|
Name |
Accession |
Description |
Interval |
E-value |
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
245-551 |
1.48e-132 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 388.94 E-value: 1.48e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 245 CDMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEE 324
Cdd:pfam09311 1 CDMCSNYEKQLQAIQEQEAETRDQVKKLQEMLRQANDQLEKTMKDKKELEDKMNQLSEETSNQVSTLAKRNQKSETLLDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 325 LQQGLSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDFILPDTTEALRELVLKYREDIINVR 404
Cdd:pfam09311 81 LQQAFSQAKRNFQDQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHVSLQQAEKFDMPDTVQELQELVLKYREELIEVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 405 TAADHVEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESL 484
Cdd:pfam09311 161 TAADHMEEKLKAEILFLKEQIQAEQCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQLENGLTEKIRQLEDL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217314695 485 QEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQAD 551
Cdd:pfam09311 241 QTTKGSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQAD 307
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
11-207 |
6.54e-71 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 235.77 E-value: 6.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 11 KEDDEQQRLNKRKDHKKADVEEEIKIPVVCALTQEESSAQLSNEEktpfkikitdrssypevttnilEHLDSTRGSVHSL 90
Cdd:pfam03528 313 QEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPLSNVE----------------------EQINSAHGSVHSL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 91 DAGLLLPSGDPFSKSDnDMFKDGLRRAQSTDSLGTSGSLQSKALGYNYKAKSAGNLDESDFGPLVGADSVSENFDTASLG 170
Cdd:pfam03528 371 DTDVVLGAGDSFNKQE-DPFKEGLRRAQSTDSLGSSSSLQHKFLGHNQKAKSAGNLDESDFGPLVGADSVSENFDTSSLG 449
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217314695 171 SLQMPSGFMLTKDQERAIKAMTPEQEETASLLSSVTQ 207
Cdd:pfam03528 450 SLKMPSGFMLTKDQEKAIKAMTPEQEETASLLSSVTQ 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
252-533 |
2.13e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 252 EKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDsSHQISALVLRAQASEILLEELQQGLSQ 331
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 332 AKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKhslhvsLQQAEdfilpdttEALRELVLKYREDIINVRTAADHVE 411
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEE------LEEAE--------AELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 412 EKLKAEILFLKEQIQAEQcLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISL 491
Cdd:COG1196 383 ELAEELLEALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2217314695 492 EEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDF 533
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-561 |
4.64e-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: 65.85 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 252 EKQLQGIQIQEAetRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSsEDSSHQISALVLRAQASEILLEELQQGLSQ 331
Cdd:TIGR02168 226 ELALLVLRLEEL--REELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 332 AKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKhslhVSLQQAEDFILPDTTEALRELVLKYREDIINVRTAADHVE 411
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEE----LAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 412 EKL---KAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKgqLESTLREKSQQLESLQEIK 488
Cdd:TIGR02168 379 EQLetlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEEL 456
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217314695 489 ISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTL-QVQLERIRQADSLERIRAILN 561
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkALLKNQSGLSGILGVLSELIS 530
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
263-503 |
2.76e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 263 AETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEdsshQISALVLRAQASEILLEELQQGLSQAKRDVQEQMAV 342
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 343 LMQSREQVSEELVRLQKdndslQGKHSLHVSLQQAEDFilpdtTEALRelVLKYREDIINVRTAADHVEEKLKAEILFLK 422
Cdd:COG4942 99 LEAQKEELAELLRALYR-----LGRQPPLALLLSPEDF-----LDAVR--RLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 423 EQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEEQLKKETAAK 502
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
.
