|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
570-613 |
9.69e-23 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 96.37 E-value: 9.69e-23
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217281374 570 YVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQ 613
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQ 44
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
401-613 |
6.71e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 401 AIVERAQQMVEILTEENRVLHQELQgyyDNADKLHKFEKELQRISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 480
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 481 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 560
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217281374 561 EEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQ 613
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
404-612 |
5.14e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 404 ERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDL 483
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 484 RDRLETANRQLSSREYEGHEDKA----AEGHYASQNKEFLKEKE---KLEMELAAVRTA--------------SEDHRRH 542
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAeieeLEAQIEQLKEELKALREaldELRAELTLLNEEaanlrerleslerrIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 543 IEILDQALSNAQARVIKLEEELREKQAYVEKVEK--------LQQALTQLQSACEKREQMERRLRTW------LERELDA 608
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESeleallneRASLEEALALLRSELEELSEELRELeskrseLRRELEE 919
|
....
gi 2217281374 609 LRTQ 612
Cdd:TIGR02168 920 LREK 923
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
429-613 |
1.15e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 429 DNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEgEIRRLHDFNRDLRDRLETAnrqlssREYEGHEDKAAE 508
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIDVASAE------REIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 509 ghyASQNKEFLKEkekLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSAC 588
Cdd:COG4913 680 ---LDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALL 751
|
170 180 190
....*....|....*....|....*....|.
gi 2217281374 589 EKR------EQMERRLRTWLERELDALRTQQ 613
Cdd:COG4913 752 EERfaaalgDAVERELRENLEERIDALRARL 782
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
398-613 |
1.68e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 398 DAFAIVERAQQMVEilteenrvlH-QELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDkAMRNKL-----EG 471
Cdd:COG4913 219 EEPDTFEAADALVE---------HfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELE-YLRAALrlwfaQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 472 EIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDK--AAEGHYASQNkefLKEKEKLEMELAAVRTASEDHRRHIEILD 547
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELErlEARLDALREEldELEAQIRGNG---GDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217281374 548 QALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSACE--------KREQMERRLRTwLERELDALRTQQ 613
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEealaeaeaALRDLRRELRE-LEAEIASLERRK 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
404-613 |
2.26e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 404 ERAQQmveiLTEENRVLHQELQGYydnadKLHKFEKELQRISEAYESLvksTTKRESLDKAMRnKLEGEIRRLHDFNRDL 483
Cdd:COG1196 213 ERYRE----LKEELKELEAELLLL-----KLRELEAELEELEAELEEL---EAELEELEAELA-ELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 484 RDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE 563
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217281374 564 LREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQ 613
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
401-600 |
3.05e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 401 AIVERAQQMVEILTEENRVLHQELQGYYDN-----------ADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKL 469
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQleeleskldelAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 470 EGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYA--SQNKEFLkEKEKLEMELAAVRTASEDHRRHIEILD 547
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlQQEIEEL-LKKLEEAELKELQAELEELEEELEELQ 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217281374 548 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKREQMERRLRT 600
Cdd:TIGR02168 454 EELERLEEALEELREELEEAE---QALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
401-610 |
3.43e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 401 AIVERAQQMVEILTEE---NRVLHQELQ-GYYDNADK-LHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEG---E 472
Cdd:PRK03918 129 AIYIRQGEIDAILESDesrEKVVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 473 IRRLHDFNRDLRDRLETANRQLssREYEGHEDKAAEghYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD----- 547
Cdd:PRK03918 209 INEISSELPELREELEKLEKEV--KELEELKEEIEE--LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvke 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217281374 548 ----QALSNAQARVIKLEEELREKQAYVEK-VEKLQQALTQLQSACEKREQMERRLRtWLERELDALR 610
Cdd:PRK03918 285 lkelKEKAEEYIKLSEFYEEYLDELREIEKrLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELE 351
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
422-605 |
3.64e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 422 QELQGYYDNADKLHKFEKELQRISEAYESLvksttkRESLDKAmRNKLEGEIRRLhdfnRDLRDRLETANRQLSSREYEG 501
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEE 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 502 HEDkaaeghyasqnkeflkEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 581
Cdd:PRK03918 664 LRE----------------EYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720
|
170 180
....*....|....*....|....
