|
Name |
Accession |
Description |
Interval |
E-value |
| DUF3668 |
pfam12416 |
Cep120 protein; This family includes the Cep120 protein which is associated with centriole ... |
1-149 |
9.92e-86 |
|
Cep120 protein; This family includes the Cep120 protein which is associated with centriole structure and function.
Pssm-ID: 463569 Cd Length: 226 Bit Score: 271.51 E-value: 9.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 1 MSVTIAFATQLEQLIPCTMKLPERQPEFFFYYSLLGNDVTNEPFNDLINPNFEPERASVRIRSSVEILRVYLALQSKLQI 80
Cdd:pfam12416 78 LSVTIAFATNLEQLVPSSMKLPEEKPGFFFYYSLLGNDVTNEPFKNLLNPNFEPERASVRIRSSLRVLRAYLSSQPYLQI 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843692 81 HLCCGDQSLGSTEIPLTGLLKKGSTEINQHPVTVEGAFTLDPPNRAKQKLAPIPVELAPTVGVSVALQR 149
Cdd:pfam12416 158 HLCCGNQSLGSTEVSLQGLLPDNSTELERKPVTIEGAFVLNPPNRAKQDLPEVPLELKPTVGVTVTLRR 226
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
478-732 |
4.03e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 478 ENQLKQKELahmQA-LAEEWKK-RDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQR 555
Cdd:COG1196 199 ERQLEPLER---QAeKAERYRElKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 556 nLQELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPE--IRLQSEINLLT 633
Cdd:COG1196 276 -LEELELELEEAQA----EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEelEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 634 LEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIR 713
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250
....*....|....*....
gi 1769843692 714 NELNRLRQQEQKQYQDSTE 732
Cdd:COG1196 431 AELEEEEEEEEEALEEAAE 449
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
459-728 |
1.02e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 459 EYKAALELEMWKEMQEDIfenQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASV 538
Cdd:COG1196 224 ELEAELLLLKLRELEAEL---EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 539 ESELQREKKELQsERQRNLQELQDSIRRAKEDCIH---QVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKD 615
Cdd:COG1196 301 EQDIARLEERRR-ELEERLEELEEELAELEEELEEleeELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 616 QQN--NKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRLRY 693
Cdd:COG1196 380 ELEelAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270
....*....|....*....|....*....|....*
gi 1769843692 694 LAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQ 728
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
527-764 |
2.35e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 527 DLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKIL 606
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 607 EKEFQQFKDQQnnkpeIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEEL 686
Cdd:COG1196 301 EQDIARLEERR-----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843692 687 EQMRLRylaAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKDgphgsvLEEGLDDYLTRLIEERDTL 764
Cdd:COG1196 376 EAEEEL---EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE------LEEALAELEEEEEEEEEAL 444
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
484-789 |
2.84e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.48 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 484 KELAHMQALAEEWKKRDRERESLVKKKvaeyTILEGKLQKTLIDLEKREQQLASVESELQR--EKKELQSERQRNLQELQ 561
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSEL----RRIENRLDELSQELSDASRKIGEIEKEIEQleQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 562 DSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYkiLEKEFQQFKDQQNNKPEIRlqSEINLLTlekVELER 641
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEV--SRIEARL---REIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 642 KLEsatksKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELeQMRLRYLAAEEKDTVKTERQ---ELLDIRNELNR 718
Cdd:TIGR02169 820 KLN-----RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL-NGKKEELEEELEELEAALRDlesRLGDLKKERDE 893
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1769843692 719 ----LRQQEQKQYQDSTEIASGKKdgpHGSVLEEGLDDYLTRLIEERDTLMRTGVYNHEDRIISELDRQIREILA 789
Cdd:TIGR02169 894 leaqLRELERKIEELEAQIEKKRK---RLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
455-764 |
1.20e-11 |
|
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: 68.54 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 455 RETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQ 534
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 535 LASVESELQREKKELQsERQRNLQELQDSIRRAKEDC---IHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQ 611
Cdd:TIGR02168 763 IEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 612 QFKDQ--QNNKPEIRLQSEINLLTLEKVELERKLESATKSKlhykqqwgRALKELARLKQREQESQMARLkkQQEELEQM 689
Cdd:TIGR02168 842 DLEEQieELSEDIESLAAEIEELEELIEELESELEALLNER--------ASLEEALALLRSELEELSEEL--RELESKRS 911
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1769843692 690 RLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGSvlEEGLDDYLTRLIEERDTL 764
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDD--EEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
479-725 |
1.39e-11 |
|
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: 68.54 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 479 NQLKQKELAhmqALAEEWKKRDRERESLvKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQSErqrnLQ 558
Cdd:TIGR02168 220 AELRELELA---LLVLRLEELREELEEL-QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE----LY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 559 ELQDSIRRAKEDCIHQVElerlKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNnkpeiRLQSEINLLTLEKVE 638
Cdd:TIGR02168 292 ALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKLE-----ELKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 639 LERKLESATKSKLHYKQQWGRALKELARLKQRE--QESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNEL 716
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQIasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
|
....*....
gi 1769843692 717 NRLRQQEQK 725
Cdd:TIGR02168 443 EELEEELEE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
461-732 |
1.47e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 461 KAALELEMWKEMQEDIfENQLKQKELAHMQALAEEwkKRDRERESLVKKKVAEytiLEGKLQKTLIDLEKREQQLASVES 540
Cdd:COG1196 250 ELEAELEELEAELAEL-EAELEELRLELEELELEL--EEAQAEEYELLAELAR---LEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 541 ELQREKKELQSERQRnLQELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQnnk 620
Cdd:COG1196 324 ELAELEEELEELEEE-LEELEEELEEAEE----ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA--- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 621 peIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKD 700
Cdd:COG1196 396 --AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270
....*....|....*....|....*....|..
gi 1769843692 701 TVKTERQELLDIRNELnRLRQQEQKQYQDSTE 732
Cdd:COG1196 474 LLEAALAELLEELAEA-AARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
449-693 |
1.00e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 449 EIQTEPRETLEYKAALELEMwKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDL 528
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEV-SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 529 EKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDcihQVELERL--KIKQLEEDKHRLQQQLNDAENKYKIL 606
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL---EEQLETLrsKVAQLELQIASLNNEIERLEARLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 607 EKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQ--ESQMARLKKQQE 684
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDaaERELAQLQARLD 492
|
....*....
gi 1769843692 685 ELEQMRLRY 693
Cdd:TIGR02168 493 SLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
518-732 |
1.59e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 518 EGKLQKTLIDLEKREQQLASVESELqrEKKELQSERQRNLQELQDSIRRAkedcihQVELERLKIKQLEEDKHRLQQQLN 597
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQL--KSLERQAEKAERYKELKAELREL------ELALLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 598 DAENKYKILEKEFQQfkdqqnnkpeirLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQ--ESQ 675
Cdd:TIGR02168 250 EAEEELEELTAELQE------------LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlERQ 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1769843692 676 MARLKKQQEELEQMRLRYLA-----AEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTE 732
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEelaelEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
475-728 |
1.70e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 475 DIFENQLKQKElAHMQALAEEWKKRDRERESLVKKKVAEYTILEgkLQKTLIDLEKREQQLASVESELQR------EKKE 548
Cdd:COG4913 613 AALEAELAELE-EELAEAEERLEALEAELDALQERREALQRLAE--YSWDEIDVASAEREIAELEAELERldassdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 549 LQSERQRnLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKI-----LEKEFQQFKDQQNNKpEI 623
Cdd:COG4913 690 LEEQLEE-LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAALGDAVER-EL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 624 R--LQSEINLLTLEKVELERKLESATKSklhYKQQW--------------GRALKELARLKQR---EQESQMARLKKQQE 684
Cdd:COG4913 768 RenLEERIDALRARLNRAEEELERAMRA---FNREWpaetadldadleslPEYLALLDRLEEDglpEYEERFKELLNENS 844
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1769843692 685 ELEQMRLRYLAAEEKDTVkteRQELLDIRNELNRLRQQEQKQYQ 728
Cdd:COG4913 845 IEFVADLLSKLRRAIREI---KERIDPLNDSLKRIPFGPGRYLR 885
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
484-783 |
3.91e-10 |
|
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: 63.60 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 484 KELAHMQALAEEWKKRDRERESL-----VKKKVAEYTILEGKlqKTLIDLEKREQQLASVESELQREKKELQSERQRNLQ 558
Cdd:pfam17380 221 KEVQGMPHTLAPYEKMERRKESFnlaedVTTMTPEYTVRYNG--QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 559 ElqdSIRRAKEDCIHQVELERlkikQLEEDKHRLQQQLND-----AENKYKILEKEFQ----QFKDQQNNKPEIRlQSEI 629
Cdd:pfam17380 299 E---RLRQEKEEKAREVERRR----KLEEAEKARQAEMDRqaaiyAEQERMAMEREREleriRQEERKRELERIR-QEEI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 630 -----NLLTLEKVELERK---------LESATKSKLhykqqwgraLKELARLKQREQESQMARLKKQQEELEQMRLRYLA 695
Cdd:pfam17380 371 ameisRMRELERLQMERQqknervrqeLEAARKVKI---------LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 696 AEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGS-----VLEEGLDDYLTRLIEERDTLM----- 765
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEeqrrkILEKELEERKQAMIEEERKRKlleke 521
|
330 340
....*....|....*....|..
gi 1769843692 766 ----RTGVYNHEDRIISELDRQ 783
Cdd:pfam17380 522 meerQKAIYEEERRREAEEERR 543
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
461-794 |
2.01e-09 |
|
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: 61.24 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 461 KAALELEmwkEMQEDIFENQLKQKELA-HMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVE 539
Cdd:TIGR02169 174 KALEELE---EVEENIERLDLIIDEKRqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 540 SELQREKKELQ------SERQRNLQELQDSIRRAKEDCIHQV--ELERLK--IKQLEEDKHRLQQQLNDAENKYKILEKE 609
Cdd:TIGR02169 251 EELEKLTEEISelekrlEEIEQLLEELNKKIKDLGEEEQLRVkeKIGELEaeIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 610 FQQFKDQ---------QNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKqREQESQMARLK 680
Cdd:TIGR02169 331 IDKLLAEieelereieEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK-REINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 681 KQQEELEQMrlrylaaeekdtvkteRQELLDIRNELNRLRQQeQKQYQDSTE--IASGKKDGPHGSVLEEGLDDYLTRLI 758
Cdd:TIGR02169 410 RLQEELQRL----------------SEELADLNAAIAGIEAK-INELEEEKEdkALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350
....*....|....*....|....*....|....*.
gi 1769843692 759 EERDTLMRTgvynhEDRiISELDRQIREILAKSNAS 794
Cdd:TIGR02169 473 DLKEEYDRV-----EKE-LSKLQRELAEAEAQARAS 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
548-795 |
3.02e-09 |
|
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: 59.78 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 548 ELQSERQRNLQELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQ--QNNKPEIRL 625
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEK----ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 626 QSEINLLtleKVELERKLESATKSKLHYK-------QQWGRALKELARLKQ--REQESQMARLKKQQEELEQmrLRYLAA 696
Cdd:COG4942 96 RAELEAQ---KEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAA--LRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 697 EEKDTVKTERQELLDIRNELNRLRQQEQKQyqdsteIASGKKDgphgsvlEEGLDDYLTRLIEERDTLmrtgvynheDRI 776
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKL------LARLEKE-------LAELAAELAELQQEAEEL---------EAL 228
|
250
....*....|....*....
