|
Name |
Accession |
Description |
Interval |
E-value |
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
97-359 |
2.96e-105 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 323.31 E-value: 2.96e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 97 LTSCEAELQELMKQIDIMVAHKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYK 176
Cdd:pfam17045 1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 177 EELLKLQEELSRLKRSYEKLQKKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 256
Cdd:pfam17045 81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 257 AEQSEIIQA-----QLANRKQKLEsvelSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKE 331
Cdd:pfam17045 161 AEQSSLIQSaayqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLL 236
|
250 260
....*....|....*....|....*...
gi 1039793411 332 EKLRESEKLLEALQEEQKELKASLQSQE 359
Cdd:pfam17045 237 EELRMSQRQLQVLQNELMELKATLQSQD 264
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-443 |
1.36e-12 |
|
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: 71.64 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 118 KKSEWEGQTHALEtcLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAmeykeellklqeelSRLKRSYEKLQ 197
Cdd:TIGR02169 219 EKREYEGYELLKE--KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE--------------QLLEELNKKIK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 198 KKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQ---AQLANRKQKL 274
Cdd:TIGR02169 283 DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 275 ESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKAS 354
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 355 LqsqETFILEAKMQE-KLQTTLKAVGT-QQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGS 432
Cdd:TIGR02169 443 K---EDKALEIKKQEwKLEQLAADLSKyEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS 519
|
330
....*....|.
gi 1039793411 433 LESVSATCKQL 443
Cdd:TIGR02169 520 IQGVHGTVAQL 530
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
137-456 |
1.85e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 137 DRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLQKKQlREFRGNTKSFREDRS 216
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE-QEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 217 EIERLTGKIEEFRQKSLDWEkqRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQ---SEIQHLNSKLE 293
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEyleKEIQELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 294 RAKDTICANELEIERLNIRVNDLmgtnmtiLQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQ----E 369
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEEL-------EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQiekkR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 370 KLQTTLKA-VGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDfshSSEELLQA-------------EVTRLEGSLES 435
Cdd:TIGR02169 917 KRLSELKAkLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQ---RVEEEIRAlepvnmlaiqeyeEVLKRLDELKE 993
|
330 340
....*....|....*....|....
gi 1039793411 436 VSATCKQLS---QELMEKYEELKR 456
Cdd:TIGR02169 994 KRAKLEEERkaiLERIEEYEKKKR 1017
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
193-500 |
2.82e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 193 YEKLQKKqLREFRGN--TKSFREDRSEIERLTGKIEEFRQKSLDWEKQRliyQQQVSSLEAQRKALAEQSEIIqaqlaNR 270
Cdd:TIGR02169 213 YQALLKE-KREYEGYelLKEKEALERQKEAIERQLASLEEELEKLTEEI---SELEKRLEEIEQLLEELNKKI-----KD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 271 KQKLESVELssQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKE 350
Cdd:TIGR02169 284 LGEEEQLRV--KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 351 LKASLQsqetfILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERkysSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLE 430
Cdd:TIGR02169 362 LKEELE-----DLRAELEEVDKEFAETRDELKDYREKLEKLKREI---NELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 431 GSLesvsatcKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSalegMKMEISQLTREL 500
Cdd:TIGR02169 434 AKI-------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQREL 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
188-496 |
7.03e-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: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 188 RLKRSYEKLQKKQLRefrgNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQL 267
Cdd:TIGR02168 236 ELREELEELQEELKE----AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 268 ANRKQKLESVELssqsEIQHLNSKLERAKDTICANELEIERLNIRVNDLmgtnmtilqdhrqkEEKLRESEKLLEALQEE 347
Cdd:TIGR02168 312 ANLERQLEELEA----QLEELESKLDELAEELAELEEKLEELKEELESL--------------EAELEELEAELEELESR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 348 QKELKASLQSQETFILEAKMQEKLQTtlkavGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEEL--LQAE 425
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLN-----NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELeeLEEE 448
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039793411 426 VTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLkEQILQADQTYSSALEGMKMEISQL 496
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGL 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-475 |
1.34e-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: 62.00 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 136 RDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEykeellklqeelsrlKRSYEKLQKKQLREFRGNTKSFREDR 215
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE---------------LEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 216 SEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVElssqSEIQHLNSklera 295
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR----EALDELRA----- 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 296 kdticanelEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFIleAKMQEKLQTTL 375
Cdd:TIGR02168 811 ---------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 376 KAVgtqQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHsseELLQAEVTRLEGSLESVSATCKQLSQELMEKYE-EL 454
Cdd:TIGR02168 880 NER---ASLEEALALLRSELEELSEELRELESKRSELRREL---EELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTL 953
|
330 340
....*....|....*....|.
gi 1039793411 455 KRMEGHNNEYRTEIKKLKEQI 475
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRL 974
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-405 |
7.94e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 101 EAELQELMKQIDIMVAhKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQemameykeell 180
Cdd:COG1196 238 EAELEELEAELEELEA-ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 181 klqEELSRLKRSYEKLQKKQLREfrgntksfREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQS 260
Cdd:COG1196 306 ---RLEERRRELEERLEELEEEL--------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 261 EIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDticaNELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKL 340
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA----LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039793411 341 LEALQEEQKELKASLQSQETfiLEAKMQEKLQTTLKAVGTQQSVERPLEdcQKERKYSSPGQGVL 405
Cdd:COG1196 451 EAELEEEEEALLELLAELLE--EAALLEAALAELLEELAEAAARLLLLL--EAEADYEGFLEGVK 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-415 |
1.64e-08 |
|
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: 58.53 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 102 AELQELmkQIDIMVAHKKSEwEGQTHALETCLDIRDRELKALRSQLDMkhkevgiLHQQIEEHEKTKQEMAMEYKEELLK 181
Cdd:TIGR02168 220 AELREL--ELALLVLRLEEL-REELEELQEELKEAEEELEELTAELQE-------LEEKLEELRLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 182 LQEELSRLKRSyeKLQKKQLREfrgntkSFREDRSEIERLTGKIEEfrqksldWEKQRLIYQQQVSSLEAQRKALAEQSE 261
Cdd:TIGR02168 290 LYALANEISRL--EQQKQILRE------RLANLERQLEELEAQLEE-------LESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 262 IIQAQLANRKQKLESVELSSQS---EIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRES- 337
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEEleeQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAe 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 338 -----------EKLLEALQEEQKELKASLQSQETFILEAkmQEKLQTTLKAVGTQQSVERPLEDCQkeRKYSSPGQGVLD 406
Cdd:TIGR02168 435 lkelqaeleelEEELEELQEELERLEEALEELREELEEA--EQALDAAERELAQLQARLDSLERLQ--ENLEGFSEGVKA 510
|
....*....
