|
Name |
Accession |
Description |
Interval |
E-value |
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
2-662 |
0e+00 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 1121.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 2 KRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFV 81
Cdd:pfam09726 1 KRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLLIRSVYDSFKYQGLAFSVFFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 82 CVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIGY 161
Cdd:pfam09726 81 CIAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTEKGICLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 162 PVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILiHHNGGIPANK 241
Cdd:pfam09726 161 PVVTLGFGFKSYVSYKMRLRKQREVQKENEFYMQLLQQALPKEQQMLDRQERETSETAKGLSEVDPLAL-NQNGHSLNKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 242 KLSTTLPEIEYREKGKEKDKDAKKH-NLGINNNNILQPVDSKIQEIEYMENHINSKRLNND-LVGSTENLLKEDSC---- 315
Cdd:pfam09726 240 DSTLQLPELEYREKKNSGTSSGSDSkKSHNHNIHNLNHVDSKLQEKEYMENHSNSKRLNIStSPGSEEDLLVRESVssks 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 316 ----TASSKNYKNAS----GVVNSSPRSHSATNGSIPSSSS-KNEKKQKC-TSKGPSAHKDLMENCIPNNQLSKPDALVR 385
Cdd:pfam09726 320 ssssSSSNKNYKNASggsaNSSNSSPRSHSHNSGSVTSSSSsKNSKKQKGpGGKSGARHKDPAENCIPNNQLSKPDALVR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 386 LEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQE 465
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 466 ARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELRKYK 545
Cdd:pfam09726 480 ARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKYK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 546 ENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSit 625
Cdd:pfam09726 560 ESEKDTEVLMSALSAMQDKNQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEVMAVMPS-- 637
|
650 660 670
....*....|....*....|....*....|....*..
gi 40254350 626 ysaaTSPLSPVSPHYSSKFVETSPSGLDPNASVYQPL 662
Cdd:pfam09726 638 ----TSRITPVTPHYSSKFMDTSPSMRDPNASVYPPL 670
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
374-616 |
4.09e-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: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 374 NNQLSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNI 453
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 454 SQLEKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECtETLRSRIRELEAEGKKLTMDMKVKEEQI-- 531
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-KALREALDELRAELTLLNEEAANLRERLes 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 532 --RELELKVQELRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFS----ALGDAKRQLEIAQGQILQKDQ 605
Cdd:TIGR02168 829 leRRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleeALALLRSELEELSEELRELES 908
|
250
....*....|.
gi 40254350 606 EIKDLKQKIAE 616
Cdd:TIGR02168 909 KRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-624 |
5.86e-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: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 383 LVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAvqmkqkdKQNISQLEKKLKA 462
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-------ANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 463 EQEARSFVEKQLmEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELR 542
Cdd:TIGR02168 307 LRERLANLERQL-EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 543 -KYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAkrQLEIAQGQILQKDQEIKDLKQKIAEVMAVM 621
Cdd:TIGR02168 386 sKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEAL 463
|
...
gi 40254350 622 PSI 624
Cdd:TIGR02168 464 EEL 466
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
381-616 |
2.05e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 381 DALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKL 460
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 461 KAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTmdmKVKEEQIRELELKVQE 540
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR---AAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40254350 541 ---LRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 616
Cdd:COG1196 410 ealLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-616 |
5.78e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 385 RLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAvqmkqkdKQNISQLEKKLKAEQ 464
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL-------LAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 465 EARSFVEKQLmeekkrkkleeataaravafaaasrgectETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELR-K 543
Cdd:COG1196 309 ERRRELEERL-----------------------------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEaE 359
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40254350 544 YKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 616
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
374-616 |
2.82e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 374 NNQLSKPDA-LVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQN 452
Cdd:TIGR02168 711 EEELEQLRKeLEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 453 ISQLEKKLKAEQEARSFVEKQLmEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDMKVKEEQIR 532
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAEL-TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 533 ELELKVQELRK-YKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQK-------- 603
Cdd:TIGR02168 870 ELESELEALLNeRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlseey 949
|
250 260 270
....*....|....*....|....*....|....