gi 1769843692 777 ISELDRQIREILAKSNASN 795
Cdd:COG4942 229 IARLEAEAAAAAERTPAAG 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
479-795 |
4.60e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 479 NQLKQKELAHMQA----LAEEWKKRDRERESLVKKKVAEYTILEgklQKTLIDLEKREQQLASVESELQREKKELQSERQ 554
Cdd:PTZ00121 1500 DEAKKAAEAKKKAdeakKAEEAKKADEAKKAEEAKKADEAKKAE---EKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 555 RNLQELQDSIRRAKEDCIHQV-----ELERLKIKQL--EEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQS 627
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 628 EINllTLEKVELERKLESATKSKlhykqqwgralkELARLKQREQESQMARLKKQQEELEQM-RLRYLAAEEK---DTVK 703
Cdd:PTZ00121 1657 EEN--KIKAAEEAKKAEEDKKKA------------EEAKKAEEDEKKAAEALKKEAEEAKKAeELKKKEAEEKkkaEELK 1722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 704 TERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGSVLEEGLDDYLTRlieERDTLMRTGVYNHEDRIISELDRQ 783
Cdd:PTZ00121 1723 KAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK---EKEAVIEEELDEEDEKRRMEVDKK 1799
|
330
....*....|..
gi 1769843692 784 IREIlaKSNASN 795
Cdd:PTZ00121 1800 IKDI--FDNFAN 1809
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
539-726 |
5.69e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 539 ESELQREKKELQSERQRNLQELQDSIRRAKEDcIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQN 618
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEE-LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 619 NKPEI----RLQSEINLLTLEKVELERKLE---SATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRL 691
Cdd:COG4717 127 LLPLYqeleALEAELAELPERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|....*
gi 1769843692 692 RYLAAEEKdtVKTERQELLDIRNELNRLRQQEQKQ 726
Cdd:COG4717 207 RLAELEEE--LEEAQEELEELEEELEQLENELEAA 239
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
449-711 |
7.55e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.39 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 449 EIQTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYtiLEGKLQKTLIDL 528
Cdd:pfam13868 95 EKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEY--LKEKAEREEERE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 529 EKREQQLASVESELQREKKELQSERQRnlQELQDSIRRAKEDCIHQVElERLKIKQLEEDKHRLQQQLNDAENKYKILEK 608
Cdd:pfam13868 173 AEREEIEEEKEREIARLRAQQEKAQDE--KAERDELRAKLYQEEQERK-ERQKEREEAEKKARQRQELQQAREEQIELKE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 609 EFQQFkdqqnnkpEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQwgralkELAR--LKQREQESQMARLKKQQEEL 686
Cdd:pfam13868 250 RRLAE--------EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL------EHRRelEKQIEEREEQRAAEREEELE 315
|
250 260
....*....|....*....|....*
gi 1769843692 687 EQMRLRYLAAEEKDTVKTERQELLD 711
Cdd:pfam13868 316 EGERLREEEAERRERIEEERQKKLK 340
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
499-787 |
9.08e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 499 RDRERESLV-----KKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQ-----SERQRNLQELQDSIRRAK 568
Cdd:COG4913 595 RRRIRSRYVlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeySWDEIDVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 569 EdcihqvELERLK--IKQLEEdkhrLQQQLNDAENKYKILEKEFQQFKDQQnnkpeIRLQSEINLLTLEKVELERKLESA 646
Cdd:COG4913 675 A------ELERLDasSDDLAA----LEEQLEELEAELEELEEELDELKGEI-----GRLEKELEQAEEELDELQDRLEAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 647 TKSKLHYKQQwgRALKELARLKQREQESQMAR-LKKQQEELEQMRLRylaaeekdtvkterqelldIRNELNRLRQQEQK 725
Cdd:COG4913 740 EDLARLELRA--LLEERFAAALGDAVERELREnLEERIDALRARLNR-------------------AEEELERAMRAFNR 798
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843692 726 QYQDST-EIASGKKDGP-----HGSVLEEGLDDYLTRLIEERDTLMRTGVynheDRIISELDRQIREI 787
Cdd:COG4913 799 EWPAETaDLDADLESLPeylalLDRLEEDGLPEYEERFKELLNENSIEFV----ADLLSKLRRAIREI 862
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
469-721 |
1.01e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 469 WKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERE---SLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQRE 545
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEkelEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 546 KKELQSERQrNLQELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQLNDAEnKYKILEKEFQQFKDQQNN--KPEI 623
Cdd:PRK03918 244 EKELESLEG-SKRKLEEKIRELEE----RIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREieKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 624 RLQSEINLLTLEKVELERKLESATKSKLHYKQqwgrALKELARLKQREQESQMARLKKqqEELEQMRLRyLAAEEKDTVK 703
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKK--EELERLKKR-LTGLTPEKLE 390
|
250 260
....*....|....*....|..
gi 1769843692 704 TERQEL----LDIRNELNRLRQ 721
Cdd:PRK03918 391 KELEELekakEEIEEEISKITA 412
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
469-722 |
1.11e-08 |
|
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: 58.93 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 469 WKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKR----------------- 531
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelskle 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 532 ------EQQLASVESELQR---EKKELQSERQrNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENK 602
Cdd:TIGR02169 805 eevsriEARLREIEQKLNRltlEKEYLEKEIQ-ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 603 YKILEKEFQQFKDQQNNkpeirLQSEINLLTLEkVELERKLESATKSKLHYKQQwgrALKELARLKQREQES-------- 674
Cdd:TIGR02169 884 LGDLKKERDELEAQLRE-----LERKIEELEAQ-IEKKRKRLSELKAKLEALEE---ELSEIEDPKGEDEEIpeeelsle 954
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1769843692 675 --QMARLKKQQ-------------EELEQMRLRYLAAEEK-DTVKTERQELLDIRNELNRLRQQ 722
Cdd:TIGR02169 955 dvQAELQRVEEeiralepvnmlaiQEYEEVLKRLDELKEKrAKLEEERKAILERIEEYEKKKRE 1018
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
522-703 |
1.43e-08 |
|
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: 56.09 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 522 QKTLIDLEKREQQLASVESELQREKKELQsERQRNLQELQDSIRRAKEDcIHQVELER----LKIKQLEEDKHRLQQQLN 597
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELA-ELEDELAALEARLEAAKTE-LEDLEKEIkrleLEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 598 DAENkykilEKEFQQfkdqqnnkpeirLQSEINLLTLEKVELE-------RKLESATKSKLHYKQQWGRALKELARLKQr 670
Cdd:COG1579 84 NVRN-----NKEYEA------------LQKEIESLKRRISDLEdeilelmERIEELEEELAELEAELAELEAELEEKKA- 145
|
170 180 190
....*....|....*....|....*....|...
gi 1769843692 671 EQESQMARLKKQQEELEQMRLRYLAAEEKDTVK 703
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPPELLA 178
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
453-763 |
1.98e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 453 EPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKRE 532
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 533 QQLAsveSELQREKKELQSERQRNLQElqdsiRRAKEDCIHQVELERLKIKQL---EEDKHRLQQQLNDAENKYKILEKE 609
Cdd:PTZ00121 1594 IEEV---MKLYEEEKKMKAEEAKKAEE-----AKIKAEELKKAEEEKKKVEQLkkkEAEEKKKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 610 FQQFKDQQNNKPEIRLQSEinlltlekvELERKLESATKSKLHYKqqwgRALKELArlKQREQESQMARLKKQQEELEQM 689
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAE---------EDEKKAAEALKKEAEEA----KKAEELK--KKEAEEKKKAEELKKAEEENKI 1730
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843692 690 RLRYLAAEEKDTvKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKdgphgSVLEEGLD--DYLTRLIEERDT 763
Cdd:PTZ00121 1731 KAEEAKKEAEED-KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE-----AVIEEELDeeDEKRRMEVDKKI 1800
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
448-723 |
2.13e-08 |
|
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: 58.06 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 448 SEIQTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEwkKRDRERESLVKKKVAEYTILEGKLQKTLID 527
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE--REKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 528 LEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQ-----VELERLKIKQLEEDKHRLQQQLNDAENK 602
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELerleeEITKEELLQELLLKEEELEEQKLKDELE 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 603 YKIL----EKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHykqqwGRALKELARLKQREQESQMAR 678
Cdd:pfam02463 890 SKEEkekeEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE-----EADEKEKEENNKEEEEERNKR 964
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1769843692 679 LKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQE 723
Cdd:pfam02463 965 LLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR 1009
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
467-726 |
1.58e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 467 EMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKvAEYTILEGKLQKTLIDLEKREQQLASVESELqREK 546
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEINGIEERIKELEEKEERL-EEL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 547 KELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQ 626
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 627 SEINLLTLEKVELE-----RKLESATKSKL--HYKQQWGRALKELARLKQREQEsqmarLKKQQEELEQMRLRylaAEEK 699
Cdd:PRK03918 424 LKKAIEELKKAKGKcpvcgRELTEEHRKELleEYTAELKRIEKELKEIEEKERK-----LRKELRELEKVLKK---ESEL 495
|
250 260
....*....|....*....|....*..
gi 1769843692 700 DTVKTERQELLDIRNELNRLRQQEQKQ 726
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYNLEELEK 522
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
511-735 |
2.16e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 511 VAEYTILEGkLQKTLIDLEKREQQLASVEsELQREKKELQseRQRNLQELQDSIRRAKEDcIHQVELERLKIKQLEEDKH 590
Cdd:COG4913 231 VEHFDDLER-AHEALEDAREQIELLEPIR-ELAERYAAAR--ERLAELEYLRAALRLWFA-QRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 591 RLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQseinlltlekvELERKLESATKSKLHYKQQWGRALKELARLKQR 670
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGGDRLE-----------QLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843692 671 EQESQmarlkkqqEELEQMRLRylAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQD-STEIAS 735
Cdd:COG4913 375 LPASA--------EEFAALRAE--AAALLEALEEELEALEEALAEAEAALRDLRRELRElEAEIAS 430
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
490-732 |
2.56e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.10 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 490 QALAEEWKKRDRER-----ESLVKKKVAEYTILEGKL----QKTLIDLEKRE--QQLASVESELQREKKELQSERQRNLQ 558
Cdd:pfam02029 62 EAFLDRTAKREERRqkrlqEALERQKEFDPTIADEKEsvaeRKENNEEEENSswEKEEKRDSRLGRYKEEETEIREKEYQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 559 E--LQDSIRRAKEDCIHQvELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQSEINLLTLEK 636
Cdd:pfam02029 142 EnkWSTEVRQAEEEGEEE-EDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLK 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 637 VELERKLESATKSKLHYKQQWGR--ALKELARLKQREQEsqmarlkKQQEELEQMRLRYLAAE-EKDTVKTERQELLDIR 713
Cdd:pfam02029 221 VTTKRRQGGLSQSQEREEEAEVFleAEQKLEELRRRRQE-------KESEEFEKLRQKQQEAElELEELKKKREERRKLL 293
|
250
....*....|....*....
gi 1769843692 714 NELNRLRQQEQKQYQDSTE 732
Cdd:pfam02029 294 EEEEQRRKQEEAERKLREE 312
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
472-710 |
4.89e-07 |
|
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: 52.98 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 472 MQEDIFENQLKQKELAHMQALAEEWKKRDRERESlvkkKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQS 551
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELES----RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 552 ERQRNLQ---ELQDSIRRAKEDCI-HQVELERLK---------IKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQN 618
Cdd:pfam07888 123 QRAAHEArirELEEDIKTLTQRVLeRETELERMKerakkagaqRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 619 NKPE--IRLQSEINLLTL-------EKVELERKLE--SATKSKLHYKQQ----WGRALKELARLKQREQ-ESQMARLKKQ 682
Cdd:pfam07888 203 QRDTqvLQLQDTITTLTQklttahrKEAENEALLEelRSLQERLNASERkvegLGEELSSMAAQRDRTQaELHQARLQAA 282
|
250 260
....*....|....*....|....*...