gi 1039793411 407 NVLSQLDFS 415
Cdd:TIGR02168 511 LLKNQSGLS 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
187-613 |
2.76e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 187 SRLKRSYEKLQKKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKsldwEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ 266
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 267 LANRKQKLESVELSSQ---------------SEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNM-TILQDHRQK 330
Cdd:COG4717 125 LQLLPLYQELEALEAElaelperleeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELqDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 331 EEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKLQTT--LKAVGTQQSVERPLEDCQKERKYSSPGQGVLDNV 408
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 409 LSQLDFSHSSEELLQAEVTRLEGSLEsvsATCKQLSQELMEKYeeLKRMEGHNNEYRTEIKKLKEQILQADQTYSSALEG 488
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQAL---PALEELEEEELEEL--LAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 489 MKmEIsQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETV----MKLELGLH 564
Cdd:COG4717 360 EE-EL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeLEEELEEL 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1039793411 565 EAKEISLADLQENYIEALNKLVSENQQLQKDlmSTKSELEHATNMCKKK 613
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAE 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
302-604 |
7.94e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 302 NELEIERLNI-RVNDLMG---TNMTILQDHRQKEEKLREseklleaLQEEQKELKASLQSQETFILEAKMQEKLQTTLKA 377
Cdd:COG1196 179 RKLEATEENLeRLEDILGeleRQLEPLERQAEKAERYRE-------LKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 378 VGTQQSVERPLEDCQKERKysspgqgVLDNVLSQLDFS----HSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEE 453
Cdd:COG1196 252 EAELEELEAELAELEAELE-------ELRLELEELELEleeaQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 454 LKRMEGHNNEYRTEIKKLKEQILQADQTYSSALEgmkmEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAV 533
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039793411 534 EHKEILSQLESLKLENHRLSETVMKLELGL--HEAKEISLADLQENYIEALNKLVSENQQLQKDLMSTKSELE 604
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALaeLEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
160-438 |
1.14e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 160 QIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSyEKLQKKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQR 239
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEEL-EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 240 LIYQQQVSSLEAQRKALAEQSEIIQAQLAN-----------------RKQKLESVELSSQSEIQHLNSKLERAKDTICAN 302
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAEleeeleeleeeleeleeELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 303 ELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKM--QEKLQTTLKAVGT 380
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEalEEAAEEEAELEEE 457
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039793411 381 QQSVERPLEDCQKERKYsspGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSA 438
Cdd:COG1196 458 EEALLELLAELLEEAAL---LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
138-617 |
1.44e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 138 RELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMA---MEYKEELLKLQEELSRLKRSYEKLQK-----KQLREFRGNTK 209
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIEeleKELESLEGSKRKLEEKIRELEERIEElkkeiEELEEKVKELK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 210 SFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEiiqaqlanRKQKLESVELSSQSEIQHLN 289
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE--------RLEELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 290 SKlERAKDTICANELEIERLNIRVNDLmgtnmtilqDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKmqE 369
Cdd:PRK03918 359 ER-HELYEEAKAKKEELERLKKRLTGL---------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK--K 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 370 KLQTTLKAVGTQQSVERPLEDCQKE---RKYSSPgqgvLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLsqE 446
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEHRKellEEYTAE----LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK--E 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 447 LMEKYEELK-RMEGHNNEY----RTEIKKLKEQilqadqtyssaLEGMKMEISQLTRELHqrditiasakcSSSDMEKQL 521
Cdd:PRK03918 501 LAEQLKELEeKLKKYNLEElekkAEEYEKLKEK-----------LIKLKGEIKSLKKELE-----------KLEELKKKL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 522 KAEMQKAEEKAVEHKEILSQLESLKLenhrlsETVMKLELGLHEAKEIsladlQENYIEALNkLVSENQQLQKDLMSTKS 601
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGF------ESVEELEERLKELEPF-----YNEYLELKD-AEKELEREEKELKKLEE 626
|
490
....*....|....*.
gi 1039793411 602 ELEHATNMCKKKDGEI 617
Cdd:PRK03918 627 ELDKAFEELAETEKRL 642
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
102-667 |
1.50e-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: 55.12 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 102 AELQELMKQIDIMVAHKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEE-----HEKTKQemameyk 176
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlHKREKE------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 177 eellklqeelsrlkRSYEKLQKKQLREF-RGNTKSFREDRSEIERLTGKIEEFRQ--KSLDWEKQRLIYQQ--------- 244
Cdd:pfam15921 393 --------------LSLEKEQNKRLWDRdTGNSITIDHLRRELDDRNMEVQRLEAllKAMKSECQGQMERQmaaiqgkne 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 245 ---QVSSLEAQRKALAEQSEIIQAQLANRKQKLESvelsSQSEIQHLNSKLERAKDTICANELEIERLNIRVNdlmgTNM 321
Cdd:pfam15921 459 sleKVSSLTAQLESTKEMLRKVVEELTAKKMTLES----SERTVSDLTASLQEKERAIEATNAEITKLRSRVD----LKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 322 TILQDHRQKEEKLRESEKLLEALQEEQKELKASLQsqetfILEAKMQEKLQ------TTLKAVGTQQS-VERPLEDCQKE 394
Cdd:pfam15921 531 QELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIE-----ILRQQIENMTQlvgqhgRTAGAMQVEKAqLEKEINDRRLE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 395 RKYSSPGQGVLDNVLSQLDFSHSSEELlqAEVTRLEGSLESVSATcKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQ 474
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLEL--EKVKLVNAGSERLRAV-KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 475 ILQADQTYSSALEGMKMEISQLTRELHQRDITIASAKCSSSD-------MEKQLKAE-----------------MQKA-- 528
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKrgqidalqskiqfleeaMTNAnk 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 529 ------EEK----------AVEHKEILSQLESLKLENHRLSETVMKLELGLHEAkEISLADLQEnyiealnkLVSENQQl 592
Cdd:pfam15921 763 ekhflkEEKnklsqelstvATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA-SLQFAECQD--------IIQRQEQ- 832
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039793411 593 qkdlMSTKSELEHATNMckkkdGEIFNPAHSRAAGFKNAELKPIHGQHRHDGIKTEQYKT---GHHSPRGQTLDSiDP 667
Cdd:pfam15921 833 ----ESVRLKLQHTLDV-----KELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTAsflSHHSRKTNALKE-DP 900
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
142-613 |
2.16e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 54.73 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 142 ALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLK---------RSYEKLQKKQLREFRGNTKSFR 212
Cdd:pfam05483 96 SIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKdlikennatRHLCNLLKETCARSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 213 EDRseierltgkiEEFRQKSLDWEKQrliYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKL 292
Cdd:pfam05483 176 YER----------EETRQVYMDLNNN---IEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 293 ERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLqsQETFILEAKMQEKLQ 372
Cdd:pfam05483 243 SLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSL--QRSMSTQKALEEDLQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 373 TTLKAV-GTQQSVERPLEDCQKERKYSSpgqgvldNVLSQLDFSHSS-EELLQAEVTRLEGSLESVsatcKQLSQELMEK 450
Cdd:pfam05483 321 IATKTIcQLTEEKEAQMEELNKAKAAHS-------FVVTEFEATTCSlEELLRTEQQRLEKNEDQL----KIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 451 YEELKRMEGHNNEYRTEIKKLKeQILQADQTY----------SSALEGMKMEISQL----TRELHQRDITIASAKCSSSD 516
Cdd:pfam05483 390 SSELEEMTKFKNNKEVELEELK-KILAEDEKLldekkqfekiAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEH 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 517 MEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETV--MKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQK 594
Cdd:pfam05483 469 YLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAsdMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRD 548
|
490
....*....|....*....