gi 40254350 604 ---------------------DQEIKDLKQKIAE 616
Cdd:TIGR02168 950 sltleeaealenkieddeeeaRRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-618 |
6.95e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 383 LVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNaVQMKQKD------KQNISQL 456
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK-LEEALNDlearlsHSRIPEI 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 457 EKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTEtLRSRIRELEAEGKKLTMDMKVKEEQIRELEL 536
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-LKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 537 KVQELRK-YKENEKDTEVLMSALSAMQDKTQHLENSLSaetriklDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIA 615
Cdd:TIGR02169 876 ALRDLESrLGDLKKERDELEAQLRELERKIEELEAQIE-------KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
...
gi 40254350 616 EVM 618
Cdd:TIGR02169 949 EEL 951
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-616 |
1.24e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 385 RLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQ 464
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 465 EARSFVEKQLMEEKKRKkleeataaravafaaasrgectETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELRKY 544
Cdd:COG1196 379 EELEELAEELLEALRAA----------------------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40254350 545 KENEKDTEvlmsaLSAMQDKTQHLENSLSAETRIKLDLFSALGdAKRQLEIAQGQILQKDQEIKDLKQKIAE 616
Cdd:COG1196 437 EEEEEEAL-----EEAAEEEAELEEEEEALLELLAELLEEAAL-LEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
382-638 |
4.02e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 382 ALVRLEQDIKKLKADLQASRQVEQELRSQ--ISALSSTERGIRSEMGQLRQENELLQNKLHNAvqmkqkdKQNISQLEKK 459
Cdd:COG3206 176 ALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEA-------EARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 460 LKAEQEARSFVekqlmeekkrkkleeataaravafaaaSRGECTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQ 539
Cdd:COG3206 249 LGSGPDALPEL---------------------------LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 540 ELRKYKENEKDTEV--LMSALSAMQDKTQHLENSLsAETRIKLDLFSA----LGDAKRQLEIAQG---QILQKDQEIkdl 610
Cdd:COG3206 302 ALRAQLQQEAQRILasLEAELEALQAREASLQAQL-AQLEARLAELPEleaeLRRLEREVEVARElyeSLLQRLEEA--- 377
|
250 260
....*....|....*....|....*...
gi 40254350 611 kqKIAEVMAVMPSITYSAATSPLSPVSP 638
Cdd:COG3206 378 --RLAEALTVGNVRVIDPAVVPLKPVSP 403
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
367-615 |
1.59e-05 |
|
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: 48.43 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 367 LMENCIPNNQLSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERgIRSEMGQLRQENELLQNKLhnAVQMK 446
Cdd:TIGR00618 205 LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQE--AVLEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 447 QKDKQNISQLEKKLKAEQEARSFVEKQlmeekkrkkleeataaravafaaasRGECTETLRSRIRELEAEGKKLTMDMKV 526
Cdd:TIGR00618 282 TQERINRARKAAPLAAHIKAVTQIEQQ-------------------------AQRIHTELQSKMRSRAKLLMKRAAHVKQ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 527 KEEQIRELELKVQELRKYKENEKDTEVLMSALsAMQDKTQHLENSLSAETRIK---LDLFSALGDAKRQLEIAQGQILQK 603
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR-EISCQQHTLTQHIHTLQQQKttlTQKLQSLCKELDILQREQATIDTR 415
|
250
....*....|..
gi 40254350 604 DQEIKDLKQKIA 615
Cdd:TIGR00618 416 TSAFRDLQGQLA 427
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
386-616 |
2.55e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 386 LEQDIKKLKADLQASRQVEQELRSQ----------ISALSSTERGIRSEMGQLR---QENELLQNKLHNAVQMKQKDKQN 452
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKekeleevlreINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 453 ISQLEKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASrgECTETLRSRIRELEAEGKKLTMDMKVKEEQIR 532
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS--EFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 533 ELELKVQELR----KYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDlfsALGDAKRQLEIAQGQILQKDQEIK 608
Cdd:PRK03918 332 ELEEKEERLEelkkKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL---TPEKLEKELEELEKAKEEIEEEIS 408
|
....*...