gi 1769843692 683 QEELEQMRLRYLAAEEKDTVKTERQELL 710
Cdd:pfam07888 283 QLTLQLADASLALREGRARWAQERETLQ 310
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
465-709 |
5.21e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 465 ELEMWKEMQEDIFENQLKQKELAHMQaLAEEWKKRDREREslvkkkvaEYTILEGKLQKTLIDLEKREQQLaSVESELQR 544
Cdd:pfam15921 332 ELREAKRMYEDKIEELEKQLVLANSE-LTEARTERDQFSQ--------ESGNLDDQLQKLLADLHKREKEL-SLEKEQNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 545 E---------------KKELqSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKE 609
Cdd:pfam15921 402 RlwdrdtgnsitidhlRREL-DDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 610 FQQFKDQQnnkpeIRLQSE---INLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQEsqmarLKKQQEEL 686
Cdd:pfam15921 481 VEELTAKK-----MTLESSertVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDH-----LRNVQTEC 550
|
250 260
....*....|....*....|...
gi 1769843692 687 EQMRLRylAAEEKDTVKTERQEL 709
Cdd:pfam15921 551 EALKLQ--MAEKDKVIEILRQQI 571
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
482-649 |
5.46e-07 |
|
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: 51.46 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 482 KQKELAHMQALAEEWKKRDRERESLvKKKVAEytiLEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQR--NLQE 559
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKEL-PAELAE---LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 560 LQDSIRRAKE--DCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKpEIRLQSEINLLTLEKV 637
Cdd:COG1579 81 QLGNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK-KAELDEELAELEAELE 159
|
170
....*....|..
gi 1769843692 638 ELERKLESATKS 649
Cdd:COG1579 160 ELEAEREELAAK 171
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
527-689 |
6.29e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.11 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 527 DLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDcIHQVELER----LKIKQLEEDKHRLQQQLNDAENK 602
Cdd:pfam05667 307 QFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESS-IQELEKEIkkleSSIKQVEEELEELKEQNEELEKQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 603 YKILEKEFQQFKDQQNNkpeirlqseinlltLEKveLERKLESATKSKLHYKQQWG----------RALKELARLKQREQ 672
Cdd:pfam05667 386 YKVKKKTLDLLPDAEEN--------------IAK--LQALVDASAQRLVELAGQWEkhrvplieeyRALKEAKSNKEDES 449
|
170
....*....|....*..
gi 1769843692 673 ESQMARLKKQQEELEQM 689
Cdd:pfam05667 450 QRKLEEIKELREKIKEV 466
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
507-790 |
1.10e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 507 VKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQsERQRNLQELQDSIRRAKEDCIHQVElerlKIKQLE 586
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE-QLEEELEELNEQLQAAQAELAQAQE----ELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 587 EDKHRLQQQLNDAENKYKILEKEFQQFKDQQNnkpeiRLQSEINLLTLEKVELERKLESAtksklhykqqwgraLKELAR 666
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIA-----ELQSEIAEREEELKELEEQLESL--------------QEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 667 LKQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGSVL 746
Cdd:COG4372 169 LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1769843692 747 EEGLDDYLTRLIEERDTLMRTGVYNHEDRIISELDRQIREILAK 790
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
449-617 |
3.31e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 449 EIQTEPRETLEYKAALElEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLvkkkvAEYTILEGKLQKTLIDL 528
Cdd:COG4717 85 EKEEEYAELQEELEELE-EELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEL-----AELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 529 EKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEdcihqvELERL--KIKQLEEDKHRLQQQLNDAENKYKIL 606
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE------ELEELqqRLAELEEELEEAQEELEELEEELEQL 232
|
170
....*....|.
gi 1769843692 607 EKEFQQFKDQQ 617
Cdd:COG4717 233 ENELEAAALEE 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
486-722 |
3.34e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 486 LAHMQALAEEWKKRDRERESLVKKKvAEYTILEG------KLQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQE 559
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAR-EQIELLEPirelaeRYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 560 lqdsirrakedcihqvelerlKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQnnkpEIRLQSEINLLTLEKVEL 639
Cdd:COG4913 303 ---------------------ELARLEAELERLEARLDALREELDELEAQIRGNGGDR----LEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 640 ERKLESAtksklhykQQWGRALKELARLKQREQESQMARLKKQQEELEQMR--LRYLAAEEKDTVKTERQELLDIRNELN 717
Cdd:COG4913 358 ERRRARL--------EALLAALGLPLPASAEEFAALRAEAAALLEALEEELeaLEEALAEAEAALRDLRRELRELEAEIA 429
|
....*
gi 1769843692 718 RLRQQ 722
Cdd:COG4913 430 SLERR 434
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
532-729 |
4.08e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 532 EQQLASVESELQREKKELQSERQRN-LQELQDsirrakedcihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEkef 610
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNgLVDLSE-----------EAKLLLQQLSELESQLAEARAELAEAEARLAALR--- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 611 QQFKDQQNNKPEIRLQSEINLLTLEKVELERKL--ESATKSKLHYK-QQWGRALKELARLKQREQESQMARLKKQQEELE 687
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAELEAELaeLSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1769843692 688 QmRLRYLAAEEkDTVKTERQELLDIRNELNRLRQQ---EQKQYQD 729
Cdd:COG3206 327 A-REASLQAQL-AQLEARLAELPELEAELRRLEREvevARELYES 369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
455-667 |
4.67e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 455 RETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQ 534
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 535 LASVESELQREKKELQS---------ERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKI 605
Cdd:COG1196 388 LLEALRAAAELAAQLEEleeaeeallERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1769843692 606 LEKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARL 667
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
498-734 |
7.22e-06 |
|
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: 49.97 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 498 KRDRERESLVKKKVAEYtilegkLQKTLIDLEKREQQLasvESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVEL 577
Cdd:pfam02463 168 KRKKKEALKKLIEETEN------LAELIIDLEELKLQE---LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 578 ERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIrlQSEINLLTLEKVELERKLESATKSKLHYKQQW 657
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ--EEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843692 658 GRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIA 734
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
473-726 |
9.97e-06 |
|
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: 48.61 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 473 QEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQSE 552
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 553 RQRNLQELQDSIRRAkedcihqvelerLKIKQLEEDKHRLQQQ-LNDAENKYKILEKEFQQFKDQQNnkpeiRLQSEINL 631
Cdd:COG4942 99 LEAQKEELAELLRAL------------YRLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAE-----ELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 632 LTlekvELERKLESATKSKLHYKQQWGRALKELARLKQrEQESQMARLKKQQEELEQmRLRYLAAEEKdtvkterqellD 711
Cdd:COG4942 162 LA----ALRAELEAERAELEALLAELEEERAALEALKA-ERQKLLARLEKELAELAA-ELAELQQEAE-----------E 224
|
250
....*....|....*
gi 1769843692 712 IRNELNRLRQQEQKQ 726
Cdd:COG4942 225 LEALIARLEAEAAAA 239
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
478-604 |
1.02e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 478 ENQLKQKELahmQAlAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELqSERQRNL 557
Cdd:PRK12704 52 EAIKKEALL---EA-KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKEL-EQKQQEL 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1769843692 558 QELQDSIRRAKEDciHQVELERLKIKQLEEDKHRLqqqLNDAENKYK 604
Cdd:PRK12704 127 EKKEEELEELIEE--QLQELERISGLTAEEAKEIL---LEKVEEEAR 168
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
451-725 |
1.03e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 451 QTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAE---YTILEGKL---QKT 524
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLerrKVDDEEKLkesEKE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 525 LIDLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRakedcihQVELERLKIKQLeeDKHRLQQQLNDAENKYK 604
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL-------QEKLEQLEEELL--AKKKLESERLSSAAKLK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 605 ILEKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKlhykqqwgraLKELARLKQREQESQMARLKKQQE 684
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI----------ELKQGKLTEEKEELEKQELKLLKD 463
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1769843692 685 ELEQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQK 725
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK 504
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
470-726 |
1.07e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 470 KEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKEL 549
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 550 QSERQRNLQeLQDSIRRAKEDcIHQVElerLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKpeirlQSEI 629
Cdd:TIGR04523 429 ERLKETIIK-NNSEIKDLTNQ-DSVKE---LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK-----EKEL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 630 NLLTLEKVELERKLESATKSKLHYKQQwgraLKELARLKqREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQEL 709
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEK-KEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEEL 573
|
250
....*....|....*..
gi 1769843692 710 LDIRNELnrLRQQEQKQ 726
Cdd:TIGR04523 574 KQTQKSL--KKKQEEKQ 588
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
566-726 |
1.77e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.02 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 566 RAKEDCIHQVELERlKIKQLEEDKHRLQQQLNDAENKYKILEKEfqqfkdQQNNKPEIRL----QSEINLLTLEKVELER 641
Cdd:pfam15709 339 RAERAEMRRLEVER-KRREQEEQRRLQQEQLERAEKMREELELE------QQRRFEEIRLrkqrLEEERQRQEEEERKQR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 642 KLESATKSKLHYKQQ-WGRALKELARLKQREQESQMARLKKQQEEL------EQMRLRYLAAEEKDTVKTERQELLD-IR 713
Cdd:pfam15709 412 LQLQAAQERARQQQEeFRRKLQELQRKKQQEEAERAEAEKQRQKELemqlaeEQKRLMEMAEEERLEYQRQKQEAEEkAR 491
|
170
....*....|...
gi 1769843692 714 NELNRLRQQEQKQ 726
Cdd:pfam15709 492 LEAEERRQKEEEA 504
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
453-748 |
2.47e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 453 EPRETLEYKAALELEMWKEMQEdifENQLKQKelAHMQALAEEWKKRDREreslvKKKVAEYTILEGKLQKTLIDLEKRE 532
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKK---ADEAKKK--AEEAKKADEAKKKAEE-----AKKKADAAKKKAEEAKKAAEAAKAE 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 533 QQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELErlkiKQLEEDKHRLQQQLNDAENKYKilekefqq 612
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK----KKAEEDKKKADELKKAAAAKKK-------- 1419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 613 fKDQQNNKPEIRLQSEinlltlekvELERKLESATKS-KLHYKQQWGRALKELArlKQREQESQMARLKKQQEELEQMRL 691
Cdd:PTZ00121 1420 -ADEAKKKAEEKKKAD---------EAKKKAEEAKKAdEAKKKAEEAKKAEEAK--KKAEEAKKADEAKKKAEEAKKADE 1487
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843692 692 RYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGSVLEE 748
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
461-639 |
3.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 461 KAALELEMWKEMQE--DIFENQLKQKEL-AHMQALAEEWKKRDRERESLVKKKVAeytiLEGKLQKTLIDLEKRE-QQLA 536
Cdd:COG4913 266 AARERLAELEYLRAalRLWFAQRRLELLeAELEELRAELARLEAELERLEARLDA----LREELDELEAQIRGNGgDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 537 SVESELQREKKELQsERQRNLQELQDSIR--------------RAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENK 602
Cdd:COG4913 342 QLEREIERLERELE-ERERRRARLEALLAalglplpasaeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1769843692 603 YKILEKEFQQFKDQQNNKPE--IRLQSEIN-LLTLEKVEL 639
Cdd:COG4913 421 LRELEAEIASLERRKSNIPArlLALRDALAeALGLDEAEL 460
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
425-738 |
3.97e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.17 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 425 SDSSQGVSAVQQKPSSLPPAPCPSEIQTEPRETLEYKAALELEMWK---EMQEDIFENQLKQKELAHMQALAEE-WKKRD 500
Cdd:pfam02029 25 EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKreeRRQKRLQEALERQKEFDPTIADEKEsVAERK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 501 RERESLVKKKVAEYTILEGKLQKTLID----LEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVE 576
Cdd:pfam02029 105 ENNEEEENSSWEKEEKRDSRLGRYKEEeteiREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 577 LERLKIKqlEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQS-EINLLTLEKVELERKLESATKS------ 649
Cdd:pfam02029 185 KKEKKVK--YESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSqEREEEAEVFLEAEQKLEELRRRrqekes 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 650 ----KLHYKQQwgRALKELARLKQREQESQMARlkkqqEELEQMRlrylAAEEKDTVKTERQELLDIRNELNRLRQQ--E 723
Cdd:pfam02029 263 eefeKLRQKQQ--EAELELEELKKKREERRKLL-----EEEEQRR----KQEEAERKLREEEEKRRMKEEIERRRAEaaE 331
|
330
....*....|....*
gi 1769843692 724 QKQYQDSTEIASGKK 738
Cdd:pfam02029 332 KRQKLPEDSSSEGKK 346
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
511-688 |
4.15e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 511 VAEYTILEGKLQKTLIDLEKREQQLasveseLQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEdkh 590
Cdd:PRK12704 19 VIGYFVRKKIAEAKIKEAEEEAKRI------LEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEK--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 591 RLQQqlndaenKYKILEKefqqfKDQQNNKPEIRLQSEINLLTLEKVELERKLESAtkSKLHYKQQwgRALKELARLKQR 670
Cdd:PRK12704 90 RLLQ-------KEENLDR-----KLELLEKREEELEKKEKELEQKQQELEKKEEEL--EELIEEQL--QELERISGLTAE 153
|
170
....*....|....*...