gi 1039793411 595 DLMSTKSELEHATNMCKKK 613
Cdd:pfam05483 549 ELESVREEFIQKGDEVKCK 567
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
121-617 |
3.67e-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: 53.97 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 121 EWEGQTHaLETCLDIRDRELKALRSQL----DMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKlqeelsrlkRSYEKL 196
Cdd:pfam15921 69 AYPGKEH-IERVLEEYSHQVKDLQRRLnesnELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADI---------RRRESQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 197 QKKQLREFRGNT-------KSFRED-----RSEIERL-------TGKIEEFRQKSLDWEKQ--RLIYQQQV--------- 246
Cdd:pfam15921 139 SQEDLRNQLQNTvheleaaKCLKEDmledsNTQIEQLrkmmlshEGVLQEIRSILVDFEEAsgKKIYEHDSmstmhfrsl 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 247 -SSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHL-NSKLERAKDTICANELEIERLNIRVN------DLMG 318
Cdd:pfam15921 219 gSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASsarsqaNSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 319 TNMTILQDH--RQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKLQTTlkavgtqqsverPLEDCQKERK 396
Cdd:pfam15921 299 SQLEIIQEQarNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS------------ELTEARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 397 YSSPGQGVLDNVLSQL--DFSHSSEEL-LQAEVT-RLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLK 472
Cdd:pfam15921 367 QFSQESGNLDDQLQKLlaDLHKREKELsLEKEQNkRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQM 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 473 EQILQADQ----------TYSSALEGMKMEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEI---- 538
Cdd:pfam15921 447 ERQMAAIQgkneslekvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLrsrv 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 539 ---LSQLESLKLENHRLSETVMKLE-LGLHEAKEISLADLQENYIEALNKLVS-----------ENQQLQKDLMSTKSEL 603
Cdd:pfam15921 527 dlkLQELQHLKNEGDHLRNVQTECEaLKLQMAEKDKVIEILRQQIENMTQLVGqhgrtagamqvEKAQLEKEINDRRLEL 606
|
570
....*....|....
gi 1039793411 604 EHATNMCKKKDGEI 617
Cdd:pfam15921 607 QEFKILKDKKDAKI 620
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-606 |
3.73e-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: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 263 IQAQLANR----KQKLESVELSSQS-EIQHLNSKLERAKDTICANELEIERLNIRVNdlmgtnmTILQDHRQKEEKLRES 337
Cdd:TIGR02168 207 RQAEKAERykelKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQ-------ELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 338 EKLLEALQEEQKELKASLQSQETFILEAKMQEK-LQTTLKAVGTQQSVERPLEDCQKERKYSspgqgvLDNVLSQLDFSH 416
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLAnLERQLEELEAQLEELESKLDELAEELAE------LEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 417 SSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQIlqadqtySSALEGMKMEISQL 496
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL-------EDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 497 TRELHQRDITIASAKCSSSDMEkqlKAEMQKAEEKAVEHKEILSQLeslkLENHRLSETVMKLELGLHEAKEISLADLQE 576
Cdd:TIGR02168 427 LKKLEEAELKELQAELEELEEE---LEELQEELERLEEALEELREE----LEEAEQALDAAERELAQLQARLDSLERLQE 499
|
330 340 350
....*....|....*....|....*....|....*....
gi 1039793411 577 N---YIEALNKLVSENQQLQ------KDLMSTKSELEHA 606
Cdd:TIGR02168 500 NlegFSEGVKALLKNQSGLSgilgvlSELISVDEGYEAA 538
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
187-617 |
4.46e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 187 SRLKRSYEKLqKKQLREFRGNTKSF----REDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEI 262
Cdd:TIGR04523 120 NKLEVELNKL-EKQKKENKKNIDKFlteiKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 263 IQAQLANRKQKLESVElSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLE 342
Cdd:TIGR04523 199 LELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 343 ALQEEQKELKASLQSQETFILEAKmQEKLQTTLKAVGTQqsverpLEDCQKErkysspgqgvLDNVLSQLDFSHSSEELL 422
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKSEISDLN-NQKEQDWNKELKSE------LKNQEKK----------LEEIQNQISQNNKIISQL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 423 QAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQIlqadqtysSALEGMKMEISQLTRELhq 502
Cdd:TIGR04523 341 NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI--------NDLESKIQNQEKLNQQK-- 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 503 rditiasakcsssdmEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETVMKLELGLHEAKeiSLADLQENYIEAL 582
Cdd:TIGR04523 411 ---------------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD--NTRESLETQLKVL 473
|
410 420 430
....*....|....*....|....*....|....*....
gi 1039793411 583 ----NKLVSENQQLQKDLMSTKSELEHATNMCKKKDGEI 617
Cdd:TIGR04523 474 srsiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
118-619 |
9.72e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 118 KKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMameykeelLKLQEELSRLKRSYEKLQ 197
Cdd:TIGR04523 167 QKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI--------SELKKQNNQLKDNIEKKQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 198 KKqlrefrgntksFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLAN-RKQKLES 276
Cdd:TIGR04523 239 QE-----------INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlNNQKEQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 277 VELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQ 356
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 357 SQETFI--LEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEEL-----------LQ 423
Cdd:TIGR04523 388 NLESQIndLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELiiknldntresLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 424 AEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQI---LQADQTYSSALEGMKMEISQLTREL 500
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIsslKEKIEKLESEKKEKESKISDLEDEL 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 501 HQRDITIASAKCSSSDMEK-----QLKAEMQKAEEKAVEHKEILSQLESLKLE-NHRLSETVMKL-----ELGLHEAKEI 569
Cdd:TIGR04523 548 NKDDFELKKENLEKEIDEKnkeieELKQTQKSLKKKQEEKQELIDQKEKEKKDlIKEIEEKEKKIsslekELEKAKKENE 627
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1039793411 570 SLADLQENYIEALNKLVSENQQLQKDL---MSTKSELEHATNMCKKKDGEIFN 619
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVKQIKETIkeiRNKWPEIIKKIKESKTKIDDIIE 680
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
238-558 |
2.02e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.38 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 238 QRLIYQQQVSSLEAQRKALAEQSEIIQAQLAnRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDL- 316
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSARE-KQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEk 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 317 MGTNMTILQDHRQKEEKLRESEKLLEALQeeqKELKASLQSQETFILEAKMQeKLQTTLKAVGT---------------Q 381
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQLD---KKHQAWLEEQKEQKREARTE-KQAYWQVVEGAldaqlallkaaiaarR 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 382 QSVERPLEDCQKERKYSSPGQGVLDNVLSQLdfshsseellQAEVTRLEGSLESvsatCKQLSQELMEKYEELK-RMEGH 460
Cdd:pfam12128 743 SGAKAELKALETWYKRDLASLGVDPDVIAKL----------KREIRTLERKIER----IAVRRQEVLRYFDWYQeTWLQR 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 461 NNEYRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRELHQRDitiaSAKCSSSDMEKQLKAEMQK---------AEEK 531
Cdd:pfam12128 809 RPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASE----KQQVRLSENLRGLRCEMSKlatlkedanSEQA 884
|
330 340
....*....|....*....|....*..
