|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
437-720 |
3.35e-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: 67.00 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 437 NIEDLIEKlqagvmVKDQISDIRISdimdvyEMKLSTLASKESRLQDLLEAKALALAQADRLIAQYRCQRTQAETEARTL 516
Cdd:TIGR02168 678 EIEELEEK------IEELEEKIAEL------EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 517 AGMLREVERKNEELSVLLKSQQLESERAQNDIEHLFQHSKKLESVAAEHEIltksymELVQRNEATEKKNTDLQTTCESL 596
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE------ELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 597 NKHIETMKKLN---EALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLhkiaksqEEKLNVLQKEKEDKQETIDIL 673
Cdd:TIGR02168 820 ANLRERLESLErriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-------ESELEALLNERASLEEALALL 892
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568995253 674 RKELS-------RTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELN 720
Cdd:TIGR02168 893 RSELEelseelrELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
508-719 |
4.50e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 508 QAETEARTLAGMLREVERKNEELSVLLKSQQLESERAQNDIEHLFQHSKKLESVAAEHEILTKSYMELVQRNEATEKKNT 587
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 588 DLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQ 667
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568995253 668 ETIDILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEEL 719
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
499-710 |
1.83e-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: 60.16 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 499 IAQYRCQRTQAETEARTLAGMLREVERKNEELSVLLKSQQLESERAQNDIEhlfQHSKKLESVAAEHEILTKSYMELV-- 576
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA---ELEKEIAELRAELEAQKEELAELLra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 577 -QRNEATEKKNTDL-QTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADrecklsnLHKIAKSQEE 654
Cdd:COG4942 113 lYRLGRQPPLALLLsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE-------LEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568995253 655 KLNVLQKEKEDKQETIDILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKES 710
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
435-713 |
2.69e-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: 60.84 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 435 ALNIEDLIEKLQAGVMVKDQISDIR--ISDIMDVYEMKLSTL----ASKESRLQDLLEAKALALAQADRL---IAQYRCQ 505
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELeeLTAELQELEEKLEELrlevSELEEEIEELQKELYALANEISRLeqqKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 506 RTQAETEARTLAGMLREVERKNEELSVLLKSQQLESERAQNDIEHLfqhSKKLESVAAEHEILTKSYMELVQRNEATEKK 585
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL---EAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 586 NTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIE-----KEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQ 660
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEllkklEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568995253 661 KEKEDKQETIDILRKELSRteqirkeLSIKASSLEMHKAQLEGRLEEKESLLK 713
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQ-------LQARLDSLERLQENLEGFSEGVKALLK 513
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
452-721 |
8.20e-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: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 452 KDQISDIRIS---DIMDVYEMKLSTLASKESRLQDLLEAKALALAQADRLIAQYRCQRTQAETEARTLAGML-------- 520
Cdd:TIGR02168 219 KAELRELELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneis 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 521 ---REVERKNEELSVLLKSQqlesERAQNDIEHLFQHSKKLEsvaaehEILTKSymelvqrneatEKKNTDLQTTCESLN 597
Cdd:TIGR02168 299 rleQQKQILRERLANLERQL----EELEAQLEELESKLDELA------EELAEL-----------EEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 598 KHIETMKKLNEALKQQNEktiaqliEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKEL 677
Cdd:TIGR02168 358 AELEELEAELEELESRLE-------ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568995253 678 SRTEqiRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNK 721
Cdd:TIGR02168 431 EEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
503-702 |
1.61e-08 |
|
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: 58.21 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 503 RCQRTQAETEARTLAGMLREVE--RKNEELSVLLKSQQLESERAqndiehlfqhsKKLESVAAEhEILTKSYMELVQRNE 580
Cdd:pfam17380 402 RKVKILEEERQRKIQQQKVEMEqiRAEQEEARQREVRRLEEERA-----------REMERVRLE-EQERQQQVERLRQQE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 581 ATEKKNTDLQTTCESLNKHIETMKKlnEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNvlQ 660
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAEEQRR--KILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK--Q 545
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568995253 661 KEKEDK---QETIDILRKELSRTEQIRKELSIKASSLEMHKAQLE 702
Cdd:pfam17380 546 QEMEERrriQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
522-721 |
2.33e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 522 EVERKNEELsvllKSQQLESERAQNdiehlfqHSKKLESVAAEHEILTKSymELVQRNEATEKKNTDLQTTCESLNKHIE 601
Cdd:PTZ00121 1441 EEAKKADEA----KKKAEEAKKAEE-------AKKKAEEAKKADEAKKKA--EEAKKADEAKKKAEEAKKKADEAKKAAE 1507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 602 TMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKI--AKSQEEKLNVLQKEKEDKQETIDILRKELSR 679
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAeeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568995253 680 -TEQIRKELSIKASSLEMHKAQLEGRLEEKEsllKLQQEELNK 721
Cdd:PTZ00121 1588 kAEEARIEEVMKLYEEEKKMKAEEAKKAEEA---KIKAEELKK 1627
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
516-731 |
4.25e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.05 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 516 LAGMLREVERKNEELS--VLLKSQQLESERA--QNDIEHLFQ-HSKKLESVAAEHEI----LT-------------KSYM 573
Cdd:pfam15921 222 ISKILRELDTEISYLKgrIFPVEDQLEALKSesQNKIELLLQqHQDRIEQLISEHEVeitgLTekassarsqansiQSQL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 574 ELVQ-----RNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKTI----AQLIEKEEQRKEVQSQLADRECKLSN 644
Cdd:pfam15921 302 EIIQeqarnQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQLQK 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 645 LHKIAKSQEEKLNvLQKEKEDK--------QETIDILRKEL-SRTEQIRKELSIkassLEMHKAQLEGRLEEKESLLKLQ 715
Cdd:pfam15921 382 LLADLHKREKELS-LEKEQNKRlwdrdtgnSITIDHLRRELdDRNMEVQRLEAL----LKAMKSECQGQMERQMAAIQGK 456
|
250
....*....|....*.
gi 568995253 716 QEELNKHSHMIAMIHS 731
Cdd:pfam15921 457 NESLEKVSSLTAQLES 472
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
505-726 |
5.24e-08 |
|
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: 56.29 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 505 QRTQAETEARTLAGMLREveRKNEELSVLLKSQQL-ESERA-QNDIEhlfqhskKLESVAAEHEILTKSYMELVQRNEAT 582
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQ--EKEEKAREVERRRKLeEAEKArQAEMD-------RQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 583 EKKNTDLQTTCESLNKHIETMKKL----------NEALKQQNEKTIAQLIEKEEQRKEVQSQLADREcklsnlhKIAKSQ 652
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMRELerlqmerqqkNERVRQELEAARKVKILEEERQRKIQQQKVEME-------QIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 653 EE----KLNVLQKEKEDKQETIDilRKELSRTEQI----RKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNKHSH 724
Cdd:pfam17380 430 EEarqrEVRRLEEERAREMERVR--LEEQERQQQVerlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
..