gi 1769843692 671 EQESQMarLKKQQEELEQ 688
Cdd:PRK12704 154 EAKEIL--LEKVEEEARH 169
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
520-738 |
4.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 520 KLQKTLIDLEKREQQLASVESELQREKKELQSErqrnLQELQDSIRRAKEdcihqvelerlKIKQLEEDKHRLQQQLNDA 599
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEE----YNELQAELEALQA-----------EIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 600 ENKYKilekefQQFKDQQNNKpeiRLQSEINLLT--------LEKVELERKLESATKSKLhyKQQwgRALKELARLKQRE 671
Cdd:COG3883 85 REELG------ERARALYRSG---GSVSYLDVLLgsesfsdfLDRLSALSKIADADADLL--EEL--KADKAELEAKKAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843692 672 QESQMARLKKQQEELEQMRlrylaaEEKDTVKTERQELldirneLNRLRQQEQKQYQDSTEIASGKK 738
Cdd:COG3883 152 LEAKLAELEALKAELEAAK------AELEAQQAEQEAL------LAQLSAEEAAAEAQLAELEAELA 206
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
486-726 |
5.73e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 486 LAHMQALAEEWKKRDRERESLVKKKVAEYtiLEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQElqdsiR 565
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERA--LEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQE-----R 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 566 RAKEDCIHQVELERLKIKQLeedKHRLQQQLNdaenkykileKEFQQFKDQQNNKPEIRLQSEinlltlekVELERKLES 645
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEE---KLEKQRQLR----------EEIDEFNEEQAEWKELEKEEE--------REEDERILE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 646 ATKSKLHYKQQWGRALKELARLKQREQE---SQMARLKKQQEELEQMRL-RYLAAEEKDTVKTERQELLDIRNELNRLRQ 721
Cdd:pfam13868 160 YLKEKAEREEEREAEREEIEEEKEREIArlrAQQEKAQDEKAERDELRAkLYQEEQERKERQKEREEAEKKARQRQELQQ 239
|
....*
gi 1769843692 722 QEQKQ 726
Cdd:pfam13868 240 AREEQ 244
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
453-787 |
6.53e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 453 EPRETLEYKAALELEmwKEMQEDIFENQLKQKelahmqalAEEWKKRDRE--RESLVKKKVAEYTILEGKLQKTLIDLEK 530
Cdd:PTZ00121 1294 EAKKAEEKKKADEAK--KKAEEAKKADEAKKK--------AEEAKKKADAakKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 531 REQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERL--------KIKQLEEDKHRLQQQLNDAENK 602
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAaaakkkadEAKKKAEEKKKADEAKKKAEEA 1443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 603 YKI--LEKEFQQFKDQQNNKPEIRLQSEINLLTlEKVELERKLESATKSKLHYKQQwGRALKELARLKQREQESQMARLK 680
Cdd:PTZ00121 1444 KKAdeAKKKAEEAKKAEEAKKKAEEAKKADEAK-KKAEEAKKADEAKKKAEEAKKK-ADEAKKAAEAKKKADEAKKAEEA 1521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 681 KQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNR---LRQQEQKQYQDSTEIASGKKDGPHGSVLEEGLDDYLTRL 757
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKaeeKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
330 340 350
....*....|....*....|....*....|
gi 1769843692 758 IEERDTLMRTGVYNHEDRIISELDRQIREI 787
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
534-711 |
7.26e-05 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 44.15 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 534 QLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDK---HR----LQQQLNDAENKYKIL 606
Cdd:pfam08614 11 RLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELaelYRsrgeLAQRLVDLNEELQEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 607 EKEFQQfkdqqnnkpeirLQSEINLLTLEKVELERKLESATksklhykqqwgRALKELARLKQReqesqmarlkkQQEEL 686
Cdd:pfam08614 91 EKKLRE------------DERRLAALEAERAQLEEKLKDRE-----------EELREKRKLNQD-----------LQDEL 136
|
170 180
....*....|....*....|....*.
gi 1769843692 687 EQMRLRYLAAEEK-DTVKTERQELLD 711
Cdd:pfam08614 137 VALQLQLNMAEEKlRKLEKENRELVE 162
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
509-729 |
8.71e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 509 KKVAEYtilegKLQKTLIDLEKREQQLASVESELQREKKELQSERQRnLQELQDSIRRakedcihQVELERLKIKQLEED 588
Cdd:COG3206 196 AALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE-AEARLAALRA-------QLGSGPDALPELLQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 589 KH--RLQQQLNDAENKYKILEKEFqqfkdqQNNKPEIR-LQSEINlltlekvELERKLESATksklhyKQQWGRALKELA 665
Cdd:COG3206 263 PViqQLRAQLAELEAELAELSARY------TPNHPDVIaLRAQIA-------ALRAQLQQEA------QRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843692 666 RLKQREQE--SQMARLKKQQEELEQMRLRYLAAEEKdtVKTERQELLDIRNELNRLRQQEQKQYQD 729
Cdd:COG3206 324 ALQAREASlqAQLAQLEARLAELPELEAELRRLERE--VEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
451-732 |
8.79e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 451 QTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQAlaEEWKKRDRERESL--VKKKVAEYTILEGKLQKTLIDL 528
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVeqLKKKEAEEKKKAEELKKAEEEN 1659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 529 EKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEK 608
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE----AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 609 EFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQwgrALKELARLKQREQESQMARLKKQQEELEQ 688
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE---ELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1769843692 689 --MRLRYLAAEEKDTVKTERQELLDIRN-ELNRLRQQEQKQYQDSTE 732
Cdd:PTZ00121 1813 ggKEGNLVINDSKEMEDSAIKEVADSKNmQLEEADAFEKHKFNKNNE 1859
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
552-722 |
9.31e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 552 ERQRNLQELQDSIRRAKEDC-IHQVELERLK---------IKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNnkp 621
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIaELEKALAELRkeleeleeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA--- 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 622 eiRLQSEINLLTLEKVELERKLESATKsklhykqqwgrALKELARLKQrEQESQMARLkkqQEELEQMRLRYLAAEEKdt 701
Cdd:TIGR02168 751 --QLSKELTELEAEIEELEERLEEAEE-----------ELAEAEAEIE-ELEAQIEQL---KEELKALREALDELRAE-- 811
|
170 180
....*....|....*....|.
gi 1769843692 702 VKTERQELLDIRNELNRLRQQ 722
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERR 832
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
478-764 |
1.18e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 478 ENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELqSERQRNL 557
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE-AELEATL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 558 QELQDSIRRAK------------------------EDCIHQVELERLKIKQLEEDKHRLQQQLNDAEnKYKILEKEFQQF 613
Cdd:PRK02224 436 RTARERVEEAEalleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERL 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 614 KDQQNNKPEIRLQSEINL---------LTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQEsqmarLKKQQE 684
Cdd:PRK02224 515 EERREDLEELIAERRETIeekreraeeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE-----LKERIE 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 685 ELEQMRLRYLAAEEKDTVKTERQELLDIRNELN------------RLRQQEQKQYQDSTEIASGKKDgpHGSVLEEGLDD 752
Cdd:PRK02224 590 SLERIRTLLAAIADAEDEIERLREKREALAELNderrerlaekreRKRELEAEFDEARIEEAREDKE--RAEEYLEQVEE 667
|
330
....*....|..
gi 1769843692 753 YLTRLIEERDTL 764
Cdd:PRK02224 668 KLDELREERDDL 679
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
448-690 |
1.21e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 448 SEIQTEPRETLEYKAALELEMWKEMQEDIFENQLKQKElahmqALAEEWKKRDRERE---SLVKKKVAEYTILEGKLQKT 524
Cdd:PRK03918 487 KVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA-----EEYEKLKEKLIKLKgeiKSLKKELEKLEELKKKLAEL 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 525 LIDLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKE--DCIHQVELERLKIKQLEEDKHRLQQQLNDAENK 602
Cdd:PRK03918 562 EKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLElkDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 603 YKILEKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSklhyKQQWGRALKEL-ARLKQREQ-ESQMARLK 680
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR----REEIKKTLEKLkEELEEREKaKKELEKLE 717
|
250
....*....|
gi 1769843692 681 KQQEELEQMR 690
Cdd:PRK03918 718 KALERVEELR 727
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
531-698 |
1.30e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 531 REQQLASVESELQrEKKELQSERQRNLQELQdsirRAKEDcihqveLERLKIKQL--------EEDKHRLQQQLNDAENK 602
Cdd:PRK04863 784 REKRIEQLRAERE-ELAERYATLSFDVQKLQ----RLHQA------FSRFIGSHLavafeadpEAELRQLNRRRVELERA 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 603 YKILEKEFQQFKDQ-QNNKPEI----RLQSEINLL---TLEK--VELERKLESATKSKLhYKQQWGRALKELarlkqreq 672
Cdd:PRK04863 853 LADHESQEQQQRSQlEQAKEGLsalnRLLPRLNLLadeTLADrvEEIREQLDEAEEAKR-FVQQHGNALAQL-------- 923
|
170 180
....*....|....*....|....*.
