|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
87-405 |
2.08e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 87 ELKWEMEKEEKRLL---WEQLQGLESSKQAETSRLQEELAKLSEKLKKKQEsfcRLQTEKETLfNDSRNKIEELQQRkEA 163
Cdd:COG1196 217 ELKEELKELEAELLllkLRELEAELEELEAELEELEAELEELEAELAELEA---ELEELRLEL-EELELELEEAQAE-EY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 164 DHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVsiqsADAQEQVEGLLAENNALRTSLAALEQIQ 243
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL----EELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 244 TAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKR 323
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 324 KAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVE 403
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
..
gi 119571101 404 EL 405
Cdd:COG1196 528 VL 529
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
187-516 |
1.52e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 187 AELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQ 266
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 267 QQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAmETLQEKSQHKEELG 346
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-EALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 347 AVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQAqvhsmdgakgwfERRLKEA 426
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE------------EEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 427 EESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLEQAQEERDchlktiSSLKQEVKDTVDGQRILEKKGSAALK 506
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL------LLLEAEADYEGFLEGVKAALLLAGLR 520
|
330
....*....|
gi 119571101 507 DLKRQLHLER 516
Cdd:COG1196 521 GLAGAVAVLI 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
88-615 |
4.59e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 88 LKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLsEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRK------ 161
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEELELELEEAQAEEYELLAELARLEQDIarleer 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 162 ----EADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLA 237
Cdd:COG1196 311 rrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 238 ALEQIQTAKTQELNmLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEAR 317
Cdd:COG1196 391 ALRAAAELAAQLEE-LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 318 KSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRH-------EKEVLGVRARYERELRELHEDKKRQEEEL--RGQIREE 388
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvkAALLLAGLRGLAGAVAVLIGVEAAYEAALeaALAAALQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 389 KARTRELETLQQTVEELQAQVHS-MDGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLE 467
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 468 QAQEERDCHLKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRSGLEELVLSEM 547
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119571101 548 NspSRTQTGDSSSISSFSYREILREKESSAVPARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQE 615
Cdd:COG1196 710 A--EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
158-408 |
2.50e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 158 QQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEhAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLA 237
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 238 ALEQiqtaktqELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEAR 317
Cdd:COG1196 299 RLEQ-------DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 318 KSAEKRKAMLDELAMETLQEKSQhkeelgAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRE-LE 396
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRA------AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEaLE 445
|
250
....*....|..
gi 119571101 397 TLQQTVEELQAQ 408
Cdd:COG1196 446 EAAEEEAELEEE 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-417 |
4.30e-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: 66.62 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 88 LKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEkLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEAdHKA 167
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQI-LRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 168 QLARtqkLQQELEAANQSLAELRDQRQgerlehaaALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAkt 247
Cdd:TIGR02168 310 RLAN---LERQLEELEAQLEELESKLD--------ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 248 qelnmlreqttgLAAELQQQQAEYEDLMGQKDDLNSQLQeslransRLLEQLQEIGQEKEQLTQELQEARKSAEkrKAML 327
Cdd:TIGR02168 377 ------------LEEQLETLRSKVAQLELQIASLNNEIE-------RLEARLERLEDRRERLQQEIEELLKKLE--EAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 328 DELAMEtLQEKSQHKEELGAVRLRHEKEVLGVRARYErELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQA 407
Cdd:TIGR02168 436 KELQAE-LEELEEELEELQEELERLEEALEELREELE-EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
330
....*....|
gi 119571101 408 QVHSMDGAKG 417
Cdd:TIGR02168 514 NQSGLSGILG 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
109-471 |
1.58e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 109 SSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETL--FNDSRNKIEELQQRKEAdhKAQLA-RTQKLQQELEAANQS 185
Cdd:TIGR02168 151 EAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLdrLEDILNELERQLKSLER--QAEKAeRYKELKAELRELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 186 LAELRDQRQGERLEhaaALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQ 265
Cdd:TIGR02168 229 LLVLRLEELREELE---ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 266 QQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAmETLQEKSQHKEEL 345
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE-SRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 346 GAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTR-ELETLQQTVEELQAQVHSMDGAKGWFERRLK 424
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 119571101 425 EAEESLQQQQQEQEEALKQcreqhAAELKGKEEELQDVRDQLEQAQE 471
Cdd:TIGR02168 465 ELREELEEAEQALDAAERE-----LAQLQARLDSLERLQENLEGFSE 506
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
94-646 |
1.73e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 94 KEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESfcRLQTEKETLFNDSRNKIEELQQRKEADHK---AQLA 170
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKKKAEEAKKaaeAAKA 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 171 RTQKLQQELEAANQSlAELRDQRQGERLEHAAALRALQDQVSiQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTqel 250
Cdd:PTZ00121 1351 EAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADEAKK--- 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 251 nmlREQTTGLAAELQQQQAEYEdlmgQKDDLNSQLQESLRANSrlLEQLQEIGQEKEQLTQELQEARKSAE-KRKAMLDE 329
Cdd:PTZ00121 1426 ---KAEEKKKADEAKKKAEEAK----KADEAKKKAEEAKKAEE--AKKKAEEAKKADEAKKKAEEAKKADEaKKKAEEAK 1496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 330 LAMETLQEKSQHKEELGAVRLRHEKevlgvraRYERELRELhEDKKRQEEELRGQIREEKARTRELETLQQTVEELQA-Q 408
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEA-------KKADEAKKA-EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAeE 1568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 409 VHSMDGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKgKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVK 488
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 489 DTvDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDiltnskSRSGLEELVLSEMNSPSRTQTGDSSSISSFSYRE 568
Cdd:PTZ00121 1648 KA-EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101 569 ILREKESSAVPARSLSSSPQAQPPRPAELS-DEEVAELFQRLAETQQEKWMLEEKVKHLEVSSASMAEDLCRKSAIIET 646
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
86-409 |
3.34e-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: 60.46 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 86 VELKWEMEKEEKRLlwEQLQGLESSKQAETSRLQEELAKLSEKLKKKQesfcRLQTEKETLFNDSRNKIEELQQRKEAdH 165
Cdd:TIGR02168 673 LERRREIEELEEKI--EELEEKIAELEKALAELRKELEELEEELEQLR----KELEELSRQISALRKDLARLEAEVEQ-L 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 166 KAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVsiqsADAQEQVEGLLAENNALRTSLAALEQIQTA 245
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI----EQLKEELKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 246 KTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKrka 325
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE--- 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 326 mldelAMETLQEKSQHKEElgavrLRHEKEvlgvraryerELRELHEDKKRQEEELRGQIREEKARTREL-ETLQQTVEE 404
Cdd:TIGR02168 899 -----LSEELRELESKRSE-----LRRELE----------ELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEA 958
|
....*
gi 119571101 405 LQAQV 409
Cdd:TIGR02168 959 LENKI 963
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-522 |
5.29e-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: 59.69 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 192 QRQGERLEHAAALRALQDQVsiqsADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEY 271
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKI----AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 272 EDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAMetlqEKSQHKEELGAVRLR 351
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA----ELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 352 HEKEVLGVrARYERELRELHEDKKRQEEELrgqireeKARTRELETLQQTVEELQAQVHSMDGAKGWFERRLKEAEESLQ 431
Cdd:TIGR02168 826 LESLERRI-AATERRLEDLEEQIEELSEDI-------ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 432 QQQQEQEEALKQCREQHaAELKGKEEELQDVRDQLEQAQEERDchlKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQ 511
Cdd:TIGR02168 898 ELSEELRELESKRSELR-RELEELREKLAQLELRLEGLEVRID---NLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
330
....*....|.