gi 1039793411 532 AVEHKEILSQLESLKLENHRLSETVMK 558
Cdd:pfam12128 885 QGSIGERLAQLEDLKLKRDYLSESVKK 911
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
290-619 |
5.11e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 290 SKLERAKdticaNELEIERLNIRVNDLmgtnmtILQDHRQKEEKLR-ESEKLlealqEEQKELKASLQSQETFILeAKMQ 368
Cdd:TIGR02169 170 RKKEKAL-----EELEEVEENIERLDL------IIDEKRQQLERLRrEREKA-----ERYQALLKEKREYEGYEL-LKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 369 EKLQTTLKAVGTQ-QSVERPLEDCQKERKYSSPGQGVLDNVLSQLdfSHSSEELLQAEVTRLEGSLESVSATCKQLSQEL 447
Cdd:TIGR02169 233 EALERQKEAIERQlASLEEELEKLTEEISELEKRLEEIEQLLEEL--NKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 448 MEKYEELKRMEGHNNEYRTEIKKLKEQILQADQtyssALEGMKMEISQLTRELhqrditiasakcssSDMEKQLKAEMQK 527
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELER----EIEEERKRRDKLTEEY--------------AELKEELEDLRAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 528 AEEKAVEHKE--------------ILSQLESLKLENHRLSETVMKLELGLHEAKEiSLADLqenyIEALNKLVSENQQLQ 593
Cdd:TIGR02169 373 LEEVDKEFAEtrdelkdyreklekLKREINELKRELDRLQEELQRLSEELADLNA-AIAGI----EAKINELEEEKEDKA 447
|
330 340
....*....|....*....|....*.
gi 1039793411 594 KDLMSTKSELEHATNMCKKKDGEIFN 619
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYD 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
319-617 |
1.57e-05 |
|
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: 48.51 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 319 TNMTILqdHRQKEekLRESEKLLEALQEEQKELKASLQSqetfiLEAKMQEKLQTTLKAVGTQQSVERPLEDCQKerkys 398
Cdd:TIGR02168 668 TNSSIL--ERRRE--IEELEEKIEELEEKIAELEKALAE-----LRKELEELEEELEQLRKELEELSRQISALRK----- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 399 spgqgvldnvlsQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQA 478
Cdd:TIGR02168 734 ------------DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 479 DQTYSSAlegmKMEISQLTRELHQRDITIASakcsssdMEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETVMK 558
Cdd:TIGR02168 802 REALDEL----RAELTLLNEEAANLRERLES-------LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039793411 559 LELGLHEAKEISlaDLQENYIEALNKLVSENQQLQKDLMSTKSELEHATNMCKKKDGEI 617
Cdd:TIGR02168 871 LESELEALLNER--ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
215-427 |
1.79e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 215 RSEIERLTGKIEEFRQKS--LDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESV-----ELSSQSEIQH 287
Cdd:COG3206 188 RKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 288 LNSKLERAkdticanELEIERLNIRVNDlmgtnmtilqDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFIL--EA 365
Cdd:COG3206 268 LRAQLAEL-------EAELAELSARYTP----------NHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQarEA 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039793411 366 KMQEKLQTTLKAVGTQQSVERPLEdcQKERKYSSpGQGVLDNVLSQLDFSHSSEELLQAEVT 427
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAELR--RLEREVEV-ARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
224-396 |
3.12e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 224 KIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelssQSEIQHLNSKLERAKDTI---- 299
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELgera 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 300 --------CANELE-----------IERLNIrVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQET 360
Cdd:COG3883 93 ralyrsggSVSYLDvllgsesfsdfLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039793411 361 fILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERK 396
Cdd:COG3883 172 -ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
215-475 |
3.40e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 215 RSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEI---------IQAQLANRKQKLESVELSSqSEI 285
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELERLDASS-DDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 286 QHLNSKLERAkdticanELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQK-----ELKASLQSQET 360
Cdd:COG4913 688 AALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 361 FILEAKMQEKLQTTLKAVGTQQS-VERPLEDCQKE--RKYSSPGQGVLDNVLSQLDFshsseellQAEVTRLEGSlesvs 437
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNrAEEELERAMRAfnREWPAETADLDADLESLPEY--------LALLDRLEED----- 827
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1039793411 438 atckqlsqELMEKYEELKRMEGHNN---------EYRTEIKKLKEQI 475
Cdd:COG4913 828 --------GLPEYEERFKELLNENSiefvadllsKLRRAIREIKERI 866
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
101-308 |
4.80e-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: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 101 EAELQELMKQIDIM------VAHKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAME 174
Cdd:COG4942 26 EAELEQLQQEIAELekelaaLKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 175 YkeellklqeelSRLKRSYEKLQKKQLREFRGNTKSF--------------REDRSEIERLTGKIEEFRQKSLDWEKQRL 240
Cdd:COG4942 106 L-----------AELLRALYRLGRQPPLALLLSPEDFldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039793411 241 IYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLEsvelSSQSEIQHLNSKLERAKDTICANELEIER 308
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELA----ELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
197-602 |
5.26e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 197 QKKQLREFRGNTKS----FREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLAnrkq 272
Cdd:PRK02224 228 QREQARETRDEADEvleeHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG---- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 273 kLESVELSSQSEIQhlnSKLERAKDTiCANELEIERLNIrvndlmgtnmtilQDHRQKEEKLRESEKLLEA----LQEEQ 348
Cdd:PRK02224 304 -LDDADAEAVEARR---EELEDRDEE-LRDRLEECRVAA-------------QAHNEEAESLREDADDLEEraeeLREEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 349 KELKASLQSQETFIleakmqEKLQTTLKAVGTQ-QSVERPLEDCQKERKYSspgQGVLDNVLSQLDFSHSSEELLQAEVT 427
Cdd:PRK02224 366 AELESELEEAREAV------EDRREEIEELEEEiEELRERFGDAPVDLGNA---EDFLEELREERDELREREAELEATLR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 428 RLEGSLESVSA--------TCKQLSQE------LMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSA--LEGMKM 491
Cdd:PRK02224 437 TARERVEEAEAlleagkcpECGQPVEGsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrIERLEE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 492 EISQLTRELHQRDITIA--SAKCSSSDMEKQ-LKAEMQKAEEKAVE-HKEILSQLESLKLENHRLSETVMKLElglHEAK 567
Cdd:PRK02224 517 RREDLEELIAERRETIEekRERAEELRERAAeLEAEAEEKREAAAEaEEEAEEAREEVAELNSKLAELKERIE---SLER 593
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1039793411 568 EISLADLQENYIEALNKLVSENQQLQ------KDLMSTKSE 602
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAelnderRERLAEKRE 634
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
188-613 |
5.81e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 188 RLKRSYEKLQ------KKQLREFRGNTK----SFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALA 257
Cdd:pfam05483 216 KLKEDHEKIQhleeeyKKEINDKEKQVSllliQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 258 EQSEII----QAQLANRKQKLESVELSSQSEIQHLNSK------LERAKDTICANELEIERLNIRVNDLMGTNMTILQDH 327
Cdd:pfam05483 296 KELEDIkmslQRSMSTQKALEEDLQIATKTICQLTEEKeaqmeeLNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 328 -----------RQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKLQTTLKavGTQQSVERPLEDCQKErk 396
Cdd:pfam05483 376 edqlkiitmelQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK--GKEQELIFLLQAREKE-- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 397 ysspgqgvLDNVLSQLDFSHSSEELLQAEVTRLEGSLES-------VSATCKQLSQELMEKYEELKRMEGHNNEYRTEI- 468
Cdd:pfam05483 452 --------IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklknieLTAHCDKLLLENKELTQEASDMTLELKKHQEDIi 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 469 --KKLKEQILQADQTYSSALEGMKMEISQLTRELHQRDITIasaKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQLESLK 546