gi 40254350 609 DLKQKIAE 616
Cdd:PRK03918 409 KITARIGE 416
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
381-613 |
3.89e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 381 DALVRLEQDIKKLkADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQEneLLQNKLHNAVQMKQKDKQNISQLEKKL 460
Cdd:COG4913 242 EALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 461 KAEQEARSFVEKQLMEekkrkkleeataaravafaaaSRGECTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQE 540
Cdd:COG4913 319 DALREELDELEAQIRG---------------------NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40254350 541 LRKykenekdtevlmsALSAMQDKTQHLENSLSAETRiklDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQK 613
Cdd:COG4913 378 SAE-------------EFAALRAEAAALLEALEEELE---ALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| CarR_dom_SF |
TIGR03462 |
lycopene cyclase domain; This domain is often repeated twice within the same polypeptide, as ... |
29-113 |
4.70e-05 |
|
lycopene cyclase domain; This domain is often repeated twice within the same polypeptide, as is observed in Archaea, Thermus, Sphingobacteria and Fungi. In the fungal sequences, this tandem domain pair is observed as the N-terminal half of a bifunctional protein, where it has been characterized as a lycopene beta-cyclase and the C-terminal half is a phytoene synthetase. In Myxococcus and Actinobacterial genomes this domain appears as a single polypeptide, tandemly repeated and usually in a genomic context consistent with a role in carotenoid biosynthesis. It is unclear whether any of the sequences in this family truly encode lycopene epsilon cyclases. However a number are annotated as such. The domain is generally hydrophobic with a number of predicted membrane spanning segments and contains a distinctive motif (hPhEEhhhhhh). In certain sequences one of either the proline or glutamates may vary, but always one of the tandem pair appear to match this canonical sequence exactly.
Pssm-ID: 274590 Cd Length: 89 Bit Score: 42.20 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 29 FLYLKFLVVWALVLLA-DFVLEFRFEYLWPFWLFI------RSVYDSFryqGLAFSVFFVCVAFTSNiICLLFIPIQ-WL 100
Cdd:TIGR03462 1 YLYLGVLLVWALPVLAlLWVFRGPFLRLRALALALlialptFLVWDNL---AIRRGVWTYNPRYILG-IRLGDLPIEeFL 76
|
90
....*....|...
gi 40254350 101 FFAASTYVWVQYV 113
Cdd:TIGR03462 77 FFLLTPLLTVLWL 89
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
388-651 |
7.39e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 388 QDIKKLKADLQasrqveqELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEAR 467
Cdd:COG4942 20 DAAAEAEAELE-------QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 468 SFVEKQLMEEKKRKKLEEATAARAVAFAAA----SRGECTETLRSRIREleaegKKLTMDMKVKEEQIRELELKVQELRK 543
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLalllSPEDFLDAVRRLQYL-----KYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 544 YKENEKDTevLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPS 623
Cdd:COG4942 168 ELEAERAE--LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
250 260
....*....|....*....|....*....
gi 40254350 624 ITYSAATSPLS-PVSPHYSSKFVETSPSG 651
Cdd:COG4942 246 AGFAALKGKLPwPVSGRVVRRFGERDGGG 274
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
393-617 |
1.76e-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: 44.83 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 393 LKADLQA-----SRQVEQELRSQISALSST-------ERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKL 460
Cdd:pfam12128 583 VKLDLKRidvpeWAASEEELRERLDKAEEAlqsarekQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEK 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 461 KAEQEArsfVEKQLMEEKKRKKleeataaravafaaasrgectetlrSRIRELEAEGKKLTMDMKVKEEQIRE--LELKV 538
Cdd:pfam12128 663 QSEKDK---KNKALAERKDSAN-------------------------ERLNSLEAQLKQLDKKHQAWLEEQKEqkREART 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 539 QELRKYKENEKDTEVLMSALSAMQDK--TQHLENSLSAETRIKLDLFSalgdakrqLEIAQGQILQKDQEIKDLKQKIAE 616
Cdd:pfam12128 715 EKQAYWQVVEGALDAQLALLKAAIAArrSGAKAELKALETWYKRDLAS--------LGVDPDVIAKLKREIRTLERKIER 786
|
.