gi 2217314695 503 A 503
Cdd:COG4942 247 G 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-550 |
6.31e-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: 58.91 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 252 EKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDsshqisalVLRAQASEILLEELQQGLSQ 331
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD--------LARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 332 AKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKhslhvsLQQAEDfILPDTTEALRELVLKYREDIINVRTAADhVE 411
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ------IEQLKE-ELKALREALDELRAELTLLNEEAANLRE-RL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 412 EKLKAEILFLKEQIQAEQCLKENLEET---LQLEIENCKEEIASISSlkaELERIKVEKGQLESTLREKSQQLESL---- 484
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDiesLAAEIEELEELIEELES---ELEALLNERASLEEALALLRSELEELseel 903
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217314695 485 -------QEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRL----QTELDVSEQVQRDFVKLSQTLQVQLERIRQA 550
Cdd:TIGR02168 904 releskrSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
322-571 |
1.39e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 322 LEELQQGLSQAK-RDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKhslhvsLQQAEDfilpdTTEALRELVLKYREDI 400
Cdd:COG1196 222 LKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAE------LEELRL-----ELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 401 INVRTAAdhveEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQ 480
Cdd:COG1196 291 YELLAEL----ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 481 LESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAIL 560
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250
....*....|.
gi 2217314695 561 NDTKLTDINQL 571
Cdd:COG1196 447 AAEEEAELEEE 457
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
252-552 |
1.86e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 252 EKQLQGIQIQEAETRDQVKKLQlmlRQANDQLE--KTMKDKQELEDFIKqssedsSHQISALVLRAQASEILLEELQQGL 329
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLR---REREKAERyqALLKEKREYEGYEL------LKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 330 SQAKRDVQE---QMAVLMQSREQVSEELVRLqKDNDSLQGK---HSLHVSLQQAEDFI--LPDTTEALRELVLKYREDII 401
Cdd:TIGR02169 254 EKLTEEISElekRLEEIEQLLEELNKKIKDL-GEEEQLRVKekiGELEAEIASLERSIaeKERELEDAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 402 NVRTAADHVEEKLKAEILfLKEQIQAEQCLKENLEETLQLEIENCKEEIAS----ISSLKAELERIKVEKGQLESTLR-- 475
Cdd:TIGR02169 333 KLLAEIEELEREIEEERK-RRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdeLKDYREKLEKLKREINELKRELDrl 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217314695 476 --EKSQQLESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADS 552
Cdd:TIGR02169 412 qeELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-536 |
5.31e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 184 QERAIKAMTPEQEETASLLSSVTQGMESAYVSPSGYRLVSE---TEWNLLQKEVHNAGNKLGRRCDMCSNYEKQLQGIQI 260
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 261 QEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALV-LRAQASE-------------------I 320
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDeLRAELTLlneeaanlrerleslerriA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 321 LLEELQQGLSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQ---GKHSLHVSLQQAEDFILPDTTEALRELVLKYR 397
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnerASLEEALALLRSELEELSEELRELESKRSELR 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 398 EDIINVRTAADHVE---EKLKAEILFLKEQIQAEQCLKENLEETLQLEIEnckeeiASISSLKAELERIKVEKGQLESTL 474
Cdd:TIGR02168 915 RELEELREKLAQLElrlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE------DDEEEARRRLKRLENKIKELGPVN 988
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217314695 475 REKSQQLESLQEIKISLEEQLKKETAAKATVEQLMfEEKNKAQRLQTeLDVSEQVQRDFVKL 536
Cdd:TIGR02168 989 LAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAI-EEIDREARERF-KDTFDQVNENFQRV 1048
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-565 |
3.61e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 304 SSHQISALVLRAQASEILLEELQQGLSQAkRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKhslhVSLQQAEDFILp 383
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKI-AELEKALAELRKELEELEEELEQLRKELEELSRQ----ISALRKDLARL- 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 384 dttEALRELVLKYREDIINVRTAADHVEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERI 463
Cdd:TIGR02168 739 ---EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 464 KVE-------KGQLESTLREKSQQLESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQ----VQRD 532
Cdd:TIGR02168 816 NEEaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalalLRSE 895
|
250 260 270
....*....|....*....|....*....|....
gi 2217314695 533 FVKLSQTLQVQLERIRQA-DSLERIRAILNDTKL 565
Cdd:TIGR02168 896 LEELSEELRELESKRSELrRELEELREKLAQLEL 929
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
311-558 |
2.22e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 311 LVLRAQASEILLEELQQGLSQakrdVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKhslhVSLQQAEdfiLPDTTEALR 390
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQ----LQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARR---IRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 391 ELvlkyREDIINVRTAADHVEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQL 470
Cdd:COG4942 80 AL----EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 471 ESTLREKSQQLESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQA 550
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*...