gi 119571101 512 LHLERKRADKL 522
Cdd:TIGR02168 974 LKRLENKIKEL 984
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
110-325 |
8.41e-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: 57.85 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 110 SKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADHKAQLARTQKLQQELEAANQSLAEL 189
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL-LKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 190 RDQRQGERLEHAAALRALQDQVSI-------------QSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQ 256
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101 257 TTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKA 325
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
87-337 |
1.91e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 87 ELKWEMEKEEKRLlwEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEadhk 166
Cdd:TIGR02168 271 ELRLEVSELEEEI--EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE---- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 167 aqlaRTQKLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAK 246
Cdd:TIGR02168 345 ----KLEELKEELESLEAELEELEAELE-ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 247 TQELNMLREqttglaaelQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAM 326
Cdd:TIGR02168 420 QQEIEELLK---------KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
250
....*....|.
gi 119571101 327 LDelAMETLQE 337
Cdd:TIGR02168 491 LD--SLERLQE 499
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
83-531 |
5.82e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 83 LAEVELKWEMEKEEKRLLWEQLQGLESSKQAETSRlQEELAKLSEKLKKKQESFCRLQTEKETL---FNDSRNKIEELQQ 159
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELETLEAEIEDLRETIAETEREREELaeeVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 160 RKE----------ADHKAQLARTQKLQQELEAANQSLAELRdQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAEN 229
Cdd:PRK02224 294 ERDdllaeaglddADAEAVEARREELEDRDEELRDRLEECR-VAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 230 NALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQEsLRANSRLLEQLQEIGQEkeql 309
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE-LEATLRTARERVEEAEA---- 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 310 tqeLQEARKSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYER-------------------ELREL 370
Cdd:PRK02224 448 ---LLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERaedlveaedrierleerreDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 371 HEDKKRQEEELRGQIREEKARTRELETLQQTVEELQAQVHSMDGAK----GWFERRLKEAEESLQQQQQEQEEALKqcre 446
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAreevAELNSKLAELKERIESLERIRTLLAA---- 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 447 qhAAELKGKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVKDTVDGQRILEKKGsaalkdlkrqlhlERKRADKLQERL 526
Cdd:PRK02224 601 --IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEARE-------------DKERAEEYLEQV 665
|
....*
gi 119571101 527 QDILT 531
Cdd:PRK02224 666 EEKLD 670
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
166-408 |
8.12e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 166 KAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQ---EQVEGLLAENNALRTSLAALEQI 242
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 243 QTAKTQELNMLREQTTGLAAELQQQQAEYEDL-----MGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEAR 317
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 318 KSAEKRKAMLDELameTLQEKSQHKE-ELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELE 396
Cdd:TIGR02169 833 KEIQELQEQRIDL---KEQIKSIEKEiENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
250
....*....|..
gi 119571101 397 TLQQTVEELQAQ 408
Cdd:TIGR02169 910 AQIEKKRKRLSE 921
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
91-512 |
1.17e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 91 EMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEA--DHKAQ 168
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEllEALRA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 169 LARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVsiqsADAQEQVEGLLAENNALRTSLAALEQIQTAKTQ 248
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE----EEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 249 ELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRAN---------------------------SRLLEQLQE 301
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALllaglrglagavavligveaayeaaleAALAAALQN 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 302 IGQEKEQLTQELQEARKSAEKRKAM---LDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQE 378
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 379 EELRGQIREEKARTRELETLQQTVEELQAQVHSMDGAKGWFER----------------RLKEAEESLQQQQQEQEEALK 442
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAlleaeaeleelaerlaEEELELEEALLAEEEEERELA 710
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 443 QCREQHAAELKGKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVKDTVDGQRILEKKgsaaLKDLKRQL 512
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE----LERLEREI 776
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
235-473 |
1.37e-07 |
|
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: 54.38 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 235 SLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQ 314
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 315 EARKSAEKRKAMLDELaMETLQEKSQHKEELGAVRLRHEKEVLgVRARYereLRELHEDKKRQEEELRGQIREEKARTRE 394
Cdd:COG4942 94 ELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAV-RRLQY---LKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101 395 LETLQQTVEELQAQVHSmdgakgwfERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLEQAQEER 473
Cdd:COG4942 169 LEAERAELEALLAELEE--------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-409 |
5.17e-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: 53.15 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 95 EEKRLLWEQLQGlESSKQAETSRLQEEL--AKLSEKLKKKQEsfcrLQTEKETLFNDSRNKIEELQQRKEadhkaqlaRT 172
Cdd:TIGR02169 194 DEKRQQLERLRR-EREKAERYQALLKEKreYEGYELLKEKEA----LERQKEAIERQLASLEEELEKLTE--------EI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 173 QKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNM 252
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 253 LREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKrkamLDELAM 332
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR----LQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 333 ETLQEKSQHKEELGAVRLRH-----EKEVLGVR-ARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQ 406
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKIneleeEKEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
...