Cdd:pfam05483 524 ncKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV---KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK 600
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039793411 547 LENHRLSETVMKLElglHEAKEISLADLQENyiEALNKLVSENQQLQKDLMSTKSELEHATNMCKKK 613
Cdd:pfam05483 601 KQIENKNKNIEELH---QENKALKKKGSAEN--KQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE 662
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
157-396 |
3.05e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 157 LHQQIEEHEKTKQEMAmeykeellKLQEELSRLKRSYEKLQKKQlrefrgntksfREDRSEIERLTGKIEEFRQKSLDWE 236
Cdd:COG4942 15 AAAQADAAAEAEAELE--------QLQQEIAELEKELAALKKEE-----------KALLKQLAALERRIAALARRIRALE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 237 KQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESveLSSQSEIQHLNSKlerakdticANELEIERLNIRVNDL 316
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR--LGRQPPLALLLSP---------EDFLDAVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 317 MGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETfILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERK 396
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA-ALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
99-365 |
3.27e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 99 SCEAELQELMKQIDIMVAhKKSEWEgqthALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEE 178
Cdd:COG4913 665 SAEREIAELEAELERLDA-SSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 179 LLKLQEELSRL--KRSYEKLQKKQLREFRGN-TKSFREDRSEIERLTGKIEE-FRQKSLDWekqRLIYQQQVSSLEAQRK 254
Cdd:COG4913 740 EDLARLELRALleERFAAALGDAVERELRENlEERIDALRARLNRAEEELERaMRAFNREW---PAETADLDADLESLPE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 255 ALAEQSEIIQAQLANRKQKL-ESVELSSQSEIQHLNSKLERAKDTIcanELEIERLNirvndlmgtnmTILQDHRQKEE- 332
Cdd:COG4913 817 YLALLDRLEEDGLPEYEERFkELLNENSIEFVADLLSKLRRAIREI---KERIDPLN-----------DSLKRIPFGPGr 882
|
250 260 270
....*....|....*....|....*....|....*
gi 1039793411 333 --KLRESEKLLEALQEEQKELKASLQSQETFILEA 365
Cdd:COG4913 883 ylRLEARPRPDPEVREFRQELRAVTSGASLFDEEL 917
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
230-604 |
3.42e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 230 QKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEiqhlnsKLERAKDTICANELEIERL 309
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA------PLAAHIKAVTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 310 NIRVNDLMGTNMTIL---QDHRQKEEKLRESEKLLEALQEEQKELkASLQSQETFILEAKMQEKlqTTLKAVGTQQSVER 386
Cdd:TIGR00618 313 HTELQSKMRSRAKLLmkrAAHVKQQSSIEEQRRLLQTLHSQEIHI-RDAHEVATSIREISCQQH--TLTQHIHTLQQQKT 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 387 PLEDcqkERKYSSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNE--- 463
Cdd:TIGR00618 390 TLTQ---KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaq 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 464 -YRTEIKKL--KEQILQADQTYSSALEGMKMEISQLTREL---------HQRDITIASAKCSSSDMEKQLKAEMQKAEEK 531
Cdd:TIGR00618 467 sLKEREQQLqtKEQIHLQETRKKAVVLARLLELQEEPCPLcgscihpnpARQDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039793411 532 aVEHK--EILSQLESLKLENHRLSETVMKLELGLHEAKEIslADLQENYIEALNKLVSENQQLQKDLMSTKSELE 604
Cdd:TIGR00618 547 -VYHQltSERKQRASLKEQMQEIQQSFSILTQCDNRSKED--IPNLQNITVRLQDLTEKLSEAEDMLACEQHALL 618
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
212-358 |
6.22e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 212 REDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelSSQSEIQHLNSK 291
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQKE 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039793411 292 LERAKDTICANELEIERLNIRVNdlmgtnmtilqdhrQKEEKLRESEKLLEALQEEQKELKASLQSQ 358
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIE--------------ELEEELAELEAELAELEAELEEKKAELDEE 150
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
382-604 |
9.61e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 382 QSVERPLEDCQKERkysSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQ-------LSQELMEKYEEL 454
Cdd:TIGR02169 684 EGLKRELSSLQSEL---RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 455 KRMEGHNNEYRTEIKKLKEQILQADQTYSSAlegmkmEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVE 534
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 535 HKEILSQLESLKLENHRLSETVMKLELGLHEAKEIsladlQENYIEALNKLVSENQQLQKDLMSTKSELE 604
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-----LEELEAALRDLESRLGDLKKERDELEAQLR 899
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
97-515 |
1.28e-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: 42.41 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 97 LTSCEAELQELMKQIDIMVA---HKKSEWEGQTHALETCldirdrelKALRSQLDMKHKEVGILHQQIE-------EHEK 166
Cdd:pfam15921 512 IEATNAEITKLRSRVDLKLQelqHLKNEGDHLRNVQTEC--------EALKLQMAEKDKVIEILRQQIEnmtqlvgQHGR 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 167 TKQEMAMEYKEELLKLQEELSRLKRsYEKLQKKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQV 246
Cdd:pfam15921 584 TAGAMQVEKAQLEKEINDRRLELQE-FKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEV 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 247 SSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDT---------------------ICANELE 305
Cdd:pfam15921 663 KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghamkvamgmqkqITAKRGQ 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 306 IERLNIRVNDL--MGTNMTiLQDHRQKEEKLRESEKL-------------LEALQEEQKELKASLQSQETFILEAKMQEK 370
Cdd:pfam15921 743 IDALQSKIQFLeeAMTNAN-KEKHFLKEEKNKLSQELstvateknkmageLEVLRSQERRLKEKVANMEVALDKASLQFA 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 371 LQTTLKAVGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLdfshsseeLLQAEVTRLEGSLESVSATCKQLSQELMeK 450
Cdd:pfam15921 822 ECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRL--------LQPASFTRTHSNVPSSQSTASFLSHHSR-K 892
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039793411 451 YEELKrmEGHNNEYRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRELHQRDITIASAKCSSS 515
Cdd:pfam15921 893 TNALK--EDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIESSLRSDI 955
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
135-491 |
1.31e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 135 IRDRELKALRSQLDMKHKEVGILHQQIEEHEKTK---QEMAMEYKEELLKLQEELSRLKRSYEKLQKKQLREFRGNtksf 211
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKeqaKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 212 REDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEaqrKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSK 291
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ---EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 292 LERAKDTICANELEIERLNIRvndlmgtnMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKL 371
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKE--------LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 372 QTTLKAVGTQQSVERPLEdcqkerkysspgqgVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKY 451
Cdd:pfam02463 395 EELELKSEEEKEAQLLLE--------------LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1039793411 452 EELKRMEGHNNEYRTEIKKLKEQILQADQTYSSALEGMKM 491
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQ 500
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
192-511 |
1.43e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 192 SYEKLQKKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRK 271
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 272 QKLESvelsSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKEL 351
Cdd:COG4372 94 AELAQ----AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 352 KASLQSQETFILEAKMQEKLQTTLKAVGTQQ---SVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEELLQAEVTR 428
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEelaEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 429 LEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRELHQRDITIA 508
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
...
