|
Name |
Accession |
Description |
Interval |
E-value |
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
92-354 |
8.91e-107 |
|
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: 327.16 E-value: 8.91e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 92 LTSCEAELQELMKQIDIMVAHKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYK 171
Cdd:pfam17045 1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 172 EELLKLQEELSRLKRSYEKLQKKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 251
Cdd:pfam17045 81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 252 AEQSEIIQA-----QLANRKQKLEsvelSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKE 326
Cdd:pfam17045 161 AEQSSLIQSaayqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLL 236
|
250 260
....*....|....*....|....*...
gi 755531331 327 EKLRESEKLLEALQEEQKELKASLQSQE 354
Cdd:pfam17045 237 EELRMSQRQLQVLQNELMELKATLQSQD 264
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
113-438 |
8.23e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.41 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 113 KKSEWEGQTHALEtcLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAmeykeellklqeelSRLKRSYEKLQ 192
Cdd:TIGR02169 219 EKREYEGYELLKE--KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE--------------QLLEELNKKIK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 193 KKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQ---AQLANRKQKL 269
Cdd:TIGR02169 283 DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 270 ESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKAS 349
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 350 LqsqETFILEAKMQE-KLQTTLKAVGT-QQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGS 427
Cdd:TIGR02169 443 K---EDKALEIKKQEwKLEQLAADLSKyEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS 519
|
330
....*....|.
gi 755531331 428 LESVSATCKQL 438
Cdd:TIGR02169 520 IQGVHGTVAQL 530
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
132-451 |
1.11e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 132 DRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLQKKQlREFRGNTKSFREDRS 211
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE-QEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 212 EIERLTGKIEEFRQKSLDWEkqRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQ---SEIQHLNSKLE 288
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEyleKEIQELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 289 RAKDTICANELEIERLNIRVNDLmgtnmtiLQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQ----E 364
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEEL-------EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQiekkR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 365 KLQTTLKA-VGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDfshSSEELLQA-------------EVTRLEGSLES 430
Cdd:TIGR02169 917 KRLSELKAkLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQ---RVEEEIRAlepvnmlaiqeyeEVLKRLDELKE 993
|
330 340
....*....|....*....|....
gi 755531331 431 VSATCKQLS---QELMEKYEELKR 451
Cdd:TIGR02169 994 KRAKLEEERkaiLERIEEYEKKKR 1017
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
188-495 |
1.48e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 188 YEKLQKKqLREFRGN--TKSFREDRSEIERLTGKIEEFRQKSLDWEKQRliyQQQVSSLEAQRKALAEQSEIIqaqlaNR 265
Cdd:TIGR02169 213 YQALLKE-KREYEGYelLKEKEALERQKEAIERQLASLEEELEKLTEEI---SELEKRLEEIEQLLEELNKKI-----KD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 266 KQKLESVELssQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKE 345
Cdd:TIGR02169 284 LGEEEQLRV--KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 346 LKASLQsqetfILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERkysSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLE 425
Cdd:TIGR02169 362 LKEELE-----DLRAELEEVDKEFAETRDELKDYREKLEKLKREI---NELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 426 GSLesvsatcKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSalegMKMEISQLTREL 495
Cdd:TIGR02169 434 AKI-------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQREL 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
183-491 |
4.54e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 183 RLKRSYEKLQKKQLRefrgNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQL 262
Cdd:TIGR02168 236 ELREELEELQEELKE----AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 263 ANRKQKLESVELssqsEIQHLNSKLERAKDTICANELEIERLNIRVNDLmgtnmtilqdhrqkEEKLRESEKLLEALQEE 342
Cdd:TIGR02168 312 ANLERQLEELEA----QLEELESKLDELAEELAELEEKLEELKEELESL--------------EAELEELEAELEELESR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 343 QKELKASLQSQETFILEAKMQEKLQTtlkavGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEEL--LQAE 420
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLN-----NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELeeLEEE 448
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755531331 421 VTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLkEQILQADQTYSSALEGMKMEISQL 491
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGL 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-590 |
5.87e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 184 LKRSYEKL--QKKQLREFrgntKSFREDRSEIER--LTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQ 259
Cdd:TIGR02168 198 LERQLKSLerQAEKAERY----KELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 260 AQLANRKQKLESVelssQSEIQHLNSKLERAkdticanELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEAL 339
Cdd:TIGR02168 274 LEVSELEEEIEEL----QKELYALANEISRL-------EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 340 QEEQKELKASLQSqetfiLEAKMQEKlqttlkaVGTQQSVERPLEDCQKErkysspgqgvLDNVLSQLDFSHSSEELLQA 419
Cdd:TIGR02168 343 EEKLEELKEELES-----LEAELEEL-------EAELEELESRLEELEEQ----------LETLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 420 EVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYR-TEIKKLKEQILQADQTYSSALEGMKMEISQLTRELHQ- 497
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAa 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 498 -RDITIASAKCSSsdmekqLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSEtVMKLELGLHEAKEISLAdlqenyiEA 576
Cdd:TIGR02168 481 eRELAQLQARLDS------LERLQENLEGFSEGVKALLKNQSGLSGILGVLSE-LISVDEGYEAAIEAALG-------GR 546
|
410
....*....|....
gi 755531331 577 LNKLVSENQQLQKD 590
Cdd:TIGR02168 547 LQAVVVENLNAAKK 560
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
131-470 |
7.14e-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: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 131 RDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEykeellklqeelsrlKRSYEKLQKKQLREFRGNTKSFREDR 210
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE---------------LEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 211 SEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVElssqSEIQHLNSklera 290
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR----EALDELRA----- 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 291 kdticanelEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFIleAKMQEKLQTTL 370
Cdd:TIGR02168 811 ---------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 371 KAVgtqQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHsseELLQAEVTRLEGSLESVSATCKQLSQELMEKYE-EL 449
Cdd:TIGR02168 880 NER---ASLEEALALLRSELEELSEELRELESKRSELRREL---EELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTL 953
|
330 340
....*....|....*....|.
gi 755531331 450 KRMEGHNNEYRTEIKKLKEQI 470
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRL 974
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-400 |
5.54e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 96 EAELQELMKQIDIMVAhKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQemameykeell 175
Cdd:COG1196 238 EAELEELEAELEELEA-ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 176 klqEELSRLKRSYEKLQKKQLREfrgntksfREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQS 255
Cdd:COG1196 306 ---RLEERRRELEERLEELEEEL--------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 256 EIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDticaNELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKL 335
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA----LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755531331 336 LEALQEEQKELKASLQSQETfiLEAKMQEKLQTTLKAVGTQQSVERPLEdcQKERKYSSPGQGVL 400
Cdd:COG1196 451 EAELEEEEEALLELLAELLE--EAALLEAALAELLEELAEAAARLLLLL--EAEADYEGFLEGVK 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-410 |
9.11e-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: 59.30 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 97 AELQELmkQIDIMVAHKKSEwEGQTHALETCLDIRDRELKALRSQLDMkhkevgiLHQQIEEHEKTKQEMAMEYKEELLK 176
Cdd:TIGR02168 220 AELREL--ELALLVLRLEEL-REELEELQEELKEAEEELEELTAELQE-------LEEKLEELRLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 177 LQEELSRLKRSyeKLQKKQLREfrgntkSFREDRSEIERLTGKIEEfrqksldWEKQRLIYQQQVSSLEAQRKALAEQSE 256
Cdd:TIGR02168 290 LYALANEISRL--EQQKQILRE------RLANLERQLEELEAQLEE-------LESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 257 IIQAQLANRKQKLESVELSSQS---EIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRES- 332
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEEleeQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAe 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 333 -----------EKLLEALQEEQKELKASLQSQETFILEAkmQEKLQTTLKAVGTQQSVERPLEDCQkeRKYSSPGQGVLD 401
Cdd:TIGR02168 435 lkelqaeleelEEELEELQEELERLEEALEELREELEEA--EQALDAAERELAQLQARLDSLERLQ--ENLEGFSEGVKA 510
|
....*....
