|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
10-482 |
1.21e-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: 57.82 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 10 FSISGSEGKRLWHRTKWKSLSFPSLETQIAKWNLQVkmnkqeavaikeasrQKAVALKKASKVYRQrlrhftGDIERLAS 89
Cdd:pfam15921 393 LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV---------------QRLEALLKAMKSECQ------GQMERQMA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 90 QVRDQEAKLSETVSASSDWKSQFE---KIAIEKTELEVQIETMKKQIANLLEDLRKMETHGKNSCEEILR-------KLH 159
Cdd:pfam15921 452 AIQGKNESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrvdlKLQ 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 160 SLED-ENEALNIENVKLKgtLDALKDEVASvENELVEL--QEVEKRQKTLVEGYRT----QVQKLQEAAEMVKSRCKnlL 232
Cdd:pfam15921 532 ELQHlKNEGDHLRNVQTE--CEALKLQMAE-KDKVIEIlrQQIENMTQLVGQHGRTagamQVEKAQLEKEINDRRLE--L 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 233 HENNLIITNKNKKLEKTVSCTSPLLLG-----NAVKAQVKATKGRNRMRGQVesnLKQVEQARSSFTSaeqrLQECQEKL 307
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDLELEkvklvNAGSERLRAVKDIKQERDQL---LNEVKTSRNELNS----LSEDYEVL 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 308 QR-CKEKCAEQALTIRELQGQVDGNQSLL-----TKLSLE-EENHLIQLKC---ENLKEKLEQMDAenkeLEKKLADQEE 377
Cdd:pfam15921 680 KRnFRNKSEEMETTTNKLKMQLKSAQSELeqtrnTLKSMEgSDGHAMKVAMgmqKQITAKRGQIDA----LQSKIQFLEE 755
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 378 CLKHSDLELKEKAAEYTALSRQLEAALEEgRQKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQLVDKMNTKTQhQ 457
Cdd:pfam15921 756 AMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ-E 833
|
490 500 510
....*....|....*....|....*....|.
gi 568923227 458 AICLKeIQHSLEKSE------TRNESIKNYL 482
Cdd:pfam15921 834 SVRLK-LQHTLDVKElqgpgyTSNSSMKPRL 863
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
285-474 |
7.48e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 285 QVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLSLEEEnhliqlkcENLKEKLEQMDAE 364
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL--------EQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 365 NKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERALQikilDLEAELRKKNEEQN 444
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR----DLRRELRELEAEIA 429
|
170 180 190
....*....|....*....|....*....|
gi 568923227 445 QLVDKMNTKTQHQAICLKEIQHSLEKSETR 474
Cdd:COG4913 430 SLERRKSNIPARLLALRDALAEALGLDEAE 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-409 |
1.13e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 61 QKAVALKKASKVYRQRL-----RHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIAN 135
Cdd:COG1196 213 ERYRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 136 LLEDLRKMEthgkNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEvekRQKTLVEGYRTQVQ 215
Cdd:COG1196 293 LLAELARLE----QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE---ELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 216 KLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKTvsctspLLLGNAVKAQVKATKGRNRMRGQVESNLKQVEQARSSFTS 295
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELA------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 296 AEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLSLEEENHLIQLK-CENLKEKLEQMDAENKELEKKLAD 374
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLlLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350
....*....|....*....|....*....|....*
gi 568923227 375 QEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQ 409
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
34-425 |
7.83e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 34 LETQIAKWNLQVKMNKQEAVAikEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFE 113
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKI--AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 114 KIAIEKTELEVQIETMKKQIANLLEDLrkmethgknscEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENEL 193
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEEL-----------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 194 VELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKTVSctspllLGNAVKAQVKATKGRN 273
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA------LLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 274 RMRGQVESNLKQVEQARSsftSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLSLEEENhliqlkceN 353
Cdd:TIGR02168 894 SELEELSEELRELESKRS---ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN--------K 962
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568923227 354 LKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEaALEEGRQKVSEEVEKMSSRERAL 425
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKE-DLTEAKETLEEAIEEIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
284-483 |
8.98e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 284 KQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLSLEEENhliqlkcenLKEKLEQMDA 363