gi 1039793411 509 SAK 511
Cdd:COG4372 330 LAL 332
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
145-612 |
1.58e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 145 SQLDMKHKEVGILHQQIEEHEKtkqEMAMEYKEELLKLQEELSRLkRSYEKLQKKQLREFRGNTKSFRED----RSEIER 220
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDET---LIASRQEERQETSAELNQLL-RTLDDQWKEKRDELNGELSAADAAvakdRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 221 LTGKIEEFRQKSLDWEKQRL----IYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKlesVELSSQSEIQHLNSKLERAK 296
Cdd:pfam12128 327 LEDQHGAFLDADIETAAADQeqlpSWQSELENLEERLKALTGKHQDVTAKYNRRRSK---IKEQNNRDIAGIKDKLAKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 297 DTICANELEIErlnirvNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEA--------KMQ 368
Cdd:pfam12128 404 EARDRQLAVAE------DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLenfderieRAR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 369 EKLQTTLKAVGTQQSVERPL--------EDCQKERKYSSPGQGVLDNVLSQLD-FSHSSEELLQAEVTRLEGSLESVSAT 439
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQArkrrdqasEALRQASRRLEERQSALDELELQLFpQAGTLLHFLRKEAPDWEQSIGKVISP 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 440 cKQLSQELMEKYEELKRMEGHNNEYrteikKLKEQILQADQTYSSALEgmkmeiSQLTRELHQRDITIASAKCSSSDMEK 519
Cdd:pfam12128 558 -ELLHRTDLDPEVWDGSVGGELNLY-----GVKLDLKRIDVPEWAASE------EELRERLDKAEEALQSAREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 520 QLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETVMKLELGLHEAkeisLADLQENYIEALNKLVSENQQLQKDLMST 599
Cdd:pfam12128 626 QLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKA----LAERKDSANERLNSLEAQLKQLDKKHQAW 701
|
490
....*....|....*...
gi 1039793411 600 KSE-----LEHATNMCKK 612
Cdd:pfam12128 702 LEEqkeqkREARTEKQAY 719
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
143-515 |
2.27e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 143 LRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLqKKQLREFRGNTKSFREDRSEIERLT 222
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAEL-KEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 223 GKIEEFRQKSLDwekQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQK-----------------LESVELSSQSEI 285
Cdd:pfam07888 111 EELSEEKDALLA---QRAAHEARIRELEEDIKTLTQRVLERETELERMKERakkagaqrkeeeaerkqLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 286 QHLNSKLERAKDTICANELEIERLNIRVNDLMGT----------NMTILQDHRQKEEKLRESEKLLEALQEEQKELkASL 355
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrkeaeNEALLEELRSLQERLNASERKVEGLGEELSSM-AAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 356 QSQETFILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKysspgqgvldNVLSQLDFSHSSEELLQAEVTRLEgsles 435
Cdd:pfam07888 267 RDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERE----------TLQQSAEADKDRIEKLSAELQRLE----- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 436 vsatcKQLSQELMEKYE---ELKRMEGHN----NEYRTEIKKLKEQiLQADQTYSSALEGMKMEISQLTRELHQRDITIA 508
Cdd:pfam07888 332 -----ERLQEERMEREKlevELGREKDCNrvqlSESRRELQELKAS-LRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
....*..
gi 1039793411 509 SAKCSSS 515
Cdd:pfam07888 406 DAKWSEA 412
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
241-510 |
3.38e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 241 IYQQQvsSLEAQRKALAEQSEIIQAQLANRKQKLESVElssqseiqhlnsklerakdticaNELEIERLNIRVNDLMGTN 320
Cdd:COG3206 160 AYLEQ--NLELRREEARKALEFLEEQLPELRKELEEAE-----------------------AALEEFRQKNGLVDLSEEA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 321 MTILQdhrqkeeKLRESEKLLEALQEEQKELKASLQSqetfiLEAKMQEKLQT--TLKAVGTQQSVERPLEDCQKE---- 394
Cdd:COG3206 215 KLLLQ-------QLSELESQLAEARAELAEAEARLAA-----LRAQLGSGPDAlpELLQSPVIQQLRAQLAELEAElael 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 395 RKYSSPGQGVLDNVLSQLDfshSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQ 474
Cdd:COG3206 283 SARYTPNHPDVIALRAQIA---ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
250 260 270
....*....|....*....|....*....|....*.
gi 1039793411 475 ILQADQTYSSALEgmKMEISQLTRELHQRDITIASA 510
Cdd:COG3206 360 VEVARELYESLLQ--RLEEARLAEALTVGNVRVIDP 393
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
318-518 |
4.04e-03 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 318 GTNMTILQDHRQKEEKLRES-EKLLEALQEEQKELKASLQSQETFILEAKMQEK--LQTTLKAVGTQQSVERPLEDCQKE 394
Cdd:pfam07902 132 GIATRISEDTDKKLALINETiSGIRREYQDADRQLSSSYQAGIEGLKATMASDKigLQAEIQASAQGLSQRYDNEIRKLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 395 RKYSSPGQGVLDNVLSQLD-----FSHSSEELLQAEVTRLEGSLESVSATCKQLSQelmekyeELKRMEGHNNEYRTEIK 469
Cdd:pfam07902 212 AKITTTSSGTTEAYESKLDdlraeFTRSNQGMRTELESKISGLQSTQQSTAYQISQ-------EISNREGAVSRVQQDLD 284
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039793411 470 KLKEQILQADQTYSS---ALEGMKMEISQLTRELHQRDITIA---SAKCSSSDME 518
Cdd:pfam07902 285 SYQRRLQDAEKNYSSltqTVKGLQSTVSDPNSKLESRITQLAgliEQKVTRGDVE 339
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
127-299 |
4.11e-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: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 127 HALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLqkkqlrefrG 206
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL---------G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 207 NTKSFREdrseIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQ 286
Cdd:COG1579 84 NVRNNKE----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|...