gi 755531331 402 NVLSQLDFS 410
Cdd:TIGR02168 511 LLKNQSGLS 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
182-608 |
9.33e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 9.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 182 SRLKRSYEKLQKKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKsldwEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ 261
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 262 LANRKQKLESVELSSQ---------------SEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNM-TILQDHRQK 325
Cdd:COG4717 125 LQLLPLYQELEALEAElaelperleeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELqDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 326 EEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKLQTT--LKAVGTQQSVERPLEDCQKERKYSSPGQGVLDNV 403
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 404 LSQLDFSHSSEELLQAEVTRLEGSLEsvsATCKQLSQELMEKYeeLKRMEGHNNEYRTEIKKLKEQILQADQTYSSALEG 483
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQAL---PALEELEEEELEEL--LAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 484 MKmEIsQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETV----MKLELGLH 559
Cdd:COG4717 360 EE-EL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeLEEELEEL 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 755531331 560 EAKEISLADLQENYIEALNKLVSENQQLQKDlmSTKSELEHATNMCKKK 608
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAE 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
297-599 |
5.05e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 297 NELEIERLNI-RVNDLMG---TNMTILQDHRQKEEKLREseklleaLQEEQKELKASLQSQETFILEAKMQEKLQTTLKA 372
Cdd:COG1196 179 RKLEATEENLeRLEDILGeleRQLEPLERQAEKAERYRE-------LKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 373 VGTQQSVERPLEDCQKERKysspgqgVLDNVLSQLDFS----HSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEE 448
Cdd:COG1196 252 EAELEELEAELAELEAELE-------ELRLELEELELEleeaQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 449 LKRMEGHNNEYRTEIKKLKEQILQADQTYSSALEgmkmEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAV 528
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755531331 529 EHKEILSQLESLKLENHRLSETVMKLELGL--HEAKEISLADLQENYIEALNKLVSENQQLQKDLMSTKSELE 599
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALaeLEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
137-608 |
5.64e-08 |
|
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: 56.27 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 137 ALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLK---------RSYEKLQKKQLREFRGNTKSFR 207
Cdd:pfam05483 96 SIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKdlikennatRHLCNLLKETCARSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 208 EDRseierltgkiEEFRQKSLDWEKQrliYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKL 287
Cdd:pfam05483 176 YER----------EETRQVYMDLNNN---IEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 288 ERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLqsQETFILEAKMQEKLQ 367
Cdd:pfam05483 243 SLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSL--QRSMSTQKALEEDLQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 368 TTLKAV-GTQQSVERPLEDCQKERKYSSpgqgvldNVLSQLDFSHSS-EELLQAEVTRLEGSLESVsatcKQLSQELMEK 445
Cdd:pfam05483 321 IATKTIcQLTEEKEAQMEELNKAKAAHS-------FVVTEFEATTCSlEELLRTEQQRLEKNEDQL----KIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 446 YEELKRMEGHNNEYRTEIKKLKeQILQADQTY----------SSALEGMKMEISQL----TRELHQRDITIASAKCSSSD 511
Cdd:pfam05483 390 SSELEEMTKFKNNKEVELEELK-KILAEDEKLldekkqfekiAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEH 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 512 MEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETV--MKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQK 589
Cdd:pfam05483 469 YLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAsdMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRD 548
|
490
....*....|....*....
gi 755531331 590 DLMSTKSELEHATNMCKKK 608
Cdd:pfam05483 549 ELESVREEFIQKGDEVKCK 567
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-612 |
7.08e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 133 RELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMA---MEYKEELLKLQEELSRLKRSYEKLQK-----KQLREFRGNTK 204
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIEeleKELESLEGSKRKLEEKIRELEERIEElkkeiEELEEKVKELK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 205 SFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEiiqaqlanRKQKLESVELSSQSEIQHLN 284
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE--------RLEELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 285 SKlERAKDTICANELEIERLNIRVNDLmgtnmtilqDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKmqE 364
Cdd:PRK03918 359 ER-HELYEEAKAKKEELERLKKRLTGL---------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK--K 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 365 KLQTTLKAVGTQQSVERPLEDCQKE---RKYSSPgqgvLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLsqE 441
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEHRKellEEYTAE----LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK--E 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 442 LMEKYEELK-RMEGHNNEY----RTEIKKLKEQilqadqtyssaLEGMKMEISQLTRELHqrditiasakcSSSDMEKQL 516
Cdd:PRK03918 501 LAEQLKELEeKLKKYNLEElekkAEEYEKLKEK-----------LIKLKGEIKSLKKELE-----------KLEELKKKL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 517 KAEMQKAEEKAVEHKEILSQLESLKLenhrlsETVMKLELGLHEAKEIsladlQENYIEALNkLVSENQQLQKDLMSTKS 596
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGF------ESVEELEERLKELEPF-----YNEYLELKD-AEKELEREEKELKKLEE 626
|
490
....*....|....*.
gi 755531331 597 ELEHATNMCKKKDGEI 612
Cdd:PRK03918 627 ELDKAFEELAETEKRL 642
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
155-433 |
7.41e-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: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 155 QIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSyEKLQKKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQR 234
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEEL-EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 235 LIYQQQVSSLEAQRKALAEQSEIIQAQLAN-----------------RKQKLESVELSSQSEIQHLNSKLERAKDTICAN 297
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAEleeeleeleeeleeleeELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 298 ELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKM--QEKLQTTLKAVGT 375
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEalEEAAEEEAELEEE 457
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 755531331 376 QQSVERPLEDCQKERKYsspGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSA 433
Cdd:COG1196 458 EEALLELLAELLEEAAL---LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
97-662 |
8.05e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.28 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 97 AELQELMKQIDIMVAHKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEE-----HEKTKQemameyk 171
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlHKREKE------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 172 eellklqeelsrlkRSYEKLQKKQLREF-RGNTKSFREDRSEIERLTGKIEEFRQ--KSLDWEKQRLIYQQ--------- 239
Cdd:pfam15921 393 --------------LSLEKEQNKRLWDRdTGNSITIDHLRRELDDRNMEVQRLEAllKAMKSECQGQMERQmaaiqgkne 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 240 ---QVSSLEAQRKALAEQSEIIQAQLANRKQKLESvelsSQSEIQHLNSKLERAKDTICANELEIERLNIRVNdlmgTNM 316
Cdd:pfam15921 459 sleKVSSLTAQLESTKEMLRKVVEELTAKKMTLES----SERTVSDLTASLQEKERAIEATNAEITKLRSRVD----LKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 317 TILQDHRQKEEKLRESEKLLEALQEEQKELKASLQsqetfILEAKMQEKLQ------TTLKAVGTQQS-VERPLEDCQKE 389
Cdd:pfam15921 531 QELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIE-----ILRQQIENMTQlvgqhgRTAGAMQVEKAqLEKEINDRRLE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 390 RKYSSPGQGVLDNVLSQLDFSHSSEELlqAEVTRLEGSLESVSATcKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQ 469
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLEL--EKVKLVNAGSERLRAV-KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 470 ILQADQTYSSALEGMKMEISQLTRELHQRDITIASAKCSSSD-------MEKQLKAE-----------------MQKA-- 523
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKrgqidalqskiqfleeaMTNAnk 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 524 ------EEK----------AVEHKEILSQLESLKLENHRLSETVMKLELGLHEAkEISLADLQEnyiealnkLVSENQQl 587
Cdd:pfam15921 763 ekhflkEEKnklsqelstvATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA-SLQFAECQD--------IIQRQEQ- 832
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755531331 588 qkdlMSTKSELEHATNMckkkdGEIFNPAHSRAAGFKNAELKPIHGQHRHDGIKTEQYKT---GHHSPRGQTLDSiDP 662
Cdd:pfam15921 833 ----ESVRLKLQHTLDV-----KELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTAsflSHHSRKTNALKE-DP 900
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
182-612 |
1.16e-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: 55.41 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 182 SRLKRSYEKLqKKQLREFRGNTKSF----REDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEI 257
Cdd:TIGR04523 120 NKLEVELNKL-EKQKKENKKNIDKFlteiKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 258 IQAQLANRKQKLESVElSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLE 337
Cdd:TIGR04523 199 LELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 338 ALQEEQKELKASLQSQETFILEAKmQEKLQTTLKAVGTQqsverpLEDCQKErkysspgqgvLDNVLSQLDFSHSSEELL 417
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKSEISDLN-NQKEQDWNKELKSE------LKNQEKK----------LEEIQNQISQNNKIISQL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 418 QAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQIlqadqtysSALEGMKMEISQLTRELhq 497
Cdd:TIGR04523 341 NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI--------NDLESKIQNQEKLNQQK-- 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 498 rditiasakcsssdmEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETVMKLELGLHEAKeiSLADLQENYIEAL 577
Cdd:TIGR04523 411 ---------------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD--NTRESLETQLKVL 473
|
410 420 430
....*....|....*....|....*....|....*....