gi 119571101 407 AQV 409
Cdd:TIGR02169 497 AQA 499
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
149-366 |
1.18e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 149 DSRNKIEELQQRKeadhkaqlartQKLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQVS--IQSADAQEQVEGLL 226
Cdd:COG4913 607 DNRAKLAALEAEL-----------AELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWdeIDVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 227 AENNALRTSLAALEQiqtaktqelnmLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEK 306
Cdd:COG4913 675 AELERLDASSDDLAA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 307 EQLTQELQEARKSAEKRKAMLDELAMETLQEKSQHKEELGavrlRHEKEVLGVRARYERE 366
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERELRENLEERIDALRARLN----RAEEELERAMRAFNRE 799
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-542 |
2.15e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 4 LEQENQQLKEGAAGAGVAQAGplVDGELLRLQAENTALQKNVAALQERYGKEAGKFSAVSEgqgdppggpaptvlapmPL 83
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEE--LEAQLEELESKLDELAEELAELEEKLEELKEELESLEA-----------------EL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 84 AEVELKWEMEK---EEKRLLWE-------------------------QLQGLESSKQ---------------AETSRLQE 120
Cdd:TIGR02168 361 EELEAELEELEsrlEELEEQLEtlrskvaqlelqiaslnneierleaRLERLEDRRErlqqeieellkkleeAELKELQA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 121 ELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQ--RKEADHKAQLARTQKLQQELEAANQSLAELRDQRQG--- 195
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAaeRELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsg 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 196 ------------ERLEHA--AALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTT--- 258
Cdd:TIGR02168 521 ilgvlselisvdEGYEAAieAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIegf 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 259 -GLAAELQQQQAEYEDLM--------------------------------------------GQKDDLNSQLQESLRANS 293
Cdd:TIGR02168 601 lGVAKDLVKFDPKLRKALsyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitGGSAKTNSSILERRREIE 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 294 RLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAMEtLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHE- 372
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEl 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 373 -DKKRQEEELRGQIREEKART-RELETLQQTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEqeealkqcREQHAA 450
Cdd:TIGR02168 760 eAEIEELEERLEEAEEELAEAeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LESLER 831
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 451 ELKGKEEELQDVRDQLEQAQEErdchlktISSLKQEVKDTVDGQRILEKKGSAALKD---LKRQLHLERKRADKLQERLQ 527
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSED-------IESLAAEIEELEELIEELESELEALLNErasLEEALALLRSELEELSEELR 904
|
650
....*....|....*.
gi 119571101 528 DILT-NSKSRSGLEEL 542
Cdd:TIGR02168 905 ELESkRSELRRELEEL 920
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
85-637 |
2.20e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 85 EVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKL-----SEKLKKKQESFCRLQTEKEtlfNDSRNKIEELQQ 159
Cdd:PTZ00121 1186 EVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAeavkkAEEAKKDAEEAKKAEEERN---NEEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 160 ----RKEADHKAQLARTQKLQQELEAANQS--LAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALR 233
Cdd:PTZ00121 1263 ahfaRRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 234 TSLAALEQIQTAKTQELNMLREQTTglAAELQQQQAEyedlmgQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQEL 313
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAE--AAEKKKEEAK------KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 314 QEARKSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKevlgvrARYERELRELHEDKKRQEEelrgqIREEKARTR 393
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE------AKKAEEAKKKAEEAKKADE-----AKKKAEEAK 1483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 394 ELETLQQTVEELQAQVhsmDGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQdvRDQLEQAQEER 473
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKA---DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK--ADELKKAEELK 1558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 474 DChlKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRSGLEELVLSEMNSPSRT 553
Cdd:PTZ00121 1559 KA--EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 554 QTGDSSSISSFSYREILREKESSAVPARSLSSSPQ-----AQPPRPAELSDEEVAELFQRLAETQQEKwmleEKVKHLEV 628
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkkkAEEAKKAEEDEKKAAEALKKEAEEAKKA----EELKKKEA 1712
|
....*....
gi 119571101 629 SSASMAEDL 637
Cdd:PTZ00121 1713 EEKKKAEEL 1721
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
253-512 |
4.01e-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: 50.45 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 253 LREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAM 332
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 333 ETLQEKSQHKE--------ELGAVRLRHEKEVLGVRARYER------ELRELHEDKKRQEEELRGQIREEKARTRELETL 398
Cdd:TIGR02169 752 EIENVKSELKElearieelEEDLHKLEEALNDLEARLSHSRipeiqaELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 399 QQTVEELQAQVHSMDGAKGWFERRLkeaeeslqqqqqEQEEALKQCREQHAAELKGKEEELQDVRDQLEQAQEERDCHLK 478
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEI------------ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270
....*....|....*....|....*....|....
gi 119571101 479 TISSLKQEVKDTVDGQRILEKKGSAALKDLKRQL 512
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
182-409 |
4.70e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 182 ANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSlaaleqiqtaktQELNMLREQTTGLA 261
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------------EEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 262 AELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLE--QLQEIGQEKEQLTQELQEARksaekrkamldelamETLQEKS 339
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELS---------------ARYTPNH 290
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119571101 340 ----QHKEELGAVRLRHEKEVLGVRARYERELRELhedkKRQEEELRGQIREEKARTRELETLQQTVEELQAQV 409
Cdd:COG3206 291 pdviALRAQIAALRAQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
76-525 |
4.71e-06 |
|
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: 49.97 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 76 TVLAPMPLAEVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKL--KKKQESFCRLQTEKETLFNDSRNK 153
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERInrARKAAPLAAHIKAVTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 154 IEELQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEhaaalralqdqvsiQSADAQEQVEGLLAENNALR 233
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR--------------DAHEVATSIREISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 234 TSLAALEQIQTAKTQELNMLR---EQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLT 310
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCkelDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 311 QELQEARKSAEKRKAMLDELAMETLQEKSQHKEElgavrlrhekevlGVRARYERELRELHEDKKRQEEELRGQIREEKA 390
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVV-------------LARLLELQEEPCPLCGSCIHPNPARQDIDNPGP 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 391 RTRELETLQQTVEELQAQVHSMDGaKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLEQAQ 470
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSEEDVYH-QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS 604
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 119571101 471 EERDCHLKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQLHLERKRADKLQER 525
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER 659
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
148-387 |
5.59e-06 |
|
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: 49.95 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 148 NDSRNKIE---ELQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALR--ALQDQVSIQS-ADAQEQ 221
Cdd:COG3096 842 RQRRSELErelAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELdaAQEAQAFIQQhGKALAQ 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 222 VEGLLAennALRTSLAALEQIQTAKTQ---ELNMLREQTTGLAAELQQQQA-EYED---LMGQKDDLNSQLQESLR---- 290
Cdd:COG3096 922 LEPLVA---VLQSDPEQFEQLQADYLQakeQQRRLKQQIFALSEVVQRRPHfSYEDavgLLGENSDLNEKLRARLEqaee 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 291 ANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAMETLQ---------------EKSQHKEELGAVRLRhEKE 355
Cdd:COG3096 999 ARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqadaeaeerariRRDELHEELSQNRSR-RSQ 1077
|
250 260 270
....*....|....*....|....*....|..
gi 119571101 356 VLGVRARYERELRELHEDKKRQEEELRGQIRE 387
Cdd:COG3096 1078 LEKQLTRCEAEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
91-523 |
1.21e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 91 EMEKEEKRLLWEQLQGLESsKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEAdhKAQLA 170
Cdd:COG4717 67 ELNLKELKELEEELKEAEE-KEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEAL--EAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 171 RTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQEL 250
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 251 NMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDEL 330
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 331 AMETLQEKSqHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARtRELETLQQTVEELQAQVH 410
Cdd:COG4717 303 EAEELQALP-ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE-LQLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 411 SMDGAK-----GWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLEQAQEERDCHLKTISSLKQ 485
Cdd:COG4717 381 VEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430
....*....|....*....|....*....|....*...
