|
Name |
Accession |
Description |
Interval |
E-value |
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
223-529 |
2.16e-130 |
|
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: 382.78 E-value: 2.16e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 223 CDMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEE 302
Cdd:pfam09311 1 CDMCSNYEKQLQAIQEQEAETRDQVKKLQEMLRQANDQLEKTMKDKKELEDKMNQLSEETSNQVSTLAKRNQKSETLLDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 303 LQQGLSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDFILPDTTEALRELVLKYREDIINVR 382
Cdd:pfam09311 81 LQQAFSQAKRNFQDQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHVSLQQAEKFDMPDTVQELQELVLKYREELIEVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 383 TAADHVEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESL 462
Cdd:pfam09311 161 TAADHMEEKLKAEILFLKEQIQAEQCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQLENGLTEKIRQLEDL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217314697 463 QEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQAD 529
Cdd:pfam09311 241 QTTKGSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQAD 307
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
11-185 |
9.28e-75 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 245.40 E-value: 9.28e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 11 KEDDEQQRLNKRKDHKKADVEEEIKIPVVCALTQEESSAQLSNEEEHLDSTRGSVHSLDAGLLLPSGDPFSKSDnDMFKD 90
Cdd:pfam03528 313 QEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPLSNVEEQINSAHGSVHSLDTDVVLGAGDSFNKQE-DPFKE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 91 GLRRAQSTDSLGTSGSLQSKALGYNYKAKSAGNLDESDFGPLVGADSVSENFDTASLGSLQMPSGFMLTKDQERAIKAMT 170
Cdd:pfam03528 392 GLRRAQSTDSLGSSSSLQHKFLGHNQKAKSAGNLDESDFGPLVGADSVSENFDTSSLGSLKMPSGFMLTKDQEKAIKAMT 471
|
170
....*....|....*
gi 2217314697 171 PEQEETASLLSSVTQ 185
Cdd:pfam03528 472 PEQEETASLLSSVTQ 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
230-511 |
4.88e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 230 EKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDsSHQISALVLRAQASEILLEELQQGLSQ 309
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 310 AKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKhslhvsLQQAEdfilpdttEALRELVLKYREDIINVRTAADHVE 389
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEE------LEEAE--------AELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 390 EKLKAEILFLKEQIQAEQcLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISL 469
Cdd:COG1196 383 ELAEELLEALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2217314697 470 EEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDF 511
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
229-518 |
9.50e-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: 64.69 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 229 YEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIkQSSEDSSHQISALVLRAQASEILLEELQQGLS 308
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 309 QAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDFILPDTTEALRELvlkyREDIINVRTAADHV 388
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL----EEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 389 EEKLkaeilflkEQIQAEQCLKENLEETLQLEIENCKEEIasiSSLKAELERIKVEKgqLESTLREKSQQLESLQEIKIS 468
Cdd:TIGR02168 392 ELQI--------ASLNNEIERLEARLERLEDRRERLQQEI---EELLKKLEEAELKE--LQAELEELEEELEELQEELER 458
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2217314697 469 LEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTL 518
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
241-481 |
4.87e-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: 58.24 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 241 AETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEdsshQISALVLRAQASEILLEELQQGLSQAKRDVQEQMAV 320
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 321 LMQSREQVSEELVRLQKdndslQGKHSLHVSLQQAEDFilpdtTEALRelVLKYREDIINVRTAADHVEEKLKAEILFLK 400
Cdd:COG4942 99 LEAQKEELAELLRALYR-----LGRQPPLALLLSPEDF-----LDAVR--RLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 401 EQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEEQLKKETAAK 480
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
.