gi 2217314695 551 DSLERIRA 558
Cdd:COG4942 236 AAAAAERT 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
335-558 |
3.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 335 DVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEdfilpdttealrELVLKYREDIINVRTAADHVEEkl 414
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL------------QRLAEYSWDEIDVASAEREIAE-- 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 415 kaeilfLKEQIqaEQCLKENLE-ETLQLEIENCKEEIAsisSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEE 493
Cdd:COG4913 673 ------LEAEL--ERLDASSDDlAALEEQLEELEAELE---ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217314695 494 QLKKETAAKAtveqlmfeeknkAQRLQTEL--DVSEQVQRDFVKLSQTLQVQLERIRQAdsLERIRA 558
Cdd:COG4913 742 LARLELRALL------------EERFAAALgdAVERELRENLEERIDALRARLNRAEEE--LERAMR 794
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
252-526 |
3.48e-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: 46.98 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 252 EKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEdsshqisalvlRAQASEILLEELQQGLSQ 331
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE-----------RLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 332 AKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLqgKHSLHVSLQQAEDFIlpDTTEALRELVLKYREDIINVRTAADHVE 411
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKL--EEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 412 EK----LKAEILFLKEQIQAEQCLKENLE---ETLQLEIENCKEEI-----------ASISSLKAELERIKVEKGQLEST 473
Cdd:TIGR02169 832 EKeiqeLQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALrdlesrlgdlkKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217314695 474 LREKSQQLESLQEIKISLEEQLKKETAAKAT----VEQLMFEEKNKAQRLQTELDVS 526
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeiPEEELSLEDVQAELQRVEEEIR 968
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
252-507 |
6.54e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 252 EKQLQGIQIQEAETRDQVkklqlmlrqanDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEELQQGLSQ 331
Cdd:COG1196 280 ELELEEAQAEEYELLAEL-----------ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 332 AKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDFILPDTTEALRELvlkyrEDIINVRTAADHVE 411
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE-----EALLERLERLEEEL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 412 EKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISL 491
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
250
....*....|....*.
gi 2217314695 492 EEQLKKETAAKATVEQ 507
Cdd:COG1196 504 EGFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
412-566 |
7.85e-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: 45.82 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 412 EKLKAEILFLKEQI-QAEQCLKENLEETLQLEIENCK------EEIASISSLKAELERIKVEKGQLESTLREKSQQLESL 484
Cdd:TIGR02168 680 EELEEKIEELEEKIaELEKALAELRKELEELEEELEQlrkeleELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 485 QEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEqvqRDFVKLSQtlQVQLERIRQADSLERIRAILNDTK 564
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR---EALDELRA--ELTLLNEEAANLRERLESLERRIA 834
|
..