gi 568995253 725 MI 726
Cdd:pfam17380 508 MI 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
513-719 |
5.66e-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: 56.61 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 513 ARTLAGMLREVERKNEELSVLLKSQQLESERAQNdieHLFQHSKKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTT 592
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIEN---RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 593 CESLNKHIE---TMKKLNEALKQQNEKTIAQLIEKEE--QRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQ 667
Cdd:TIGR02169 746 LSSLEQEIEnvkSELKELEARIEELEEDLHKLEEALNdlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568995253 668 ETIDILRKELSRTEQIRKELSIKASS-------LEMHKAQLEGRLEEKESLLKLQQEEL 719
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSiekeienLNGKKEELEEELEELEAALRDLESRL 884
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
473-724 |
5.73e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 473 TLASKESRLQDLLEAKALALAQADRLIAQYRCQRTQAETEARTLAgmlREVERKNEELSVLlksQQLESERAQNDiEHLF 552
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA---RLEERRRELEERL---EELEEELAELE-EELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 553 QHSKKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQ 632
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 633 SQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLL 712
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
250
....*....|..
gi 568995253 713 KLQQEELNKHSH 724
Cdd:COG1196 494 LLLLEAEADYEG 505
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
496-721 |
6.02e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 496 DRLIAQYRCQRTQAETEARTLAGMLREVERKNEELSVLLKSQQL-----ESERAQNDIEHLFQHSKKLESVAAEHEILTK 570
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 571 SYMELVQRNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNE--KTIAQLIEKEEQRK----EVQSQLADRECKLSN 644
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKkkaeELKKAEEENKIKAEE 1734
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995253 645 LHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSRTEQIRKElsikasslemHKAQLEGRLEEKESLLKLQQEELNK 721
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE----------KEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
472-693 |
2.90e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 472 STLASKESRLQDLLEakalalaqadrliaqyrcQRTQAETEARTLAGMLREVERKNEELSVLLKSQQLESERAQNDIEHL 551
Cdd:TIGR02169 308 RSIAEKERELEDAEE------------------RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 552 FQhskKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTTcesLNKHIETMKKLNEALKQQNEK---TIAQLIEKEEQR 628
Cdd:TIGR02169 370 RA---ELEEVDKEFAETRDELKDYREKLEKLKREINELKRE---LDRLQEELQRLSEELADLNAAiagIEAKINELEEEK 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995253 629 KEVQSQLADRECKLSNLHKIAKSqeeklnvLQKEKEDKQETIDILRKELS--RTEQIRKELSIKASS 693
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSK-------YEQELYDLKEEYDRVEKELSklQRELAEAEAQARASE 503
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
451-712 |
1.05e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 451 VKDQISDIRISDIMDV---YEMKLSTLASKESRLQDLLEAKALALAQADRLIAQYRCQRTQAET---EARTLAGMLREVE 524
Cdd:PRK02224 192 LKAQIEEKEEKDLHERlngLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETleaEIEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 525 RKNEELSVLLKSQQLESERAQNDIEHLFQhskKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNKHIETMK 604
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLA---EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 605 KLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSRTEQIR 684
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
250 260
....*....|....*....|....*...
gi 568995253 685 KELSIKASSlemhkaqLEGRLEEKESLL 712
Cdd:PRK02224 429 AELEATLRT-------ARERVEEAEALL 449
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
499-670 |
2.04e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 499 IAQYRCQRTQAETEartLAGMLREVERKNEELSVL---LKSQQLESERAQNDIEHLFQHSKKLESVAAEH---------- 565
Cdd:COG3883 25 LSELQAELEAAQAE---LDALQAELEELNEEYNELqaeLEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 566 ----EILT--KSYMELVQRNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRE 639
Cdd:COG3883 102 vsylDVLLgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190
....*....|....*....|....*....|.
gi 568995253 640 CKLSNLHKIAKSQEEKLNVLQKEKEDKQETI 670
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
594-719 |
3.01e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 594 ESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDIL 673
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568995253 674 RKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEEL 719
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
505-704 |
3.29e-06 |
|
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: 50.34 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 505 QRTQAE-TEARTLagmlrEVERKNEELSVLLKSQQLESERAQNDIEHLFQHSKKLesvaAEHEILTKSYMELVQRNEATE 583
Cdd:pfam15709 336 DRLRAErAEMRRL-----EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRR----FEEIRLRKQRLEEERQRQEEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 584 KKNTDLQTTCESLNKHI---ETMKKLNEaLKQQNEKTIAQLIEKEEQR-KEVQSQLADrECKlsnlHKIAKSQEEKLNVL 659
Cdd:pfam15709 407 ERKQRLQLQAAQERARQqqeEFRRKLQE-LQRKKQQEEAERAEAEKQRqKELEMQLAE-EQK----RLMEMAEEERLEYQ 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568995253 660 QKekedKQETIDILRKELSRTEQIRKELSIKASSLEMHKAQLEGR 704
Cdd:pfam15709 481 RQ----KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
467-712 |
3.56e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 467 YEMKLSTLASKESRLQDLLEAKALALAQADRLIAQYRCQRTQAETEARTLAGMLREVERKNEELSVLLKSQQLESERAQN 546
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 547 DIEhlfqhskKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEE 626
Cdd:COG1196 370 AEA-------ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 627 QRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSRTEQIRKELSIKASS-LEMHKAQLEGRL 705
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGL 522
|
....*..
gi 568995253 706 EEKESLL 712
Cdd:COG1196 523 AGAVAVL 529
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
424-716 |
5.05e-06 |
|
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: 50.12 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 424 LTPPPSKDNAPALNIEDLIEKLQAGVMVKDQISDIRISDIMDVYEMKLSTLASKESRLQDLLEAKALALAQADRLIAQYR 503
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEAR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 504 CQRTQAETEA----RTLAGMLREVERKNEELSVLLKSQQLESERAQND---IEHLFQH-----------SKKLESVAAEH 565
Cdd:pfam15921 363 TERDQFSQESgnldDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNsitIDHLRRElddrnmevqrlEALLKAMKSEC 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 566 EILTKSYMELVQ-RNEATEKKNT---DLQTTCESLNKHIE--TMKKLNealKQQNEKTI----AQLIEKEEQRKEVQSQL 635
Cdd:pfam15921 443 QGQMERQMAAIQgKNESLEKVSSltaQLESTKEMLRKVVEelTAKKMT---LESSERTVsdltASLQEKERAIEATNAEI 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 636 ADR----ECKLSNLHKIaKSQEEKLNVLQKEKE-------DKQETIDILRKELSRTEQIRKELSIKASSLEMHKAQLEGR 704
Cdd:pfam15921 520 TKLrsrvDLKLQELQHL-KNEGDHLRNVQTECEalklqmaEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE 598
|
330
....*....|..