gi 2217314697 481 A 481
Cdd:COG4942 247 G 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-528 |
1.43e-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: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 230 EKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDsshqisalVLRAQASEILLEELQQGLSQ 309
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD--------LARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 310 AKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKhslhvsLQQAEDfILPDTTEALRELVLKYREDIINVRTAADhVE 389
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ------IEQLKE-ELKALREALDELRAELTLLNEEAANLRE-RL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 390 EKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESL------- 462
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELseelrel 906
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217314697 463 ----QEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRL----QTELDVSEQVQRDFVKLSQTLQVQLERIRQA 528
Cdd:TIGR02168 907 eskrSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
300-549 |
2.78e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 300 LEELQQGLSQAK-RDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKhslhvsLQQAEDfilpdTTEALRELVLKYREDI 378
Cdd:COG1196 222 LKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAE------LEELRL-----ELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 379 INVRTAAdhveEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQ 458
Cdd:COG1196 291 YELLAEL----ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 459 LESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAIL 538
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250
....*....|.
gi 2217314697 539 NDTKLTDINQL 549
Cdd:COG1196 447 AAEEEAELEEE 457
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
230-530 |
3.38e-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: 53.53 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 230 EKQLQGIQIQEAETRDQVKKLQlmlRQANDQLE--KTMKDKQELEDFIKQSS-EDSSHQISALVLRAQASEILLEELQQG 306
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLR---REREKAERyqALLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 307 LSQAKRDVQEQMAVLMQSREQV----SEELVRLQKDndslqgKHSLHVSLQQAEDFI--LPDTTEALRELVLKYREDIIN 380
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIkdlgEEEQLRVKEK------IGELEAEIASLERSIaeKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 381 VRTAADHVEEKLKAEILfLKEQIQAEQCLKENLEETLQLEIENCKEEIAS----ISSLKAELERIKVEKGQLESTLR--- 453
Cdd:TIGR02169 334 LLAEIEELEREIEEERK-RRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdeLKDYREKLEKLKREINELKRELDrlq 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217314697 454 -EKSQQLESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADS 530
Cdd:TIGR02169 413 eELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-514 |
1.07e-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: 51.60 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 162 QERAIKAMTPEQEETASLLSSVTQGMESAYVSPSGYRLVSE---TEWNLLQKEVHNAGNKLGRRCDMCSNYEKQLQGIQI 238
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 239 QEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALV-LRAQASE-------------------I 298
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDeLRAELTLlneeaanlrerleslerriA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 299 LLEELQQGLSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQ---GKHSLHVSLQQAEDFILPDTTEALRELVLKYR 375
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnerASLEEALALLRSELEELSEELRELESKRSELR 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 376 EDIINVRTAADHVE---EKLKAEILFLKEQIQAEQCLKENLEETLQLEIEnckeeiASISSLKAELERIKVEKGQLESTL 452
Cdd:TIGR02168 915 RELEELREKLAQLElrlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE------DDEEEARRRLKRLENKIKELGPVN 988
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217314697 453 REKSQQLESLQEIKISLEEQLKKETAAKATVEQLMfEEKNKAQRLQTeLDVSEQVQRDFVKL 514
Cdd:TIGR02168 989 LAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAI-EEIDREARERF-KDTFDQVNENFQRV 1048
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
282-543 |
6.52e-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: 49.28 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 282 SSHQISALVLRAQASEILLEELQQGLSQAkRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKhslhVSLQQAEDFILp 361
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKI-AELEKALAELRKELEELEEELEQLRKELEELSRQ----ISALRKDLARL- 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 362 dttEALRELVLKYREDIINVRTAADHVEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERI 441
Cdd:TIGR02168 739 ---EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 442 KVE-------KGQLESTLREKSQQLESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQ----VQRD 510
Cdd:TIGR02168 816 NEEaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalalLRSE 895
|
250 260 270
....*....|....*....|....*....|....
gi 2217314697 511 FVKLSQTLQVQLERIRQA-DSLERIRAILNDTKL 543
Cdd:TIGR02168 896 LEELSEELRELESKRSELrRELEELREKLAQLEL 929
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
289-536 |
3.78e-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: 46.30 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 289 LVLRAQASEILLEELQQGLSQakrdVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKhslhVSLQQAEdfiLPDTTEALR 368
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQ----LQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARR---IRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 369 ELvlkyREDIINVRTAADHVEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQL 448
Cdd:COG4942 80 AL----EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 449 ESTLREKSQQLESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQA 528
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*...