gi 2217314695 565 LT 566
Cdd:TIGR02168 835 AT 836
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
415-547 |
1.38e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.05 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 415 KAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIA-------SISSLKAELERIKVEKGQLEStlreksqQLESLQEI 487
Cdd:pfam05911 680 TEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSqlqeseqLIAELRSELASLKESNSLAET-------QLKCMAES 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 488 KISLEEQLkkeTAAKATVEQLmfeeKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERI 547
Cdd:pfam05911 753 YEDLETRL---TELEAELNEL----RQKFEALEVELEEEKNCHEELEAKCLELQEQLERN 805
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
338-552 |
2.24e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 338 EQMAVLMQSREQVSEELVRLQKDNDSLQgkhSLHvslQQAEDFI--------LPDTTEALRELVLKYREdIINVRTAADH 409
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQKLQ---RLH---QAFSRFIgshlavafEADPEAELRQLNRRRVE-LERALADHES 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 410 VEEKLKAEILFLKEQIQA-EQCLKEN---LEETLQLEIENCKEEIASISSLKAELERIKVEKGQLE---STLREKSQQLE 482
Cdd:PRK04863 859 QEQQQRSQLEQAKEGLSAlNRLLPRLnllADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEpivSVLQSDPEQFE 938
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217314695 483 SLQEIKISLEEQLKKETAAKATVEQLM-----FEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADS 552
Cdd:PRK04863 939 QLKQDYQQAQQTQRDAKQQAFALTEVVqrrahFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQA 1013
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
333-556 |
2.76e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 333 KRDVQEQMAVLMQSREQVSEELVRLQKDndslqgkhslhvsLQQAEdfilpdttEALRELvlKYREDIINVRTAADHVEE 412
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKE-------------LEEAE--------AALEEF--RQKNGLVDLSEEAKLLLQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 413 KLK---AEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIAS--ISSLKAELERIKVEKGQLESTLREKSQQLESLQEI 487
Cdd:COG3206 220 QLSeleSQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 488 KISLEEQLKKETA-AKATVEQLMFEEKNKAQRLQTELdvsEQVQRDFVKLSQTLQVQLERIRQADSLERI 556
Cdd:COG3206 300 IAALRAQLQQEAQrILASLEAELEALQAREASLQAQL---AQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
255-573 |
2.85e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 255 LQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEdsshqisalvLRAQASE-ILLEELQQGLSQAK 333
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE----------LKEKAEEyIKLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 334 RDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQqaedfilpDTTEALRELVLKYrEDIINVRTAADHVEEK 413
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE--------KRLEELEERHELY-EEAKAKKEELERLKKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 414 LKAEIlflKEQIQAEQCLKENLEETLQLEIENCKEEIAS----ISSLKAELERIKVEKGQLESTLREksqqleslqeiki 489
Cdd:PRK03918 381 LTGLT---PEKLEKELEELEKAKEEIEEEISKITARIGElkkeIKELKKAIEELKKAKGKCPVCGRE------------- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 490 sLEEQLKKETAAKATVEQlmfeeKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAILNDTKLTDIN 569
Cdd:PRK03918 445 -LTEEHRKELLEEYTAEL-----KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE 518
|
....
gi 2217314695 570 QLPE 573
Cdd:PRK03918 519 ELEK 522
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
316-541 |
4.32e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 316 QASEILLEELQQGLsqakRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGK-HSLHVSLQQAEDFILPDT-----TEAL 389
Cdd:PLN02939 124 QLSDFQLEDLVGMI----QNAEKNILLLNQARLQALEDLEKILTEKEALQGKiNILEMRLSETDARIKLAAqekihVEIL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 390 RELVLKYREDIINVRTAADHVEEKLKAEILFLKEqiqaeqclkENLeeTLQLEIENCKEEIASISSLKAELERIKVEKGQ 469
Cdd:PLN02939 200 EEQLEKLRNELLIRGATEGLCVHSLSKELDVLKE---------ENM--LLKDDIQFLKAELIEVAETEERVFKLEKERSL 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217314695 470 LESTLREKSQQLESLQEiKISLEEQLKKET--AAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQ 541
Cdd:PLN02939 269 LDASLRELESKFIVAQE-DVSKLSPLQYDCwwEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLK 341
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
261-566 |
4.70e-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: 43.42 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 261 QEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEELQQGLSQAKRDVQEQM 340
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 341 AVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDfilpdtTEALRELVLKYREDIINVRTAADHVEEKLKAEILF 420
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE------EELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 421 LKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQqlESLQEIKISLEEQLKKETA 500
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA--AKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217314695 501 AKATVEQ-----LMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQ-LERIRQADSLERIRAILNDTKLT 566
Cdd:pfam02463 409 LLLELARqledlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQeLKLLKDELELKKSEDLLKETQLV 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
386-570 |
4.72e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 386 TEALRELVLKYREdiINVRTAADHVEEkLKAEILFLKEQIQAEQCLKENLE----------ETLQLEIENCKEEIAS--- 452
