
|
250
....*....|....
gi 3093476 693 IGE--LKDQIAELN 704
Cdd:pfam12128 437 EEEyrLKSRLGELK 450
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
572-685 |
7.67e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 38.01 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 572 REAETQAEIREIKQRMMEMETQnqinsnhLRRAEQEVISLQEKVQYLSAQNKglltqlSEAKRKQAEIECKNKEEVMAVR 651
Cdd:PRK07352 51 RREAILQALKEAEERLRQAAQA-------LAEAQQKLAQAQQEAERIRADAK------ARAEAIRAEIEKQAIEDMARLK 117
|
90 100 110
....*....|....*....|....*....|....*....
gi 3093476 652 ---LREADSIA--AVAELRQHIAELEIQKEEGKLQGQLN 685
Cdd:PRK07352 118 qtaAADLSAEQerVIAQLRREAAELAIAKAESQLPGRLD 156
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
501-708 |
9.48e-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: 38.98 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 501 ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwqrhLARTTgrwkdppkKNAMNELQDELMTIRLREAETQAEI 580
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-----RIRAL--------EQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 581 REIKQRMMEMETQNQINSNH----LRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIEcknkeevmavrlread 656
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA---------------- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3093476 657 siaavaELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAELNHELR 708
Cdd:COG4942 164 ------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
419-667 |
9.63e-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: 39.42 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 419 KTKEMEEQVEIKR---LRTENRLLK-QRIETLEKHKCSSNyneDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKR 494
Cdd:pfam10174 518 KLKSLEIAVEQKKeecSKLENQLKKaHNAEEAVRTNPEIN---DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 495 NNSlpDENNIARLqEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARttgRWKDPPKKNAMNELQDELMTIRLRea 574
Cdd:pfam10174 595 KND--KDKKIAEL-ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEAR---RREDNLADNSQQLQLEELMGALEK-- 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476 575 eTQAEIREIKQRMMEMETQNQINSNHL------RRAEQEVIsLQEKVQYLSA------QNKGLLtQLSEAKRKqaeiecK 642
Cdd:pfam10174 667 -TRQELDATKARLSSTQQSLAEKDGHLtnlraeRRKQLEEI-LEMKQEALLAaisekdANIALL-ELSSSKKK------K 737
|
250 260
....*....|....*....|....*
gi 3093476 643 NKEEVMAVRlREADSIaaVAELRQH 667
Cdd:pfam10174 738 TQEEVMALK-REKDRL--VHQLKQQ 759
|
|
| |