gi 40254350 617 V 617
Cdd:pfam12128 787 I 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
436-620 |
5.75e-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: 42.83 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 436 QNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLmeekkrkkleeataaravafaaasrgectETLRSRIRELEA 515
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-----------------------------AALERRIAALAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 516 EGKKLTMDMKVKEEQIRELELKVQELRKYKENEKdtEVLMSALSAMQdktqhlenSLSAETRIKLdLFSA--LGDAKRQL 593
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQK--EELAELLRALY--------RLGRQPPLAL-LLSPedFLDAVRRL 138
|
170 180
....*....|....*....|....*..
gi 40254350 594 EIAQGQILQKDQEIKDLKQKIAEVMAV 620
Cdd:COG4942 139 QYLKYLAPARREQAEELRADLAELAAL 165
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
352-621 |
1.20e-03 |
|
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: 42.02 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 352 KKQKCTSKGPSAHKDLMenCIPNNQLSKPDALVRLEqdIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQE 431
Cdd:pfam05483 481 EKEKLKNIELTAHCDKL--LLENKELTQEASDMTLE--LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 432 nellqnklhnavqMKQKDKQNISQLEkklKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRgectetlrsRIR 511
Cdd:pfam05483 557 -------------FIQKGDEVKCKLD---KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK---------NIE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 512 ELEAEGKKLTMDMKVKEEQIRELELKVQELrkykENEkdtevlmsaLSAMQDKTQHLENSLSAETRI-KLDLFSALGDAK 590
Cdd:pfam05483 612 ELHQENKALKKKGSAENKQLNAYEIKVNKL----ELE---------LASAKQKFEEIIDNYQKEIEDkKISEEKLLEEVE 678
|
250 260 270
....*....|....*....|....*....|..
gi 40254350 591 RQLEIAQGQI-LQKDQEIKdLKQKIAEVMAVM 621
Cdd:pfam05483 679 KAKAIADEAVkLQKEIDKR-CQHKIAEMVALM 709
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
179-624 |
1.34e-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: 41.96 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 179 RLRKQKEVQKENEFYMQLLQQALppeqqMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPANKKLSTTLPEIEyREKGKE 258
Cdd:TIGR00606 516 KLRKLDQEMEQLNHHTTTRTQME-----MLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKS-KEINQT 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 259 KDKDAKkhnlginnnnilqpVDSKIQEIEYMENHINS--KRLNNDLVGSTENLLKEDSCTASSKNYKNASGVVNSSPRSH 336
Cdd:TIGR00606 590 RDRLAK--------------LNKELASLEQNKNHINNelESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQR 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 337 SATNGS-------IPSSSSKNEKKQKCTSKGPSAHKDLME--NCIPNNQLSKPDALVRLEQDIKKL---------KADLQ 398
Cdd:TIGR00606 656 AMLAGAtavysqfITQLTDENQSCCPVCQRVFQTEAELQEfiSDLQSKLRLAPDKLKSTESELKKKekrrdemlgLAPGR 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 399 AS--RQVEQELRSQISALSSTERGIRSEMGQLRQENELLQN---KLHNA------------VQMKQKD-KQNISQLEKKL 460
Cdd:TIGR00606 736 QSiiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTimpEEESAkvcltdvtimerFQMELKDvERKIAQQAAKL 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 461 KAEQEARSFVE-KQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDMKVK---EEQIRELEL 536
Cdd:TIGR00606 816 QGSDLDRTVQQvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRqqfEEQLVELST 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 537 KVQEL-RKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKD--LKQK 613
Cdd:TIGR00606 896 EVQSLiREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdyLKQK 975
|
490
....*....|.