gi 1769843692 673 ESQMARLKKQQEELEQMRLRYLAAEE 698
Cdd:PRK04863 924 EPIVSVLQSDPEQFEQLKQDYQQAQQ 949
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
415-763 |
1.46e-04 |
|
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: 45.42 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 415 GLVKMREIFISDSSQGVSAVQQKPSSLPPAPCPSEIQTEPRETLEYKAALELEMWKEMQEDI-----FENQLKQKELAHM 489
Cdd:TIGR00606 730 GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtimerFQMELKDVERKIA 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 490 QALAE-----------EWKKRDRERESLVKKKVAEYTILegklQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQ 558
Cdd:TIGR00606 810 QQAAKlqgsdldrtvqQVNQEKQEKQHELDTVVSKIELN----RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 559 ELQDSIRRAKE--DCIHQVELERLKIKQLEEDKHRLQQQ----LNDAENKYKILEKEFQQFKDQ---------------Q 617
Cdd:TIGR00606 886 FEEQLVELSTEvqSLIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKvknihgymkdienkiQ 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 618 NNKPEIRLQSEINLLTLEKvelerKLESATKSKLHYKQQWGRALKELARLKQREQ--ESQMARLKKQQE--ELEQMRLRY 693
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNA-----QLEECEKHQEKINEDMRLMRQDIDTQKIQERwlQDNLTLRKRENElkEVEEELKQH 1040
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843692 694 LAAEEKDTVKTERQELLDIRNELNRLRQQE------QKQYQDSTEIASGKKDGPHGSVLEEgldDYLTRLIEERDT 763
Cdd:TIGR00606 1041 LKEMGQMQVLQMKQEHQKLEENIDLIKRNHvlalgrQKGYEKEIKHFKKELREPQFRDAEE---KYREMMIVMRTT 1113
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
592-724 |
1.53e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 592 LQQQLNDAENKYKILEKEFQQFKdQQNNkpEIRLQSEINLLTLEKVELERKLESAT------KSKLHY-KQQWGRALKEL 664
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFR-QKNG--LVDLSEEAKLLLQQLSELESQLAEARaelaeaEARLAAlRAQLGSGPDAL 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1769843692 665 ARLKQREQESQM-ARLKKQQEELEQMRLRYLAA--------EEKDTVKTERQE-----LLDIRNELNRLRQQEQ 724
Cdd:COG3206 257 PELLQSPVIQQLrAQLAELEAELAELSARYTPNhpdvialrAQIAALRAQLQQeaqriLASLEAELEALQAREA 330
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
478-718 |
1.71e-04 |
|
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: 45.12 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 478 ENQLKQKELAHMQALAEewkkrdRERESLVKKKVAEYTILEGK-LQKTLIDLEKRE---QQLASVESELQREKKELQSER 553
Cdd:pfam05557 15 QNEKKQMELEHKRARIE------LEKKASALKRQLDRESDRNQeLQKRIRLLEKREaeaEEALREQAELNRLKKKYLEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 554 QRNLQELQDSIRRAKE--DCI--------HQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQ--NNKP 621
Cdd:pfam05557 89 NKKLNEKESQLADAREviSCLknelselrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQssLAEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 622 EIRLQseinlltlekvELERKLESATKSKLHYKQqwgrALKELARLKQREQEsqmarLKKQQEELEQMRlrylaaEEKDT 701
Cdd:pfam05557 169 EQRIK-----------ELEFEIQSQEQDSEIVKN----SKSELARIPELEKE-----LERLREHNKHLN------ENIEN 222
|
250
....*....|....*..
gi 1769843692 702 VKTERQELLDIRNELNR 718
Cdd:pfam05557 223 KLLLKEEVEDLKRKLER 239
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
501-754 |
1.83e-04 |
|
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: 45.42 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 501 RERESLVKKKVAEYTILEGK--LQKTLIDLEKRE-----QQLASVESELQREKKELqsERQRNLQELQDSIRRAKEDCIH 573
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLapGRQSIIDLKEKEipelrNKLQKVNRDIQRLKNDI--EEQETLLGTIMPEEESAKVCLT 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 574 QVELERLKIKQLEEDKHRLQQQLndAENKYKILEKEFQQFKDQQNNKpeirlQSEINLLTlEKVELERKLESATKSKLHY 653
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQA--AKLQGSDLDRTVQQVNQEKQEK-----QHELDTVV-SKIELNRKLIQDQQEQIQH 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 654 KQQWGRALK----ELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQD 729
Cdd:TIGR00606 862 LKSKTNELKseklQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
|
250 260 270
....*....|....*....|....*....|.
gi 1769843692 730 STEIASGKKDGPHG------SVLEEGLDDYL 754
Cdd:TIGR00606 942 KVNDIKEKVKNIHGymkdieNKIQDGKDDYL 972
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
452-780 |
1.95e-04 |
|
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: 45.10 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 452 TEPRETLEYKAALELEMwKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKR 531
Cdd:pfam05483 391 SELEEMTKFKNNKEVEL-EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 532 EQQLASVESELQREK----------KELQSERQRNLQELQD---SIRRAKEDCIHQVELERLKIKQLEEdkhrLQQQLND 598
Cdd:pfam05483 470 LKEVEDLKTELEKEKlknieltahcDKLLLENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQIEN----LEEKEMN 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 599 AENKYKILEKEFQQFKDQ--------QNNKPEIRLQSEINLLTLEKVE-----LERKLESATKSkLHYKQQWGRALKELA 665
Cdd:pfam05483 546 LRDELESVREEFIQKGDEvkckldksEENARSIEYEVLKKEKQMKILEnkcnnLKKQIENKNKN-IEELHQENKALKKKG 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 666 RLKQREQESQMARLKKQQEELEQMRLRYlaAEEKDTVKTE------RQELLDIRNELNRLRQQEQKQYQDSTEIASGKKD 739
Cdd:pfam05483 625 SAENKQLNAYEIKVNKLELELASAKQKF--EEIIDNYQKEiedkkiSEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKI 702
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1769843692 740 GPHGSVLEEGLDDYlTRLIEERDTLMrtGVYNHEDRIISEL 780
Cdd:pfam05483 703 AEMVALMEKHKHQY-DKIIEERDSEL--GLYKNKEQEQSSA 740
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
483-766 |
2.54e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 483 QKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQktlidLEKREQQLASVESELQREKKELQSERQRNLQELQD 562
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN-----ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 563 SIRRAKEDCIHQVELErlkikQLEEDKHRLQQQLNDAENKYKILE-KEFQQFKDQQNNKPEIRLQSEINLLTLEKVELER 641
Cdd:TIGR00618 627 LQDVRLHLQQCSQELA-----LKLTALHALQLTLTQERVREHALSiRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 642 K-------LESATKSKLHYKQQWGRALKELARLKQRE----------QESQMARLKKQQEELEQMRLRYLAAEEKDtvkT 704
Cdd:TIGR00618 702 CqtllrelETHIEEYDREFNEIENASSSLGSDLAAREdalnqslkelMHQARTVLKARTEAHFNNNEEVTAALQTG---A 778
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1769843692 705 ERQELldIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGSVLEEGLDDYLTRLIEERDTLMR 766
Cdd:TIGR00618 779 ELSHL--AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
463-722 |
2.91e-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: 44.72 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 463 ALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKlQKTLIDL----EKREQQLASV 538
Cdd:pfam15921 437 AMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLtaslQEKERAIEAT 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 539 ESELQRekkeLQSERQRNLQELQ------DSIRRAKEDCihqvelERLKIKQLEEDK--HRLQQQLndaENKYKILEKEF 610
Cdd:pfam15921 516 NAEITK----LRSRVDLKLQELQhlknegDHLRNVQTEC------EALKLQMAEKDKviEILRQQI---ENMTQLVGQHG 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 611 QQFKDQQNNKPEirLQSEINLLTLEKVELerklesatksklhykqqwgRALKELARLKQREQESQMARLkkqqeELEQMR 690
Cdd:pfam15921 583 RTAGAMQVEKAQ--LEKEINDRRLELQEF-------------------KILKDKKDAKIRELEARVSDL-----ELEKVK 636
|
250 260 270
....*....|....*....|....*....|..
gi 1769843692 691 LRYLAAEEKDTVKTERQELLDIRNELNRLRQQ 722
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQERDQLLNEVKTSRNE 668
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
528-718 |
3.42e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 528 LEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEdkhRLQQQLNDAENKYKile 607
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEE---RLVQKEEQLDARAE--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 608 kefqqfkdqqnnkpeirlqsEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEElE 687
Cdd:PRK12705 99 --------------------KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELE-E 157
|
170 180 190
....*....|....*....|....*....|.
gi 1769843692 688 QMRLRYLAAEEKDTVKTERQELLDIRNELNR 718
Cdd:PRK12705 158 EKAQRVKKIEEEADLEAERKAQNILAQAMQR 188
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
532-732 |
3.44e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.27 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 532 EQQLASVESELQREKKELQSERQRnLQELQDSIrrakedcihqvelerLKIKQLEEDKHRlqqQLNDAENKYKILEKEFQ 611
Cdd:PRK10929 108 EQEILQVSSQLLEKSRQAQQEQDR-AREISDSL---------------SQLPQQQTEARR---QLNEIERRLQTLGTPNT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 612 QFKDQQNnkpeIRLQSEINLLTLEKVELERKLESAtksklHYKQqwgralkELARLkqreqesQMARLKKQQEELEQmrl 691
Cdd:PRK10929 169 PLAQAQL----TALQAESAALKALVDELELAQLSA-----NNRQ-------ELARL-------RSELAKKRSQQLDA--- 222
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1769843692 692 rylaaeekdtvkterqELLDIRNELNRLRQQEQKQYQDSTE 732
Cdd:PRK10929 223 ----------------YLQALRNQLNSQRQREAERALESTE 247
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
448-725 |
3.69e-04 |
|
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: 43.73 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 448 SEIQTEPRETLEYKAALELEMWKEMQEDIfeNQLKQKELAHMQALaEEWKKRDRERESLVKKKVAEYTILEGKLQKTlid 527
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRELEEDI--KTLTQRVLERETEL-ERMKERAKKAGAQRKEEEAERKQLQAKLQQT--- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 528 lekrEQQLASVESELQrEKKELQSERQRNLQELQDSIRR--AKEDCIHQVELErlkIKQLEEDKHRLQQQLNDAENKYKI 605
Cdd:pfam07888 184 ----EEELRSLSKEFQ-ELRNSLAQRDTQVLQLQDTITTltQKLTTAHRKEAE---NEALLEELRSLQERLNASERKVEG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 606 LEKEFQQFKDQQNnkpeiRLQSEINLLTLEKVELERKLESATKSKLHYKQQWG---------------RALK---ELARL 667
Cdd:pfam07888 256 LGEELSSMAAQRD-----RTQAELHQARLQAAQLTLQLADASLALREGRARWAqeretlqqsaeadkdRIEKlsaELQRL 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843692 668 KQREQESQMARLKKQQE-----------------ELEQMR--LRyLAAEEKDTVKTERQELLDirnelnRLRQQEQK 725
Cdd:pfam07888 331 EERLQEERMEREKLEVElgrekdcnrvqlsesrrELQELKasLR-VAQKEKEQLQAEKQELLE------YIRQLEQR 400
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
515-788 |
4.36e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 515 TILEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDkhrlqq 594
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE------ 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 595 QLNDAENKYKILEKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQES 674
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 675 QMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNRL------------RQQEQKQYqdsteiasgkkdgph 742
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaieeyeELEERYDF--------------- 799
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1769843692 743 gsvLEEGLDDyltrLIEERDTLMrtgvynhedRIISELDRQIREIL 788
Cdd:COG1196 800 ---LSEQRED----LEEARETLE---------EAIEEIDRETRERF 829
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
517-699 |
4.49e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 517 LEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRnLQELQDSIRRAKEdcihqvELERLKiKQLEEDKHRLQQQL 596
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQA------EIAEAE-AEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 597 NDAenkYK----------ILE-KEFQQFKDQ---------QNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQ 656
Cdd:COG3883 93 RAL---YRsggsvsyldvLLGsESFSDFLDRlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1769843692 657 wgraLKELARlKQREQESQMARLKKQQEELEQMRLRYLAAEEK 699
Cdd:COG3883 170 ----KAELEA-QQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
507-786 |
4.69e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 507 VKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRrakedcihQVELERLKIKQLE 586
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEE--------ELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 587 EDKHRLQQQLNDAENKYKILEKEFQQFKDQQNnkpeiRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELAR 666
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAE-----ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 667 LkqreqESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGSVL 746