gi 1039793411 287 HLNSKLERAKDTI 299
Cdd:COG1579 160 ELEAEREELAAKI 172
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
141-614 |
4.28e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 141 KALRSQLDMKHKEVGILHQQIEEHEKTKQ--EMAMEYKEELLKLQEELSRLKRSYEKLQKKQLREFRGNTKSFREDRSEI 218
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 219 ERLTGKIEEFRQKsldwEKQRLIYQQQVSSLEAQRKAlAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDT 298
Cdd:PTZ00121 1447 DEAKKKAEEAKKA----EEAKKKAEEAKKADEAKKKA-EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 299 ICANELEIERLNIRVNDLMGTnmtilqDHRQKEEKLRESEKLLEAlqEEQKELKASLQSQETFILEAKMQEKLQTTLKAv 378
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKA------EEKKKADELKKAEELKKA--EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA- 1592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 379 gtqqSVERPLEDCQKERKYSSPgqgvldnvlsqlDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRME 458
Cdd:PTZ00121 1593 ----RIEEVMKLYEEEKKMKAE------------EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 459 GHNNEYRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRElhqrditiASAKCSSSDMEKQLKAEMQKAEEKAVEHKEI 538
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE--------AEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039793411 539 LSQLESLKLENHRlsETVMKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMSTKSELEHATNMCKKKD 614
Cdd:PTZ00121 1729 KIKAEEAKKEAEE--DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
157-366 |
5.01e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 157 LHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLQKKQlREFRGNTKSFREDRSEIERLTGKIEEfRQKSLdwe 236
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-QELAALEAELAELEKEIAELRAELEA-QKEEL--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 237 kQRLIYQQQVSSLEAQRKALAEQSEIIQAQ---------LANRKQKLESVElSSQSEIQHLNSKLERAKDTICANELEIE 307
Cdd:COG4942 107 -AELLRALYRLGRQPPLALLLSPEDFLDAVrrlqylkylAPARREQAEELR-ADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039793411 308 RLNIRVNDLMGTNMTILQDHRQKEEKLRESeklLEALQEEQKELKASLQSQETFILEAK 366
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAE---LAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
190-576 |
5.16e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 190 KRSYEKLqKKQLREFRGNTKSFREDRSEIERLTGKIEEFR--QKSLDWEKQRLIYQQQV--SSLEAQRKALAEQSEIIQA 265
Cdd:PRK01156 345 KSRYDDL-NNQILELEGYEMDYNSYLKSIESLKKKIEEYSknIERMSAFISEILKIQEIdpDAIKKELNEINVKLQDISS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 266 QLANRKQKLESVeLSSQSEIQHLNSKLE-RAKDTICANELEIERLNIRVNDLMgtnmtilQDHRQKEEKLRESEKLLEAL 344
Cdd:PRK01156 424 KVSSLNQRIRAL-RENLDELSRNMEMLNgQSVCPVCGTTLGEEKSNHIINHYN-------EKKSRLEEKIREIEIEVKDI 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 345 QEEQKELKASLQSqetfiLEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQL---DFSHSSEEL 421
Cdd:PRK01156 496 DEKIVDLKKRKEY-----LESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkleDLDSKRTSW 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 422 LQAEVTRLEGSLESVSATCKQLSQEL----------------MEKYEE--LKRMEGHNNEYRTEIKKLKEQILQADqTYS 483
Cdd:PRK01156 571 LNALAVISLIDIETNRSRSNEIKKQLndlesrlqeieigfpdDKSYIDksIREIENEANNLNNKYNEIQENKILIE-KLR 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 484 SALEGMKMEISQLtRELHQRDITIASAKCSSSDMEKQLKAEMQKAEekaVEHKEILSQLESLKLENHRLSETVMKLELGL 563
Cdd:PRK01156 650 GKIDNYKKQIAEI-DSIIPDLKEITSRINDIEDNLKKSRKALDDAK---ANRARLESTIEILRTRINELSDRINDINETL 725
|
410
....*....|....*
gi 1039793411 564 HEAKEI--SLADLQE 576
Cdd:PRK01156 726 ESMKKIkkAIGDLKR 740
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
110-570 |
5.61e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 110 QIDIMVAHKKSEWEGQTHALE--------TCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLK 181
Cdd:TIGR00618 423 QGQLAHAKKQQELQQRYAELCaaaitctaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 182 LQEELSRLKRSYEKLQkkQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSE 261
Cdd:TIGR00618 503 PCPLCGSCIHPNPARQ--DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDN 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 262 IIQAQLANRKQKLEsvelssqsEIQHLNSKLERAKDTI-CANELEIERLNIRVNDLmgtnmTILQDHRQKEeklresekl 340
Cdd:TIGR00618 581 RSKEDIPNLQNITV--------RLQDLTEKLSEAEDMLaCEQHALLRKLQPEQDLQ-----DVRLHLQQCS--------- 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 341 lealQEEQKELKASLQSQETFILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEE 420
Cdd:TIGR00618 639 ----QELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 421 LLQAEVTRLEGSLESVSATCKQ---LSQELMEKYEELKRMEGHNNEYRTEIKKLKEQI-LQADQTYSSALEGMKMEISQL 496
Cdd:TIGR00618 715 EYDREFNEIENASSSLGSDLAAredALNQSLKELMHQARTVLKARTEAHFNNNEEVTAaLQTGAELSHLAAEIQFFNRLR 794
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039793411 497 TRELHQRDITIASAKCSSSDMEKQLKAE---MQKAEEKAVEHKEILSQ-LESLKLENHRLSETVMKLELGLHEAKEIS 570
Cdd:TIGR00618 795 EEDTHLLKTLEAEIGQEIPSDEDILNLQcetLVQEEEQFLSRLEEKSAtLGEITHQLLKYEECSKQLAQLTQEQAKII 872
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
149-393 |
6.04e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 149 MKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLQ---KKQLREFRGNTKSFREDRSEIERL---- 221
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQaemDRQAAIYAEQERMAMERERELERIrqee 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 222 -TGKIEEFRQKSLDWEKQRLiyqQQVSSLEAQRKALAEQseIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDTIc 300
Cdd:pfam17380 358 rKRELERIRQEEIAMEISRM---RELERLQMERQQKNER--VRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 301 ANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESE---KLLEALQEEQKELKASLQSQETFILEAKMQEKLQTTLKA 377
Cdd:pfam17380 432 ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEeerKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEE 511
|
250
....*....|....*.
gi 1039793411 378 VGTQQSVERPLEDCQK 393
Cdd:pfam17380 512 ERKRKLLEKEMEERQK 527
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-378 |
6.24e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 97 LTSCEAELQELMKQIDIMVAHKKsEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYK 176
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 177 EELLKLQEELSRLKRsyeklQKKQLREFRGNTKSFREDRSEIER-LTGKIEEFRQKSLDWEKQRLIYQQ---QVSSLEAQ 252
Cdd:TIGR02168 835 ATERRLEDLEEQIEE-----LSEDIESLAAEIEELEELIEELESeLEALLNERASLEEALALLRSELEElseELRELESK 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 253 RKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIE-----------RLNIRVNDLMGTNM 321
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEddeeearrrlkRLENKIKELGPVNL 989
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039793411 322 TILQDHRQKEEKLREseklleaLQEEQKELKASLQSQETFILE--AKMQEKLQTTLKAV 378
Cdd:TIGR02168 990 AAIEEYEELKERYDF-------LTAQKEDLTEAKETLEEAIEEidREARERFKDTFDQV 1041
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
188-371 |
6.59e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.11 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 188 RLKRSYEKLQkkqlREFRGNTKSFREDRSEIER----LTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAE----- 258
Cdd:pfam05557 6 ESKARLSQLQ----NEKKQMELEHKRARIELEKkasaLKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 259 -QSEIIQAQLANRK----QKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRvNDLMGTNMtilQDHRQKEEK 333
Cdd:pfam05557 82 kKYLEALNKKLNEKesqlADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQER-LDLLKAKA---SEAEQLRQN 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039793411 334 LRESEKLLEALQEEQKELKASLQSQETFILEAK-MQEKL 371
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKnSKSEL 196
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
325-634 |
6.68e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 325 QDHRQKEEKLRESEKLLEALQEEQKELKasLQSQETFILEAKMQEKLQTTLKAVGTQQSVERPLED------CQKERKYS 398
Cdd:TIGR00606 613 ELESKEEQLSSYEDKLFDVCGSQDEESD--LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvCQRVFQTE 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 399 SPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQA 478
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 479 DQTYSSALEGMK-----------MEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQLESLKL 547
Cdd:TIGR00606 771 ETLLGTIMPEEEsakvcltdvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 548 ENHRLSETVMKL-----ELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMSTKSELEHATNMCKKKDGEIFNPAH 622
Cdd:TIGR00606 851 LIQDQQEQIQHLksktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
330
....*....|..