gi 568995253 705 LEEKEslLKLQQ 716
Cdd:pfam15921 599 INDRR--LELQE 608
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
534-721 |
5.87e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 534 LKSQQLESERAQNDIEHLfqhSKKLESVAAEHEILTKSYMELVQRNEATEKK----NTDLQTTCESLNKHIETMKKLNEA 609
Cdd:COG3883 18 IQAKQKELSELQAELEAA---QAELDALQAELEELNEEYNELQAELEALQAEidklQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 610 LKQQ--NEKTIAQLIEKEEQrkevqSQLADReckLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSRTEQIRKEL 687
Cdd:COG3883 95 LYRSggSVSYLDVLLGSESF-----SDFLDR---LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 568995253 688 SIKASSLEMHKAQLEG---RLEEKESLLKLQQEELNK 721
Cdd:COG3883 167 EAAKAELEAQQAEQEAllaQLSAEEAAAEAQLAELEA 203
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
496-727 |
6.36e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 496 DRLIAQYRCQRTQAETEARTLAGMLREVERKNEELSVLLKsqqlESERAQNDIEHLFQHSKKLESVAAEHEI----LTKS 571
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLEEkireLEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 572 YMELVQRNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQN--EKTIAQLiekEEQRKEVQSQLADRECKLSNLHKIA 649
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELReiEKRLSRL---EEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568995253 650 KSQEEKLNVLQKEKEDKQETIDILRKeLSRTEQIRKELSIKasSLEMHKAQLEGRLEEKESLlklqQEELNKHSHMIA 727
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTGL--TPEKLEKELEELEKAKEEI----EEEISKITARIG 415
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
499-717 |
6.84e-06 |
|
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: 49.63 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 499 IAQYRCQRTQAETEARTLAGMLREVER-----KNEELSVLLKSQQLESERaqNDIEHLFQHSKK--------LESVAAEH 565
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNeieklKKENQSYKQEIKNLESQI--NDLESKIQNQEKlnqqkdeqIKKLQQEK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 566 EILTKSYMELVQRNE--------------ATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEV 631
Cdd:TIGR04523 422 ELLEKEIERLKETIIknnseikdltnqdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 632 QSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSRTEQIRKELSIKASSLEMHKaQLEGRLEEKESL 711
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNK-EIEELKQTQKSL 580
|
....*.
gi 568995253 712 LKLQQE 717
Cdd:TIGR04523 581 KKKQEE 586
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
524-721 |
1.64e-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: 48.48 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 524 ERKNEELSVLLKSQQLESERAQNDIEHLFQHSKKLESvaaEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNKHIETM 603
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES---QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 604 KKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSRTEQI 683
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
170 180 190
....*....|....*....|....*....|....*...
gi 568995253 684 RKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNK 721
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
589-721 |
2.25e-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: 46.46 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 589 LQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADREcklsnlHKIAKSQEEKLNVL-QKEKEDKQ 667
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE------ARIKKYEEQLGNVRnNKEYEALQ 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568995253 668 ETIDILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNK 721
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
551-721 |
2.42e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 551 LFQHSKKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKE 630
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 631 VQSQLADRECKLSN----LHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLE 706
Cdd:COG4942 95 LRAELEAQKEELAEllraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170
....*....|....*
gi 568995253 707 EKESLLKLQQEELNK 721
Cdd:COG4942 175 ELEALLAELEEERAA 189
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
511-719 |
2.55e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 511 TEARTLAGMLreVERKNEELSVLLKSQQLESERAQNDIEHLFQHSKKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQ 590
Cdd:COG4717 38 TLLAFIRAML--LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 591 TTCESLNK------HIETMKKLNEALKQQNEKtIAQLIEKEEQRKEVQSQLADRECKLSNLH-KIAKSQEEKLNVLQKEK 663
Cdd:COG4717 116 EELEKLEKllqllpLYQELEALEAELAELPER-LEELEERLEELRELEEELEELEAELAELQeELEELLEQLSLATEEEL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568995253 664 EDKQETIDILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEEL 719
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
509-722 |
2.69e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 509 AETEARTLAGMLREVERKNEelsvllkSQQLESERAQNDIEHLfqhSKKLESVAAEHEILTKS-----YMELVQRNEATE 583
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAE-------AAEKKKEEAKKKADAA---KKKAEEKKKADEAKKKAeedkkKADELKKAAAAK 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 584 KKNTDLQTTCES------LNKHIETMKKLNEALKQQNEKTIAQLIEK--EEQRK-EVQSQLADRECKLSNLHKIAKSQEE 654
Cdd:PTZ00121 1418 KKADEAKKKAEEkkkadeAKKKAEEAKKADEAKKKAEEAKKAEEAKKkaEEAKKaDEAKKKAEEAKKADEAKKKAEEAKK 1497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 655 KLNVLQKEKEDKQETiDILRK--ELSRTEQIRK-ELSIKASSL----------EMHKAQLEGRLEEKESLLKLQQEELNK 721
Cdd:PTZ00121 1498 KADEAKKAAEAKKKA-DEAKKaeEAKKADEAKKaEEAKKADEAkkaeekkkadELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
.
gi 568995253 722 H 722
Cdd:PTZ00121 1577 N 1577
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
508-721 |
3.00e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 508 QAETEARTLAGMLREVERKNEELSVLLKSQQLESERAQNDIEHLFQHSKKLESVAAEHEILTKSYMELVQRNEATEKKNT 587
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 588 DLQTTCESLNKHiETMKKLNEALKQQNEKTIAQLIEK----------------EEQRKEVQSQLADRECKlsnlHKIAKS 651
Cdd:PTZ00121 1287 EEKKKADEAKKA-EEKKKADEAKKKAEEAKKADEAKKkaeeakkkadaakkkaEEAKKAAEAAKAEAEAA----ADEAEA 1361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568995253 652 QEEKLNVLQKEKEDKQETIDILRKelsRTEQIRK--ELSIKASSLEMHKAQLEGRLEEKESL--LKLQQEELNK 721
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKK---KAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKAdeAKKKAEEKKK 1432
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
594-721 |
3.14e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 594 ESLNKHIETMKKLN---EALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETI 670
Cdd:COG4372 31 EQLRKALFELDKLQeelEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568995253 671 DILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNK 721
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
521-721 |
4.35e-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: 47.27 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 521 REVERKNEELSVLL---KSQQLESERAQNDIEHLFqhsKKLESVAAEHEILTKSYMELVQ-RNEATEKKNTDLQTTCESL 596
Cdd:pfam02463 180 EETENLAELIIDLEelkLQELKLKEQAKKALEYYQ---LKEKLELEEEYLLYLDYLKLNEeRIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 597 NKHIE-------TMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQET 669
Cdd:pfam02463 257 KQEIEkeeeklaQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568995253 670 IDILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNK 721
Cdd:pfam02463 337 IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
438-675 |
4.37e-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: 46.97 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 438 IEDLIEKLQAGV-MVKDQISDIRisdimdvyemklSTLASKESRLQDLLEAKALALAQADRLIAQYRCQRTQAETEARTL 516
Cdd:TIGR02168 780 AEAEIEELEAQIeQLKEELKALR------------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 517 AGMLREVERKNEELSvllkSQQLESERAQNDIEHLfqhSKKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTTCESL 596
Cdd:TIGR02168 848 EELSEDIESLAAEIE----ELEELIEELESELEAL---LNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 597 NKHIETMKKLNEALKQQNEKTIAQLIEK---------------EEQRKEVQSQLADRECKLSNLHKI-------AKSQEE 654
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERLSEEysltleeaealenkiEDDEEEARRRLKRLENKIKELGPVnlaaieeYEELKE 1000
|
250 260
....*....|....*....|.