gi 2217281374 582 TQLQsacEKREQMeRRLRTWLERE 605
Cdd:PRK03918 721 ERVE---ELREKV-KKYKALLKER 740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
432-600 |
7.73e-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: 55.84 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 432 DKLHKFEKELQRISEAYES----LVKSTTKRESLDKAMRNKLEgEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAA 507
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREieqkLNRLTLEKEYLEKEIQELQE-QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 508 EGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSA 587
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV 956
|
170
....*....|...
gi 2217281374 588 CEKREQMERRLRT 600
Cdd:TIGR02169 957 QAELQRVEEEIRA 969
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
395-612 |
9.75e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 395 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGyydnADKLHKFEKE-LQRISEAYESLVKSTTKRESLDKAMrNKL 469
Cdd:TIGR02168 133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQL-KSL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 470 EGEIRRLHDFnRDLRDRLETANRQLSSREYEGHEDKAAEghYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQA 549
Cdd:TIGR02168 206 ERQAEKAERY-KELKAELRELELALLVLRLEELREELEE--LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217281374 550 LSNAQARVIKLEEELREKQAYVE-KVEKLQQALTQLQSACEKREQMERRLRTwLERELDALRTQ 612
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQiLRERLANLERQLEELEAQLEELESKLDE-LAEELAELEEK 345
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
423-604 |
2.51e-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: 51.85 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 423 ELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQL----SSRE 498
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 499 YEG--HEDKAAEghyasqnkeflKEKEKLEMELAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQA-YVEKVE 575
Cdd:COG1579 91 YEAlqKEIESLK-----------RRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAeLDEELA 152
|
170 180 190
....*....|....*....|....*....|
gi 2217281374 576 KLQQALTQLQSACEK-REQMERRLRTWLER 604
Cdd:COG1579 153 ELEAELEELEAEREElAAKIPPELLALYER 182
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
399-613 |
2.05e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 399 AFAIVERAQQMVEILTEENRVLHQELQgyyDNADKLHKFEKELQRISEAYESLvksttkresldKAMRNKLEGEIRRLhd 478
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLE---ELRLEVSELEEEIEELQKELYAL-----------ANEISRLEQQKQIL-- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 479 fnrdlRDRLETANRQLSSREYEGHEDKaaeghyaSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVI 558
Cdd:TIGR02168 308 -----RERLANLERQLEELEAQLEELE-------SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217281374 559 KLEEELRE-KQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQ 613
Cdd:TIGR02168 376 ELEEQLETlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
441-613 |
2.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 441 LQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRL---HDFNRDLRDRLETANRQLSS--REYEGHEDKAAEGHYASQN 515
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEELEEleAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 516 KEFLKEKEKLEMELAAVRTASEDHRRHIEI---LDQALSNAQARVIKLEEELREKQAY------------VEKVEKLQQA 580
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQlslateeelqdlAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|...
gi 2217281374 581 LTQLQsacEKREQMERRLRTwLERELDALRTQQ 613
Cdd:COG4717 208 LAELE---EELEEAQEELEE-LEEELEQLENEL 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
455-612 |
5.37e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 455 TTKRESLDKAMRNKLEGEIRRLHDFNRDLRdrlETANRQLSSREYEGHEDKAAEGHYAsqnkEFLKEKEKLEMELAAVRT 534
Cdd:COG4717 37 STLLAFIRAMLLERLEKEADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYA----ELQEELEELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 535 ASEDHRRHIEILDQALSNAQ--ARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKREQMERRLRTwLERELDALRTQ 612
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPlyQELEALEAELAELP---ERLEELEERLEELRELEEELEELEAELAE-LQEELEELLEQ 185
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
432-612 |
1.27e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 432 DKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETanrqlSSREYEGHEDKAAEghy 511
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELE-SLEGSKRKLEEKIRELEERIEE-----LKKEIEELEEKVKE--- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 512 asqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKR 591
Cdd:PRK03918 285 ----LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
170 180
....*....|....*....|.