gi 755531331 578 ----NKLVSENQQLQKDLMSTKSELEHATNMCKKKDGEI 612
Cdd:TIGR04523 474 srsiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-601 |
2.04e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 258 IQAQLANR----KQKLESVELSSQS-EIQHLNSKLERAKDTICANELEIERLNIRVNdlmgtnmTILQDHRQKEEKLRES 332
Cdd:TIGR02168 207 RQAEKAERykelKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQ-------ELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 333 EKLLEALQEEQKELKASLQSQETFILEAKMQEK-LQTTLKAVGTQQSVERPLEDCQKERKYSspgqgvLDNVLSQLDFSH 411
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLAnLERQLEELEAQLEELESKLDELAEELAE------LEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 412 SSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQIlqadqtySSALEGMKMEISQL 491
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL-------EDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 492 TRELHQRDITIASAKCSSSDMEkqlKAEMQKAEEKAVEHKEILSQLeslkLENHRLSETVMKLELGLHEAKEISLADLQE 571
Cdd:TIGR02168 427 LKKLEEAELKELQAELEELEEE---LEELQEELERLEEALEELREE----LEEAEQALDAAERELAQLQARLDSLERLQE 499
|
330 340 350
....*....|....*....|....*....|....*....
gi 755531331 572 N---YIEALNKLVSENQQLQ------KDLMSTKSELEHA 601
Cdd:TIGR02168 500 NlegFSEGVKALLKNQSGLSgilgvlSELISVDEGYEAA 538
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
116-612 |
2.28e-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: 54.74 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 116 EWEGQTHaLETCLDIRDRELKALRSQL----DMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKlqeelsrlkRSYEKL 191
Cdd:pfam15921 69 AYPGKEH-IERVLEEYSHQVKDLQRRLnesnELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADI---------RRRESQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 192 QKKQLREFRGNT-------KSFRED-----RSEIERL-------TGKIEEFRQKSLDWEKQ--RLIYQQQV--------- 241
Cdd:pfam15921 139 SQEDLRNQLQNTvheleaaKCLKEDmledsNTQIEQLrkmmlshEGVLQEIRSILVDFEEAsgKKIYEHDSmstmhfrsl 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 242 -SSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHL-NSKLERAKDTICANELEIERLNIRVN------DLMG 313
Cdd:pfam15921 219 gSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASsarsqaNSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 314 TNMTILQDH--RQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKLQTTlkavgtqqsverPLEDCQKERK 391
Cdd:pfam15921 299 SQLEIIQEQarNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS------------ELTEARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 392 YSSPGQGVLDNVLSQL--DFSHSSEEL-LQAEVT-RLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLK 467
Cdd:pfam15921 367 QFSQESGNLDDQLQKLlaDLHKREKELsLEKEQNkRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQM 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 468 EQILQADQ----------TYSSALEGMKMEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEI---- 533
Cdd:pfam15921 447 ERQMAAIQgkneslekvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLrsrv 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 534 ---LSQLESLKLENHRLSETVMKLE-LGLHEAKEISLADLQENYIEALNKLVS-----------ENQQLQKDLMSTKSEL 598
Cdd:pfam15921 527 dlkLQELQHLKNEGDHLRNVQTECEaLKLQMAEKDKVIEILRQQIENMTQLVGqhgrtagamqvEKAQLEKEINDRRLEL 606
|
570
....*....|....
gi 755531331 599 EHATNMCKKKDGEI 612
Cdd:pfam15921 607 QEFKILKDKKDAKI 620
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
113-614 |
2.47e-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: 54.26 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 113 KKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMameykeelLKLQEELSRLKRSYEKLQ 192
Cdd:TIGR04523 167 QKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI--------SELKKQNNQLKDNIEKKQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 193 KKqlrefrgntksFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLAN-RKQKLES 271
Cdd:TIGR04523 239 QE-----------INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlNNQKEQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 272 VELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQ 351
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 352 SQETFI--LEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEEL-----------LQ 418
Cdd:TIGR04523 388 NLESQIndLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELiiknldntresLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 419 AEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQI---LQADQTYSSALEGMKMEISQLTREL 495
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIsslKEKIEKLESEKKEKESKISDLEDEL 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 496 HQRDITIASAKCSSSDMEK-----QLKAEMQKAEEKAVEHKEILSQLESLKLE-NHRLSETVMKL-----ELGLHEAKEI 564
Cdd:TIGR04523 548 NKDDFELKKENLEKEIDEKnkeieELKQTQKSLKKKQEEKQELIDQKEKEKKDlIKEIEEKEKKIsslekELEKAKKENE 627
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 755531331 565 SLADLQENYIEALNKLVSENQQLQKDL---MSTKSELEHATNMCKKKDGEIFN 614
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVKQIKETIkeiRNKWPEIIKKIKESKTKIDDIIE 680
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
233-553 |
1.15e-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: 52.53 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 233 QRLIYQQQVSSLEAQRKALAEQSEIIQAQLAnRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDL- 311
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSARE-KQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEk 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 312 MGTNMTILQDHRQKEEKLRESEKLLEALQeeqKELKASLQSQETFILEAKMQeKLQTTLKAVGT---------------Q 376
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQLD---KKHQAWLEEQKEQKREARTE-KQAYWQVVEGAldaqlallkaaiaarR 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 377 QSVERPLEDCQKERKYSSPGQGVLDNVLSQLdfshsseellQAEVTRLEGSLESvsatCKQLSQELMEKYEELK-RMEGH 455
Cdd:pfam12128 743 SGAKAELKALETWYKRDLASLGVDPDVIAKL----------KREIRTLERKIER----IAVRRQEVLRYFDWYQeTWLQR 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 456 NNEYRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRELHQRDitiaSAKCSSSDMEKQLKAEMQK---------AEEK 526
Cdd:pfam12128 809 RPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASE----KQQVRLSENLRGLRCEMSKlatlkedanSEQA 884
|
330 340
....*....|....*....|....*..
gi 755531331 527 AVEHKEILSQLESLKLENHRLSETVMK 553
Cdd:pfam12128 885 QGSIGERLAQLEDLKLKRDYLSESVKK 911
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
285-614 |
2.79e-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: 51.22 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 285 SKLERAKdticaNELEIERLNIRVNDLmgtnmtILQDHRQKEEKLR-ESEKLlealqEEQKELKASLQSQETFILeAKMQ 363
Cdd:TIGR02169 170 RKKEKAL-----EELEEVEENIERLDL------IIDEKRQQLERLRrEREKA-----ERYQALLKEKREYEGYEL-LKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 364 EKLQTTLKAVGTQ-QSVERPLEDCQKERKYSSPGQGVLDNVLSQLdfSHSSEELLQAEVTRLEGSLESVSATCKQLSQEL 442
Cdd:TIGR02169 233 EALERQKEAIERQlASLEEELEKLTEEISELEKRLEEIEQLLEEL--NKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 443 MEKYEELKRMEGHNNEYRTEIKKLKEQILQADQtyssALEGMKMEISQLTRELhqrditiasakcssSDMEKQLKAEMQK 522
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELER----EIEEERKRRDKLTEEY--------------AELKEELEDLRAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 523 AEEKAVEHKE--------------ILSQLESLKLENHRLSETVMKLELGLHEAKEiSLADLqenyIEALNKLVSENQQLQ 588
Cdd:TIGR02169 373 LEEVDKEFAEtrdelkdyreklekLKREINELKRELDRLQEELQRLSEELADLNA-AIAGI----EAKINELEEEKEDKA 447
|
330 340
....*....|....*....|....*.