gi 568995253 655 KLNVLQKEKEDKQETIDILRK 675
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
500-721 |
5.96e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 500 AQYRCQRTQAETEARTLAGMLREVE--RKNEELSVLLKSQQLESERAQNDIEHLfQHSKKLESVAAEHEIltksyMELVQ 577
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEeaKKADEAKKAEEAKKADEAKKAEEKKKA-DELKKAEELKKAEEK-----KKAEE 1568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 578 RNEATEKKNTDL----------QTTCESLNKHIETMKKLN--EALKQQNEKTIAQLIEKEEQRKEVQSQLADRE------ 639
Cdd:PTZ00121 1569 AKKAEEDKNMALrkaeeakkaeEARIEEVMKLYEEEKKMKaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaeekkk 1648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 640 ------------CKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRK---ELSRTEQIRKELSIKASSLEMHKAQLEGR 704
Cdd:PTZ00121 1649 aeelkkaeeenkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaeEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
250
....*....|....*..
gi 568995253 705 LEEKESLLKLQQEELNK 721
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKK 1745
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
606-737 |
6.78e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 606 LNEALkqqnEKTIAQLIEKEEQRKEVQSQLADREC-----KLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSRT 680
Cdd:COG2433 378 IEEAL----EELIEKELPEEEPEAEREKEHEERELteeeeEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 681 -EQIRKEL--SIKASSLEMHKAQLEGRLEEKESLLKLQQEELNKHSHMIAMIHslSGGKI 737
Cdd:COG2433 454 rSEERREIrkDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH--SGELV 511
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
496-729 |
7.02e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 496 DRLIAQYRCQRTQAETEARTLAgmlREVERKNEELSVLLKsqqLESERAQNDIEHLFQHSKKLESVAAEHEILTKSYMEL 575
Cdd:PRK01156 468 NHIINHYNEKKSRLEEKIREIE---IEVKDIDEKIVDLKK---RKEYLESEEINKSINEYNKIESARADLEDIKIKINEL 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 576 VQR----NEATEKKNT----DLQTTCESLNKHIETMKKLN-EALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSN-L 645
Cdd:PRK01156 542 KDKhdkyEEIKNRYKSlkleDLDSKRTSWLNALAVISLIDiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKsI 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 646 HKI---AKSQEEKLNVLQKEK---EDKQETIDILRKELSRTEQI---RKELSIKASSLEMHKAQLEGRLE-------EKE 709
Cdd:PRK01156 622 REIeneANNLNNKYNEIQENKiliEKLRGKIDNYKKQIAEIDSIipdLKEITSRINDIEDNLKKSRKALDdakanraRLE 701
|
250 260
....*....|....*....|
gi 568995253 710 SLLKLQQEELNKHSHMIAMI 729
Cdd:PRK01156 702 STIEILRTRINELSDRINDI 721
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
530-721 |
8.30e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 530 LSVLLKSQQLESERAQNDIEhlfQHSKKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNKHIETMKKLNEA 609
Cdd:COG4942 11 LALAAAAQADAAAEAEAELE---QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 610 LKQQNEKTIAQLIEKEEQRKEV------------------QSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETID 671
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568995253 672 ILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNK 721
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
505-721 |
1.13e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 505 QRTQAETEARTLAGMLREVERKNEELSVLLKSQQLESERAQNDIEhlfQHSKKLESVAAEHEILTKSYMELVQRNEATEK 584
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE---AAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 585 KNTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEK--EEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKE 662
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568995253 663 KEDKQETiDILRKelsRTEQIRKELSIKASSLEMHKAQLEGRLEEKEsllKLQQEELNK 721
Cdd:PTZ00121 1466 AEEAKKA-DEAKK---KAEEAKKADEAKKKAEEAKKKADEAKKAAEA---KKKADEAKK 1517
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
508-721 |
1.42e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 508 QAETEARTLAGMLREVERKNEELSVLLKS-QQLESERAQNDIEhLFQHSKKLESVAAEHEILTKSYMELVQRNEATEKKN 586
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREElEQLEEELEQARSE-LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 587 TDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQ-----EEKLNVLQK 661
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALseaeaEQALDELLK 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 662 EKEDKQETIDILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNK 721
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
516-687 |
2.47e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 516 LAGMLREVERKNE---ELSVLL-KSQQLESERAQ--NDIEHL-FQHSKKLESVAAEHEILTKSYMELV---QRNEATEKK 585
Cdd:PRK03918 541 IKSLKKELEKLEElkkKLAELEkKLDELEEELAEllKELEELgFESVEELEERLKELEPFYNEYLELKdaeKELEREEKE 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 586 NTDLQTTCESLNKHI--------ETMKKLNEALKQQNEKTIAQLIEK-EEQRKEVQSQLADREcKLSNLHKIAKSQEEKL 656
Cdd:PRK03918 621 LKKLEEELDKAFEELaetekrleELRKELEELEKKYSEEEYEELREEyLELSRELAGLRAELE-ELEKRREEIKKTLEKL 699
|
170 180 190
....*....|....*....|....*....|.
gi 568995253 657 NVLQKEKEDKQETIDILRKELSRTEQIRKEL 687
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALERVEELREKV 730
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
520-685 |
2.63e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 520 LREVERKNEELSVLLKSQQLESERAQNDIEHLFQHSKKLESVAAEHEILTKSYMELVQRNEA---TEKKNTDLQttceSL 596
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgNVRNNKEYE----AL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 597 NKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADREcklSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKE 676
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
170
....*....|....