gi 119571101 486 EVKDTVDGQRILEKKgsAALKDLKRQLHLERKRADKLQ 523
Cdd:COG4717 461 ELEQLEEDGELAELL--QELEELKAELRELAEEWAALK 496
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
91-631 |
1.59e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 91 EMEKEEKRLLWEQLQGLESSKQAETSRLQEElAKLSEKLKKKQESfcrlqteketlFNDSRNKIEELQQRKEADHKAQLA 170
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKAEDARKAEE-ARKAEDARKAEEA-----------RKAEDAKRVEIARKAEDARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 171 RTQKLQQELEAANQSLAELRDQ--RQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQ 248
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEVRKAEelRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 249 ELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSrlLEQLQEIgQEKEQLTQELQEARKSAE-KRKAML 327
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADE--AKKAEEK-KKADEAKKKAEEAKKADEaKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 328 DELAMETLQEKSQHKEELGAVRlRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQA 407
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAA-KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKK 1405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 408 QVHSMDGAKGwfERRLKEAEESLQQQQQEQEEALKQCREQHAA-ELKGKEEELQDVRDQLEQAQEERDChlktiSSLKQE 486
Cdd:PTZ00121 1406 KADELKKAAA--AKKKADEAKKKAEEKKKADEAKKKAEEAKKAdEAKKKAEEAKKAEEAKKKAEEAKKA-----DEAKKK 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 487 VKDTVDGQRILEKKGSAALK-DLKRQLHLERKRADKL----QERLQDILTNSKSRSGLEELVLSEMNSPS---RTQTGDS 558
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKaDEAKKAAEAKKKADEAkkaeEAKKADEAKKAEEAKKADEAKKAEEKKKAdelKKAEELK 1558
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119571101 559 SSISSFSYREILREKESSAVPARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQEKwmlEEKVKHLEVSSA 631
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE---EAKIKAEELKKA 1628
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
301-554 |
1.68e-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: 48.14 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 301 EIGQEKEQLTQELQEARKSAEKRKAMLDELA--METLQEKSQHKEELGAVRLRHEKEVLGVRARyerELRELHEDKKRQE 378
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRqqLERLRREREKAERYQALLKEKREYEGYELLK---EKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 379 EELRGQIREEKARTRELETLQQTVEELQAQVHSMdgakgwfERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEE 458
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEEL-------NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 459 LQDVRDQLEQAQEERDCHLKTISSLKQEVKDtvdgQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRSG 538
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEE----ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250
....*....|....*.
gi 119571101 539 LEELVLSEMNSPSRTQ 554
Cdd:TIGR02169 393 KLEKLKREINELKREL 408
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
159-534 |
1.71e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 159 QRKEADHKAQLARTQKLQQELEAANQSLaelrdQRQGERLEHAAALRALQDQVSIQSA-----DAQEQVEGLLAENNALR 233
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKSL-----ERQAEKAERYKELKAELRELELALLvlrleELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 234 TSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQEL 313
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 314 QEARKSAEKRKAMLDELAMETLQEKSQHKEElgavrlrhekevlgvraryERELRELHEDKKRQEEELRGQIREEKARTR 393
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEEL-------------------EAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 394 ELETLQQTVEELqaqvhsmdgakgwferrlkeaEES----LQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLEQA 469
Cdd:TIGR02168 394 QIASLNNEIERL---------------------EARlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119571101 470 QEERDCHLKTISSLKQEVkdtvdgqrileKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSK 534
Cdd:TIGR02168 453 QEELERLEEALEELREEL-----------EEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
74-340 |
1.78e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.13 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 74 APTVLAPMPLAEVELKWEMEKEE------KRLLWEQLQG----LESSKQAETSRLQ-----EELAKLSEKLKKKqesfcr 138
Cdd:PRK10929 14 SWGAYAATAPDEKQITQELEQAKaaktpaQAEIVEALQSalnwLEERKGSLERAKQyqqviDNFPKLSAELRQQ------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 139 LQTEKETLFNDSRN-KIEELQQRKEADHKAQLARTQKLQQELEAANQ---SLAELRDQRQGERLEHAAALRALQDQVSIQ 214
Cdd:PRK10929 88 LNNERDEPRSVPPNmSTDALEQEILQVSSQLLEKSRQAQQEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 215 SADAQEQVEGLLAENNALRTSLAALE--QIQTAKTQELNMLReqttglaAELQQQQAEYEDLMGQ--KDDLNSQLQE--- 287
Cdd:PRK10929 168 TPLAQAQLTALQAESAALKALVDELElaQLSANNRQELARLR-------SELAKKRSQQLDAYLQalRNQLNSQRQReae 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 288 -SLRANSRLLEQ-------LQEIGQEKEQLTQEL-QEARK----SAEKRKAMLDEL----AMETLQEKSQ 340
Cdd:PRK10929 241 rALESTELLAEQsgdlpksIVAQFKINRELSQALnQQAQRmdliASQQRQAASQTLqvrqALNTLREQSQ 310
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
91-409 |
1.97e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 91 EMEKEEKRLLwEQLQGLESSKQAETSrLQEELAKLSEKLKKKQESfcRLQTEKETLFNDSRNKIEE-LQQRKEADHKAQL 169
Cdd:PRK04863 301 QLAAEQYRLV-EMARELAELNEAESD-LEQDYQAASDHLNLVQTA--LRQQEKIERYQADLEELEErLEEQNEVVEEADE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 170 ARTQkLQQELEAANQSLAELRDQ----RQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENnaLRTSLAALEQIQTA 245
Cdd:PRK04863 377 QQEE-NEARAEAAEEEVDELKSQladyQQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADN--AEDWLEEFQAKEQE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 246 KTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLN-SQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRK 324
Cdd:PRK04863 454 ATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSrSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQ 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 325 A---MLDELAMEtLQEKSQHKEELGAVRLRHEKEVLGVRArYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQT 401
Cdd:PRK04863 534 RaerLLAEFCKR-LGKNLDDEDELEQLQEELEARLESLSE-SVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDA 611
|
....*...