gi 755531331 589 KDLMSTKSELEHATNMCKKKDGEIFN 614
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYD 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-612 |
9.21e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 314 TNMTILqdHRQKEekLRESEKLLEALQEEQKELKASLQSqetfiLEAKMQEKLQTTLKAVGTQQSVERPLEDCQKerkys 393
Cdd:TIGR02168 668 TNSSIL--ERRRE--IEELEEKIEELEEKIAELEKALAE-----LRKELEELEEELEQLRKELEELSRQISALRK----- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 394 spgqgvldnvlsQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQA 473
Cdd:TIGR02168 734 ------------DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 474 DQTYSSAlegmKMEISQLTRELHQRDITIASakcsssdMEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETVMK 553
Cdd:TIGR02168 802 REALDEL----RAELTLLNEEAANLRERLES-------LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 755531331 554 LELGLHEAKEISlaDLQENYIEALNKLVSENQQLQKDLMSTKSELEHATNMCKKKDGEI 612
Cdd:TIGR02168 871 LESELEALLNER--ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
210-425 |
1.20e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 210 RSEIERLTGKIEEFRQKS--LDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESV-----ELSSQSEIQH 282
Cdd:COG3206 188 RKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 283 LNSKLERAkdticanELEIERLNIRVNDlmgtnmtilqDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFIL--EA 360
Cdd:COG3206 268 LRAQLAEL-------EAELAELSARYTP----------NHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQarEA 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755531331 361 KMQEKLQTTLKAVGTQQSVERPLEdcQKERKYSSpGQGVLDNVLSQLDFSHSSEELLQAEVTRLE 425
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAELR--RLEREVEV-ARELYESLLQRLEEARLAEALTVGNVRVID 392
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
183-608 |
1.69e-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: 48.56 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 183 RLKRSYEKLQ------KKQLREFRGNTK----SFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALA 252
Cdd:pfam05483 216 KLKEDHEKIQhleeeyKKEINDKEKQVSllliQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 253 EQSEII----QAQLANRKQKLESVELSSQSEIQHLNSK------LERAKDTICANELEIERLNIRVNDLMGTNMTILQDH 322
Cdd:pfam05483 296 KELEDIkmslQRSMSTQKALEEDLQIATKTICQLTEEKeaqmeeLNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 323 -----------RQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKLQTTLKavGTQQSVERPLEDCQKErk 391
Cdd:pfam05483 376 edqlkiitmelQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK--GKEQELIFLLQAREKE-- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 392 ysspgqgvLDNVLSQLDFSHSSEELLQAEVTRLEGSLES-------VSATCKQLSQELMEKYEELKRMEGHNNEYRTEI- 463
Cdd:pfam05483 452 --------IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklknieLTAHCDKLLLENKELTQEASDMTLELKKHQEDIi 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 464 --KKLKEQILQADQTYSSALEGMKMEISQLTRELHQRDITIasaKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQLESLK 541
Cdd:pfam05483 524 ncKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV---KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK 600
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755531331 542 LENHRLSETVMKLElglHEAKEISLADLQENyiEALNKLVSENQQLQKDLMSTKSELEHATNMCKKK 608
Cdd:pfam05483 601 KQIENKNKNIEELH---QENKALKKKGSAEN--KQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE 662
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
219-391 |
2.13e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 219 KIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelssQSEIQHLNSKLERAKDTI---- 294
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELgera 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 295 --------CANELE-----------IERLNIrVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQET 355
Cdd:COG3883 93 ralyrsggSVSYLDvllgsesfsdfLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 755531331 356 fILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERK 391
Cdd:COG3883 172 -ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
210-470 |
2.28e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 210 RSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEI---------IQAQLANRKQKLESVELSSqSEI 280
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELERLDASS-DDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 281 QHLNSKLERAkdticanELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQK-----ELKASLQSQET 355
Cdd:COG4913 688 AALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 356 FILEAKMQEKLQTTLKAVGTQQS-VERPLEDCQKE--RKYSSPGQGVLDNVLSQLDFshsseellQAEVTRLEGSlesvs 432
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNrAEEELERAMRAfnREWPAETADLDADLESLPEY--------LALLDRLEED----- 827
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 755531331 433 atckqlsqELMEKYEELKRMEGHNN---------EYRTEIKKLKEQI 470
Cdd:COG4913 828 --------GLPEYEERFKELLNENSiefvadllsKLRRAIREIKERI 866
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
192-597 |
2.85e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 192 QKKQLREFRGNTKS----FREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLAnrkq 267
Cdd:PRK02224 228 QREQARETRDEADEvleeHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG---- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 268 kLESVELSSQSEIQhlnSKLERAKDTiCANELEIERLNIrvndlmgtnmtilQDHRQKEEKLRESEKLLEA----LQEEQ 343
Cdd:PRK02224 304 -LDDADAEAVEARR---EELEDRDEE-LRDRLEECRVAA-------------QAHNEEAESLREDADDLEEraeeLREEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 344 KELKASLQSQETFIleakmqEKLQTTLKAVGTQ-QSVERPLEDCQKERKYSspgQGVLDNVLSQLDFSHSSEELLQAEVT 422
Cdd:PRK02224 366 AELESELEEAREAV------EDRREEIEELEEEiEELRERFGDAPVDLGNA---EDFLEELREERDELREREAELEATLR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 423 RLEGSLESVSA--------TCKQLSQE------LMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSA--LEGMKM 486
Cdd:PRK02224 437 TARERVEEAEAlleagkcpECGQPVEGsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrIERLEE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 487 EISQLTRELHQRDITIA--SAKCSSSDMEKQ-LKAEMQKAEEKAVE-HKEILSQLESLKLENHRLSETVMKLElglHEAK 562
Cdd:PRK02224 517 RREDLEELIAERRETIEekRERAEELRERAAeLEAEAEEKREAAAEaEEEAEEAREEVAELNSKLAELKERIE---SLER 593
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 755531331 563 EISLADLQENYIEALNKLVSENQQLQ------KDLMSTKSE 597
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAelnderRERLAEKRE 634
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
96-303 |
3.57e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 96 EAELQELMKQIDIM------VAHKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAME 169
Cdd:COG4942 26 EAELEQLQQEIAELekelaaLKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 170 YkeellklqeelSRLKRSYEKLQKKQLREFRGNTKSF--------------REDRSEIERLTGKIEEFRQKSLDWEKQRL 235
Cdd:COG4942 106 L-----------AELLRALYRLGRQPPLALLLSPEDFldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755531331 236 IYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLEsvelSSQSEIQHLNSKLERAKDTICANELEIER 303
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELA----ELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
225-599 |
1.16e-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: 45.73 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 225 QKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEiqhlnsKLERAKDTICANELEIERL 304
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA------PLAAHIKAVTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 305 NIRVNDLMGTNMTIL---QDHRQKEEKLRESEKLLEALQEEQKELkASLQSQETFILEAKMQEKlqTTLKAVGTQQSVER 381
Cdd:TIGR00618 313 HTELQSKMRSRAKLLmkrAAHVKQQSSIEEQRRLLQTLHSQEIHI-RDAHEVATSIREISCQQH--TLTQHIHTLQQQKT 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 382 PLEDcqkERKYSSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNE--- 458
Cdd:TIGR00618 390 TLTQ---KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaq 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 459 -YRTEIKKL--KEQILQADQTYSSALEGMKMEISQLTREL---------HQRDITIASAKCSSSDMEKQLKAEMQKAEEK 526
Cdd:TIGR00618 467 sLKEREQQLqtKEQIHLQETRKKAVVLARLLELQEEPCPLcgscihpnpARQDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755531331 527 aVEHK--EILSQLESLKLENHRLSETVMKLELGLHEAKEIslADLQENYIEALNKLVSENQQLQKDLMSTKSELE 599
Cdd:TIGR00618 547 -VYHQltSERKQRASLKEQMQEIQQSFSILTQCDNRSKED--IPNLQNITVRLQDLTEKLSEAEDMLACEQHALL 618
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
94-360 |
2.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 94 SCEAELQELMKQIDIMVAhKKSEWEgqthALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEE 173
Cdd:COG4913 665 SAEREIAELEAELERLDA-SSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 174 LLKLQEELSRL--KRSYEKLQKKQLREFRGN-TKSFREDRSEIERLTGKIEE-FRQKSLDWekqRLIYQQQVSSLEAQRK 249
Cdd:COG4913 740 EDLARLELRALleERFAAALGDAVERELRENlEERIDALRARLNRAEEELERaMRAFNREW---PAETADLDADLESLPE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 250 ALAEQSEIIQAQLANRKQKL-ESVELSSQSEIQHLNSKLERAKDTIcanELEIERLNirvndlmgtnmTILQDHRQKEE- 327
Cdd:COG4913 817 YLALLDRLEEDGLPEYEERFkELLNENSIEFVADLLSKLRRAIREI---KERIDPLN-----------DSLKRIPFGPGr 882
|
250 260 270
....*....|....*....|....*....|....*
gi 755531331 328 --KLRESEKLLEALQEEQKELKASLQSQETFILEA 360
Cdd:COG4913 883 ylRLEARPRPDPEVREFRQELRAVTSGASLFDEEL 917
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
152-391 |
2.33e-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: 44.37 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 152 LHQQIEEHEKTKQEMAmeykeellKLQEELSRLKRSYEKLQKKQlrefrgntksfREDRSEIERLTGKIEEFRQKSLDWE 231
Cdd:COG4942 15 AAAQADAAAEAEAELE--------QLQQEIAELEKELAALKKEE-----------KALLKQLAALERRIAALARRIRALE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 232 KQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESveLSSQSEIQHLNSKlerakdticANELEIERLNIRVNDL 311
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR--LGRQPPLALLLSP---------EDFLDAVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 312 MGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETfILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERK 391
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA-ALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
187-506 |
4.09e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 187 SYEKLQKKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRK 266
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 267 QKLESvelsSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKEL 346
Cdd:COG4372 94 AELAQ----AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 347 KASLQSQETFILEAKMQEKLQTTLKAVGTQQ---SVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEELLQAEVTR 423
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEelaEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 424 LEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRELHQRDITIA 503
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
...