Cdd:TIGR02168 212 AERYKELKAELRE--LELALLVLRLEE-LREELEELQEELKEAEEELEELTaelqeleeklEELRLEVSELEEEIEElqk 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 453 --------ISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELD 524
Cdd:TIGR02168 289 elyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217314695 525 VSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAILNDTKLTDINQ 570
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
146-369 |
9.04e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 146 LDESDFGPLvgADSVSENFDTASLGSLQMpsgfmltKDQERAIKAMTPEQEETASLLSSVTQGMESAYVSPSGYRLVSET 225
Cdd:COG4913 218 LEEPDTFEA--ADALVEHFDDLERAHEAL-------EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 226 EWNLLQKEVHNAGNKLGRRcdmcsnyEKQLQGIQIQEAETRDQVKKLQLMLRQAN----DQLEKTMKDKQELEDFIKQSS 301
Cdd:COG4913 289 RLELLEAELEELRAELARL-------EAELERLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217314695 302 EDSSHQISALVLRAQASEILLEELQ-------QGLSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHS 369
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRaeaaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
261-531 |
9.14e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 261 QEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEELQQGLSQAKRDVQEQm 340
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK- 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 341 avlmQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEdfilpdttealrelvlKYREDIINVRTAADHVEEKLKAEILF 420
Cdd:PTZ00121 1391 ----KKADEAKKKAEEDKKKADELKKAAAAKKKADEAK----------------KKAEEKKKADEAKKKAEEAKKADEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 421 LK--EQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEEQLKKE 498
Cdd:PTZ00121 1451 KKaeEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
250 260 270
....*....|....*....|....*....|....*
gi 2217314695 499 TAAKATVEQLMFEEKNKAQRLQT--ELDVSEQVQR 531
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKaeELKKAEEKKK 1565
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
246-567 |
1.58e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 246 DMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEdsshQISALVLRAQASEILLEEL 325
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKE----QNKRLWDRDTGNSITIDHL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 326 QQGLSQAKRDVQEQMAVLM----QSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDFI-------------------- 381
Cdd:pfam15921 418 RRELDDRNMEVQRLEALLKamksECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLrkvveeltakkmtlessert 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 382 LPDTTEALRE---LVLKYREDIINVRTAAD-----------------HVEEKLKAEILFLKEQIQAEQCLKENLEETLQL 441
Cdd:pfam15921 498 VSDLTASLQEkerAIEATNAEITKLRSRVDlklqelqhlknegdhlrNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 442 -----------EIENCKEEiASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISL----EEQLKKETAAKATVE 506
Cdd:pfam15921 578 vgqhgrtagamQVEKAQLE-KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERD 656
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217314695 507 QLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQ-----ADSLERIRAILNDTKLTD 567
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqlksaQSELEQTRNTLKSMEGSD 722
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
252-440 |
1.63e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 252 EKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEELQQGLSQ 331
Cdd:COG4942 54 LKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 332 AKRDVQeQMAVLMQSREQVSEELVRLQKDNDSLQgkhslhVSLQQAEdfilpDTTEALRELVLKYREDIINVRTAADHVE 411
Cdd:COG4942 134 AVRRLQ-YLKYLAPARREQAEELRADLAELAALR------AELEAER-----AELEALLAELEEERAALEALKAERQKLL 201
|
170 180
....*....|....*....|....*....
gi 2217314695 412 EKLKAEILFLKEQIQAEQCLKENLEETLQ 440
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
336-564 |
3.92e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 336 VQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDFILPDTTEALRelvlKYREDIINVRTAADHVEEKLK 415
Cdd:TIGR02169 182 VEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE----RQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 416 AEILFLKEQI-QAEQCLKENLEETLQL---EIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISL 491
Cdd:TIGR02169 258 EEISELEKRLeEIEQLLEELNKKIKDLgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217314695 492 EEQLKKE-TAAKATVEQLMFEEKNKAQRLQTEL----DVSEQVQRDFVKLSQtLQVQLER-IRQADSLERIRAILNDTK 564
Cdd:TIGR02169 338 IEELEREiEEERKRRDKLTEEYAELKEELEDLRaeleEVDKEFAETRDELKD-YREKLEKlKREINELKRELDRLQEEL 415
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
260-500 |
4.77e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 260 IQEAETRDQVKKLQLMLrqanDQLEKTMKDKQELEDFIKQSSEdsshQISALVLRAQASEILLEELQQGLSQAKRDVQEQ 339
Cdd:PRK03918 141 LESDESREKVVRQILGL----DDYENAYKNLGEVIKEIKRRIE----RLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 340 MAVLMQSREQ---VSEELVRLQKDNDSLQGKHSLHVSLQQ---AEDFILPDTTEALRELVLKYREDIINVRTAADHVEEK 413
Cdd:PRK03918 213 SSELPELREElekLEKEVKELEELKEEIEELEKELESLEGskrKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 414 LKAEIL--FLKEQIQAEQCLKENLEeTLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISL 491
Cdd:PRK03918 293 EEYIKLseFYEEYLDELREIEKRLS-RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK 371
|
250
....*....|.