gi 119571101 402 VEELQAQV 409
Cdd:PRK04863 612 LARLREQS 619
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
115-417 |
2.01e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 48.29 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 115 TSRLQEELAKLSEKLKKKQESFCRLQTEKetlfndsrnKIEELQQRKEADHKAQLARTQKLQQELEAANQSLAElrdqrq 194
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNALADKE---------RAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALE------ 1601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 195 gerlehaaalralqdqvsiqsADAQEQVEGLLAENNALRTSLaaleqiqTAKTQELNMLREQTTGLAAELQQQQAEYEDl 274
Cdd:NF012221 1602 ---------------------TNGQAQRDAILEESRAVTKEL-------TTLAQGLDALDSQATYAGESGDQWRNPFAG- 1652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 275 mGQKDDLNSQLQEslrANSRLLEQLQEIgqeKEQLTQELQEARKSAEKRkamldelamETLQEKSQHKeelgavrlRHEK 354
Cdd:NF012221 1653 -GLLDRVQEQLDD---AKKISGKQLADA---KQRHVDNQQKVKDAVAKS---------EAGVAQGEQN--------QANA 1708
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119571101 355 EVLGVRARYERELRELHEDKKRQEEELR---GQIREEKARTRElETLQQTVEELQAQVHSmdGAKG 417
Cdd:NF012221 1709 EQDIDDAKADAEKRKDDALAKQNEAQQAesdANAAANDAQSRG-EQDASAAENKANQAQA--DAKG 1771
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
120-318 |
2.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 120 EELAKLSEKLKKKQESFCRLQTEKETL--FNDSR--NKIEELQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQ- 194
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALrlWFAQRrlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 195 --GERLEHAAAlralqdqvsiQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYE 272
Cdd:COG4913 335 ngGDRLEQLER----------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 119571101 273 DlmgQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARK 318
Cdd:COG4913 405 E---ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
85-527 |
2.11e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 85 EVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfndsrnkieELQQRKEAD 164
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ---------EEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 165 HKAQLARTQKLQQELEAANQSLAELRDQRQGERL-EHAAALRALQDQVSIQSADAQEQvEGLLAENNALRTSLAALEQIQ 243
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERINRARKAAPLaAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 244 TAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNS--QLQESLRAnsrLLEQLQEIGQEKEQLTQEL-QEARKSA 320
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHihTLQQQKTT---LTQKLQSLCKELDILQREQaTIDTRTS 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 321 EKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQ 400
Cdd:TIGR00618 418 AFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 401 TVEELQ----------AQVHSMDGAKGWFERRLKEAEESLQQQQQEQEEALKQCRE--QHAAELKGKEEELQDVRDQLEQ 468
Cdd:TIGR00618 498 ELQEEPcplcgscihpNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSerKQRASLKEQMQEIQQSFSILTQ 577
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101 469 AQEERDCHLKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQ 527
Cdd:TIGR00618 578 CDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ 636
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
83-412 |
6.56e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 83 LAEVELKWEMEKEEKRLLWEQLQGLESsKQAETSRLQEELAKLSEKLKKKQESFCRLQ----TEKETLFNDSRNKIEELQ 158
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEE-RLEELRELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELEELQ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 159 QRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTS--- 235
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgl 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 236 LAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQE 315
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 316 ARkSAEKRKAMLDELAMETLQEKSQHKEELGAvRLRHEKEVLGVRARYERELRELHE-----DKKRQEEELRGQIREEKA 390
Cdd:COG4717 366 EE-LEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEEllealDEEELEEELEELEEELEE 443
|
330 340
....*....|....*....|..
gi 119571101 391 RTRELETLQQTVEELQAQVHSM 412
Cdd:COG4717 444 LEEELEELREELAELEAELEQL 465
|
|
| DUF4407 |
pfam14362 |
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ... |
93-232 |
7.00e-05 |
|
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.
Pssm-ID: 464151 [Multi-domain] Cd Length: 295 Bit Score: 45.32 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 93 EKE-EKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKkqesfcrLQTEKETLFNDSRNKIEELQQRKEADHKAQLAR 171
Cdd:pfam14362 105 EKEiDRELLEIQQEEADAAKAQLAAAYRARLAELEAQIAA-------LDAEIDAAEARLDALQAEARCELDGTPGTGTGV 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 172 ------TQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVE---GLLAENNAL 232
Cdd:pfam14362 178 pgdgpvAKTKQAQLDAAQAELAALQAQNDARLAALRAELARLTAERAAARARSQAAIDgddGLLARLEAL 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-312 |
7.46e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 2 EQLEQENQQLKEGAAGAGVaqagplVDGELLRLQAENTALQKNVAALQERYGKEAGKFSAVSEGQGDppggpaptvlapm 81
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEE------LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES------------- 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 82 pLAEVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQqrk 161
Cdd:TIGR02168 829 -LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR--- 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 162 EADHKAQlartqKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQ 241
Cdd:TIGR02168 905 ELESKRS-----ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119571101 242 iQTAKTQELNMLREQttglaaelqqqqaEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQE 312
Cdd:TIGR02168 980 -KIKELGPVNLAAIE-------------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
148-316 |
1.03e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 148 NDSRNKIEELQQRK--EADHKA-----------------QLARTQKLQQELEAANQSLAElrDQRQGERLEHAAA----- 203
Cdd:PRK11281 39 ADVQAQLDALNKQKllEAEDKLvqqdleqtlalldkidrQKEETEQLKQQLAQAPAKLRQ--AQAELEALKDDNDeetre 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 204 ------LRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTA------KTQELN-MLREQTTG---LAAELQQQ 267
Cdd:PRK11281 117 tlstlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAAlyansqRLQQIRnLLKGGKVGgkaLRPSQRVL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119571101 268 -QAEYEDLMGQkddlNSQLQESLRANSrlleQLQEIGQEK-----------EQLTQELQEA 316
Cdd:PRK11281 197 lQAEQALLNAQ----NDLQRKSLEGNT----QLQDLLQKQrdyltariqrlEHQLQLLQEA 249
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
153-371 |
1.06e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 153 KIEEL-QQRKEADHKA-----QLARTQKLQQELEAAN-QSLAELRDQRQgERLEHAAALRALQDQVSIQSADAQEQVEGL 225
Cdd:PHA02562 175 KIRELnQQIQTLDMKIdhiqqQIKTYNKNIEEQRKKNgENIARKQNKYD-ELVEEAKTIKAEIEELTDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 226 LAENNALRTSLAALE-QIQTAK---------------TQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESL 289
Cdd:PHA02562 254 SAALNKLNTAAAKIKsKIEQFQkvikmyekggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 290 RANSRLLEQLQEIGQEKeqltQELQEARKSAEKRKAMLDELAMETLqeksQHKEELGAVRlRHEKEVLGVRARYERELRE 369
Cdd:PHA02562 334 EQSKKLLELKNKISTNK----QSLITLVDKAKKVKAAIEELQAEFV----DNAEELAKLQ-DELDKIVKTKSELVKEKYH 404
|
..