gi 755531331 504 SAK 506
Cdd:COG4372 330 LAL 332
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
207-353 |
4.18e-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: 42.60 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 207 REDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelSSQSEIQHLNSK 286
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQKE 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755531331 287 LERAKDTICANELEIERLNIRVNdlmgtnmtilqdhrQKEEKLRESEKLLEALQEEQKELKASLQSQ 353
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIE--------------ELEEELAELEAELAELEAELEEKKAELDEE 150
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
130-486 |
5.65e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 130 IRDRELKALRSQLDMKHKEVGILHQQIEEHEKTK---QEMAMEYKEELLKLQEELSRLKRSYEKLQKKQLREFRGNtksf 206
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKeqaKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 207 REDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEaqrKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSK 286
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ---EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 287 LERAKDTICANELEIERLNIRvndlmgtnMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKL 366
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKE--------LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 367 QTTLKAVGTQQSVERPLEdcqkerkysspgqgVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKY 446
Cdd:pfam02463 395 EELELKSEEEKEAQLLLE--------------LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 755531331 447 EELKRMEGHNNEYRTEIKKLKEQILQADQTYSSALEGMKM 486
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQ 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
377-599 |
7.14e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 377 QSVERPLEDCQKERkysSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQ-------LSQELMEKYEEL 449
Cdd:TIGR02169 684 EGLKRELSSLQSEL---RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 450 KRMEGHNNEYRTEIKKLKEQILQADQTYSSAlegmkmEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVE 529
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 530 HKEILSQLESLKLENHRLSETVMKLELGLHEAKEIsladlQENYIEALNKLVSENQQLQKDLMSTKSELE 599
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-----LEELEAALRDLESRLGDLKKERDELEAQLR 899
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
140-607 |
8.88e-04 |
|
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: 42.90 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 140 SQLDMKHKEVGILHQQIEEHEKtkqEMAMEYKEELLKLQEELSRLkRSYEKLQKKQLREFRGNTKSFRED----RSEIER 215
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDET---LIASRQEERQETSAELNQLL-RTLDDQWKEKRDELNGELSAADAAvakdRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 216 LTGKIEEFRQKSLDWEKQRL----IYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKlesVELSSQSEIQHLNSKLERAK 291
Cdd:pfam12128 327 LEDQHGAFLDADIETAAADQeqlpSWQSELENLEERLKALTGKHQDVTAKYNRRRSK---IKEQNNRDIAGIKDKLAKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 292 DTICANELEIErlnirvNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEA--------KMQ 363
Cdd:pfam12128 404 EARDRQLAVAE------DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLenfderieRAR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 364 EKLQTTLKAVGTQQSVERPL--------EDCQKERKYSSPGQGVLDNVLSQLD-FSHSSEELLQAEVTRLEGSLESVSAT 434
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQArkrrdqasEALRQASRRLEERQSALDELELQLFpQAGTLLHFLRKEAPDWEQSIGKVISP 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 435 cKQLSQELMEKYEELKRMEGHNNEYrteikKLKEQILQADQTYSSALEgmkmeiSQLTRELHQRDITIASAKCSSSDMEK 514
Cdd:pfam12128 558 -ELLHRTDLDPEVWDGSVGGELNLY-----GVKLDLKRIDVPEWAASE------EELRERLDKAEEALQSAREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 515 QLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETVMKLELGLHEAkeisLADLQENYIEALNKLVSENQQLQKDLMST 594
Cdd:pfam12128 626 QLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKA----LAERKDSANERLNSLEAQLKQLDKKHQAW 701
|
490
....*....|....*...
gi 755531331 595 KSE-----LEHATNMCKK 607
Cdd:pfam12128 702 LEEqkeqkREARTEKQAY 719
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
97-510 |
9.42e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 97 AELQELMKQIDIMVA---HKKSEWEGQTHALETCldirdrelKALRSQLDMKHKEVGILHQQIE-------EHEKTKQEM 166
Cdd:pfam15921 517 AEITKLRSRVDLKLQelqHLKNEGDHLRNVQTEC--------EALKLQMAEKDKVIEILRQQIEnmtqlvgQHGRTAGAM 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 167 AMEYKEELLKLQEELSRLKRsYEKLQKKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEA 246
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQE-FKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRN 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 247 QRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDT---------------------ICANELEIERLN 305
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghamkvamgmqkqITAKRGQIDALQ 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 306 IRVNDL--MGTNMTiLQDHRQKEEKLRESEKL-------------LEALQEEQKELKASLQSQETFILEAKMQEKLQTTL 370
Cdd:pfam15921 748 SKIQFLeeAMTNAN-KEKHFLKEEKNKLSQELstvateknkmageLEVLRSQERRLKEKVANMEVALDKASLQFAECQDI 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 371 KAVGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLdfshsseeLLQAEVTRLEGSLESVSATCKQLSQELMeKYEELK 450
Cdd:pfam15921 827 IQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRL--------LQPASFTRTHSNVPSSQSTASFLSHHSR-KTNALK 897
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 451 rmEGHNNEYRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRELHQRDITIASAKCSSS 510
Cdd:pfam15921 898 --EDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIESSLRSDI 955
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
138-510 |
1.21e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 138 LRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLqKKQLREFRGNTKSFREDRSEIERLT 217
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAEL-KEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 218 GKIEEFRQKSLDwekQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQK-----------------LESVELSSQSEI 280
Cdd:pfam07888 111 EELSEEKDALLA---QRAAHEARIRELEEDIKTLTQRVLERETELERMKERakkagaqrkeeeaerkqLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 281 QHLNSKLERAKDTICANELEIERLNIRVNDLMGT----------NMTILQDHRQKEEKLRESEKLLEALQEEQKELkASL 350
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrkeaeNEALLEELRSLQERLNASERKVEGLGEELSSM-AAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 351 QSQETFILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKysspgqgvldNVLSQLDFSHSSEELLQAEVTRLEgsles 430
Cdd:pfam07888 267 RDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERE----------TLQQSAEADKDRIEKLSAELQRLE----- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 431 vsatcKQLSQELMEKYE---ELKRMEGHN----NEYRTEIKKLKEQiLQADQTYSSALEGMKMEISQLTRELHQRDITIA 503
Cdd:pfam07888 332 -----ERLQEERMEREKlevELGREKDCNrvqlSESRRELQELKAS-LRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
....*..