gi 2217314697 529 DSLERIRA 536
Cdd:COG4942 236 AAAAAERT 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
313-536 |
5.82e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 313 DVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEdfilpdttealrELVLKYREDIINVRTAADHVEEkl 392
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL------------QRLAEYSWDEIDVASAEREIAE-- 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 393 kaeilfLKEQIqaEQCLKENLE-ETLQLEIENCKEEIAsisSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEE 471
Cdd:COG4913 673 ------LEAEL--ERLDASSDDlAALEEQLEELEAELE---ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217314697 472 QLKKETAAKAtveqlmfeeknkAQRLQTEL--DVSEQVQRDFVKLSQTLQVQLERIRQAdsLERIRA 536
Cdd:COG4913 742 LARLELRALL------------EERFAAALgdAVERELRENLEERIDALRARLNRAEEE--LERAMR 794
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
230-504 |
6.68e-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: 45.83 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 230 EKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEdsshqisalvlRAQASEILLEELQQGLSQ 309
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE-----------RLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 310 AKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLqgKHSLHVSLQQAEDFIlpDTTEALRELVLKYREDIINVRTAADHVE 389
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKL--EEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 390 EK----LKAEILFLKEQIQAEQCLKENLE---ETLQLEIENCKEEI-----------ASISSLKAELERIKVEKGQLEST 451
Cdd:TIGR02169 832 EKeiqeLQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALrdlesrlgdlkKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217314697 452 LREKSQQLESLQEIKISLEEQLKKETAAKAT----VEQLMFEEKNKAQRLQTELDVS 504
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeiPEEELSLEDVQAELQRVEEEIR 968
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
230-480 |
1.10e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 230 EKQLQGIQIQEAETRDQVkklqlmlrqanDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEELQQGLSQ 309
Cdd:COG1196 280 ELELEEAQAEEYELLAEL-----------ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 310 AKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDFILPDTTEALRELvlkyrEDIINVRTAADHVE 389
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE-----EALLERLERLEEEL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 390 EKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISL 469
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
250
....*....|.
gi 2217314697 470 EEQLKKETAAK 480
Cdd:COG1196 504 EGFLEGVKAAL 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
390-544 |
1.33e-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: 45.05 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 390 EKLKAEILFLKEQI-QAEQCLKENLEETLQLEIENCK------EEIASISSLKAELERIKVEKGQLESTLREKSQQLESL 462
Cdd:TIGR02168 680 EELEEKIEELEEKIaELEKALAELRKELEELEEELEQlrkeleELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 463 QEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKlsqtlQVQLERIRQADSLERIRAILNDTK 542
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA-----ELTLLNEEAANLRERLESLERRIA 834
|
..