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE---------LEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 364 ENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERALQiKILDLEAELRKKNEEQ 443
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA-QLEELEEAEEALLERL 416
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568923227 444 NQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIKNYLQ 483
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
82-446 |
9.01e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 82 GDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKMETHGKNSCEEI------- 154
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeleekv 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 155 --LRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEKR---QKTLVEGYRTQVQKLQEAAEMVKSRCK 229
Cdd:PRK03918 283 keLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 230 nlLHENNLIITNKNKKLEKTVSCTSPLLLGNAVKAQVKATKgrnrmrgQVESNLKQVEQARSSFTSAEQRLQECQEKLQR 309
Cdd:PRK03918 363 --LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKE-------EIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 310 CKEKCaeqALTIRELQGQVDGNqsLLTKLSLEEENhlIQLKCENLKEKLEQMDAENKELEKKLADQEECLKhsdleLKEK 389
Cdd:PRK03918 434 AKGKC---PVCGRELTEEHRKE--LLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKEL 501
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 568923227 390 AAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQL 446
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
121-438 |
1.45e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 121 ELEVQIETMKKQIANLLEDLRKMETH---GKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQ 197
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRldeLSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 198 EVEKRQKTLVEGYRTQVQKLQEAAEMVKSRcknLLHENNLIITNKNKKLEKTVSctsplllgnavkaqvkatkgrnRMRG 277
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVS----------------------RIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 278 QVESNLKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKL-----SLEEENHLIQLKCE 352
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaalrDLESRLGDLKKERD 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 353 NLKEKLEQMDAENKELEKKLadqeECLKHSDLELKEKAAeytALSRQLEAALEEGRQKVSEEVEKMSsrERALQIKILDL 432
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQI----EKKRKRLSELKAKLE---ALEEELSEIEDPKGEDEEIPEEELS--LEDVQAELQRV 963
|
....*.
gi 568923227 433 EAELRK 438
Cdd:TIGR02169 964 EEEIRA 969
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
152-449 |
2.31e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 152 EEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKsrcKNL 231
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE---RQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 232 LHENNLIITNKNKKLEKtvsctsplllgNAVKAQVKATKgrNRMRGQVESNLKQVEQARSSFTSAEQRLQECQEKLQRCK 311
Cdd:TIGR02168 319 EELEAQLEELESKLDEL-----------AEELAELEEKL--EELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 312 EKCAEQALTIRELQGQVDGNQSLLTKLSLEEENhliqLKCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAA 391
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEE 461
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568923227 392 EYTALSRQLEAALEEgRQKVSEEVEKMSSRERALQikilDLEAELRKKNEEQNQLVDK 449
Cdd:TIGR02168 462 ALEELREELEEAEQA-LDAAERELAQLQARLDSLE----RLQENLEGFSEGVKALLKN 514
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
256-459 |
4.04e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 256 LLLGNAVKAQVKATKGRNRMRGQVESNLKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLL 335
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 336 TKLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKhsdlELKEKAAEYTALSRQLEAALEEGRQKVSEEV 415
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA----ELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568923227 416 EKMSSRERALQIKILDLEAELRKKNEEQNQLVDKMNTKTQHQAI 459
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
273-486 |
1.01e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 273 NRMRGQVESNLKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKL------------SL 340
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkqilrerlaNL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 341 EEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQ---LEAALEEGRQKVSE---E 414
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQlelQ 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568923227 415 VEKMSSRERALQIKILDLEAELRKKNEEQNQLVDKM-NTKTQHQAICLKEIQHSLEKSETRNESIKNYLQFLQ 486
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
296-483 |
3.04e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 296 AEQRLQECQEKLQRCK-------------EKCAEQALTIRELQGQ---VDGNQSLLTKLSLEEENHLIQLKCENLKEKLE 359
Cdd:COG1196 177 AERKLEATEENLERLEdilgelerqleplERQAEKAERYRELKEElkeLEAELLLLKLRELEAELEELEAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 360 QMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLE------AALEEGRQKVSEEVEKMSSRERALQIKILDLE 433