Cdd:COG4372 155 L-----EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1769843692 747 EEGLDDYLTRLIEERDTLMRTGVYNHEDRIISELDRQIRE 786
Cdd:COG4372 230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
528-725 |
4.99e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 528 LEKREQQLASVESELQREK---KELQSERQRNLQELQDSIRRAKEDCIH------QVELERLKiKQLEEDKHRLQQ-QLN 597
Cdd:pfam06160 181 LEKLEEETDALEELMEDIPplyEELKTELPDQLEELKEGYREMEEEGYAlehlnvDKEIQQLE-EQLEENLALLENlELD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 598 DAENK-----------YKILEKEFQQFKDQQNNKPEIRlqSEINLLTLEKVELERKLEsatksklHYKQQWGRALKELAR 666
Cdd:pfam06160 260 EAEEAleeieeridqlYDLLEKEVDAKKYVEKNLPEIE--DYLEHAEEQNKELKEELE-------RVQQSYTLNENELER 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 667 lkQREQESQMARLKKQQEELEQ-----------MRLRYLAAEEKDTVKTERQEllDIRNELNRLRQQEQK 725
Cdd:pfam06160 331 --VRGLEKQLEELEKRYDEIVErleekevayseLQEELEEILEQLEEIEEEQE--EFKESLQSLRKDELE 396
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
507-679 |
5.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 507 VKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQS-ERQRNLQELQDSIRRAKE------DCIHQVELER 579
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAelaelpERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 580 LKIKQLEEDKHRLQQQLNDAENKykiLEKEFQQFkDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGR 659
Cdd:COG4717 156 EELRELEEELEELEAELAELQEE---LEELLEQL-SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180
....*....|....*....|
gi 1769843692 660 ALKELARLKQREQESQMARL 679
Cdd:COG4717 232 LENELEAAALEERLKEARLL 251
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
492-685 |
5.93e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.40 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 492 LAEEWKKRDRERESLVKKKVAEytiLEGKLQKtliDLEKREQQLASVESElQREKKELQSERQRNLQELQDSIRRAKEDC 571
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLE---VERKRRE---QEEQRRLQQEQLERA-EKMREELELEQQRRFEEIRLRKQRLEEER 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 572 IHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQfKDQQNNKPEIRLQSEINLLTLEkvELERKLESATKSKL 651
Cdd:pfam15709 401 QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ-EEAERAEAEKQRQKELEMQLAE--EQKRLMEMAEEERL 477
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1769843692 652 HYKQQWGRAlKELARLK---QREQESQMARL-----KKQQEE 685
Cdd:pfam15709 478 EYQRQKQEA-EEKARLEaeeRRQKEEEAARLaleeaMKQAQE 518
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
452-721 |
6.38e-04 |
|
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: 43.24 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 452 TEPRETLEYKAALELEMWKEMQED---IFENQLKQKELAHMQA---LAEEWKKRDRERESLVKKKVAeytilegklqktl 525
Cdd:pfam01576 315 TAAQQELRSKREQEVTELKKALEEetrSHEAQLQEMRQKHTQAleeLTEQLEQAKRNKANLEKAKQA------------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 526 idLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVEL-ERLKIKQLEEDKhrLQQQLNDAENKYK 604
Cdd:pfam01576 382 --LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELaEKLSKLQSELES--VSSLLNEAEGKNI 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 605 ILEKEF----QQFKD-----QQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQ 675
Cdd:pfam01576 458 KLSKDVssleSQLQDtqellQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA 537
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843692 676 MA------RLKKQQEELEQMRLRY----LAAEEKDTVKTE-RQELLDIRNELNRLRQ 721
Cdd:pfam01576 538 GTlealeeGKKRLQRELEALTQQLeekaAAYDKLEKTKNRlQQELDDLLVDLDHQRQ 594
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
448-751 |
7.53e-04 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 43.10 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 448 SEIQTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQ-ALAEEWKKRDRERESLVKKKVAEYTilegklQKTLI 526
Cdd:pfam01271 98 NEPGGHSRENQPYALQVEKEFKTDHSDDYETQQWEEEKLKHMRfPLRYEENSEEKHSEREGELSEVFEN------PRSQA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 527 DLEKREQQLASVESElQREKKELQSERQRNLQELQDSIRRAKEdciHQVELERLKIKQlEEDKHRLQQQLNDAENKYKIL 606
Cdd:pfam01271 172 TLKKVFEEVSRLDTP-SKQKREKSDEREKSSQESGEDTYRQEN---IPQEDQVGPEDQ-EPSEEGEEDATQEEVKRSRPR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 607 EKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQ--QE 684
Cdd:pfam01271 247 THHGRSLPDESSRGGQLGLEEEASEEEEEYGEESRGLSAVQTYLLRLVNARGRGRSEKRAERERSEESEEEELKRAspYE 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 685 ELEQMRLRYL--AAEEKDTVKTERQ-----------ELLDIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGSVLEEGLD 751
Cdd:pfam01271 327 ELEITANLQIppSEEERMLKKAGRSprgrvdeagalEALEALEEKRKLDLDHSRVFESSEDGAPRAPQGAWVEALRNYLS 406
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
541-739 |
8.36e-04 |
|
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: 42.57 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 541 ELQREKKELQSER---QRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILE-------KEF 610
Cdd:pfam07888 38 ECLQERAELLQAQeaaNRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSasseelsEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 611 QQFKDQQ-NNKPEIR-LQSEINLLTLEKVELERKLESATKsklhykqqwgRALKELARLKQREQESQMARLKKQQEELEQ 688
Cdd:pfam07888 118 DALLAQRaAHEARIReLEEDIKTLTQRVLERETELERMKE----------RAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1769843692 689 MRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKD 739
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEE 238
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
488-728 |
8.57e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 488 HMQALAEEWKKRDRERESL---VKKKVAEYTILEGKLQKTlidlekreQQLASVEselqREKKELqSERQRNLQelQDSI 564
Cdd:pfam10174 504 HASSLASSGLKKDSKLKSLeiaVEQKKEECSKLENQLKKA--------HNAEEAV----RTNPEI-NDRIRLLE--QEVA 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 565 RRAKEDCIHQVELERL--KIKQLEEDKHrlqqqlnDAENKYKILEK-EFQQFKDQQNNKPEIR-LQSEINLLTLEKVELE 640
Cdd:pfam10174 569 RYKEESGKAQAEVERLlgILREVENEKN-------DKDKKIAELESlTLRQMKEQNKKVANIKhGQQEMKKKGAQLLEEA 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 641 RKLESATKSKlHYKQQWGRALKELARLKQrEQESQMARL---------------------KKQQEELEQMRLRYL--AAE 697
Cdd:pfam10174 642 RRREDNLADN-SQQLQLEELMGALEKTRQ-ELDATKARLsstqqslaekdghltnlraerRKQLEEILEMKQEALlaAIS 719
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1769843692 698 EKDT-----------VKTERQELLDIRNELNRLRQQEQKQYQ 728
Cdd:pfam10174 720 EKDAniallelssskKKKTQEEVMALKREKDRLVHQLKQQTQ 761
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
446-643 |
9.46e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 42.36 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 446 CPSEIQTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTI----LEGKL 521
Cdd:pfam15742 144 CLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLriqqQEAQL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 522 QKTLIDLEKREQQLASVE------SELQREKKELQSERQRNLQELQDSIR--------------RAKEDCIHQVELERLK 581
Cdd:pfam15742 224 KQLENEKRKSDEHLKSNQelseklSSLQQEKEALQEELQQVLKQLDVHVRkynekhhhhkaklrRAKDRLVHEVEQRDER 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1769843692 582 IKQLEEDKHRLQQQLNdaenkykiLEKEFQQFKDQQNNKpeirlqseinlLTLEKVELERKL 643
Cdd:pfam15742 304 IKQLENEIGILQQQSE--------KEKAFQKQVTAQNEI-----------LLLEKRKLLEQL 346
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
477-621 |
1.03e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.23 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 477 FENQLKQKELAHMQ-ALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESElQREKKELQSERQR 555
Cdd:pfam13904 57 YENWLAAKQRQRQKeLQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAE-SASKSLAKPERKV 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843692 556 nlqeLQDSIRRAKEDCIhQVELERLKIKQLEEDKHRLQQQLNDAENKyKILEKEFQQFKDQQNNKP 621
Cdd:pfam13904 136 ----SQEEAKEVLQEWE-RKKLEQQQRKREEEQREQLKKEEEEQERK-QLAEKAWQKWMKNVKNKP 195
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
465-719 |
1.14e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 465 ELEMWKEMQEDIFEN------QLKQKELAHMQALAEEWK----------KRDRERESLvkkKVAEYTILEGKLQKTLIDL 528
Cdd:pfam15921 153 ELEAAKCLKEDMLEDsntqieQLRKMMLSHEGVLQEIRSilvdfeeasgKKIYEHDSM---STMHFRSLGSAISKILREL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 529 EKR----EQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDciHQVELERLKIK-------------QLE--EDK 589
Cdd:pfam15921 230 DTEisylKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISE--HEVEITGLTEKassarsqansiqsQLEiiQEQ 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 590 HRLQ-----QQLNDAENKYKILEKEFQQFKDQQNNKPEiRLQSEINLLTLEKVE--LERKLESATKSKLHYKQQwgralK 662
Cdd:pfam15921 308 ARNQnsmymRQLSDLESTVSQLRSELREAKRMYEDKIE-ELEKQLVLANSELTEarTERDQFSQESGNLDDQLQ-----K 381
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843692 663 ELARLKQREQEsqmARLKKQQEEleqmRLRYLAAEEKDTVKTERQELLDIRNELNRL 719
Cdd:pfam15921 382 LLADLHKREKE---LSLEKEQNK----RLWDRDTGNSITIDHLRRELDDRNMEVQRL 431
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
447-760 |
1.30e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.43 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 447 PSEIqtePRETLEYKAALELEMWKEMQED-------IFENQLKQKELAHMQALAEEWKKR-----DRERESLVKKKVAEY 514
Cdd:pfam07111 232 PPEV---HSQTWELERQELLDTMQHLQEDradlqatVELLQVRVQSLTHMLALQEEELTRkiqpsDSLEPEFPKKCRSLL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 515 TILEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQElQDSIRRAKEDCIHQVELERLKIKQL-------EE 587
Cdd:pfam07111 309 NRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQE-QAILQRALQDKAAEVEVERMSAKGLqmelsraQE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 588 DKHRLQQQLNDAENKYKI-----------LEKEFQQFKDQQNNKPE--------IRLQSEINLLTLEKVELER-KLESAT 647
Cdd:pfam07111 388 ARRRQQQQTASAEEQLKFvvnamsstqiwLETTMTRVEQAVARIPSlsnrlsyaVRKVHTIKGLMARKVALAQlRQESCP 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 648 KSKL-------------HYKQQWGRALKEL---ARLKQreQESQMARlkkQQEELEQMRLRYLAAEEKDTVKTERQELLD 711
Cdd:pfam07111 468 PPPPappvdadlsleleQLREERNRLDAELqlsAHLIQ--QEVGRAR---EQGEAERQQLSEVAQQLEQELQRAQESLAS 542
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1769843692 712 IRNELNRLRQQEQKQYQDSTEIAS--GKKDGPHGSVLEEGLDDYLTRLIEE 760
Cdd:pfam07111 543 VGQQLEVARQGQQESTEEAASLRQelTQQQEIYGQALQEKVAEVETRLREQ 593
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
455-734 |
1.38e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 455 RETLEYKAALELEMWKEMQEDIF-----ENQLKQKELAHMQALAEEWKKRDRERESlvkkkvaeytilegKLQKTLIDLE 529
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEeeeekEEERKEERKRYRQELEEQIEEREQKRQE--------------EYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 530 KREQQLASVESELQREKKELQSERQRNLQELQDSIR---RAKEDCIHQVELERLKIKQLEEDKHRLQQQLnDAENKYKIL 606
Cdd:pfam13868 102 QMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEeqaEWKELEKEEEREEDERILEYLKEKAEREEER-EAEREEIEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 607 EKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELErklesatksklhYKQQWGRALKELARLKQREQESQMARLKKQQEEL 686
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLYQEE------------QERKERQKEREEAEKKARQRQELQQAREEQIELK 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1769843692 687 EQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIA 734
Cdd:pfam13868 249 ERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
470-681 |
1.50e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 470 KEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLasvESELQREKKEL 549
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL---RAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 550 --------QSERQRNLQEL------QDSIRRAKEdcIHQVELERLK-IKQLEEDKHRLQQQLNDAENKYKILEKEFQQFK 614
Cdd:COG4942 107 aellralyRLGRQPPLALLlspedfLDAVRRLQY--LKYLAPARREqAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843692 615 DQQNnkpeiRLQSEINlltlEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKK 681
Cdd:COG4942 185 EERA-----ALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
536-667 |