gi 2217281374 592 EQMERRLRTwLERELDALRTQ 612
Cdd:PRK03918 361 HELYEEAKA-KKEELERLKKR 380
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
429-613 |
1.75e-05 |
|
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: 47.86 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 429 DNADKLHKFEKELQ-RISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 504
Cdd:pfam01576 145 DQNSKLSKERKLLEeRISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 505 KAaegHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTql 584
Cdd:pfam01576 224 IA---ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG-- 298
|
170 180
....*....|....*....|....*....
gi 2217281374 585 qsacekrEQMErRLRTWLERELDALRTQQ 613
Cdd:pfam01576 299 -------EELE-ALKTELEDTLDTTAAQQ 319
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-610 |
1.84e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 414 TEEN--RV--LHQELQGYYDNADKLHKFEKELQRISEAYESLVK--STTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRL 487
Cdd:TIGR02168 184 TRENldRLedILNELERQLKSLERQAEKAERYKELKAELRELELalLVLRLEELREELE-ELQEELKEAEEELEELTAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 488 ETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREK 567
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217281374 568 QAYVEKVEKLQQALT-QLQSACEKREQMERRLRTwLERELDALR 610
Cdd:TIGR02168 343 EEKLEELKEELESLEaELEELEAELEELESRLEE-LEEQLETLR 385
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
433-613 |
2.34e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 433 KLHKFEKELQRIseayeslvksTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETANRQLSSREyegHEDKAAEghya 512
Cdd:COG1579 11 DLQELDSELDRL----------EHRLKELPAELA-ELEDELAALEARLEAAKTELEDLEKEIKRLE---LEIEEVE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 513 sqnkeflKEKEKLEMELAAVRTAsedhrRHIEILDQALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKRE 592
Cdd:COG1579 73 -------ARIKKYEEQLGNVRNN-----KEYEALQKEIESLKRRISDLEDEILELM---ERIEELEEELAELEAELAELE 137
|
170 180
....*....|....*....|.
gi 2217281374 593 QMERRLRTWLERELDALRTQQ 613
Cdd:COG1579 138 AELEEKKAELDEELAELEAEL 158
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
438-577 |
3.92e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 438 EKELQRISEAYESLVKST-TKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEghyasqNK 516
Cdd:COG2433 387 EKELPEEEPEAEREKEHEeRELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE------RR 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217281374 517 EFLKEKE--KLEMELAAVRTASEDHRRHIEILdqalsnaQARVIKLEE----ELREKQAYVEKVEKL 577
Cdd:COG2433 460 EIRKDREisRLDREIERLERELEEERERIEEL-------KRKLERLKElwklEHSGELVPVKVVEKF 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
430-610 |
4.53e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 430 NADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRN------KLEGEIRRLHDF--NRDLRDRLETANRQLSS--REY 499
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEleaeleELREELEKLEKLlqLLPLYQELEALEAELAElpERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 500 EGHEDKAAEGhyasqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILD-QALSNAQARVIKLEEELREKQayvEKVEKLQ 578
Cdd:COG4717 149 EELEERLEEL------RELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELE---EELEEAQ 219
|
170 180 190
....*....|....*....|....*....|..
gi 2217281374 579 QALTQLQSACEKREQMERRLRtwLERELDALR 610
Cdd:COG4717 220 EELEELEEELEQLENELEAAA--LEERLKEAR 249
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
432-604 |
8.97e-05 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 44.27 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 432 DKLHKFEKELQRISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSsreyeGHEDKAAEGHY 511
Cdd:cd07596 11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLG-----KAAEELSSLSE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 512 ASQNKEFLKEKEKLEMEL---AAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQ----QAL 581
Cdd:cd07596 82 AQANQELVKLLEPLKEYLrycQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPA---KVEELEeeleEAE 158
|
170 180
....*....|....*....|...