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELArleqdiARLEERRRELEERLEELEEELAELEEELEELE 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568923227 434 AELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIKNYLQ 483
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-479 |
3.38e-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: 46.59 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 268 ATKGRNRMRGQVESNLKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVdgnqslltkLSLEEENHLI 347
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL---------TELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 348 QLKCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLeaaleegrQKVSEEVEKMSSRERALQI 427
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA--------ANLRERLESLERRIAATER 838
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568923227 428 KILDLEAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIK 479
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
296-441 |
5.36e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 296 AEQRLQECQEKLQRCKEKCA----EQALTIR-ELQGQVDGNQSLLTKLsleeENHLIQlKCENLKEKLEQMDAENKELEK 370
Cdd:PRK12704 40 AKRILEEAKKEAEAIKKEALleakEEIHKLRnEFEKELRERRNELQKL----EKRLLQ-KEENLDRKLELLEKREEELEK 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568923227 371 KladqEECLKHSDLELKEKAAEYTALSRQLEAALE--------EGRQKVSEEVEKMSSRERALQIKILDLEAELRKKNE 441
Cdd:PRK12704 115 K----EKELEQKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKK 189
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
295-443 |
7.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 295 SAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSL------LTKLSLEEENHL-IQLKCENLKEKLEQMDAEN-- 365
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrLAEYSWDEIDVAsAEREIAELEAELERLDASSdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 366 -KELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEgRQKVSEEVEKMSSRERALQIKILD--LEAELRKKNEE 442
Cdd:COG4913 687 lAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE-LDELQDRLEAAEDLARLELRALLEerFAAALGDAVER 765
|
.
gi 568923227 443 Q 443
Cdd:COG4913 766 E 766
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
274-486 |
9.95e-05 |
|
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: 45.06 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 274 RMRGQVESNLKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLsleeenhliQLKCEN 353
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL---------EEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 354 LKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYtalsrqleaaLEEGRQKVSEEVEKMSSRERALQIKILDLE 433
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL----------SHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568923227 434 AELRKKNEEQNQLVDKMNTKTQHQAIC---LKEIQHSLEKSETRNESIKNYLQFLQ 486
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEELE 874
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
273-450 |
2.29e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 273 NRMRGQVESNLKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLSLEEENhlIQLKCE 352
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE--LKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 353 NLKEKLEQMDAENKELEKKLADQE---ECLKHSDLELKEKAAEYTALSRQLEAALEEGRQkvseEVEKMSSRERALQIKI 429
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYReklEKLKREINELKRELDRLQEELQRLSEELADLNA----AIAGIEAKINELEEEK 443
|
170 180
....*....|....*....|.
gi 568923227 430 LDLEAELRKKNEEQNQLVDKM 450
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADL 464
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
85-475 |
2.56e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 85 ERLASQVRDQEAKLSETVSASSDWKSQFEKIaieKTELEVQIETMKKQIANLLEDLRKMETHGKNSCEEILRKLHSLEDE 164
Cdd:pfam15921 267 DRIEQLISEHEVEITGLTEKASSARSQANSI---QSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 165 NEAL-------NIENVKLKGTLDALKDEVASVENELVEL-QEVEKRQKTL---------------------------VEG 209
Cdd:pfam15921 344 IEELekqlvlaNSELTEARTERDQFSQESGNLDDQLQKLlADLHKREKELslekeqnkrlwdrdtgnsitidhlrreLDD 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 210 YRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKTVSCTSPLLLGNAVKAQVKATKGRNRMrgQVESNLKQVEQA 289
Cdd:pfam15921 424 RNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKM--TLESSERTVSDL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 290 RSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLT-----KLSLEEENHLIQL---KCENLKEKLEQ- 360
Cdd:pfam15921 502 TASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTecealKLQMAEKDKVIEIlrqQIENMTQLVGQh 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 361 ------MDAENKELEKKLADQEECLKH-------------------SDLELkEKAAEYTALSRQLEAA--LEEGRQKVSE 413
Cdd:pfam15921 582 grtagaMQVEKAQLEKEINDRRLELQEfkilkdkkdakirelearvSDLEL-EKVKLVNAGSERLRAVkdIKQERDQLLN 660