gi 568995253 677 -----LSRTEQIRK 685
Cdd:COG1579 172 ippelLALYERIRK 185
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
432-718 |
2.67e-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: 44.43 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 432 NAPALNIEDLIEKLQA-GVMVKDQISDIRISDIMDVYEMKLSTLaskESRLQDLLEAKALALAQADRliaQYRCQRTQAE 510
Cdd:pfam10174 154 GARDESIKKLLEMLQSkGLPKKSGEEDWERTRRIAEAEMQLGHL---EVLLDQKEKENIHLREELHR---RNQLQPDPAK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 511 TEA-RTLAGM----LREVERKNEELSVLLksQQLESERAQNDIEHLfQHSKKLEsVAAEHEILTKSYMElvQRNEATEKK 585
Cdd:pfam10174 228 TKAlQTVIEMkdtkISSLERNIRDLEDEV--QMLKTNGLLHTEDRE-EEIKQME-VYKSHSKFMKNKID--QLKQELSKK 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 586 NTD---LQTTCESLN-------KHIETMKK-LN-------------EALKQQNEKTIAQLIEKEEQRKEVQSQLADRECK 641
Cdd:pfam10174 302 ESEllaLQTKLETLTnqnsdckQHIEVLKEsLTakeqraailqtevDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGE 381
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995253 642 LSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEE 718
Cdd:pfam10174 382 IRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQ 458
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
521-687 |
3.10e-04 |
|
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: 44.24 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 521 REVERKNEELSVLLKSQQLESERAQN---DIEHLFQHSKKLESVAAEHEILTKSYMELVQRNEaTEKKNTDLQTTCESLN 597
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDltkKISSLKEKIEKLESEKKEKESKISDLEDELNKDD-FELKKENLEKEIDEKN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 598 KHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKEL 677
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
170
....*....|
gi 568995253 678 srtEQIRKEL 687
Cdd:TIGR04523 648 ---KQIKETI 654
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
470-717 |
3.27e-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: 44.33 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 470 KLSTLASKESRLQDLLEAKALALAQADRliaQYRCQRTQAETEARTLAGMLREVERKNEELSVLLKSQQLESERAQNDIE 549
Cdd:pfam05483 535 QIENLEEKEMNLRDELESVREEFIQKGD---EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 550 HLFQHSKKLESVA-AEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQR 628
Cdd:pfam05483 612 ELHQENKALKKKGsAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQ 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 629 KEVqsqlaDRECKlsnlHKIAksqeEKLNVLQKEKEDKQETIDILRKELSRTEQIRKELSIKASSLEMH----------- 697
Cdd:pfam05483 692 KEI-----DKRCQ----HKIA----EMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIElsnikaellsl 758
|
250 260
....*....|....*....|
gi 568995253 698 KAQLEGRLEEKESLLKLQQE 717
Cdd:pfam05483 759 KKQLEIEKEEKEKLKMEAKE 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
577-721 |
3.79e-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: 43.89 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 577 QRNEATEKKntdLQTTCESLNK----HIETMKKLNEaLKQQNEKTIaQLIEKEEQRKEVQSQLA-----DRECKLSNLHK 647
Cdd:TIGR02168 172 ERRKETERK---LERTRENLDRlediLNELERQLKS-LERQAEKAE-RYKELKAELRELELALLvlrleELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 648 IAKSQEEKLNVLQKEKEDKQETIDILRKELS----RTEQIRKEL---SIKASSLEMHK--------------AQLEGRLE 706
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSeleeEIEELQKELyalANEISRLEQQKqilrerlanlerqlEELEAQLE 326
|
170
....*....|....*
gi 568995253 707 EKESLLKLQQEELNK 721
Cdd:TIGR02168 327 ELESKLDELAEELAE 341
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
496-717 |
4.21e-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: 43.88 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 496 DRLIAQyRCQRTQAETEARTLAGMLREVERKNEELSVLLKSQQLESERAQNDIEHLFQHSKKLESVAAEHEILTKSYMEL 575
Cdd:TIGR00606 805 ERKIAQ-QAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRR 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 576 VQRNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEK 655
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995253 656 L-NVLQKEKEDKQETIDILRKELS----RTEQIRKELSIKASSLEMHKAQlEGRLEEKESLLKLQQE 717
Cdd:TIGR00606 964 IqDGKDDYLKQKETELNTVNAQLEecekHQEKINEDMRLMRQDIDTQKIQ-ERWLQDNLTLRKRENE 1029
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
459-734 |
4.38e-04 |
|
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: 43.59 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 459 RISDIMDVYEMKLSTLASKESRLQDLLEAKALALAQADRLIA---------QYRCQRTQAETEAR-TLAGMLREVerKNE 528
Cdd:pfam07111 152 QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAeaqkeaellRKQLSKTQEELEAQvTLVESLRKY--VGE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 529 ELSVLLKSQQLESERAQ--NDIEHLFQHSKKLESVAAEHEILTKS--YMELVQRNEATEKkntdLQTTcESLNKhiETMK 604
Cdd:pfam07111 230 QVPPEVHSQTWELERQEllDTMQHLQEDRADLQATVELLQVRVQSltHMLALQEEELTRK----IQPS-DSLEP--EFPK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 605 KLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDI-------LRKEL 677
Cdd:pfam07111 303 KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVermsakgLQMEL 382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568995253 678 SRTEQIRK-----------ELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNKHSHMIAMIHSLSG 734
Cdd:pfam07111 383 SRAQEARRrqqqqtasaeeQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKG 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
594-721 |
4.73e-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: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 594 ESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDIL 673
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568995253 674 RKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNK 721
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
516-741 |
6.12e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 43.13 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 516 LAGMLREVERKNEEL--SVLLKSQQLESERAQND--IEHLFQHSKKLESVAAEHEILTKSYM-----------ELVQRNE 580
Cdd:pfam15070 202 LAKKLGQLQEELGELkeTLELKSQEAQSLQEQRDqyLAHLQQYVAAYQQLASEKEELHKQYLlqtqlmdrlqhEEVQGKV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 581 ATEKKNTDLQTTCESLnkhietmkklnEALKQQNEKTIAQLIE--KEEQRKEVQSQLADRECKLSNLhkiakSQEEKLnv 658
Cdd:pfam15070 282 AAEMARQELQETQERL-----------EALTQQNQQLQAQLSLlaNPGEGDGLESEEEEEEAPRPSL-----SIPEDF-- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 659 lqkekEDKQETIDILRKELSRTEQIRkelsikasslemhkAQLEGRLEEKESL---LKLQQEELNKHSHMIAMIHSLSGG 735
Cdd:pfam15070 344 -----ESREAMVAFFNSALAQAEEER--------------AELRRQLKEQKRRcrrLAQQAAPAQEEPEHEAHAPGTGGD 404
|
....*.
gi 568995253 736 KISPET 741
Cdd:pfam15070 405 SVPVEV 410
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
519-723 |
6.32e-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: 43.17 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 519 MLREVERKNEELSVLlkSQQLESERAQNdIEHLFQHSKKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNK 598
Cdd:pfam05483 532 MLKQIENLEEKEMNL--RDELESVREEF-IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 599 HIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLsnlhkiaksqEEKLNVLQKEKEDKQETIDILRKELS 678
Cdd:pfam05483 609 NIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKF----------EEIIDNYQKEIEDKKISEEKLLEEVE 678
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 679 RTE-------QIRKELSIKASS--------LEMHKAQLEGRLEEKESLLKLQQEELNKHS 723
Cdd:pfam05483 679 KAKaiadeavKLQKEIDKRCQHkiaemvalMEKHKHQYDKIIEERDSELGLYKNKEQEQS 738
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
499-711 |
6.70e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 499 IAQYRCQRTQAETEARTLAGMLREVERKNEELSVLLKSQ-QLES--ERAQNDIEHLFQHSKKLESVAAEHEILTKSYMEL 575
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdRIERleERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 576 -----VQRNEATEK----------------KNTDLQTTCESLNKhIETMKKLNEALKQQ----NEKTiAQLIEKEEQRKE 630
Cdd:PRK02224 550 eaeaeEKREAAAEAeeeaeeareevaelnsKLAELKERIESLER-IRTLLAAIADAEDEierlREKR-EALAELNDERRE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 631 VQSQLADRECKLSNLH---KIAKSQ-------------EEKLNVLQKEKEDKQETIDILRKELSRTEQIRKELsikaSSL 694
Cdd:PRK02224 628 RLAEKRERKRELEAEFdeaRIEEARedkeraeeyleqvEEKLDELREERDDLQAEIGAVENELEELEELRERR----EAL 703
|
250
....*....|....*..