gi 1039793411 623 SRAAGFKNAELK 634
Cdd:TIGR00606 931 SKETSNKKAQDK 942
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
157-563 |
8.51e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 39.72 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 157 LHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKlQKKQLREFRGNTKSFREDRSEIER-LTGKIEEFRQKSLDW 235
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDR-ESDRNQELQKRIRLLEKREAEAEEaLREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 236 EKQRLIYQQQVSSLE-------AQRKALAEQSEIIQ-AQLANRKQKLESVELSSQSEIQH--------LNSKLERAKDTI 299
Cdd:pfam05557 86 EALNKKLNEKESQLAdarevisCLKNELSELRRQIQrAELELQSTNSELEELQERLDLLKakaseaeqLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 300 CANELEIERLnIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQEtfILEAK---MQEKLQTTLK 376
Cdd:pfam05557 166 AEAEQRIKEL-EFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKL--LLKEEvedLKRKLEREEK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 377 AVGTQQSVERPLEDCQKERK-YSSPGQGVLDNVLSQLDFSHSSEELLQ------AEVTRLEGSLESVSATCKQLSQELME 449
Cdd:pfam05557 243 YREEAATLELEKEKLEQELQsWVKLAQDTGLNLRSPEDLSRRIEQLQQreivlkEENSSLTSSARQLEKARRELEQELAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 450 KYEELKRMEGHNNEYRTEIKKLKEQILQADQ-------------------TYSSALEGMKMEISQLTRELH--------- 501
Cdd:pfam05557 323 YLKKIEDLNKKLKRHKALVRRLQRRVLLLTKerdgyrailesydkeltmsNYSPQLLERIEEAEDMTQKMQahneemeaq 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039793411 502 ----QRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEILS---QLESLKLENHRLSETVMKLELGL 563
Cdd:pfam05557 403 lsvaEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSlrrKLETLELERQRLREQKNELEMEL 471
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
101-604 |
8.82e-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: 39.77 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 101 EAELQELMKQIDIMVAHKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEykeell 180
Cdd:pfam01576 52 ETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLE------ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 181 kLQEELSRLKrsyeKLQKKQLREFRGNTKSFREDRSEIERL---TGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKala 257
Cdd:pfam01576 126 -KVTTEAKIK----KLEEDILLLEDQNSKLSKERKLLEERIsefTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 258 eQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRES 337
Cdd:pfam01576 198 -KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 338 EKLLEalQEEQKELKASLQSQETFILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKYSspgqgvldnvlsqldfshs 417
Cdd:pfam01576 277 QEDLE--SERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKA------------------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 418 seelLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKR-----------MEGHNNEYRTEIKklkeqilqadqtyssAL 486
Cdd:pfam01576 336 ----LEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRnkanlekakqaLESENAELQAELR---------------TL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 487 EGMKMEISQLTRELHQRdITIASAKCSSSDMEKQLKAEmqKAEEKAVEHKEILSQLESLKLENHRLSETVMKLELGLHEA 566
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQ-LQELQARLSESERQRAELAE--KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT 473
|
490 500 510
....*....|....*....|....*....|....*...
gi 1039793411 567 KEIsladLQENYIEALNkLVSENQQLQKDLMSTKSELE 604
Cdd:pfam01576 474 QEL----LQEETRQKLN-LSTRLRQLEDERNSLQEQLE 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
242-478 |
9.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 242 YQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTnm 321
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR-- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 322 tiLQDHRQKEEKLRESE-----KLLEALQEEQKELKASLQSQETfiLEAKMQEKLQT-TLKAVGTQQSVERpledcqker 395
Cdd:COG4913 318 --LDALREELDELEAQIrgnggDRLEQLEREIERLERELEERER--RRARLEALLAAlGLPLPASAEEFAA--------- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 396 kysspgqgVLDNVLSQLDFSHSSEELLQAEVTRLEGSLEsvsatckQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQI 475
Cdd:COG4913 385 --------LRAEAAALLEALEEELEALEEALAEAEAALR-------DLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
...
gi 1039793411 476 LQA 478
Cdd:COG4913 450 AEA 452
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
52-604 |
9.83e-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: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 52 TQSCCQNKEDLEMEALLEGIQNRGHSGRNHLGmscDWSVGACRGFLTSCEAELQELMKQIDIMVAHKKSEWEGQTHALET 131
Cdd:pfam10174 148 TQKQTLGARDESIKKLLEMLQSKGLPKKSGEE---DWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPD 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 132 cldirDRELKALRSQLDMKHKEVGILHQQIEEHEktkQEMAMEYKEELLKLQEELSRLK-----RSYEKLQKKQLREFRg 206
Cdd:pfam10174 225 -----PAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDREEEIKqmevyKSHSKFMKNKIDQLK- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 207 ntKSFREDRSEIERLTGKIEEFRQKSLDWE------KQRLIYQQQVSS-LEAQRKALAEQSEIIQAQLANRKQKLESVel 279
Cdd:pfam10174 296 --QELSKKESELLALQTKLETLTNQNSDCKqhievlKESLTAKEQRAAiLQTEVDALRLRLEEKESFLNKKTKQLQDL-- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 280 ssQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLmgtnmtilqdhrqkEEKLRESEKLLEALQEEQKELKASLQSQE 359
Cdd:pfam10174 372 --TEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL--------------QEQLRDKDKQLAGLKERVKSLQTDSSNTD 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 360 TFI--LEAKMQEKlqttlkavgtqqsvERPLEDCQKERkySSPGQGVLDNVLSQLDFSHSSEE---LLQAEVTRLEGSLE 434
Cdd:pfam10174 436 TALttLEEALSEK--------------ERIIERLKEQR--EREDRERLEELESLKKENKDLKEkvsALQPELTEKESSLI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 435 SVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSalEGMKMEISQLTRELHQRDITIA--SAKC 512
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEA--VRTNPEINDRIRLLEQEVARYKeeSGKA 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 513 sSSDMEKQLKAEMQKAEEKAVEHKEIlSQLESLKLENHR-LSETVMKLELGLHEAKEISLADLQENYIEALNKLVSENQQ 591
Cdd:pfam10174 578 -QAEVERLLGILREVENEKNDKDKKI-AELESLTLRQMKeQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL 655
|
570
....*....|....*..
gi 1039793411 592 LQKDLMS----TKSELE 604
Cdd:pfam10174 656 QLEELMGalekTRQELD 672
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
174-486 |
9.91e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.17 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 174 EYKEELLKLQEELSRLKRSYEKLQKKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIyqqqvssleaqR 253
Cdd:COG5185 240 DPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI-----------K 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 254 KALAEQSEIIQAQLANrkQKLESVELSSQSEIQHLNSKLERAKDTIcanELEIERLNIRVNDLMGTNmtilqDHRQKEEK 333
Cdd:COG5185 309 KATESLEEQLAAAEAE--QELEESKRETETGIQNLTAEIEQGQESL---TENLEAIKEEIENIVGEV-----ELSKSSEE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793411 334 LRESEKLLEALQEEQKELKASLQSQETFILEAkmqekLQTTLKAVGTQ-QSVERPLEdcQKERKYSSPGQgVLDNVLSQL 412
Cdd:COG5185 379 LDSFKDTIESTKESLDEIPQNQRGYAQEILAT-----LEDTLKAADRQiEELQRQIE--QATSSNEEVSK-LLNELISEL 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039793411 413 DFS-HSSEELLQAEVTrlegslESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSAL 486
Cdd:COG5185 451 NKVmREADEESQSRLE------EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKL 519
|
|
| |