gi 755531331 504 SAKCSSS 510
Cdd:pfam07888 406 DAKWSEA 412
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
105-565 |
2.09e-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: 41.88 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 105 QIDIMVAHKKSEWEGQTHALE--------TCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLK 176
Cdd:TIGR00618 423 QGQLAHAKKQQELQQRYAELCaaaitctaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 177 LQEELSRLKRSYEKLQkkQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSE 256
Cdd:TIGR00618 503 PCPLCGSCIHPNPARQ--DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDN 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 257 IIQAQLANRKQKLEsvelssqsEIQHLNSKLERAKDTI-CANELEIERLNIRVNDLmgtnmTILQDHRQKEeklresekl 335
Cdd:TIGR00618 581 RSKEDIPNLQNITV--------RLQDLTEKLSEAEDMLaCEQHALLRKLQPEQDLQ-----DVRLHLQQCS--------- 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 336 lealQEEQKELKASLQSQETFILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEE 415
Cdd:TIGR00618 639 ----QELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 416 LLQAEVTRLEGSLESVSATCKQ---LSQELMEKYEELKRMEGHNNEYRTEIKKLKEQI-LQADQTYSSALEGMKMEISQL 491
Cdd:TIGR00618 715 EYDREFNEIENASSSLGSDLAAredALNQSLKELMHQARTVLKARTEAHFNNNEEVTAaLQTGAELSHLAAEIQFFNRLR 794
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755531331 492 TRELHQRDITIASAKCSSSDMEKQLKAE---MQKAEEKAVEHKEILSQ-LESLKLENHRLSETVMKLELGLHEAKEIS 565
Cdd:TIGR00618 795 EEDTHLLKTLEAEIGQEIPSDEDILNLQcetLVQEEEQFLSRLEEKSAtLGEITHQLLKYEECSKQLAQLTQEQAKII 872
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
236-505 |
2.21e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 236 IYQQQvsSLEAQRKALAEQSEIIQAQLANRKQKLESVElssqseiqhlnsklerakdticaNELEIERLNIRVNDLMGTN 315
Cdd:COG3206 160 AYLEQ--NLELRREEARKALEFLEEQLPELRKELEEAE-----------------------AALEEFRQKNGLVDLSEEA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 316 MTILQdhrqkeeKLRESEKLLEALQEEQKELKASLQSqetfiLEAKMQEKLQT--TLKAVGTQQSVERPLEDCQKE---- 389
Cdd:COG3206 215 KLLLQ-------QLSELESQLAEARAELAEAEARLAA-----LRAQLGSGPDAlpELLQSPVIQQLRAQLAELEAElael 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 390 RKYSSPGQGVLDNVLSQLDfshSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQ 469
Cdd:COG3206 283 SARYTPNHPDVIALRAQIA---ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
250 260 270
....*....|....*....|....*....|....*.
gi 755531331 470 ILQADQTYSSALEgmKMEISQLTRELHQRDITIASA 505
Cdd:COG3206 360 VEVARELYESLLQ--RLEEARLAEALTVGNVRVIDP 393
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
136-609 |
2.81e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 136 KALRSQLDMKHKEVGILHQQIEEHEKTKQ--EMAMEYKEELLKLQEELSRLKRSYEKLQKKQLREFRGNTKSFREDRSEI 213
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 214 ERLTGKIEEFRQKsldwEKQRLIYQQQVSSLEAQRKAL-AEQSEIIQAQLANRKQKLEsvELSSQSEIQHLNSKLERAKD 292
Cdd:PTZ00121 1447 DEAKKKAEEAKKA----EEAKKKAEEAKKADEAKKKAEeAKKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 293 TICANELEIERLNIRVNDLMGTnmtilqDHRQKEEKLRESEKLLEAlqEEQKELKASLQSQETFILEAKMQEKLQTTLKA 372
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKA------EEKKKADELKKAEELKKA--EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA 1592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 373 vgtqqSVERPLEDCQKERKYSSPgqgvldnvlsqlDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRM 452
Cdd:PTZ00121 1593 -----RIEEVMKLYEEEKKMKAE------------EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 453 EGHNNEYRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRElhqrditiASAKCSSSDMEKQLKAEMQKAEEKAVEHKE 532
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE--------AEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755531331 533 ILSQLESLKLENHRlsETVMKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMSTKSELEHATNMCKKKD 609
Cdd:PTZ00121 1728 NKIKAEEAKKEAEE--DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
122-294 |
3.00e-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: 39.91 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 122 HALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLqkkqlrefrG 201
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL---------G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 202 NTKSFREdrseIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQ 281
Cdd:COG1579 84 NVRNNKE----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|...
gi 755531331 282 HLNSKLERAKDTI 294
Cdd:COG1579 160 ELEAEREELAAKI 172
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
152-558 |
3.11e-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: 40.88 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 152 LHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKlQKKQLREFRGNTKSFREDRSEIER-LTGKIEEFRQKSLDW 230
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDR-ESDRNQELQKRIRLLEKREAEAEEaLREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 231 EKQRLIYQQQVSSLE-------AQRKALAEQSEIIQ-AQLANRKQKLESVELSSQSEIQH--------LNSKLERAKDTI 294
Cdd:pfam05557 86 EALNKKLNEKESQLAdarevisCLKNELSELRRQIQrAELELQSTNSELEELQERLDLLKakaseaeqLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 295 CANELEIERLnIRVNDLMGTNMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQEtfILEAK---MQEKLQTTLK 371
Cdd:pfam05557 166 AEAEQRIKEL-EFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKL--LLKEEvedLKRKLEREEK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 372 AVGTQQSVERPLEDCQKERK-YSSPGQGVLDNVLSQLDFSHSSEELLQ------AEVTRLEGSLESVSATCKQLSQELME 444
Cdd:pfam05557 243 YREEAATLELEKEKLEQELQsWVKLAQDTGLNLRSPEDLSRRIEQLQQreivlkEENSSLTSSARQLEKARRELEQELAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 445 KYEELKRMEGHNNEYRTEIKKLKEQILQADQ-------------------TYSSALEGMKMEISQLTRELH--------- 496
Cdd:pfam05557 323 YLKKIEDLNKKLKRHKALVRRLQRRVLLLTKerdgyrailesydkeltmsNYSPQLLERIEEAEDMTQKMQahneemeaq 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755531331 497 ----QRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEILS---QLESLKLENHRLSETVMKLELGL 558
Cdd:pfam05557 403 lsvaEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSlrrKLETLELERQRLREQKNELEMEL 471
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
169-481 |
3.23e-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: 40.71 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 169 EYKEELLKLQEELSRLKRSYEKLQKKQLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIyqqqvssleaqR 248
Cdd:COG5185 240 DPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI-----------K 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 249 KALAEQSEIIQAQLANrkQKLESVELSSQSEIQHLNSKLERAKDTIcanELEIERLNIRVNDLMGTNmtilqDHRQKEEK 328
Cdd:COG5185 309 KATESLEEQLAAAEAE--QELEESKRETETGIQNLTAEIEQGQESL---TENLEAIKEEIENIVGEV-----ELSKSSEE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 329 LRESEKLLEALQEEQKELKASLQSQETFILEAkmqekLQTTLKAVGTQ-QSVERPLEdcQKERKYSSPGQgVLDNVLSQL 407
Cdd:COG5185 379 LDSFKDTIESTKESLDEIPQNQRGYAQEILAT-----LEDTLKAADRQiEELQRQIE--QATSSNEEVSK-LLNELISEL 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755531331 408 DFS-HSSEELLQAEVTrlegslESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSAL 481
Cdd:COG5185 451 NKVmREADEESQSRLE------EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKL 519
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
185-571 |
3.23e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 185 KRSYEKLqKKQLREFRGNTKSFREDRSEIERLTGKIEEFR--QKSLDWEKQRLIYQQQV--SSLEAQRKALAEQSEIIQA 260