gi 2217314695 492 E--EQLKKETA 500
Cdd:PRK03918 372 EelERLKKRLT 382
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
382-550 |
5.10e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 382 LPDTTEALRELVLKYREDIINVRTAAdhveEKLKAEILFLKEQIQAEQCLKENLEEtLQLEIENCKEeiasISSLKAELE 461
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTEL----EDLEKEIKRLELEIEEVEARIKKYEE-QLGNVRNNKE----YEALQKEIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 462 RIKVEKGQLESTLREKSQQLESLQEIKISLEEQLKKetaAKATVEQLMFEEKNKAQRLQTELD-VSEQVQRDFVKLSQTL 540
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAE---LEAELEEKKAELDEELAELEAELEeLEAEREELAAKIPPEL 176
|
170
....*....|
gi 2217314695 541 QVQLERIRQA 550
Cdd:COG1579 177 LALYERIRKR 186
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
293-530 |
6.73e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 293 LEDFIKQSSEDSSHQISALVLRAQASEILLEELQQGLSQAKR-----DVQEQMAVLMQSREQVSEELVRLQKDNDSLQGK 367
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 368 HSLHVSLQQAEDFILPDTTEAlrELVLKYREDIINVRTAADHVEEKLKAE---ILFLKEQIQAeqclkenLEETLQLEIE 444
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAA-------LRAQLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 445 nckeeiASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEEQLKKETAAKATVEQLMfeeknkaQRLQtELD 524
Cdd:COG3206 313 ------RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL-------QRLE-EAR 378
|
....*.
gi 2217314695 525 VSEQVQ 530
Cdd:COG3206 379 LAEALT 384
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
230-573 |
8.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 230 LQKEVHNAGNKLGRRCDMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDfiKQSSEDSSHQIS 309
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE--ELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 310 ALVLRAQASEILLEELQQGLSQAKRDVQEqMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHvSLQQAEDFIlpDTTEAL 389
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEE-LRELEEELEELEAELAELQEELEELLEQLSLA-TEEELQDLA--EELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 390 RELVLKYREDIINVRTAADHVEEKLKAeilfLKEQIQAEQCLKENLEETLQLEIENckeEIASISSLKAELERIKVEKG- 468
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQ----LENELEAAALEERLKEARLLLLIAA---ALLALLGLGGSLLSLILTIAg 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 469 -----------QLESTLREKSQQLESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLS 537
Cdd:COG4717 278 vlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357
|
330 340 350
....*....|....*....|....*....|....*.
gi 2217314695 538 QtlqvQLERIRQADSLERIRAILNDTKLTDINQLPE 573
Cdd:COG4717 358 E----LEEELQLEELEQEIAALLAEAGVEDEEELRA 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
276-507 |
8.48e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 276 LRQANDQLEKTMKDKQELEDFIKQSSEdsshQISALVLRAQASEILLEELQQGLSQAKRDVQEQMAVLMQSREQVSEELV 355
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQA----ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314695 356 RLQKDNDSLqgkhSLHVSLQQAEDFilpdttealrelvlkyrEDIINVRTAADHVEEKLKAEILFLKEQIQAEQCLKENL 435
Cdd:COG3883 94 ALYRSGGSV----SYLDVLLGSESF-----------------SDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217314695 436 EETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEEQLKKETAAKATVEQ 507
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| |