2.02e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 536 ASVESELQREKKELQSERQRNLQELQDSIRRAKEDciHQVELERL--KIKQLEEDKHRLQQQLNDAENKYKILEKEFQQF 613
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTE--EEEEIRRLeeQVERLEAEVEELEAELEEKDERIERLERELSEA 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843692 614 KDQQNNkpEIRLQSEINLLTLEKVELERKLESA--TKSKLHYKQQwgrALKELARL 667
Cdd:COG2433 454 RSEERR--EIRKDREISRLDREIERLERELEEEreRIEELKRKLE---RLKELWKL 504
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
473-726 |
2.08e-03 |
|
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: 40.96 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 473 QEDIFENQLKQKELAHMQALaeEWKKRDRERESLVKKKVAEYTILE-GKLQKTLIDLE--------KREQQLASVESELQ 543
Cdd:pfam17045 14 QIDIMVAHKKSEWEGQTRAL--ETRLDIREEELLSARNTLERKHKEiGLLRQQLEELEkgkqelvaKYEQQLQKLQEELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 544 REKKELQSERQRNLQELQDSIRRAKEDcihQVELERLKIKQ-------LEEDKHRL--QQQLNDAENKYKILEKEFQQFK 614
Cdd:pfam17045 92 KLKRSYEKLQRKQLKEAREEAKSREED---RSELSRLNGKLeefrqksLEWEQQRLqyQQQVASLEAQRKALAEQSSLIQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 615 -----DQQNNKPEI--RLQSEINLLTlekveleRKLESATKSKLhykqqwgralkelarlkqreqesqmarlkkqQEELE 687
Cdd:pfam17045 169 saayqVQLEGRKQCleASQSEIQRLR-------SKLERAQDSLC-------------------------------AQELE 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1769843692 688 QMRLRYLAAEEKDTVKT---ERQELLD-----------IRNELNRLRQQEQKQ 726
Cdd:pfam17045 211 LERLRMRVSELGDSNRKlleEQQRLLEelrmsqrqlqvLQNELMELKATLQSQ 263
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
517-619 |
2.18e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 517 LEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQEL----QDSIRRAKE--DCIHQVELERLKIKQLEEDKH 590
Cdd:PRK00409 528 LERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaQQAIKEAKKeaDEIIKELRQLQKGGYASVKAH 607
|
90 100
....*....|....*....|....*....
gi 1769843692 591 RLQQQLNDAENKYKILEKEFQQFKDQQNN 619
Cdd:PRK00409 608 ELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
522-698 |
2.22e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 40.46 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 522 QKTLIDLEKREQQLASVESELQREKKELQSERQRNlqelqdsirrakedcihqvELERLKIKQLEEDKHRLqqqlndAEN 601
Cdd:pfam13904 41 ARKLEGLKLERQPLEAYENWLAAKQRQRQKELQAQ-------------------KEEREKEEQEAELRKRL------AKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 602 KYK--ILEKEFQQFKDQQNNKPeirlQSEINLLTLEKVELERKlESATKSKLHYKQQWgraLKELARLKQREQESQMARL 679
Cdd:pfam13904 96 KYQewLQRKARQQTKKREESHK----QKAAESASKSLAKPERK-VSQEEAKEVLQEWE---RKKLEQQQRKREEEQREQL 167
|
170
....*....|....*....
gi 1769843692 680 KKQQEELEQMRLRYLAAEE 698
Cdd:pfam13904 168 KKEEEEQERKQLAEKAWQK 186
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
520-739 |
2.35e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 520 KLQKTLIDLEKREQQLASVES---ELQREKKELQSERQRNLQELQDsirraKEDCIHQVELERLK-------IKQLEEDK 589
Cdd:TIGR04523 139 NIDKFLTEIKKKEKELEKLNNkynDLKKQKEELENELNLLEKEKLN-----IQKNIDKIKNKLLKlelllsnLKKKIQKN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 590 HRLQQQLNDAENKYKILEKEFQQfkdqqnnkpeirLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQ 669
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEK------------KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1769843692 670 R--EQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNrlrQQEQKQYQDSTEIASGKKD 739
Cdd:TIGR04523 282 KikELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIS---QNNKIISQLNEQISQLKKE 350
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
579-732 |
2.37e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.89 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 579 RLKIKQLEEDKHRLQQQLNDAENKYKIL-------EKEFQQFKDQQNNKPEI--RLQSEINLLTLEKVELERKLESATKS 649
Cdd:pfam15619 10 LHKIKELQNELAELQSKLEELRKENRLLkrlqkrqEKALGKYEGTESELPQLiaRHNEEVRVLRERLRRLQEKERDLERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 650 KLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDirNELNRLRQQEQKQYQD 729
Cdd:pfam15619 90 LKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELEN--KSFRRQLAAEKKKHKE 167
|
...
gi 1769843692 730 STE 732
Cdd:pfam15619 168 AQE 170
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
452-784 |
2.66e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 452 TEPRETLEYKAALE----LEMWKEMQEDIFENQLKQKELA--HMQALAEEW-------KKRDRERESLVKKKVAEYTIL- 517
Cdd:pfam12128 374 TAKYNRRRSKIKEQnnrdIAGIKDKLAKIREARDRQLAVAedDLQALESELreqleagKLEFNEEEYRLKSRLGELKLRl 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 518 -------EGKLQKTLIDL------EKREQQLASVESeLQREKKELQSERQRNLQELQDSIRRAKEdciHQVELERLKiKQ 584
Cdd:pfam12128 454 nqatatpELLLQLENFDErierarEEQEAANAEVER-LQSELRQARKRRDQASEALRQASRRLEE---RQSALDELE-LQ 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 585 LEEDKHRLQQQLND-----AENKYKILEKEFQQFKDQQnnkPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGR 659
Cdd:pfam12128 529 LFPQAGTLLHFLRKeapdwEQSIGKVISPELLHRTDLD---PEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRER 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 660 ALK-----ELARLKQREQESQMARLKKQQEEL---------------------------EQMRLRYLAAEEKDTVKTERQ 707
Cdd:pfam12128 606 LDKaeealQSAREKQAAAEEQLVQANGELEKAsreetfartalknarldlrrlfdekqsEKDKKNKALAERKDSANERLN 685
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843692 708 ElLDIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGSVLEEGLDDYLTRLIEERDTLmRTGVYNHEDRIISELDRQI 784
Cdd:pfam12128 686 S-LEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAAR-RSGAKAELKALETWYKRDL 760
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
464-688 |
2.71e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 464 LELEMW--KEMQEDI-----FENQLKQKELAHMQALAEEWKKRDRERESLVKKK---VAEYTILEGK---------LQKT 524
Cdd:smart00787 65 LELYQFscKELKKYIsegrdLFKEIEEETLINNPPLFKEYFSASPDVKLLMDKQfqlVKTFARLEAKkmwyewrmkLLEG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 525 LIDlekreqQLASVESELQREKKELQSERQRnLQELQDSIRRAKEDCIHQVELERlkikQLEEDKHRLQQ-QLNDAENKY 603
Cdd:smart00787 145 LKE------GLDENLEGLKEDYKLLMKELEL-LNSIKPKLRDRKDALEEELRQLK----QLEDELEDCDPtELDRAKEKL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 604 KILEKEFQQFKDQQNNkpeirlqseinlLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREqESQMARLKKQQ 683
Cdd:smart00787 214 KKLLQEIMIKVKKLEE------------LEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFT-FKEIEKLKEQL 280
|
....*
gi 1769843692 684 EELEQ 688
Cdd:smart00787 281 KLLQS 285
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
432-730 |
3.24e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 432 SAVQQKPSSLPPAPCPSEIQTEPRETLEyKAALELEMWKEMQEDIfeNQLKQK------ELAHMQALAEEWKKRDRE--R 503
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLVQQDLE-QTLALLDKIDRQKEET--EQLKQQlaqapaKLRQAQAELEALKDDNDEetR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 504 ESLVKKKVAEytiLEGKLQKTLIDLEKREQQLASVESEL--QREKKE-LQSERQRNLQELQdsirrakedcihqvELERL 580
Cdd:PRK11281 116 ETLSTLSLRQ---LESRLAQTLDQLQNAQNDLAEYNSQLvsLQTQPErAQAALYANSQRLQ--------------QIRNL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 581 KIKQLEEDK---HRLQQQLNdAENKYKILEKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLEsatksklhykqqw 657
Cdd:PRK11281 179 LKGGKVGGKalrPSQRVLLQ-AEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQ------------- 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1769843692 658 grALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQ--KQYQDS 730
Cdd:PRK11281 245 --LLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQQNLrvKNWLDR 317
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
411-764 |
3.42e-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: 41.11 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 411 LEDYGLVKMREIFISDSSQGVSAVQQKPSSLPPAPCPSEIQTEPretlEYKAALELEMwKEMQEDIFENQLKQKELAHMQ 490
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYH----ERKQVLEKEL-KHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 491 ALAEEWKKRDRERESLVKKkVAEYTILEGKLQKTLIDLEKR----------------EQQLASVESELQREKKELQSERQ 554
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRAR-IEELRAQEAVLEETQERINRArkaaplaahikavtqiEQQAQRIHTELQSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 555 R---------NLQELQDSIRRAKEDCIH----------------QVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKE 609
Cdd:TIGR00618 329 KraahvkqqsSIEEQRRLLQTLHSQEIHirdahevatsireiscQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 610 F--QQFKDQQNNKPEIRL---------------------QSEINLLTLEKVELE------RKLESATKSKLHYKQQWGRA 660
Cdd:TIGR00618 409 QatIDTRTSAFRDLQGQLahakkqqelqqryaelcaaaiTCTAQCEKLEKIHLQesaqslKEREQQLQTKEQIHLQETRK 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 661 LKELARLKQREQESQmARLKKQQEELEQ---------------MRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQK 725
Cdd:TIGR00618 489 KAVVLARLLELQEEP-CPLCGSCIHPNParqdidnpgpltrrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1769843692 726 QYQDSTEIA----SGKKDGPHGSVLEEGLDDYLTRLIEERDTL 764
Cdd:TIGR00618 568 IQQSFSILTqcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
465-725 |
4.32e-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: 40.54 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 465 ELEMWKEMQEDiFENQLKQKELAH-------------MQALAEEWKKRDRERESLVKKKvaeytileGKLQKTLIDLEKR 531
Cdd:pfam01576 13 ELQKVKERQQK-AESELKELEKKHqqlceeknalqeqLQAETELCAEAEEMRARLAARK--------QELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 532 EQQLASVESELQREKKELQSerqrNLQELQDSIRrAKEDCIHQVELERL----KIKQLEEDKHRLQQQLNDAENKYKILE 607
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQ----HIQDLEEQLD-EEEAARQKLQLEKVtteaKIKKLEEDILLLEDQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 608 KEFQQFKDQQNNKPE--IRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQR--EQESQMARLK--- 680
Cdd:pfam01576 159 ERISEFTSNLAEEEEkaKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQiaELQAQIAELRaql 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1769843692 681 -KQQEELE--QMRLRYLAAEEKDTVKTERQ---ELLDIRNELNRLRQQEQK 725
Cdd:pfam01576 239 aKKEEELQaaLARLEEETAQKNNALKKIREleaQISELQEDLESERAARNK 289
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
500-732 |
4.44e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 39.59 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 500 DRERESLVKKKVAEYtilegkLQKTLIDLEKRE---QQLASVESELQREKKELQsERQRNLQELQDSIRRAKedcihQVE 576
Cdd:pfam12795 7 KAKLDEAAKKKLLQD------LQQALSLLDKIDaskQRAAAYQKALDDAPAELR-ELRQELAALQAKAEAAP-----KEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 577 LERLKIKQLEedkhrlqQQLNDAENKYKILEKEFQQFKDQ---QNNKPEiRLQSEINLLTLEKVELERKLESATKSKlhy 653
Cdd:pfam12795 75 LASLSLEELE-------QRLLQTSAQLQELQNQLAQLNSQlieLQTRPE-RAQQQLSEARQRLQQIRNRLNGPAPPG--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 654 kQQWGRALKELARLKQREQESQMARLKKQQE------ELEQMRLRYLAAEekdtVKTERQELLDIRNELNRLRQQEQKQY 727
Cdd:pfam12795 144 -EPLSEAQRWALQAELAALKAQIDMLEQELLsnnnrqDLLKARRDLLTLR----IQRLEQQLQALQELLNEKRLQEAEQA 218
|
....*
gi 1769843692 728 QDSTE 732
Cdd:pfam12795 219 VAQTE 223
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
529-734 |
5.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 529 EKREQQLASVESELQREKKELQSERQRNLQElqdsIRRAKEDCIHQVELERLKIKQLEEDKhrlQQQLNDAENKYKilek 608
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEE----IRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKK---- 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 609 efqqfKDQQNNKPEIRLQSEINlltlEKVELERKLESATKSKLHYKQQwGRALKELARLKQREQESQMARLKKQQEELEQ 688
Cdd:PTZ00121 1292 -----ADEAKKAEEKKKADEAK----KKAEEAKKADEAKKKAEEAKKK-ADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1769843692 689 MRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIA 734
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
489-575 |
5.47e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 38.66 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 489 MQALAEEWKKRDRERESLVKKKVAEYTILEGKLQK-----TLIDLEKREQQLASVESELQREKKELQSERQRNLQELQDS 563
Cdd:COG2825 41 GKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKeaatlSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQELLQP 120
|
90
....*....|..