gi 119571101 370 LH 371
Cdd:PHA02562 405 RG 406
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
112-427 |
1.27e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 112 QAETSRLQEELAKLSEKLKKKQ---ESFCRL---------QTEKETLFNDSRNKIEELQqRKEADHKAQlarTQKLQQEL 179
Cdd:PRK04863 792 RAEREELAERYATLSFDVQKLQrlhQAFSRFigshlavafEADPEAELRQLNRRRVELE-RALADHESQ---EQQQRSQL 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 180 EAANQSLAELR----------DQRQGERLEHAAA--LRALQDQVSIQSADAQ-EQVEGLLAennALRTSLAALEQIQTAK 246
Cdd:PRK04863 868 EQAKEGLSALNrllprlnllaDETLADRVEEIREqlDEAEEAKRFVQQHGNAlAQLEPIVS---VLQSDPEQFEQLKQDY 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 247 TQELNMLREQTTGLAA--ELQQQQAE--YED---LMGQKDDLNSQLQESLR----ANSRLLEQLQEIGQEKEQLTQELQE 315
Cdd:PRK04863 945 QQAQQTQRDAKQQAFAltEVVQRRAHfsYEDaaeMLAKNSDLNEKLRQRLEqaeqERTRAREQLRQAQAQLAQYNQVLAS 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 316 ARKSAEKRKAMLDELametlqeksqhKEELGAvrlrhekevLGVRARYERELRelhedKKRQEEELRGQIREEKARTREL 395
Cdd:PRK04863 1025 LKSSYDAKRQMLQEL-----------KQELQD---------LGVPADSGAEER-----ARARRDELHARLSANRSRRNQL 1079
|
330 340 350
....*....|....*....|....*....|..
gi 119571101 396 ETlQQTVEELQaqvhsMDGAkgwfERRLKEAE 427
Cdd:PRK04863 1080 EK-QLTFCEAE-----MDNL----TKKLRKLE 1101
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
304-537 |
2.60e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 304 QEKEQLTQELQEARKSAEKRKAMLDELAmetlQEKSQHKEELGAVRLRhekevlgvRARYERELRELHEDKKRQEEELRG 383
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALK----KEEKALLKQLAALERR--------IAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 384 QIREEKARTRELETLQQTVEELQAQVHSMdGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVR 463
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119571101 464 DQLEQAQEERDCHLKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRS 537
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
154-355 |
2.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 154 IEELQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQrqgerLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALR 233
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEK-----EEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 234 TSLAALEQIQtaKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQEslrANSRLLEQLQEIGQEKEQLTQEL 313
Cdd:COG4717 123 KLLQLLPLYQ--ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 119571101 314 QEARKSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKE 355
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
110-308 |
3.99e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 110 SKQAETSR----LQEELAKLSEKLKKKQESFCRLQTEKETL-----FNDSRNKIEELQQRK---EADHKAQLARTQKLQQ 177
Cdd:COG3206 168 LRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVdlseeAKLLLQQLSELESQLaeaRAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 178 ELEAANQSLAEL-RDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAA-LEQIQTAKTQELNMLRE 255
Cdd:COG3206 248 QLGSGPDALPELlQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 119571101 256 QTTGLAAELQQQQAEYEDLMGQKDDLNsQLQESLRANSR----LLEQLQEIGQEKEQ 308
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAELR-RLEREVEVARElyesLLQRLEEARLAEAL 383
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
87-394 |
4.25e-04 |
|
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: 43.81 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 87 ELKWEMEKEEKRLLWEQLQGLESSKQAETSRL--QEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRK--- 161
Cdd:pfam02463 709 KEELKKLKLEAEELLADRVQEAQDKINEELKLlkQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKlkv 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 162 EADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQ 241
Cdd:pfam02463 789 EEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 242 IQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAE 321
Cdd:pfam02463 869 LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEK 948
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119571101 322 KRKAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRE 394
Cdd:pfam02463 949 EKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
137-407 |
4.53e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 137 CRLQTEK-ETLFNDSRNKIEELQQRKEA--DHKAQLARTQKLQQELEAANQSLAELRDqRQGERLEHAAALRALQDQVSI 213
Cdd:PRK02224 473 DRERVEElEAELEDLEEEVEEVEERLERaeDLVEAEDRIERLEERREDLEELIAERRE-TIEEKRERAEELRERAAELEA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 214 QSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREqttglaaeLQQQQAEYEDLMGQKDDLNSQLQESLRANS 293
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER--------IRTLLAAIADAEDEIERLREKREALAELND 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 294 RLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAMETLQEKSQHKEElgaVRLRHEKEVLGVraryERELRELhed 373
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELRE---ERDDLQAEIGAV----ENELEEL--- 693
|
250 260 270
....*....|....*....|....*....|....
gi 119571101 374 kkrqeEELRGQIREEKARTRELETLQQTVEELQA 407
Cdd:PRK02224 694 -----EELRERREALENRVEALEALYDEAEELES 722
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
117-410 |
5.97e-04 |
|
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: 43.40 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 117 RLQEELAKLSEKLkkkqesfcRLQTEKETLFNDSRNKIEELQQRKEADH---KAQLArtqKLQQELEA----ANQSLAEL 189
Cdd:COG3096 351 RYQEDLEELTERL--------EEQEEVVEEAAEQLAEAEARLEAAEEEVdslKSQLA---DYQQALDVqqtrAIQYQQAV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 190 RDQRQGERLEHAAALRA--LQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNML----REQTTGLAAE 263
Cdd:COG3096 420 QALEKARALCGLPDLTPenAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeveRSQAWQTARE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 264 LQQQQAEYEDLMGQKDDLNSQLQEslransrlLEQLQEIGQEKEQLTQELQearKSAEKRKAMLDELAMetlqeksqHKE 343
Cdd:COG3096 500 LLRRYRSQQALAQRLQQLRAQLAE--------LEQRLRQQQNAERLLEEFC---QRIGQQLDAAEELEE--------LLA 560
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119571101 344 ELGAVRLRHEKEVlgvraryeRELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQAQVH 410
Cdd:COG3096 561 ELEAQLEELEEQA--------AEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSG 619
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
139-542 |
6.04e-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: 43.18 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 139 LQTEKETLFNDSRNKIEELQQRKEAdhkaqlaRTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADA 218
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQD-------RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 219 QEQVEGLLAENNALRTSLAALEQIQTAKTQElnmLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLranSRLLEQ 298
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL---ADLHKR 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 299 LQEIGQEKEQ---LTQELQEARKSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYE--RELRELHED 373
Cdd:pfam15921 390 EKELSLEKEQnkrLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNEslEKVSSLTAQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 374 KKRQEEELRGQIREEKARTRELETLQQTVEELQAQVHSmdgakgwferrlKEAEESLQQQQQEQEEALKQCREQHAAELK 453
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE------------KERAIEATNAEITKLRSRVDLKLQELQHLK 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 454 GKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVKDTVdgqRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNS 533
Cdd:pfam15921 538 NEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMT---QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKD 614
|
....*....