gi 40254350 614 IAEVMAVMPSI 624
Cdd:TIGR00606 976 ETELNTVNAQL 986
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
383-617 |
1.47e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 383 LVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQnklhnavQMKQKDKQNISQLEKKLKA 462
Cdd:COG4372 75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE-------QQRKQLEAQIAELQSEIAE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 463 EQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRgecTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELR 542
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQELQALSEAEAEQA---LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40254350 543 KYKE--NEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEV 617
Cdd:COG4372 225 DSLEakLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALL 301
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
506-575 |
1.91e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40254350 506 LRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELRK--YKENEKDTEVlmsalSAMQDKTQHLENSLSAE 575
Cdd:COG2433 418 LEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeeRREIRKDREI-----SRLDREIERLERELEEE 484
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
386-574 |
2.38e-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: 40.90 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 386 LEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNiSQLEKKLKAEQE 465
Cdd:COG4942 53 LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLLSPEDF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 466 ARSFVEKQLMEEKKRKKLEEATAARAVafaaasrgecTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELRKY- 544
Cdd:COG4942 132 LDAVRRLQYLKYLAPARREQAEELRAD----------LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLl 201
|
170 180 190
....*....|....*....|....*....|
gi 40254350 545 KENEKDTEVLMSALSAMQDKTQHLENSLSA 574
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
403-617 |
2.60e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 403 VEQELRSQISALSSTERGIRSEMGQLRQENELLQNKL------HNAVQMKQKDK---QNISQLEKKLKAEQEARSFVEKQ 473
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALeefrqkNGLVDLSEEAKlllQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 474 LmeekkrkkleeataaravafaaasrgectETLRSRIRELEAEGKKLTMDMKVKE--EQIRELELKVQELR-KYKENEkd 550
Cdd:COG3206 242 L-----------------------------AALRAQLGSGPDALPELLQSPVIQQlrAQLAELEAELAELSaRYTPNH-- 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40254350 551 tevlmSALSAMQDKTQHLENSLSAETRikldlfSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEV 617
Cdd:COG3206 291 -----PDVIALRAQIAALRAQLQQEAQ------RILASLEAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
378-557 |
2.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 378 SKPDALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTER--GIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQ 455
Cdd:COG4717 85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 456 LEkKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAfaaasrgectETLRSRIRELEAEGKKLTMDMKVKEEQIRELE 535
Cdd:COG4717 165 LE-ELEAELAELQEELEELLEQLSLATEEELQDLAEEL----------EELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180
....*....|....*....|..
gi 40254350 536 LKVQELRKYKENEKDTEVLMSA 557
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIA 255
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
375-616 |
2.88e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 375 NQLSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISALsstergiRSEMGQLRQENELLQNKLHNAVQMKQKDKQNIS 454
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQL-------REELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 455 QLEKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAaasrgectETLRSRIRELEAEGKKLTMDMKVKEEQIREL 534
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER--------QDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 535 ELKVQELRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKI 614
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
..
gi 40254350 615 AE 616
Cdd:COG4372 236 SA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
507-620 |
3.09e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 507 RSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELRK----------YKENEKDTEVLMSALSAMQDKTQHLENSLS--- 573
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeYSWDEIDVASAEREIAELEAELERLDASSDdla 688
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 40254350 574 -AETRIKlDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAV 620
Cdd:COG4913 689 aLEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
381-619 |
3.60e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 381 DALVRLEQDIKKLKADLQASRQVEQELRSQISALSstergirsemgQLRQENELLQNKLHNAVQMKQKDKQnISQLEKKL 460
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQ-----------ERREALQRLAEYSWDEIDVASAERE-IAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 461 KAEQEARSFVekqlmeekkrkkleeataaravafaaasrgectETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQE 540
Cdd:COG4913 678 ERLDASSDDL---------------------------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 541 LRkykenekdtevlmSALSAMQDKTQHLENSLSAETRIKLD-LFSALGDAKRQLEIA---QGQILQKDQEIKDLKQKIAE 616
Cdd:COG4913 725 AE-------------EELDELQDRLEAAEDLARLELRALLEeRFAAALGDAVERELRenlEERIDALRARLNRAEEELER 791
|
...