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568923227 414 EVEKMSSRERALQIKILDLEAELRKKNEEqnqlvdkMNTKTQHQAICLKEIQHSLEksETRN 475
Cdd:pfam15921 661 EVKTSRNELNSLSEDYEVLKRNFRNKSEE-------METTTNKLKMQLKSAQSELE--QTRN 713
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
60-443 |
2.77e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 60 RQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLED 139
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 140 LRKMET---HGK--------------NSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASvENELVELQEVEKR 202
Cdd:PRK02224 442 VEEAEAlleAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERRED 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 203 QKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKTVSCTSPLLLGNAVKAQVKATkgRNRMRgQVESN 282
Cdd:PRK02224 521 LEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER--IESLE-RIRTL 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 283 LKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQslLTKLSLEEENHLIQLkcENLKEKLEQMD 362
Cdd:PRK02224 598 LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYL--EQVEEKLDELR 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 363 AENKELEKKLADQEECLKhsdlELKEKAAEYTALSRQLEAAleegrQKVSEEVEkmssrerALQIKILDLEAELRKKNEE 442
Cdd:PRK02224 674 EERDDLQAEIGAVENELE----ELEELRERREALENRVEAL-----EALYDEAE-------ELESMYGDLRAELRQRNVE 737
|
.
gi 568923227 443 Q 443
Cdd:PRK02224 738 T 738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
115-426 |
3.17e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 115 IAIEKTELEVQIETMKKQIANLLEDLRKMETHgknsCEEILRKLHSLEDENEALNIENVKL-KGTLDALKDEVASVENEL 193
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEE----ISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 194 VELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHEnnliITNKNKKLEKtvsctspllLGNAVKaqvKATKGRN 273
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE----IEEERKRRDK---------LTEEYA---ELKEELE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 274 RMRGQVESNLKQVEQARSSFTSAEQRLQECQEKLQrckekcaeqaltirELQGQVDGNQSLLTKLSLEEENHLIQLkcEN 353
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREIN--------------ELKRELDRLQEELQRLSEELADLNAAI--AG 431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568923227 354 LKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEaALEEGRQKVSEEVEKMSSRERALQ 426
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD-RVEKELSKLQRELAEAEAQARASE 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
52-227 |
3.35e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 52 AVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKK 131
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 132 QIANLLED----LRKMETHGKNSCEEIL----------RKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQ 197
Cdd:COG4942 98 ELEAQKEElaelLRALYRLGRQPPLALLlspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190
....*....|....*....|....*....|
gi 568923227 198 EVEKRQKTLVEGYRTQVQKLQEAAEMVKSR 227
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKE 207
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
278-486 |
4.59e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 278 QVESNLKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKL--SLEEENHLIQLKCENLK 355
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAeaELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 356 EKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEA--ALEEGRQKVSEEVEKMSSRERALQIKILDLE 433
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEleELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568923227 434 AELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIKNYLQFLQ 486
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
34-220 |
4.70e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 34 LETQIAKwnLQVKMNKQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSE------------- 100
Cdd:COG3206 180 LEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlraqlgsgpdalp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 101 TVSAS---SDWKSQFEKIAIEKTELEV-------QIETMKKQIANLLEDLRkmethgknscEEILRKLHSLEDENEALNI 170
Cdd:COG3206 258 ELLQSpviQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ----------QEAQRILASLEAELEALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568923227 171 ENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEA 220
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
278-446 |
5.26e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 278 QVESNLKQVEQARSSF-------------TSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLSleeEN 344
Cdd:COG3206 186 ELRKELEEAEAALEEFrqknglvdlseeaKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL---QS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 345 HLIQlkceNLKEKLEQMDAENKELEKKLADQeeclkHSDL-ELKEKAAEytaLSRQLEAALEEGRQKVSEEVEKMSSRER 423
Cdd:COG3206 263 PVIQ----QLRAQLAELEAELAELSARYTPN-----HPDViALRAQIAA---LRAQLQQEAQRILASLEAELEALQAREA 330
|
170 180
....*....|....*....|...