gi 2217281374 582 TQLQSACEKREQMERRLRTWLER 604
Cdd:cd07596 159 SALEEARKRYEEISERLKEELKR 181
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
404-586 |
1.34e-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: 45.20 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 404 ERAQQMVEIlteENRVLHQELQgyydnadkLHKFEKELQRISEAYE---SLVKSTTKRESLDKAMRNKlEGEIRRLHDFN 480
Cdd:pfam10174 182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 481 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKeFLKEK--------EKLEMELAAVRTASE-------DHRRHIEI 545
Cdd:pfam10174 250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK-FMKNKidqlkqelSKKESELLALQTKLEtltnqnsDCKQHIEV 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217281374 546 LDQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQLQS 586
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEEKS 376
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
413-598 |
1.46e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 413 LTEENRvlhQELQGYYdnADKLHKFEKELQRISEAYESLVKSTTKresLDKAMRNklEGEIRRLH---DFNRDLRDRLET 489
Cdd:PRK03918 445 LTEEHR---KELLEEY--TAELKRIEKELKEIEEKERKLRKELRE---LEKVLKK--ESELIKLKelaEQLKELEEKLKK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 490 ANRQ---LSSREYEGHEDKAA--EGHYASQNKEfLKEKEKLEMELAAVRTASED-HRRHIEILDQALSNAQARVIKLEEE 563
Cdd:PRK03918 515 YNLEeleKKAEEYEKLKEKLIklKGEIKSLKKE-LEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEER 593
|
170 180 190
....*....|....*....|....*....|....*
gi 2217281374 564 LREKQAYVEKVEKLQQALTQLQSACEKREQMERRL 598
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
548-609 |
1.79e-04 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 43.01 E-value: 1.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217281374 548 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKREQMERRLRTwlERELDAL 609
Cdd:COG3167 46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
415-608 |
2.24e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 415 EENRVLHQELQGyyDNADKLHKFEKELQRISEAYESLVKST-TKRESLDKamRNKLEGEIRRLHDFNRDLRDRLETAnrq 493
Cdd:PRK02224 226 EEQREQARETRD--EADEVLEEHEERREELETLEAEIEDLReTIAETERE--REELAEEVRDLRERLEELEEERDDL--- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 494 LSSREYEGHEDKAAEGHYAsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEildqalsNAQARVIKLEE---ELREKQAY 570
Cdd:PRK02224 299 LAEAGLDDADAEAVEARRE----ELEDRDEELRDRLEECRVAAQAHNEEAE-------SLREDADDLEEraeELREEAAE 367
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217281374 571 VEKveKLQQALTQLQSACEKREQMERRLRTWLERELDA 608
Cdd:PRK02224 368 LES--ELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
434-609 |
2.66e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 434 LHKFEKELQRISEAYESLVKsttKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYAS 513
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 514 QNKEFLKEKEKLEMELAAVRtasedhRRHIEIldqalsnaQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQ 593
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEER------KRRDKL--------TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
170
....*....|....*.