gi 119571101 534 KSRSGLEEL 542
Cdd:pfam15921 615 KKDAKIREL 623
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
290-531 |
1.99e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 290 RANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAmetlqEKSQHKEELGAVRLRHEKEVLGVRARYER--EL 367
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELE-----EVLREINEISSELPELREELEKLEKEVKEleEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 368 RELHEDKKRQEEELRGQIREEKARTRELET----LQQTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEEALKQ 443
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEErieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 444 CR-EQHAAELKGKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVKD-------TVDGQRILEKKGSAALKDLKRQLHLE 515
Cdd:PRK03918 317 SRlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakakKEELERLKKRLTGLTPEKLEKELEEL 396
|
250
....*....|....*.
gi 119571101 516 RKRADKLQERLQDILT 531
Cdd:PRK03918 397 EKAKEEIEEEISKITA 412
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
260-424 |
3.19e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 260 LAAELQQQQAEYEDLMGQKDDLNSQ----LQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDEL----- 330
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKelkeLEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekllq 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 331 AMETLQEKSQHKEELGAV--RLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTR-ELETLQQTVEELQA 407
Cdd:COG4717 127 LLPLYQELEALEAELAELpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQ 206
|
170
....*....|....*..
gi 119571101 408 QVHSMDGAKGWFERRLK 424
Cdd:COG4717 207 RLAELEEELEEAQEELE 223
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
193-337 |
3.32e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.22 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 193 RQGERLEHAAALRALQDQVsiqsADAQEQVEglLAENNaLRTSLAALEQIQTAK-----TQELNMLREQTTGLAAELQQQ 267
Cdd:COG3524 161 AESEELVNQLSERAREDAV----RFAEEEVE--RAEER-LRDAREALLAFRNRNgildpEATAEALLQLIATLEGQLAEL 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119571101 268 QAEYEDLMGQKDDLNSQLQeSLRANSRLLEqlQEIGQEKEQLTQELQE---ARKSAEKRKAMLD-ELAMETLQE 337
Cdd:COG3524 234 EAELAALRSYLSPNSPQVR-QLRRRIAALE--KQIAAERARLTGASGGdslASLLAEYERLELErEFAEKAYTS 304
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
157-387 |
3.64e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 157 LQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSL 236
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 237 AALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEA 316
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119571101 317 RKSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIRE 387
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
84-329 |
3.94e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 84 AEVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESF-----CRLQTEKETLFNDSRNKIEELQ 158
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKKVEQLK 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 159 QRKEAD-HKAQLARTQKLQQELEAANQSLAELRDQRQGERL---EHAAALRALQDQVSIQSADAQEQVEGLLAENNALRT 234
Cdd:PTZ00121 1640 KKEAEEkKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 235 SLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEqlQEIGQEKEQLTQELQ 314
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVD 1797
|
250
....*....|....*
gi 119571101 315 EARKSAEKRKAMLDE 329
Cdd:PTZ00121 1798 KKIKDIFDNFANIIE 1812
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
118-411 |
4.18e-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: 40.39 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 118 LQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQ--RKEADHKAQLartQKLQQELEAAN-QSLAELRDQRQ 194
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnKKIKELEKQL---NQLKSEISDLNnQKEQDWNKELK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 195 GERLEHAAALRALQDQVSiqsaDAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDL 274
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQIS----QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 275 MGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAMETLQEKSQHKeELGAVRLRHEK 354
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK-NLDNTRESLET 468
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 119571101 355 EVlgvrARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQAQVHS 411
Cdd:TIGR04523 469 QL----KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
102-553 |
4.25e-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: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 102 EQLQGLESSKQAETSRLQEELAKLSEKLKKKQeSFCRLQTEKETLFNDSRNKIEELQQRKEADHKAQLART-----QKLQ 176
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQEQLPSWQ-SELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDiagikDKLA 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 177 QELEAANQSLAELRDQRQGERlehaAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQI---QTAKTQELNML 253
Cdd:pfam12128 401 KIREARDRQLAVAEDDLQALE----SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELllqLENFDERIERA 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 254 REQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQeslRANSRLLEQLQEIGQEKEQLTQE----LQEARKSAEKRKAMLDE 329
Cdd:pfam12128 477 REEQEAANAEVERLQSELRQARKRRDQASEALR---QASRRLEERQSALDELELQLFPQagtlLHFLRKEAPDWEQSIGK 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 330 LAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYER----ELRELHEDKKRQEEELRGQIREEKARTRELET-LQQTVEE 404
Cdd:pfam12128 554 VISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRidvpEWAASEEELRERLDKAEEALQSAREKQAAAEEqLVQANGE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 405 LQAQVHSMDGAKgwfeRRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQL-------EQAQEERDCHL 477
Cdd:pfam12128 634 LEKASREETFAR----TALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLkqldkkhQAWLEEQKEQK 709
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119571101 478 KTISSLKQEVKDTVDGQRilekkgSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRSGLEELVLSEMNSPSRT 553
Cdd:pfam12128 710 REARTEKQAYWQVVEGAL------DAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRT 779
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
70-384 |
4.26e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.13 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 70 PGGPAPTVLAPMPLAEVELKWEMEKEEKrllwEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFND 149
Cdd:pfam09731 79 SKEPKEEKKQVKIPRQSGVSSEVAEEEK----EATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 150 SRNKIEE-LQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAE 228
Cdd:pfam09731 155 AIQAVKAhTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 229 NNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQqqAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQeigqekEQ 308
Cdd:pfam09731 235 VEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIP--VLKEDNLLSNDDLNSLIAHAHREIDQLSKKLA------EL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 309 LTQELQEARKSAEKRKAMLDELAMETLQEKSQHK-EELGAVRLRHEKEVLGVRARYERELR-------ELHEDKKRQEEE 380
Cdd:pfam09731 307 KKREEKHIERALEKQKEELDKLAEELSARLEEVRaADEAQLRLEFEREREEIRESYEEKLRtelerqaEAHEEHLKDVLV 386
|
....