Cdd:PRK01156 345 KSRYDDL-NNQILELEGYEMDYNSYLKSIESLKKKIEEYSknIERMSAFISEILKIQEIdpDAIKKELNEINVKLQDISS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 261 QLANRKQKLESVeLSSQSEIQHLNSKLE-RAKDTICANELEIERLNIRVNDLMgtnmtilQDHRQKEEKLRESEKLLEAL 339
Cdd:PRK01156 424 KVSSLNQRIRAL-RENLDELSRNMEMLNgQSVCPVCGTTLGEEKSNHIINHYN-------EKKSRLEEKIREIEIEVKDI 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 340 QEEQKELKASLQSqetfiLEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQL---DFSHSSEEL 416
Cdd:PRK01156 496 DEKIVDLKKRKEY-----LESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkleDLDSKRTSW 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 417 LQAEVTRLEGSLESVSATCKQLSQEL----------------MEKYEE--LKRMEGHNNEYRTEIKKLKEQILQADqTYS 478
Cdd:PRK01156 571 LNALAVISLIDIETNRSRSNEIKKQLndlesrlqeieigfpdDKSYIDksIREIENEANNLNNKYNEIQENKILIE-KLR 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 479 SALEGMKMEISQLtRELHQRDITIASAKCSSSDMEKQLKAEMQKAEekaVEHKEILSQLESLKLENHRLSETVMKLELGL 558
Cdd:PRK01156 650 GKIDNYKKQIAEI-DSIIPDLKEITSRINDIEDNLKKSRKALDDAK---ANRARLESTIEILRTRINELSDRINDINETL 725
|
410
....*....|....*
gi 755531331 559 HEAKEI--SLADLQE 571
Cdd:PRK01156 726 ESMKKIkkAIGDLKR 740
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
183-366 |
3.47e-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: 40.88 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 183 RLKRSYEKLQkkqlREFRGNTKSFREDRSEIER----LTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAE----- 253
Cdd:pfam05557 6 ESKARLSQLQ----NEKKQMELEHKRARIELEKkasaLKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 254 -QSEIIQAQLANRK----QKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRvNDLMGTNMtilQDHRQKEEK 328
Cdd:pfam05557 82 kKYLEALNKKLNEKesqlADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQER-LDLLKAKA---SEAEQLRQN 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 755531331 329 LRESEKLLEALQEEQKELKASLQSQETFILEAK-MQEKL 366
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKnSKSEL 196
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
96-599 |
3.55e-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: 40.93 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 96 EAELQELMKQIDIMVAHKKSEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEykeell 175
Cdd:pfam01576 52 ETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLE------ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 176 kLQEELSRLKrsyeKLQKKQLREFRGNTKSFREDRSEIERL---TGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKala 252
Cdd:pfam01576 126 -KVTTEAKIK----KLEEDILLLEDQNSKLSKERKLLEERIsefTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 253 eQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRES 332
Cdd:pfam01576 198 -KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 333 EKLLEalQEEQKELKASLQSQETFILEAKMQEKLQTTLKAVGTQQSVERPLEDCQKERKYSspgqgvldnvlsqldfshs 412
Cdd:pfam01576 277 QEDLE--SERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKA------------------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 413 seelLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKR-----------MEGHNNEYRTEIKklkeqilqadqtyssAL 481
Cdd:pfam01576 336 ----LEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRnkanlekakqaLESENAELQAELR---------------TL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 482 EGMKMEISQLTRELHQRdITIASAKCSSSDMEKQLKAEmqKAEEKAVEHKEILSQLESLKLENHRLSETVMKLELGLHEA 561
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQ-LQELQARLSESERQRAELAE--KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT 473
|
490 500 510
....*....|....*....|....*....|....*...
gi 755531331 562 KEIsladLQENYIEALNkLVSENQQLQKDLMSTKSELE 599
Cdd:pfam01576 474 QEL----LQEETRQKLN-LSTRLRQLEDERNSLQEQLE 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
152-361 |
3.67e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 152 LHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLQKKQlREFRGNTKSFREDRSEIERLTGKIEEfRQKSLdwe 231
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-QELAALEAELAELEKEIAELRAELEA-QKEEL--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 232 kQRLIYQQQVSSLEAQRKALAEQSEIIQAQ---------LANRKQKLESVElSSQSEIQHLNSKLERAKDTICANELEIE 302
Cdd:COG4942 107 -AELLRALYRLGRQPPLALLLSPEDFLDAVrrlqylkylAPARREQAEELR-ADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 755531331 303 RLNIRVNDLMGTNMTILQDHRQKEEKLRESeklLEALQEEQKELKASLQSQETFILEAK 361
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAE---LAELQQEAEELEALIARLEAEAAAAA 240
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
144-388 |
3.78e-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: 40.88 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 144 MKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLQ---KKQLREFRGNTKSFREDRSEIERL---- 216
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQaemDRQAAIYAEQERMAMERERELERIrqee 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 217 -TGKIEEFRQKSLDWEKQRLiyqQQVSSLEAQRKalaEQSEIIQAQL-ANRKQKLESVELSSQSEIQHLNSKLERAKDTI 294
Cdd:pfam17380 358 rKRELERIRQEEIAMEISRM---RELERLQMERQ---QKNERVRQELeAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 295 cANELEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESE---KLLEALQEEQKELKASLQSQETFILEAKMQEKLQTTLK 371
Cdd:pfam17380 432 -ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEeerKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE 510
|
250
....*....|....*..
gi 755531331 372 AVGTQQSVERPLEDCQK 388
Cdd:pfam17380 511 EERKRKLLEKEMEERQK 527
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
47-599 |
3.88e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 47 TQSCCQNKEDLEMEALLEGIQNRGHSGRNHLGmscDWSVGACRGFLTSCEAELQELMKQIDIMVAHKKSEWEGQTHALET 126
Cdd:pfam10174 148 TQKQTLGARDESIKKLLEMLQSKGLPKKSGEE---DWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPD 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 127 cldirDRELKALRSQLDMKHKEVGILHQQIEEHEktkQEMAMEYKEELLKLQEELSRLK-----RSYEKLQKKQLREFRg 201
Cdd:pfam10174 225 -----PAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDREEEIKqmevyKSHSKFMKNKIDQLK- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 202 ntKSFREDRSEIERLTGKIEEFRQKSLDWE------KQRLIYQQQVSS-LEAQRKALAEQSEIIQAQLANRKQKLESVel 274
Cdd:pfam10174 296 --QELSKKESELLALQTKLETLTNQNSDCKqhievlKESLTAKEQRAAiLQTEVDALRLRLEEKESFLNKKTKQLQDL-- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 275 ssQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLmgtnmtilqdhrqkEEKLRESEKLLEALQEEQKELKASLQSQE 354
Cdd:pfam10174 372 --TEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL--------------QEQLRDKDKQLAGLKERVKSLQTDSSNTD 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 355 TFI--LEAKMQEKlqttlkavgtqqsvERPLEDCQKERkySSPGQGVLDNVLSQLDFSHSSEE---LLQAEVTRLEGSLE 429
Cdd:pfam10174 436 TALttLEEALSEK--------------ERIIERLKEQR--EREDRERLEELESLKKENKDLKEkvsALQPELTEKESSLI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 430 SVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSalEGMKMEISQLTRELHQRDITIA--SAKC 507
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEA--VRTNPEINDRIRLLEQEVARYKeeSGKA 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 508 sSSDMEKQLKAEMQKAEEKAVEHKEIlSQLESLKLENHR-LSETVMKLELGLHEAKEISLADLQENYIEALNKLVSENQQ 586
Cdd:pfam10174 578 -QAEVERLLGILREVENEKNDKDKKI-AELESLTLRQMKeQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL 655
|
570
....*....|....*..