gi 2217281374 594 MERRLRTWLERELDAL 609
Cdd:TIGR02169 396 KLKREINELKRELDRL 411
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
431-613 |
2.76e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 431 ADKLHKFEKELQRISE---AYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLSS---------RE 498
Cdd:COG4942 19 ADAAAEAEAELEQLQQeiaELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelrAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 499 YEGHEDKAAE---GHYASQNKEFLK------EKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQA 569
Cdd:COG4942 99 LEAQKEELAEllrALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217281374 570 YVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQ 613
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
402-604 |
3.02e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 402 IVERAQQMVEILTEENRVL-HQELQG------YYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIR 474
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAErYQALLKekreyeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 475 RLHDFNRDLRDRLETANRQLSSREYEGHED----KAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQAL 550
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEiaslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217281374 551 SNAQARVIKLEEELREKQAYVEKVEK-----------LQQALTQLQsacEKREQMERRLRTWLER 604
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKefaetrdelkdYREKLEKLK---REINELKRELDRLQEE 414
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
401-594 |
3.34e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 401 AIVERAQQMVEILTEENRVLHQE-LQGYYDNADKLHKFEKELQRISEAYESLVKS----TTKRESLDKAMRNKLEGEIRR 475
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKhqdvTAKYNRRRSKIKEQNNRDIAG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 476 LHDfnrDLRDRLETANRQLSSRE--YEGHEDKAAEGHYAsQNKEFLKEKEKLEMELAAVR------TASEDHRRHIEILD 547
Cdd:pfam12128 395 IKD---KLAKIREARDRQLAVAEddLQALESELREQLEA-GKLEFNEEEYRLKSRLGELKlrlnqaTATPELLLQLENFD 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217281374 548 QALSNAQ-------ARVIKLEEELRE-KQAYVEKVEKLQQA---LTQLQSACEKREQM 594
Cdd:pfam12128 471 ERIERAReeqeaanAEVERLQSELRQaRKRRDQASEALRQAsrrLEERQSALDELELQ 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
468-613 |
4.22e-04 |
|
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: 43.51 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 468 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD 547
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217281374 548 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQ 613
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAE---AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
404-579 |
4.95e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 404 ERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLvksttkresldKAMRNKLEGEIRRLHDFNR-- 481
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-----------REELEKLEKLLQLLPLYQEle 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 482 DLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELA--------AVRTASEDHRRH---IEILDQAL 550
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslateeELQDLAEELEELqqrLAELEEEL 215
|
170 180
....*....|....*....|....*....
gi 2217281374 551 SNAQARVIKLEEELREKQAYVEKVEKLQQ 579
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
404-609 |
5.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 404 ERAQQMVEILTEENRVLHQELQGYydnadKLHKFEKELQRISEAYESLvkstTKRESLDKAMRNKLEGEIRRLhdfnRDL 483
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGL-----TPEKLEKELEELEKAKEEI----EEEISKITARIGELKKEIKEL----KKA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 484 RDRLETANRQ--LSSREYEGHEDKAAEGHY-------ASQNKEFLKEKEKLEMELAAVRTASEDHRRHI---EILDQaLS 551
Cdd:PRK03918 428 IEELKKAKGKcpVCGRELTEEHRKELLEEYtaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIklkELAEQ-LK 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217281374 552 NAQAR-----VIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTwLERELDAL 609
Cdd:PRK03918 507 ELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE-LEKKLDEL 568
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
410-594 |
5.81e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.66 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 410 VEILTEENRVLHQELQGYYDNADKLHKFEKEL---------------QRISEAYESLVKSTTKResldkamRNKLEgEIR 474
Cdd:cd00176 35 VEALLKKHEALEAELAAHEERVEALNELGEQLieeghpdaeeiqerlEELNQRWEELRELAEER-------RQRLE-EAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 475 RLHDFNRDLRD---RLETANRQLSSREYEGHEDKAaeghyasqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALS 551