gi 568995253 695 EMHKAQLEGRLEEKESL 711
Cdd:PRK02224 704 ENRVEALEALYDEAEEL 720
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
623-721 |
6.71e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.90 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 623 EKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDkqetidiLRKELSRTEQIRKELSIKASSLEMHKAQLE 702
Cdd:pfam20492 10 ELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAER-------LEQKRQEAEEEKERLEESAEMEAEEKEQLE 82
|
90
....*....|....*....
gi 568995253 703 GRLEEKESLLKLQQEELNK 721
Cdd:pfam20492 83 AELAEAQEEIARLEEEVER 101
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
575-721 |
7.59e-04 |
|
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: 43.09 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 575 LVQRNEATEKKNTDLQTTCESLNKHIETMKKLNE---ALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKS 651
Cdd:TIGR04523 91 LKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVelnKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 652 QEEKLNVLQKEKEDKQETIDILRKELSRTE----------QIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNK 721
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLElllsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
520-721 |
8.71e-04 |
|
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: 42.70 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 520 LREVERKNEELSVL------LKSQQLESERAQNDIEHlfQHSKKLESVA-AEHEILTKSYM-----ELVQRNEATEKKNT 587
Cdd:TIGR04523 144 LTEIKKKEKELEKLnnkyndLKKQKEELENELNLLEK--EKLNIQKNIDkIKNKLLKLELLlsnlkKKIQKNKSLESQIS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 588 DLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADREC-------KLSNLHKIAKSQEEKLNVLQ 660
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKeleqnnkKIKELEKQLNQLKSEISDLN 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568995253 661 KEKE------------DKQETIDILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNK 721
Cdd:TIGR04523 302 NQKEqdwnkelkselkNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
521-729 |
9.42e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 521 REVERKNEELSVL-LKSQQLESERAQNDIEHLFQHSKKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNkh 599
Cdd:COG4372 6 EKVGKARLSLFGLrPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 600 iETMKKLNEALKQQnEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSR 679
Cdd:COG4372 84 -ELNEQLQAAQAEL-AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568995253 680 TEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNKHSHMIAMI 729
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIES 211
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
525-709 |
9.72e-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: 42.85 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 525 RKNEELSVLLKSQQLESERAQNDIEHLFQ-HSKKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNKHIETM 603
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQkHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 604 KKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKE----KEDKQETIDILRKElsr 679
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDvsslESQLQDTQELLQEE--- 480
|
170 180 190
....*....|....*....|....*....|
gi 568995253 680 TEQiRKELSIKASSLEMHKAQLEGRLEEKE 709
Cdd:pfam01576 481 TRQ-KLNLSTRLRQLEDERNSLQEQLEEEE 509
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
519-717 |
1.13e-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: 42.65 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 519 MLREVERKNEELSVLLKSQQLESERAQndiehLFQHSKKLEsvaAEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNK 598
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALM-----EFAKKKSLH---GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 599 HIETMKKlneaLKQQNEKTIAQLIEKEEQRKEVQSQLadrecklsnlhKIAKSQEEKLNVLQKEKEDKQETIDILRK--- 675
Cdd:TIGR00618 230 HLREALQ----QTQQSHAYLTQKREAQEEQLKKQQLL-----------KQLRARIEELRAQEAVLEETQERINRARKaap 294
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568995253 676 ---ELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQE 717
Cdd:TIGR00618 295 laaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS 339
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
511-717 |
1.20e-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: 42.47 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 511 TEARTLAGMLREVERKNEELSVLLKSQQL---ESERAQNDIEhlfqhsKKLESVAAEHEILTKSYmelvqrnEATEKKNT 587
Cdd:pfam01576 391 AELRTLQQAKQDSEHKRKKLEGQLQELQArlsESERQRAELA------EKLSKLQSELESVSSLL-------NEAEGKNI 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 588 DLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQ 667
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA 537
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568995253 668 ETIDILrkelsrtEQIRKELsikASSLEMHKAQLEGRLEEKESLLK----LQQE 717
Cdd:pfam01576 538 GTLEAL-------EEGKKRL---QRELEALTQQLEEKAAAYDKLEKtknrLQQE 581
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
590-722 |
1.24e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.35 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 590 QTTCESLNKHIETMK----KLNEALK---QQNEKTIAQLIEKEEQRKEVQSQLADR-------ECKLSNLHKIAKSQEEK 655
Cdd:pfam05911 680 TEENKRLKEEFEQLKsekeNLEVELAsctENLESTKSQLQESEQLIAELRSELASLkesnslaETQLKCMAESYEDLETR 759
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568995253 656 LNVLQKEKEDKQETIDILRKELSRTEQIRKELSIKASSLEMhkaQLEgRLEEKESLLKLQQEELNKH 722
Cdd:pfam05911 760 LTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQE---QLE-RNEKKESSNCDADQEDKKL 822
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
526-687 |
1.27e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 41.91 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 526 KNEELSVLLKSQQLESERAQndIEHL-FQHSKKLESVAaEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNKHIETMK 604
Cdd:pfam03999 132 LPLLIDPLPSLEELESFRKH--LENLrNEKERRLEEVN-ELKKQIKLLMEELDLVPGTDFEEDLLCESEDNFCLSRENID 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 605 KLNEALKQQNEktiaQLIEKEEQRKEVQSQLAdrecKLSNLHKIakSQEEKLNVLQKEKEDKQETIDILRKELSRTEQIR 684
Cdd:pfam03999 209 KLRKLIKQLEE----QKAEREEKIDDLREKIL----ELWNRLQV--PQEEQESFVRENNSLSQDTIDALREELQRLEELK 278
|
...