gi 1769843692 564 IRRAKEDCIHQV 575
Cdd:COG2825 121 ILEKIQKAIKEV 132
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
580-736 |
6.09e-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: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 580 LKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDqqnnkpeirlqsEINLLTLEKVELERKLESATKSKLHYKQQWG- 658
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKT------------ELEDLEKEIKRLELEIEEVEARIKKYEEQLGn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 659 -RALKELARLkQREQESQMARLKK-QQEELEQM----RLRYLAAEEKDTVKTERQELLDIRNELN----RLRQQEQKQYQ 728
Cdd:COG1579 85 vRNNKEYEAL-QKEIESLKRRISDlEDEILELMerieELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEA 163
|
....*...
gi 1769843692 729 DSTEIASG 736
Cdd:COG1579 164 EREELAAK 171
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
461-726 |
6.37e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 461 KAALELEMWKEMQEDIFENQLKQKELaHMQALAEEWK-KRDRERESL------VKKKVAEYTILEGKLQKTL-IDLEKRE 532
Cdd:pfam12128 265 FGYKSDETLIASRQEERQETSAELNQ-LLRTLDDQWKeKRDELNGELsaadaaVAKDRSELEALEDQHGAFLdADIETAA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 533 Q---QLASVESEL--QREKKELQSERQRNLQELQDSiRRAKEDCIHQVELERLKiKQLEEDKHRLQQQLNDAENKYKILE 607
Cdd:pfam12128 344 AdqeQLPSWQSELenLEERLKALTGKHQDVTAKYNR-RRSKIKEQNNRDIAGIK-DKLAKIREARDRQLAVAEDDLQALE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 608 KEFQQFKDQQNNkpEIRLQSEINLLTLEkvELERKLESATKSKlhykqqwgrALKElarlkqrEQESQMARLKKQQEELE 687
Cdd:pfam12128 422 SELREQLEAGKL--EFNEEEYRLKSRLG--ELKLRLNQATATP---------ELLL-------QLENFDERIERAREEQE 481
|
250 260 270
....*....|....*....|....*....|....*....
gi 1769843692 688 QMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQ 726
Cdd:pfam12128 482 AANAEVERLQSELRQARKRRDQASEALRQASRRLEERQS 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
455-651 |
6.55e-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: 39.75 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 455 RETLEYKAALELEMWKEMQEDIFENQLKQKELAhmQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLI------DL 528
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELE--KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLspedflDA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 529 EKREQQLASVESELQREKKELQSERQRnLQELQDSIRRAKEdcihqvELERLKiKQLEEDKHRLQQQLNDAENKYKILEK 608
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAE-LAALRAELEAERA------ELEALL-AELEEERAALEALKAERQKLLARLEK 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1769843692 609 EFQQFKDQ--QNNKPEIRLQSEINLLTLEKVELERKLESATKSKL 651
Cdd:COG4942 207 ELAELAAElaELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
482-696 |
6.74e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 482 KQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQseRQRNLQELQ 561
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 562 DSIRRAKEDCIHQVeleRLKIKQLEEdKHRLQQQLNDAENKykiLEKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELER 641
Cdd:COG4717 374 ALLAEAGVEDEEEL---RAALEQAEE-YQELKEELEELEEQ---LEELLGELEELLEALDEEELEEELEELEEELEELEE 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1769843692 642 KLESATKSKLHYKQQWgRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAA 696
Cdd:COG4717 447 ELEELREELAELEAEL-EQLEEDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
469-632 |
6.83e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.48 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 469 WKEMQEDIFE--NQLKQKELAHMQALAEEWKKrdrereslvKKKVAEyTILEGKLQKTLIDLEKREQQLASVESELQREK 546
Cdd:cd16269 147 YLEDREKLVEkyRQVPRKGVKAEEVLQEFLQS---------KEAEAE-AILQADQALTEKEKEIEAERAKAEAAEQERKL 216
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 547 KElqsERQRNL-QELQDSIRRakedciHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNkpeiRL 625
Cdd:cd16269 217 LE---EQQRELeQKLEDQERS------YEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAE----LL 283
|
....*..
gi 1769843692 626 QSEINLL 632
Cdd:cd16269 284 QEEIRSL 290
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| BRE1 |
pfam08647 |
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a ... |
483-600 |
7.41e-03 |
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BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a transcriptional activator through direct activator interactions.
Pssm-ID: 462547 [Multi-domain] Cd Length: 95 Bit Score: 36.41 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 483 QKELAHMQAlaeEWKKRDrereSLVKKKVAEYTILEGKLQKTLIDLEKREQQLAsvesELQREKKELQSERqRNLQelqd 562
Cdd:pfam08647 2 QTELVKLEQ---AFEELS----EQLDKKVKDLTILEEKKLRLEAEKAKADQKYF----AAMRSKDALENEN-KKLN---- 65
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90 100 110
....*....|....*....|....*....|....*...
gi 1769843692 563 sirrakedciHQVELERLKIKQLEEDKHRLQQQLNDAE 600
Cdd:pfam08647 66 ----------TLLSKSSELIEQLKETEKEFVRKLKNLE 93
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| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
529-710 |
7.75e-03 |
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Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 39.25 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 529 EKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVelERLKIKQLEEDKHRLQQQLNDAENKYKILEK 608
Cdd:pfam15558 80 RRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQE--QRLKEKEEELQALREQNSLQLQERLEEACHK 157
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 609 EFQQFKDQQNNKPEIRLQSEINLLTLEK-VELERKLESATKsKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELE 687
Cdd:pfam15558 158 RQLKEREEQKKVQENNLSELLNHQARKVlVDCQAKAEELLR-RLSLEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQ 236
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170 180
....*....|....*....|...
gi 1769843692 688 QMRLRylaAEEKDTVKTERQELL 710
Cdd:pfam15558 237 RAKWR---AEEKEEERQEHKEAL 256
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| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
474-706 |
9.38e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 474 EDIFENQLK-QKELAHMQALAEEWKKRDRERESLVKKKVAEytiLEGKLQKTLIDLEKREQQLASVESELQREKKELQSE 552
Cdd:PRK05771 46 RKLRSLLTKlSEALDKLRSYLPKLNPLREEKKKVSVKSLEE---LIKDVEEELEKIEKEIKELEEEISELENEIKELEQE 122
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 553 RQR---------NLQELQDS---------IRRAKEDCIHQVElERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFK 614
Cdd:PRK05771 123 IERlepwgnfdlDLSLLLGFkyvsvfvgtVPEDKLEELKLES-DVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLG 201
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 615 DQQNNKPEIRLQSE-INLLTLEKVELERKLESatksklhykqqwgrALKELARLKQREQESQMArlkkQQEELEQMRLRY 693
Cdd:PRK05771 202 FERLELEEEGTPSElIREIKEELEEIEKERES--------------LLEELKELAKKYLEELLA----LYEYLEIELERA 263
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250
....*....|...
gi 1769843692 694 LAAEEkdTVKTER 706
Cdd:PRK05771 264 EALSK--FLKTDK 274
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| F-BAR_PACSIN |
cd07655 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ... |
548-726 |
9.65e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153339 [Multi-domain] Cd Length: 258 Bit Score: 38.83 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 548 ELQSERQRNLQ-ELQDSIRRAKEDCIHQVELERLK-IKQLEEDKHRLQQQ-------LNDAENKYKILEKEFQQFKDQQN 618
Cdd:cd07655 78 ELHLSIRDKLLnDVVEEVKTWQKENYHKSMMGGFKeTKEAEDGFAKAQKPwakllkkVEKAKKAYHAACKAEKSAQKQEN 157
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843692 619 NKpeirlQSEINLLTlEKV-ELERKLESATKSKLHYKQQWGRALKELARLKQREQESqMARLKKQQEELEQMRLRYLaae 697
Cdd:cd07655 158 NA-----KSDTSLSP-DQVkKLQDKVEKCKQEVSKTKDKYEKALEDLNKYNPRYMED-MEQVFDKCQEFEEKRLDFF--- 227
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170 180
....*....|....*....|....*....
gi 1769843692 698 ekdtvkteRQELLDIRNELNRLRQQEQKQ 726
Cdd:cd07655 228 --------KEILLSYHRHLDLSTNPSFKA 248
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