Cdd:cd00176 107 DLQQFFRDADDleqWLEEKEAALASEDLGKDLESV---------EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217281374 552 NAQARVIKleeelrekqayvEKVEKLQQALTQLQSACEKREQM 594
Cdd:cd00176 178 PDADEEIE------------EKLEELNERWEELLELAEERQKK 208
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
422-610 |
7.16e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 422 QELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNR--DLRDRLETANRQLSSREY 499
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEyqELKEELEELEEQLEELLG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 500 EGHEDKAAEghyasqNKEFLKEK-EKLEMELAAvrtasedhrrhieiLDQALSNAQARVIKLEEELREkqayVEKVEKLQ 578
Cdd:COG4717 417 ELEELLEAL------DEEELEEElEELEEELEE--------------LEEELEELREELAELEAELEQ----LEEDGELA 472
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217281374 579 QALTQLQSACEKREQMERR------LRTWLERELDALR 610
Cdd:COG4717 473 ELLQELEELKAELRELAEEwaalklALELLEEAREEYR 510
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
419-597 |
8.74e-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: 42.40 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 419 VLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKR----ESLDKAM--RNKLEGEIRRLHDFNRDLRDRLETANR 492
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKevelEELKKILaeDEKLLDEKKQFEKIAEELKGKEQELIF 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 493 QLSSREYEGHE-------DKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEEL- 564
Cdd:pfam05483 444 LLQAREKEIHDleiqltaIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIi 523
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217281374 565 ---REKQAYVEKVEKLQQALTQLQSACEK-REQMERR 597
Cdd:pfam05483 524 nckKQEERMLKQIENLEEKEMNLRDELESvREEFIQK 560
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
506-612 |
1.52e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 41.51 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 506 AAEGHYASQNKEFLKEKEKLEMELAAVR---TASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKV-----EKL 577
Cdd:PRK10361 22 FASYQHAQQKAEQLAEREEMVAELSAAKqqiTQSEHWRAECELLNNEVRSLQSINTSLEADLREVTTRMEAAqqhadDKI 101
|
90 100 110
....*....|....*....|....*....|....*
gi 2217281374 578 QQALTQLQSACEKREQMERRLRTWLERELDALRTQ 612
Cdd:PRK10361 102 RQMINSEQRLSEQFENLANRIFEHSNRRVDEQNRQ 136
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
401-612 |
2.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 401 AIVERAQQMVEILTEEnRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLD------KAMRNKLEGEIR 474
Cdd:COG4913 631 ERLEALEAELDALQER-REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEeqleelEAELEELEEELD 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 475 RLHDFNRDLRDRLETANRQL--SSREYEGHEDKAAEGHYASqnkefLKEKEKLEMELAAVRTASEDHRRHIEILDQALSN 552
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELdeLQDRLEAAEDLARLELRAL-----LEERFAAALGDAVERELRENLEERIDALRARLNR 784
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 553 AQARVIKL--------EEELREKQAYVEKVEKLQQALTQLQS--ACEKREQMERRLRTWLERELDALRTQ 612
Cdd:COG4913 785 AEEELERAmrafnrewPAETADLDADLESLPEYLALLDRLEEdgLPEYEERFKELLNENSIEFVADLLSK 854
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
431-613 |
2.47e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 431 ADKLHKFEKELQRISEAYESLVKSTtkreSLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDKAAE 508
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQahNEEAESLREDADD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 509 ghYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQAL----------------------------SNAQARVIKL 560
Cdd:PRK02224 354 --LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdapvdlgnaedfleelreerDELREREAEL 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217281374 561 EEELREKQAYVEKVEKLQ---------QALTQLQSAC---EKREQMERrlrtwLERELDALRTQQ 613
Cdd:PRK02224 432 EATLRTARERVEEAEALLeagkcpecgQPVEGSPHVEtieEDRERVEE-----LEAELEDLEEEV 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
403-590 |
2.59e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 403 VERAQQMVEILTEENRVLHQELQgyyDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRN---KLEGEIRRLHDF 479
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIE---SLAAEIEELEELIEELESELEALLNERASLEEALALLRSeleELSEELRELESK 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 480 NRDLRDRLETANRQLSS--REYEGHEDKAAeghyasQNKEFLKEKEKLEMELAAvrtasedhrRHIEILDQALSNAQARV 557