gi 568995253 685 KEL 687
Cdd:pfam03999 279 KKN 281
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
531-726 |
1.34e-03 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 42.03 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 531 SVLLKSQQLESERAQNDIeHLFQHSKKLESVAAEHEiltKSYMELVQRNEATEKKNTDLQTTcESLNKHIETMKKLNEal 610
Cdd:COG5059 351 EIEEIKFDLSEDRSEIEI-LVFREQSQLSQSSLSGI---FAYMQSLKKETETLKSRIDLIMK-SIISGTFERKKLLKE-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 611 KQQNEKTIAQLIE----------KEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEK--EDKQETIDILRKELS 678
Cdd:COG5059 424 EGWKYKSTLQFLRieidrllllrEEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSDRVESEKasKLRSSASTKLNLRSS 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568995253 679 RTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNKHSHMI 726
Cdd:COG5059 504 RSHSKFRDHLNGSNSSTKELSLNQVDLAGSERKVSQSVGELLRETQSL 551
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
498-697 |
1.38e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 498 LIAQYRCQRTQAETEARTLAGMLREVERKNEELsvlLKSQQLESERAQNdiehlfqhsKKLESVAAEHEILTKSYMELVQ 577
Cdd:PRK12705 21 LVVLLKKRQRLAKEAERILQEAQKEAEEKLEAA---LLEAKELLLRERN---------QQRQEARREREELQREEERLVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 578 RNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLadrecklsnlhkIAKSQEEKLN 657
Cdd:PRK12705 89 KEEQLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKL------------LLKLLDAELE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568995253 658 vlqkekEDKQETIDILRKElSRTEQIRKELSIKASSLEMH 697
Cdd:PRK12705 157 ------EEKAQRVKKIEEE-ADLEAERKAQNILAQAMQRI 189
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
505-719 |
1.74e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 505 QRTQAETEARTLAGMLREVERKNEELSVLLKS-------QQLESERAQNDIEHLFQHSKKLESVAAEHEILTKSYMELVQ 577
Cdd:pfam07888 165 QRKEEEAERKQLQAKLQQTEEELRSLSKEFQElrnslaqRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 578 RNEATEKKNTDLQTTCESL-NKHIETMKKLNEALKQQNEKTIaQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKL 656
Cdd:pfam07888 245 RLNASERKVEGLGEELSSMaAQRDRTQAELHQARLQAAQLTL-QLADASLALREGRARWAQERETLQQSAEADKDRIEKL 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568995253 657 N--VLQKEKEDKQETID--ILRKELSRTEQI-RKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEEL 719
Cdd:pfam07888 324 SaeLQRLEERLQEERMEreKLEVELGREKDCnRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELL 391
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
527-687 |
1.76e-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: 40.68 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 527 NEELSVLLKSQQLESERAQndIEHLF-QHSKKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNKHIETMK- 604
Cdd:COG1579 3 PEDLRALLDLQELDSELDR--LEHRLkELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 605 KLN--------EALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDilrKE 676
Cdd:COG1579 81 QLGnvrnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE---AE 157
|
170
....*....|.
gi 568995253 677 LSRTEQIRKEL 687
Cdd:COG1579 158 LEELEAEREEL 168
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
496-682 |
1.83e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 496 DRLIAQYRCQRTQAETEARTLAGMLREVERKNEELSvlLKSQQLESERAQNDIEHLFQHSKKLESVAAEHEILTKSYMEL 575
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEALLKEAEKLKEELE--EKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 576 vQRNEATEKKNTDLQTTCESLNKHIETM-KKLNEALKQQNEKTIAQ--LIEKEEQRKEVQSQLADRE-----------CK 641
Cdd:PRK00409 597 -QKGGYASVKAHELIEARKRLNKANEKKeKKKKKQKEKQEELKVGDevKYLSLGQKGEVLSIPDDKEaivqagimkmkVP 675
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568995253 642 LSNLHKIAKSQEEKLNVLQKEKEDKQE---TIDI--LRKE--LSRTEQ 682
Cdd:PRK00409 676 LSDLEKIQKPKKKKKKKPKTVKPKPRTvslELDLrgMRYEeaLERLDK 723
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
499-698 |
2.16e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 499 IAQYRCQRTQAETEARTLAGmlrEVERKNEELSVLLKSQQLESERAQNDIEHLFQHSKKLESVAAEHEILTK-------- 570
Cdd:PHA02562 215 IARKQNKYDELVEEAKTIKA---EIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptct 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 571 -SYMELVQRNEATEKKNTDLQTTCESLNKHIETM-KKLNEALKQQNEKTiaqliekeeqrkEVQSQLADRECKLSNLHKI 648
Cdd:PHA02562 292 qQISEGPDRITKIKDKLKELQHSLEKLDTAIDELeEIMDEFNEQSKKLL------------ELKNKISTNKQSLITLVDK 359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568995253 649 AKSQEEKLNVLQKEKEDKQETIDILRKELsrteqirKELSIKASSLEMHK 698
Cdd:PHA02562 360 AKKVKAAIEELQAEFVDNAEELAKLQDEL-------DKIVKTKSELVKEK 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
588-713 |
2.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 588 DLQTTCESLNKHIETMKKLNEALkqqnEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQ 667
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERL----EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568995253 668 ET---IDILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLK 713
Cdd:PRK03918 235 ELkeeIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK 283
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
497-721 |
2.21e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 497 RLIAQYRCQRTQAETEARTLAGMLREVERKNEEL-SVLLKSQQLESERAQndIEHLFQHSKKLESVAAEHeiLTKSYMEL 575
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELeKVLKKESELIKLKEL--AEQLKELEEKLKKYNLEE--LEKKAEEY 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 576 vqrnEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKtiaqLIEKEEQRKEVQSQLADR--------ECKLSNLHK 647
Cdd:PRK03918 528 ----EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK----LDELEEELAELLKELEELgfesveelEERLKELEP 599
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568995253 648 IAKSQEEKLNVlQKEKEDKQETIDILRKELsrtEQIRKELsikasslemhkAQLEGRLEEKESLLklqqEELNK 721
Cdd:PRK03918 600 FYNEYLELKDA-EKELEREEKELKKLEEEL---DKAFEEL-----------AETEKRLEELRKEL----EELEK 654
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
597-718 |
2.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 597 NKHIETMKKlnEALKQQNEktiaqliEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKE 676
Cdd:PRK12704 48 KKEAEAIKK--EALLEAKE-------EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKE 118
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568995253 677 LSRTEQirkELSIKASSLEMHKAQLEGRLEEkesLLKLQQEE 718
Cdd:PRK12704 119 LEQKQQ---ELEKKEEELEELIEEQLQELER---ISGLTAEE 154
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
461-717 |
3.00e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 461 SDIMDVYEMKLSTLASKESRLQDLLEAKALALAQADRLIAQYRCQRTQAET-----------------EARTLAGMLREV 523
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEleeerddllaeaglddaDAEAVEARREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 524 ERKNEELSVLLKSQQLESERAQNDIEHLFQHSKKLESVAAEheiltksymelvQRNEATEkkntdLQTTCESLNKHIETM 603
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE------------LREEAAE-----LESELEEAREAVEDR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 604 KKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILR--------- 674
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpve 462
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568995253 675 -----KELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQE 717
Cdd:PRK02224 463 gsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDR 510
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
496-722 |
3.20e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 496 DRLIAQYRCQRTQAETEARTLAGMLREVERKNEELSVLL------KSQQLESER--AQNDIEHLFQHSKKLESVA----- 562
Cdd:COG3096 849 ERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLAdetladRLEELREELdaAQEAQAFIQQHGKALAQLEplvav 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 563 -----AEHEILTKSYMELVQRNEATEKKN---TDL---------QTTCESLNKHIEtmkkLNEALKQQNEKTIAQLIEKE 625
Cdd:COG3096 929 lqsdpEQFEQLQADYLQAKEQQRRLKQQIfalSEVvqrrphfsyEDAVGLLGENSD----LNEKLRARLEQAEEARREAR 1004
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 626 EQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKED------------KQETIDILRKELSRTEQIRKELSIKASS 693
Cdd:COG3096 1005 EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqadaeaeerARIRRDELHEELSQNRSRRSQLEKQLTR 1084
|
250 260
....*....|....*....|....*....