gi 568923227 424 ALQIKILDLEAELRKKNEEQNQL 446
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAEL 353
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
83-307 |
8.44e-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: 41.97 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 83 DIERLASQVRDQEAKLSETVSASSDWKSQFEKI-------AIEKTELEVQIETMKKQIANLLEDLRKMET---HGKNSCE 152
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELqkelyalANEISRLEQQKQILRERLANLERQLEELEAqleELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 153 EILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLL 232
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568923227 233 HENNLIITNK---NKKLEKTVSCTSPLLLGNAVKAQVKATKGRNRMRGQVESNLKQVEQARSSFTSAEQRLQECQEKL 307
Cdd:TIGR02168 414 DRRERLQQEIeelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
285-455 |
9.08e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.94 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 285 QVEQARSSFTSAEQRLQECQEKLQrckekcAEQALTIRELQGQVDGNQSLLTKLSLEEENhlIQLKCENLKEKLEQMDAE 364
Cdd:pfam05667 307 QFTNEAPAATSSPPTKVETEEELQ------QQREEELEELQEQLEDLESSIQELEKEIKK--LESSIKQVEEELEELKEQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 365 NKELEKK----------LADQEECLKHSDLELKEKAAEYTALSRQLEAA----LEEGRQKVSEEVEKMSSRER------A 424
Cdd:pfam05667 379 NEELEKQykvkkktldlLPDAEENIAKLQALVDASAQRLVELAGQWEKHrvplIEEYRALKEAKSNKEDESQRkleeikE 458
|
170 180 190
....*....|....*....|....*....|.
gi 568923227 425 LQIKILDLEAELRKKNEEQNQLVDKMNTKTQ 455
Cdd:pfam05667 459 LREKIKEVAEEAKQKEELYKQLVAEYERLPK 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-486 |
9.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 276 RGQVESNL----KQVEQARSSFT-SAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLS-LEEENHLIQL 349
Cdd:COG1196 195 LGELERQLepleRQAEKAERYRElKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAeLEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 350 KCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAaLEEGRQKVSEEVEKMSSRERALQIKI 429
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE-LEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568923227 430 LDLEAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIKNYLQFLQ 486
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
350-451 |
9.75e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 350 KCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEkaaeytalsrqleaALEEGRQKVSEEvEKMSSRERalqiKI 429
Cdd:COG2433 414 EIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE--------------ARSEERREIRKD-REISRLDR----EI 474
|
90 100
....*....|....*....|..
gi 568923227 430 LDLEAELRKKNEEQNQLVDKMN 451
Cdd:COG2433 475 ERLERELEEERERIEELKRKLE 496
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
44-479 |
1.49e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 44 QVKMNKQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAiEKTELE 123
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 124 VQIETMKKQIANL--LEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEK 201
Cdd:PTZ00121 1398 KKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 202 R--QKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKTVSCTSPLLLGNAVKAQ--VKATKGRNRMRG 277
Cdd:PTZ00121 1478 KaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekKKADELKKAEEL 1557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 278 QVESNLKQVEQARSSFTSAEQRLQECQEkLQRCKEKCAEQALTIRELQGQVDGNQSlltKLSLEEENHLIQLKCENLKEK 357
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEE-AKKAEEARIEEVMKLYEEEKKMKAEEA---KKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 358 LEQMDAENKELEKKLADQ----EECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERAlqikildle 433
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEElkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA--------- 1704
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 568923227 434 AELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIK 479
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-222 |
1.64e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 50 QEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETM 129
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 130 KKQIANLLEDLRKMEthgkNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEG 209
Cdd:COG1196 343 EEELEEAEEELEEAE----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
170
....*....|...
gi 568923227 210 YRTQVQKLQEAAE 222
Cdd:COG1196 419 LEEELEELEEALA 431
|
|
| prfA |
PRK00591 |
peptide chain release factor 1; Validated |
354-437 |
1.73e-03 |
|
peptide chain release factor 1; Validated
Pssm-ID: 234801 [Multi-domain] Cd Length: 359 Bit Score: 40.45 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 354 LKEKLEQMDAENKELEKKLA------DQEECLK----HSDLE-LKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRE 422
Cdd:PRK00591 4 MLDKLEALEERYEELEALLSdpevisDQKRFRKlskeYAELEpIVEAYREYKQAQEDLEEAKEMLEEESDPEMREMAKEE 83
|
90
....*....|....*.