Cdd:TIGR02168 910 RSELRRELEELREKLAQleLRLEGLEVRID------NLQERLSEEYSLTLEEAE---------ALENKIEDDEEEARRRL 974
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217281374 558 IKLE-----------------EELREKQAYVEK-VEKLQQALTQLQSACEK 590
Cdd:TIGR02168 975 KRLEnkikelgpvnlaaieeyEELKERYDFLTAqKEDLTEAKETLEEAIEE 1025
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
406-604 |
2.91e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 406 AQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRD 485
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 486 RLETANRQLSSREY-----------------EGHEDKAAEGHYASQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILD 547
Cdd:COG4942 98 ELEAQKEELAELLRalyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217281374 548 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKREQMERRLRTWLER 604
Cdd:COG4942 178 ALLAELEEERAALEALKAERQ---KLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
423-598 |
4.86e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 423 ELQGYYDNADKLHKFEKELQRISEAYESLVKSTtkRESLDKAmrnklEGEIRRLHDFNRDLRDRLETANRQLSsrEYEGH 502
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEA--REAVEDR-----REEIEELEEEIEELRERFGDAPVDLG--NAEDF 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 503 EDKAAEghyasqNKEFLKEKEK-LEMELAAVRTASEDHRR------------------HIEILD---QALSNAQARVIKL 560
Cdd:PRK02224 414 LEELRE------ERDELREREAeLEATLRTARERVEEAEAlleagkcpecgqpvegspHVETIEedrERVEELEAELEDL 487
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217281374 561 EEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRL 598
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELI 525
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
422-593 |
6.51e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 422 QELQGYYDN--------ADKLHKFEKELQRISEAYESLVKSTTK---------------RESLDKAMRNKLE--GEIRRL 476
Cdd:pfam01576 415 QELQARLSEserqraelAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesqlqdtQELLQEETRQKLNlsTRLRQL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 477 HDFNRDLRDRLETanrqlssreyEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRhieildqalsnAQAR 556
Cdd:pfam01576 495 EDERNSLQEQLEE----------EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKR-----------LQRE 553
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217281374 557 VIKLEEELREKQAYVEKVEK----LQQALT----------QLQSACEKREQ 593
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKLEKtknrLQQELDdllvdldhqrQLVSNLEKKQK 604
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
462-602 |
6.81e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 462 DKAMrNKLEGEIRRLHDF-------NRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRT 534
Cdd:PRK09039 52 DSAL-DRLNSQIAELADLlslerqgNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 535 ASEDHRRHIEILDQALSNAQARVIKLEEEL-------REKQAyvekveKLQQALTQLQSACEKR-EQMER-------RLR 599
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALdasekrdRESQA------KIADLGRRLNVALAQRvQELNRyrseffgRLR 204
|
...
gi 2217281374 600 TWL 602
Cdd:PRK09039 205 EIL 207
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
433-576 |
6.92e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281374 433 KLHKFEKELQRISEAYESLVKSTTKRESLD-----KAMRNKLEGEIR-RLHDFNR---DLRDRLETANRQLSSREYEGHE 503
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAIKKEALLEakeeiHKLRNEFEKELReRRNELQKlekRLLQKEENLDRKLELLEKREEE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217281374 504 DKAAEGHYASQNKEFLKEKEKLEmelaavrtasEDHRRHIEILDQ--ALSNAQARVI---KLEEELR-EKQAYVEKVEK 576
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELE----------ELIEEQLQELERisGLTAEEAKEIlleKVEEEARhEAAVLIKEIEE 180
|
|
| Val_tRNA-synt_C |
pfam10458 |
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA ... |
520-585 |
8.52e-03 |
|
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA synthetases.
Pssm-ID: 431296 [Multi-domain] Cd Length: 66 Bit Score: 35.32 E-value: 8.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217281374 520 KEKEKLEMELAAVRTasedhrrHIEILDQALSN------AQARVIklEEELREKQAYVEKVEKLQQALTQLQ 585
Cdd:pfam10458 4 KERARLEKELAKLQK-------EIERVQGKLANpgfvakAPAEVV--EEEKAKLAELEEQAEKLRERLSKLG 66
|
|
| PRK11020 |
PRK11020 |
YibL family ribosome-associated protein; |
469-534 |
9.11e-03 |
|
YibL family ribosome-associated protein;
Pssm-ID: 182904 [Multi-domain] Cd Length: 118 Bit Score: 36.54 E-value: 9.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217281374 469 LEGEIRRLHDfnrdlrdRLETANRQLSSREYEGHEDKAAEghyasqnkeFLKEKEKLEMELAAVRT 534
Cdd:PRK11020 3 EKNEIKRLSD-------RLDAIRHKLAAASLRGDAEKYAQ---------FEKEKATLEAEIARLKE 52
|
|
| |