gi 568995253 694 LEMHKAQLEGRLEEKESLLKLQQEELNKH 722
Cdd:COG3096 1085 CEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
542-675 |
3.45e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 542 ERAQNDIEHLfQHSKKLESVAAEHEILTKSYMELVQRNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQL 621
Cdd:PRK12704 45 EEAKKEAEAI-KKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQ 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568995253 622 IEKEEQRKEVQSQLADRECKLSNlhkIAK-SQEE-KLNVLQK-EKEDKQETIDILRK 675
Cdd:PRK12704 124 QELEKKEEELEELIEEQLQELER---ISGlTAEEaKEILLEKvEEEARHEAAVLIKE 177
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
528-707 |
3.48e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 528 EELSVLLKSQQLESERAQNDIEHLFQHSKKLESVAAEHEILTKSYMELVQRNEATE----KKNTDLQTTCESLNKHIETM 603
Cdd:pfam05483 474 EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEermlKQIENLEEKEMNLRDELESV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 604 KklnEALKQQNEKTIAQLIEKEEQRKEVQSQLADREcklsnlhKIAKSQEEKLNVLQKEKEDKQETIDILRKE----LSR 679
Cdd:pfam05483 554 R---EEFIQKGDEVKCKLDKSEENARSIEYEVLKKE-------KQMKILENKCNNLKKQIENKNKNIEELHQEnkalKKK 623
|
170 180 190
....*....|....*....|....*....|.
gi 568995253 680 TEQIRKELS---IKASSLEMHKAQLEGRLEE 707
Cdd:pfam05483 624 GSAENKQLNayeIKVNKLELELASAKQKFEE 654
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
501-687 |
3.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 501 QYRCQRTQAEtEARTLAGMLR--EVERKNEELSVLLKSQQLESERAQNDIEhlfQHSKKLESVAAEHEILTKSYMEL-VQ 577
Cdd:COG4913 263 RYAAARERLA-ELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELE---RLEARLDALREELDELEAQIRGNgGD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 578 RNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLiekEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLN 657
Cdd:COG4913 339 RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF---AALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
170 180 190
....*....|....*....|....*....|....
gi 568995253 658 VLQKEKEDKQETIDILRKELS----RTEQIRKEL 687
Cdd:COG4913 416 DLRRELRELEAEIASLERRKSnipaRLLALRDAL 449
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
632-722 |
3.91e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 632 QSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSRTEQirkelsikasslEMhkAQLEGRLEEKESL 711
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA------------EI--DKLQAEIAEAEAE 80
|
90
....*....|.
gi 568995253 712 LKLQQEELNKH 722
Cdd:COG3883 81 IEERREELGER 91
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
608-712 |
5.82e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 608 EALKQQNEKTIAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKE-----------DK--------QE 668
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaeleaelerlDAssddlaalEE 692
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568995253 669 TIDILRKELSRTEQIRKELSIKASSLEMHKAQLEGRLEEKESLL 712
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
528-736 |
6.49e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 528 EELSVLLKSQQLES----ERAQNDIEHLFQHSKKlesvaaehEILTKSYMELVQRNEATEKKNTdLQTTCESLNKHIETM 603
Cdd:pfam05483 200 EELRVQAENARLEMhfklKEDHEKIQHLEEEYKK--------EINDKEKQVSLLLIQITEKENK-MKDLTFLLEESRDKA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 604 KKLNEALKQQNEkTIAQLIEKEEQrkeVQSQLADRECKLSNLHKIAKSQEEKLNVLQKE----KEDKQETIDILRKELSR 679
Cdd:pfam05483 271 NQLEEKTKLQDE-NLKELIEKKDH---LTKELEDIKMSLQRSMSTQKALEEDLQIATKTicqlTEEKEAQMEELNKAKAA 346
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568995253 680 TEQIRKELSIKASSLEMHKAQLEGRLEEKESLLKLQQEELNKHSHMIAMIHSLSGGK 736
Cdd:pfam05483 347 HSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK 403
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
560-729 |
7.88e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 560 SVAAEHEILTKSYM-ELVQRNEATEKKNTDLQTTCESLNKHIETMKKLNEALKQQNEKTIAQLIEKEEQRKEVQSQLADR 638
Cdd:PHA02562 163 SVLSEMDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 639 eckLSNLHKIAKSQEEKLNVLQKEKEDKQETIDILRKELSR----------TEQIRKELSiKASSLEMHKAQLEGRLEek 708
Cdd:PHA02562 243 ---LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMyekggvcptcTQQISEGPD-RITKIKDKLKELQHSLE-- 316
|
170 180
....*....|....*....|.
gi 568995253 709 esLLKLQQEELNKHSHMIAMI 729
Cdd:PHA02562 317 --KLDTAIDELEEIMDEFNEQ 335
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
505-683 |
7.90e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.49 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 505 QRTQAETEArTLAGM--LREVERKNEELSVLLKSQqLESERAQNDIEHLFQHSKKLEsvAAEHEI-LTKSYMELVQRNEA 581
Cdd:pfam07888 226 HRKEAENEA-LLEELrsLQERLNASERKVEGLGEE-LSSMAAQRDRTQAELHQARLQ--AAQLTLqLADASLALREGRAR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 582 TEKKNTDLQTTCESLNKHIEtmkKLNEALkQQNEKTiaqLIEKEEQRKEVQSQLA-DRECKLSNLHKIAKSQEE---KLN 657
Cdd:pfam07888 302 WAQERETLQQSAEADKDRIE---KLSAEL-QRLEER---LQEERMEREKLEVELGrEKDCNRVQLSESRRELQElkaSLR 374
|
170 180 190
....*....|....*....|....*....|
gi 568995253 658 VLQKEKE----DKQETIDILRKELSRTEQI 683
Cdd:pfam07888 375 VAQKEKEqlqaEKQELLEYIRQLEQRLETV 404
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
499-709 |
8.56e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 499 IAQYRCQRTQAETEARTLAGMLREVERKNEELSVllKSQQLESErAQNDIEHLFQHSKKLESVAAEHEILTK-------- 570
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELRE--EAAELESE-LEEAREAVEDRREEIEELEEEIEELRErfgdapvd 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 571 -----SYMELVQ--RNEATEKKnTDLQTTCESLNKHIETMKKLNEALK---------------------QQNEKTIAQLI 622
Cdd:PRK02224 407 lgnaeDFLEELReeRDELRERE-AELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvetieedrERVEELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 623 EKEEQRKEVQSQLaDRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDilrkelsrteqirkELSIKASSLEMHKAQLE 702
Cdd:PRK02224 486 DLEEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIE--------------EKRERAEELRERAAELE 550
|
....*..
gi 568995253 703 GRLEEKE 709
Cdd:PRK02224 551 AEAEEKR 557
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
618-721 |
9.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995253 618 IAQLIEKEEQRKEVQSQLADRECKLSNLHKIAKSQEEKLNVLQKEKEDKQETIDI--LRKELSRTEQIRKELsiKASSLE 695
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERL--DASSDD 686
|
90 100
....*....|....*....|....*.
gi 568995253 696 MhkAQLEGRLEEKESLLKLQQEELNK 721
Cdd:COG4913 687 L--AALEEQLEELEAELEELEEELDE 710
|
|
| |