gi 755531331 587 LQKDLMS----TKSELE 599
Cdd:pfam10174 656 QLEELMGalekTRQELD 672
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-373 |
4.01e-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: 40.81 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 92 LTSCEAELQELMKQIDIMVAHKKsEWEGQTHALETCLDIRDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYK 171
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 172 EELLKLQEELSRLKRsyeklQKKQLREFRGNTKSFREDRSEIER-LTGKIEEFRQKSLDWEKQRLIYQQ---QVSSLEAQ 247
Cdd:TIGR02168 835 ATERRLEDLEEQIEE-----LSEDIESLAAEIEELEELIEELESeLEALLNERASLEEALALLRSELEElseELRELESK 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 248 RKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIE-----------RLNIRVNDLMGTNM 316
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEddeeearrrlkRLENKIKELGPVNL 989
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 755531331 317 TILQDHRQKEEKLREseklleaLQEEQKELKASLQSQETFILE--AKMQEKLQTTLKAV 373
Cdd:TIGR02168 990 AAIEEYEELKERYDF-------LTAQKEDLTEAKETLEEAIEEidREARERFKDTFDQV 1041
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
313-513 |
4.40e-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: 40.32 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 313 GTNMTILQDHRQKEEKLRES-EKLLEALQEEQKELKASLQSQETFILEAKMQEK--LQTTLKAVGTQQSVERPLEDCQKE 389
Cdd:pfam07902 132 GIATRISEDTDKKLALINETiSGIRREYQDADRQLSSSYQAGIEGLKATMASDKigLQAEIQASAQGLSQRYDNEIRKLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 390 RKYSSPGQGVLDNVLSQLD-----FSHSSEELLQAEVTRLEGSLESVSATCKQLSQelmekyeELKRMEGHNNEYRTEIK 464
Cdd:pfam07902 212 AKITTTSSGTTEAYESKLDdlraeFTRSNQGMRTELESKISGLQSTQQSTAYQISQ-------EISNREGAVSRVQQDLD 284
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 755531331 465 KLKEQILQADQTYSS---ALEGMKMEISQLTRELHQRDITIA---SAKCSSSDME 513
Cdd:pfam07902 285 SYQRRLQDAEKNYSSltqTVKGLQSTVSDPNSKLESRITQLAgliEQKVTRGDVE 339
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
320-629 |
4.76e-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: 40.42 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 320 QDHRQKEEKLRESEKLLEALQEEQKELKasLQSQETFILEAKMQEKLQTTLKAVGTQQSVERPLED------CQKERKYS 393
Cdd:TIGR00606 613 ELESKEEQLSSYEDKLFDVCGSQDEESD--LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvCQRVFQTE 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 394 SPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQA 473
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 474 DQTYSSALEGMK-----------MEISQLTRELHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQLESLKL 542
Cdd:TIGR00606 771 ETLLGTIMPEEEsakvcltdvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 543 ENHRLSETVMKL-----ELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMSTKSELEHATNMCKKKDGEIFNPAH 617
Cdd:TIGR00606 851 LIQDQQEQIQHLksktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
330
....*....|..
gi 755531331 618 SRAAGFKNAELK 629
Cdd:TIGR00606 931 SKETSNKKAQDK 942
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
237-473 |
6.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 237 YQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGTnm 316
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR-- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 317 tiLQDHRQKEEKLRESE-----KLLEALQEEQKELKASLQSQETfiLEAKMQEKLQT-TLKAVGTQQSVERpledcqker 390
Cdd:COG4913 318 --LDALREELDELEAQIrgnggDRLEQLEREIERLERELEERER--RRARLEALLAAlGLPLPASAEEFAA--------- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 391 kysspgqgVLDNVLSQLDFSHSSEELLQAEVTRLEGSLEsvsatckQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQI 470
Cdd:COG4913 385 --------LRAEAAALLEALEEELEALEEALAEAEAALR-------DLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
...
gi 755531331 471 LQA 473
Cdd:COG4913 450 AEA 452
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-451 |
6.63e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 260 AQLANRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVndlmgtnmtilQDHRQKEEKLRE------SE 333
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI-----------EEVEARIKKYEEqlgnvrNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 334 KLLEALQEEQKELKASLQSQETFILEAKMQ-EKLQTTLKAVGTQqsverpLEDCQKErkysspgqgvLDNVLSQLDfshS 412
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERiEELEEELAELEAE------LAELEAE----------LEEKKAELD---E 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 755531331 413 SEELLQAEVTRLEGSLESVSATckqLSQELMEKYEELKR 451
Cdd:COG1579 150 ELAELEAELEELEAEREELAAK---IPPELLALYERIRK 185
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
277-553 |
6.83e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 277 QSEIQHLNSKLERAKDTICANELEIERLNIRVNDlmgtnmtILQDHRQKEEKLRESEKllealqeeqkELKASLQSQETF 356
Cdd:PHA02562 180 NQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGE-------NIARKQNKYDELVEEAK----------TIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 357 ILEAKMQ-EKLQTTLKAVGTQQS-VERPLEDCQKERKYSSPGqGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLEsvsat 434
Cdd:PHA02562 243 LLNLVMDiEDPSAALNKLNTAAAkIKSKIEQFQKVIKMYEKG-GVCPTCTQQISEGPDRITKIKDKLKELQHSLE----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 435 ckqlsqELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSalegmkmeisqltrelhqrdiTIASAKcsssdmek 514
Cdd:PHA02562 317 ------KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLIT---------------------LVDKAK-------- 361
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 755531331 515 QLKAEMQKAEEKAVEHKEILSQL-ESLKLENHRLSETVMK 553
Cdd:PHA02562 362 KVKAAIEELQAEFVDNAEELAKLqDELDKIVKTKSELVKE 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
132-583 |
8.59e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 132 DRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLqkkqlREFRGNTKSFREDRS 211
Cdd:PRK02224 369 ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE-----AELEATLRTARERVE 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 212 EIERL--TGKIEEFRQKSLDWEkqrliyqqQVSSLEAQRkalaEQSEIIQAQLANRKQKLESVElssqseiqhlnSKLER 289
Cdd:PRK02224 444 EAEALleAGKCPECGQPVEGSP--------HVETIEEDR----ERVEELEAELEDLEEEVEEVE-----------ERLER 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 290 AKDTICAnELEIERLNIRVNDLMgtnmtilQDHRQKEEKLRESEKLLEALQEEQKELkaslqsqetfilEAKMQEKLQTT 369
Cdd:PRK02224 501 AEDLVEA-EDRIERLEERREDLE-------ELIAERRETIEEKRERAEELRERAAEL------------EAEAEEKREAA 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 370 LKAVGTQQSVERPLEDCQKERkysspgqGVLDNVLSQLDfshsseellqaevtRLEGSLESVsATCKQLSQELMEKYEEL 449
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKL-------AELKERIESLE--------------RIRTLLAAI-ADAEDEIERLREKREAL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 450 KRMeghNNEYRTEIKKLKEQILQADqtysSALEGMKMEISQLTRELHQRDITIASAKCSSSDMEKqlkAEMQKaEEKAVE 529
Cdd:PRK02224 619 AEL---NDERRERLAEKRERKRELE----AEFDEARIEEAREDKERAEEYLEQVEEKLDELREER---DDLQA-EIGAVE 687
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 530 HKeiLSQLESLKLENHRLSETVMKLELGLHEAKEIS------LADLQENYIEALNKLVSE 583
Cdd:PRK02224 688 NE--LEELEELRERREALENRVEALEALYDEAEELEsmygdlRAELRQRNVETLERMLNE 745
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
96-347 |
8.68e-03 |
|
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: 39.67 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 96 EAELQELMKQIdimvahkkSEWEGQTHALETCLDIRDRELKALRSQldMKHKEvgilhQQIEEHEKTKQEMAMEYKEELL 175
Cdd:TIGR02169 797 QAELSKLEEEV--------SRIEARLREIEQKLNRLTLEKEYLEKE--IQELQ-----EQRIDLKEQIKSIEKEIENLNG 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 176 KLQEELSRLKRSyeKLQKKQLREFRGNTKSfredrsEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQS 255
Cdd:TIGR02169 862 KKEELEEELEEL--EAALRDLESRLGDLKK------ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 256 EIIQAQLANRKQklESVELSSQSEIQhlnsklerakdticaneLEIERLNIRVNDLMGTNMTILQDHRQKEEKLRESEKL 335
Cdd:TIGR02169 934 SEIEDPKGEDEE--IPEEELSLEDVQ-----------------AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
250
....*....|..
gi 755531331 336 LEALQEEQKELK 347
Cdd:TIGR02169 995 RAKLEEERKAIL 1006
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
131-469 |
9.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 131 RDRELKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLQKKqLREFRGNTKSFREDR 210
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK-ITARIGELKKEIKEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 211 ----SEIERLTGKIEEFRQKSLDWEKQRLI--YQQQVSSLEAQRKALAEQSEiiqaQLANRKQKLESVeLSSQSEIQHLN 284
Cdd:PRK03918 425 kkaiEELKKAKGKCPVCGRELTEEHRKELLeeYTAELKRIEKELKEIEEKER----KLRKELRELEKV-LKKESELIKLK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 285 SKLERAKDT-----------ICANELEIERLNIRVNDLMGTNMTILQDHRQKEE---KLRESEKLLEALQEEQKELKASL 350
Cdd:PRK03918 500 ELAEQLKELeeklkkynleeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKEL 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531331 351 qSQETFILEAKMQEKLQ----------TTLKAVGTQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLdfshsSEELLQAE 420
Cdd:PRK03918 580 -EELGFESVEELEERLKelepfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL-----RKELEELE 653
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 755531331 421 VTRLEGSLESVSATCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQ 469
Cdd:PRK03918 654 KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| |