gi 568923227 423 -RALQIKILDLEAELR 437
Cdd:PRK00591 84 lKELEERLEELEEELK 99
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-449 |
2.15e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 49 KQEAVAIKEASRQKAVALKKASKVYRQRLRhftgdierlaSQVRDQEAKLSETVSASSDWKSQFEKiAIEKTELEVQIET 128
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKKADE----------AKKKAEEAKKADEAKKKAEEAKKAEE-AKKKAEEAKKADE 1474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 129 MKKQI--ANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIEnvKLKGTLDALKDEVASVENELVELQEVEKRQKTl 206
Cdd:PTZ00121 1475 AKKKAeeAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE--EAKKADEAKKAEEAKKADEAKKAEEKKKADEL- 1551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 207 vegyrTQVQKLQEAAEMVKSRCKNLLHENNLIITNKN---KKLEKTVSCTSPLLLGNAVKAQVKATKGRNRMRGQVESnL 283
Cdd:PTZ00121 1552 -----KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE-L 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 284 KQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLSLEEENHliQLKCENLK-------- 355
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE--KKAAEALKkeaeeakk 1703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 356 -EKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDLEA 434
Cdd:PTZ00121 1704 aEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
410
....*....|....*
gi 568923227 435 ELRKKNEEQNQLVDK 449
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDK 1798
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
57-479 |
2.75e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 57 EASRQKAValKKASKVYRQRLRHFTGDI----ERLASQVRDQEAKLS---ETVSASSDWKSQFEKIAIEKTELEVQIETM 129
Cdd:pfam12128 274 IASRQEER--QETSAELNQLLRTLDDQWkekrDELNGELSAADAAVAkdrSELEALEDQHGAFLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 130 KKQIANLLEDLRKMETHGKNSCEEILRKLHSLEDENealnienvklkgtldaLKDEVASVENELVELQEVEKRQKTLVEG 209
Cdd:pfam12128 352 WQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ----------------NNRDIAGIKDKLAKIREARDRQLAVAED 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 210 -YRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKtVSCTSPLLLGNAVKAQVKatkgrNRMRGQVESNLKQVEQ 288
Cdd:pfam12128 416 dLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQ-ATATPELLLQLENFDERI-----ERAREEQEAANAEVER 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 289 ARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDG------------------------NQSLLTKLSLEEEN 344
Cdd:pfam12128 490 LQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagtllhflrkeapdweqsigkviSPELLHRTDLDPEV 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 345 HLIQLKCEN----LKEKLEQMD-----AENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEE------GRQ 409
Cdd:pfam12128 570 WDGSVGGELnlygVKLDLKRIDvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREetfartALK 649
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568923227 410 KVSEEVEKMSSRERALQIKILD-LEAELRKKNEEQNQLVDKMNT-KTQHQAICLKEIQHSLEKSETRNESIK 479
Cdd:pfam12128 650 NARLDLRRLFDEKQSEKDKKNKaLAERKDSANERLNSLEAQLKQlDKKHQAWLEEQKEQKREARTEKQAYWQ 721
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-329 |
2.82e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 54 AIKEASRQKAVALKKASKVyRQRLRHFTGDIERLASQVRDQEAKLSEtVSASSDWKSQFEKIAIEKT--ELEVQIETMKK 131
Cdd:TIGR02169 231 EKEALERQKEAIERQLASL-EEELEKLTEEISELEKRLEEIEQLLEE-LNKKIKDLGEEEQLRVKEKigELEAEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 132 QIANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLkgtlDALKDEVASVENEL----VELQEVEKRQKTLv 207
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR----DKLTEEYAELKEELedlrAELEEVDKEFAET- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 208 egyRTQVQKLQEAAEMVKsrcknllHENNLIITNKNKKLEKTVSCTSPLLLGNA----VKAQVKATKGRNR-MRGQVESN 282
Cdd:TIGR02169 384 ---RDELKDYREKLEKLK-------REINELKRELDRLQEELQRLSEELADLNAaiagIEAKINELEEEKEdKALEIKKQ 453
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568923227 283 LKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVD 329
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| PrfA |
COG0216 |
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ... |
353-437 |
3.69e-03 |
|
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein chain release factor RF1 is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439986 [Multi-domain] Cd Length: 356 Bit Score: 39.60 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 353 NLKEKLEQMDAENKELEKKLADQE---------ECLK-HSDLE-LKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSR 421
Cdd:COG0216 1 SMLDKLEALEERYEELEALLSDPEvisdqkrfrKLSKeYAELEpIVEAYREYKKLLEDIEEAKELLEEESDPEMREMAKE 80
|
90
....*....|....*..