gi 119571101 381 LRGQ 384
Cdd:pfam09731 387 EQEI 390
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
109-241 |
4.57e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 109 SSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfndsrnkieelqqrkeadhKAQLARTQKLQQELEAANQSLAE 188
Cdd:PRK09039 49 SGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANL-------------------RASLSAAEAERSRLQALLAELAG 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 119571101 189 LRDQRQGERLEHAAALRALQDQvsiqSADAQEQVEGLLAENNALRTSLAALEQ 241
Cdd:PRK09039 110 AGAAAEGRAGELAQELDSEKQV----SARALAQVELLNQQIAALRRQLAALEA 158
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
83-239 |
4.59e-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: 40.32 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 83 LAEVELKWEMEKEEKRLLWE--QLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQR 160
Cdd:COG3096 521 LAELEQRLRQQQNAERLLEEfcQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101 161 KEADHKAQlARTQKLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAAL 239
Cdd:COG3096 601 APAWLAAQ-DALERLREQSGEALADSQEVTAAMQ-QLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLAL 677
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
216-345 |
5.05e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 216 ADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYED-----LMGQKDDLNSQLQESLR 290
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeedklLEEAEKEAQQAIKEAKK 584
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 119571101 291 ANSRLLEQLQEIGQEK--EQLTQELQEARKSAEKRKamldELAMETLQEKSQHKEEL 345
Cdd:PRK00409 585 EADEIIKELRQLQKGGyaSVKAHELIEARKRLNKAN----EKKEKKKKKQKEKQEEL 637
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
109-325 |
7.72e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 109 SSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKetlfNDSRNKIEELQQRKEadhkaqlartqKLQQELEAANQSLAE 188
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEY----NELQAELEALQAEID-----------KLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 189 LRDQRqGERLEHAAALRALQDQVSI--QSADAQEQVEGLLAENNALRTSLAALEQIQTAKtQELNMLREQTTGLAAELQQ 266
Cdd:COG3883 84 RREEL-GERARALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101 267 QQAEYEDlmgQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKA 325
Cdd:COG3883 162 LKAELEA---AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| delta-PiCoV-like_Spike_SD1-2_S1-S2_S2 |
cd22374 |
SD-1 and SD-2 subdomains, the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) ... |
223-323 |
7.77e-03 |
|
SD-1 and SD-2 subdomains, the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) glycoprotein from Pigeon coronavirus UAE-HKU29, and related avian deltacoronaviruses; This group contains the SD-1 and SD-2 subdomains of the S1 subunit C-terminal domain (C-domain), the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) glycoprotein from Pigeon coronavirus UAE-HKU29, and related avian deltacoronaviruses including Falcon coronavirus UAE-HKU27, Magpie-robin coronavirus HKU18, Sparrow coronavirus HKU17, and Night heron coronavirus HKU19. The CoV S protein is an envelope glycoprotein that plays a very important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains the coronavirus fusion machinery and is primarily alpha-helical. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the (C-domain. The S1 C-domain also contains two subdomains (SD-1 and SD-2), which connect the S1 and S2 subunits. Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs, including SARS-CoV-2, SARS-CoV and MERS-CoV use the C-domain to bind their receptors. The S2 subunit comprises the fusion peptide (FP), a second proteolytic site (S2'), followed by an internal fusion peptide (IFP) and two heptad-repeat domains (HR1 and HR2) preceding the transmembrane domain (TM). After binding of the S1 subunit RBD on the virion to its receptor on the target cell, the HR1 and HR2 domains interact with each other to form a six-helix bundle (6-HB) fusion core, bringing viral and cellular membranes into close proximity for fusion and infection. In order to catalyze the membrane fusion reaction, CoV S needs to be primed through cleavage at the S1/S2 and S2' sites. In the case of human-infecting coronaviruses such as SARS-CoV-2, HCoV-OC43, MERS-CoV, and HCoV-KU1, the spike protein contains an insertion of (R/K)-(2X)n-(R/K) (furin cleavage motif) at the S1/S2 site, which is absent in SARS-CoV and other SARS-related coronaviruses, as well as Ro-BatCoV HKU9. The region modeled in this cd (SD-1 and SD-2, the S1/S2 cleavage region, and the S2 fusion subunit) plays an essential role in viral entry by initiating fusion of the viral and cellular membranes.
Pssm-ID: 411961 [Multi-domain] Cd Length: 739 Bit Score: 39.48 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 223 EGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRL------- 295
Cdd:cd22374 395 EGLSQVSGAITTVANALTKIQTVVNSQGQALATLTEQLANNFQAISASIADIYNRLNQLEADAQVDRLITGRLaalnafv 474
|
90 100 110
....*....|....*....|....*....|.
gi 119571101 296 ---LEQLQEIGQEKEQLTQELQEARKSAEKR 323
Cdd:cd22374 475 tqtLSKLAEVRQARQLALDKINECVKSQSSR 505
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
240-329 |
9.00e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.55 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 240 EQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKS 319
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220
|
90
....*....|...
gi 119571101 320 AEKRKAM---LDE 329
Cdd:PRK11448 221 ITDQAAKrleLSE 233
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
83-528 |
9.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 83 LAEVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQ--EELAKLSEKLKKKQESFCRLQTEKETlFNDSRNKIEELqqr 160
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEE-YLDELREIEKR--- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 161 kEADHKAQLARTQKLQQELEAANQSLAELRD-----QRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENnaLRTS 235
Cdd:PRK03918 316 -LSRLEEEINGIEERIKELEEKEERLEELKKklkelEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 236 LAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDD---LNSQLQESLRAN--SRLLEQLQEIGQEKEQLT 310
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvCGRELTEEHRKEllEEYTAELKRIEKELKEIE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 311 QELQEARKSAEK-RKAMLDELAMETLQEKSQHKEELgavrlrhEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEK 389
Cdd:PRK03918 473 EKERKLRKELRElEKVLKKESELIKLKELAEQLKEL-------EEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 390 ARTRELETLQQTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQH------AAELKGKEEELQDVR 463
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYlelkdaEKELEREEKELKKLE 625
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119571101 464 DQLEQAQEERDCHLKTISSLKQEVKDTvdgQRILEKKGSAALKDLKRQLHLERKRADKLQERLQD 528
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEEL---EKKYSEEEYEELREEYLELSRELAGLRAELEELEK 687
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
231-408 |
9.67e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.27 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 231 ALRTSLAALEQIQTA--KTQELNMLREQTTGLAAELQQQQAEYED------LMGQKDDLNsqlQESLRANSRLLEQLQEI 302
Cdd:PRK10929 49 ALQSALNWLEERKGSleRAKQYQQVIDNFPKLSAELRQQLNNERDeprsvpPNMSTDALE---QEILQVSSQLLEKSRQA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 303 GQEKE----------QLTQELQEARK---------------------------SAEK--RKAMLDELAMETLQekSQHKE 343
Cdd:PRK10929 126 QQEQDrareisdslsQLPQQQTEARRqlneierrlqtlgtpntplaqaqltalQAESaaLKALVDELELAQLS--ANNRQ 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119571101 344 ELgaVRLRHEkevlgvraRYERElrelHEDKKRQEEELRGQIREEkaRTRELETLQQTVEELQAQ 408
Cdd:PRK10929 204 EL--ARLRSE--------LAKKR----SQQLDAYLQALRNQLNSQ--RQREAERALESTELLAEQ 252
|
|
|