gi 40254350 617 VMA 619
Cdd:COG4913 792 AMR 794
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-619 |
5.01e-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: 40.05 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 383 LVRLEQDIKKLKADLQASRQVEQ-ELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLK 461
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 462 AEQEARSfvekQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTmdmKVKEEQIRELELKVQEL 541
Cdd:TIGR02169 347 EERKRRD----KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN---ELKRELDRLQEELQRLS 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40254350 542 RKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMA 619
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
386-459 |
5.56e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.33 E-value: 5.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40254350 386 LEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKK 459
Cdd:COG4026 133 LREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKK 206
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
383-621 |
5.87e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 383 LVRLEQDIKKLKADL-QASRQVE---QELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISqLEK 458
Cdd:pfam15921 319 LSDLESTVSQLRSELrEAKRMYEdkiEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS-LEK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 459 K------------------LKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRSrireleaegkkL 520
Cdd:pfam15921 398 EqnkrlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS-----------L 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 521 TMDMKVKEEQIRELelkVQELRKYKENEKDTEVLMSALSA-MQDKTQHLE--NSLSAETRIKLDLF-----------SAL 586
Cdd:pfam15921 467 TAQLESTKEMLRKV---VEELTAKKMTLESSERTVSDLTAsLQEKERAIEatNAEITKLRSRVDLKlqelqhlknegDHL 543
|
250 260 270
....*....|....*....|....*....|....*
gi 40254350 587 GDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVM 621
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLV 578
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
381-570 |
9.61e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 381 DALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEmgqLRQENELLQNKLHNAVQMKQKDKQNISQLEKKL 460
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 461 KAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRgectETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQE 540
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
170 180 190
....*....|....*....|....*....|
gi 40254350 541 LRKYKENEKDTEVLMSALSAMQDKTQHLEN 570
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
390-664 |
9.85e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 39.29 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 390 IKKLKADLQASRQVEQELRSQ----ISALSSTeRGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQ--------NISQLE 457
Cdd:COG5022 774 IQVIQHGFRLRRLVDYELKWRlfikLQPLLSL-LGSRKEYRSYLACIIKLQKTIKREKKLRETEEVefslkaevLIQKFG 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 458 KKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLrsriRELEAEGKKLTMDmkVKEEQIRELELK 537
Cdd:COG5022 853 RSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVN----LELESEIIELKKS--LSSDLIENLEFK 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 538 VQELRKYKENeKDTEVLMSALSAMQDKTQHLENSLSAETRIKlDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEV 617
Cdd:COG5022 927 TELIARLKKL-LNNIDLEEGPSIEYVKLPELNKLHEVESKLK-ETSEEYEDLLKKSTILVREGNKANSELKNFKKELAEL 1004
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 40254350 618 MAVMPSITYSAATSPLSPVSP---HYSSKFVETSPSGLdpnaSVYQPLKK 664
Cdd:COG5022 1005 SKQYGALQESTKQLKELPVEVaelQSASKIISSESTEL----SILKPLQK 1050
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
379-620 |
9.87e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.33 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 379 KPDALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQ------NKLHNAVQMKQKDKQN 452
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEatnaeiTKLRSRVDLKLQELQH 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 453 ISQLEKKLKAEQEARSFVEKQlMEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDMK------- 525
Cdd:pfam15921 536 LKNEGDHLRNVQTECEALKLQ-MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefkilkd 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254350 526 VKEEQIRELELKVQ--ELRKYKENEKDTEVLMSALSAMQDKTQHLE---------NSLSAETRI--------KLDLFSAL 586
Cdd:pfam15921 615 KKDAKIRELEARVSdlELEKVKLVNAGSERLRAVKDIKQERDQLLNevktsrnelNSLSEDYEVlkrnfrnkSEEMETTT 694
|
250 260 270
....*....|....*....|....*....|....
gi 40254350 587 GDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAV 620
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKV 728
|
|
| |