gi 568923227 422 E-RALQIKILDLEAELR 437
Cdd:COG0216 81 ElEELEARLEELEEELK 97
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
84-451 |
5.25e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 84 IERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKMEThgknsceEILRKLHSLED 163
Cdd:TIGR00606 697 ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNR-------DIQRLKNDIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 164 ENEALNIENVKLKGTLDALKDeVASVENELVELQEVEKRQKtlvegyrtqvqklQEAAEMVKSRCKNLLHENNLIITNKN 243
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVCLTD-VTIMERFQMELKDVERKIA-------------QQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 244 KKLEKTVSctsplllgnAVKAQVKATKGRNRMRGQVESNLKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRE 323
Cdd:TIGR00606 836 HELDTVVS---------KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 324 LQGQVDGNQSLLTKL---------SLEEENHLIQLKCENLKEKLEQMDAENKELEKKLAD-QEECLKHSDLELKEKAAEY 393
Cdd:TIGR00606 907 AKEQDSPLETFLEKDqqekeelisSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTVNAQL 986
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 394 TAlSRQLEAALEEGRQKVSEEVEKMSSRERALQ--IKILDLEAELRKKNEEQNQLVDKMN 451
Cdd:TIGR00606 987 EE-CEKHQEKINEDMRLMRQDIDTQKIQERWLQdnLTLRKRENELKEVEEELKQHLKEMG 1045
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
105-489 |
6.98e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.23 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 105 SSDWKSQFEKIAIEKTELEVQIETMKKQIANL---LEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKGTLDA 181
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLneqISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 182 LKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRcknLLHENNLIITNKNKKLEKTVSCTSPLLLGNA 261
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET---IIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 262 VKAQVKATKGR-NRMRGQVESNLKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLSL 340
Cdd:TIGR04523 466 LETQLKVLSRSiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 341 EEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAaLEEGRQKVSEEVEKMSS 420
Cdd:TIGR04523 546 ELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE-KEKKISSLEKELEKAKK 624
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568923227 421 RERALQIKILDLEAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIKNYLQFLQISY 489
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHY 693
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
264-441 |
7.23e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 38.91 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 264 AQVKATKGRNRMRGQVESNLKQVEQARSSftsAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTK------ 337
Cdd:PRK11637 58 AKEKSVRQQQQQRASLLAQLKKQEEAISQ---ASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAqldaaf 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 338 -----------LSLEEE-------------NHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLkhSDLELKEKAAEY 393
Cdd:PRK11637 135 rqgehtglqliLSGEESqrgerilayfgylNQARQETIAELKQTREELAAQKAELEEKQSQQKTLL--YEQQAQQQKLEQ 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568923227 394 TALSRQ-----LEAALEEGRQKVSEevekMSSRERALQIKILDLEAELRKKNE 441
Cdd:PRK11637 213 ARNERKktltgLESSLQKDQQQLSE----LRANESRLRDSIARAEREAKARAE 261
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-440 |
8.83e-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: 37.98 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 284 KQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLSLEEENHLIQLKCENLKEKLEQMDA 363
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLED 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568923227 364 ENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDLEAELRKKN 440
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYERIRKRK 187
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
354-481 |
8.98e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.90 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923227 354 LKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLE------AALEEGRQKVSEEVEKMSSRERALQI 427
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEaierqlASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568923227 428 KILDLEAELRKKNE-EQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIKNY 481
Cdd:TIGR02169 273 LLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
|
| |