gi 2217314697 543 LT 544
Cdd:TIGR02168 835 AT 836
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
393-525 |
1.75e-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: 44.67 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 393 KAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIA-------SISSLKAELERIKVEKGQLEStlreksqQLESLQEI 465
Cdd:pfam05911 680 TEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSqlqeseqLIAELRSELASLKESNSLAET-------QLKCMAES 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 466 KISLEEQLkkeTAAKATVEQLmfeeKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERI 525
Cdd:pfam05911 753 YEDLETRL---TELEAELNEL----RQKFEALEVELEEEKNCHEELEAKCLELQEQLERN 805
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
316-530 |
4.24e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 316 EQMAVLMQSREQVSEELVRLQKDNDSLQgkhSLHvslQQAEDFI--------LPDTTEALRELVLKYREdIINVRTAADH 387
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQKLQ---RLH---QAFSRFIgshlavafEADPEAELRQLNRRRVE-LERALADHES 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 388 VEEKLKAEILFLKEQIQA-EQCLKEN---LEETLQLEIENCKEEIASISSLKAELERIKVEKGQLE---STLREKSQQLE 460
Cdd:PRK04863 859 QEQQQRSQLEQAKEGLSAlNRLLPRLnllADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEpivSVLQSDPEQFE 938
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217314697 461 SLQEIKISLEEQLKKETAAKATVEQLM-----FEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADS 530
Cdd:PRK04863 939 QLKQDYQQAQQTQRDAKQQAFALTEVVqrrahFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQA 1013
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
233-551 |
4.32e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 233 LQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEdsshqisalvLRAQASE-ILLEELQQGLSQAK 311
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE----------LKEKAEEyIKLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 312 RDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQqaedfilpDTTEALRELVLKYrEDIINVRTAADHVEEK 391
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE--------KRLEELEERHELY-EEAKAKKEELERLKKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 392 LKAEIlflKEQIQAEQCLKENLEETLQLEIENCKEEIAS----ISSLKAELERIKVEKGQLESTLREksqqleslqeiki 467
Cdd:PRK03918 381 LTGLT---PEKLEKELEELEKAKEEIEEEISKITARIGElkkeIKELKKAIEELKKAKGKCPVCGRE------------- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 468 sLEEQLKKETAAKATVEQlmfeeKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAILNDTKLTDIN 547
Cdd:PRK03918 445 -LTEEHRKELLEEYTAEL-----KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE 518
|
....
gi 2217314697 548 QLPE 551
Cdd:PRK03918 519 ELEK 522
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
311-534 |
5.15e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 311 KRDVQEQMAVLMQSREQVSEELVRLQKDndslqgkhslhvsLQQAEdfilpdttEALRELvlKYREDIINVRTAADHVEE 390
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKE-------------LEEAE--------AALEEF--RQKNGLVDLSEEAKLLLQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 391 KLK---AEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIAS--ISSLKAELERIKVEKGQLESTLREKSQQLESLQEI 465
Cdd:COG3206 220 QLSeleSQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 466 KISLEEQLKKETA-AKATVEQLMFEEKNKAQRLQTELdvsEQVQRDFVKLSQTLQVQLERIRQADSLERI 534
Cdd:COG3206 300 IAALRAQLQQEAQrILASLEAELEALQAREASLQAQL---AQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
294-519 |
5.24e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 294 QASEILLEELQQGLsqakRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGK-HSLHVSLQQAEDFILPDT-----TEAL 367
Cdd:PLN02939 124 QLSDFQLEDLVGMI----QNAEKNILLLNQARLQALEDLEKILTEKEALQGKiNILEMRLSETDARIKLAAqekihVEIL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 368 RELVLKYREDIINVRTAADHVEEKLKAEILFLKEqiqaeqclkENLeeTLQLEIENCKEEIASISSLKAELERIKVEKGQ 447
Cdd:PLN02939 200 EEQLEKLRNELLIRGATEGLCVHSLSKELDVLKE---------ENM--LLKDDIQFLKAELIEVAETEERVFKLEKERSL 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217314697 448 LESTLREKSQQLESLQEiKISLEEQLKKET--AAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQ 519
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 ... |
239-544 |
7.82e-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: 42.65 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 239 QEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEELQQGLSQAKRDVQEQM 318
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 319 AVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDfilpdtTEALRELVLKYREDIINVRTAADHVEEKLKAEILF 398
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE------EELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 399 LKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQL---ESLQEIKISLEEQLKK 475
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKlkeEELELKSEEEKEAQLL 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 476 ETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQ-LERIRQADSLERIRAILNDTKLT 544
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQeLKLLKDELELKKSEDLLKETQLV 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
364-548 |
7.86e-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: 42.35 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 364 TEALRELVLKYREdiINVRTAADHVEEkLKAEILFLKEQIQAEQCLKENLE----------ETLQLEIENCKEEIAS--- 430
Cdd:TIGR02168 212 AERYKELKAELRE--LELALLVLRLEE-LREELEELQEELKEAEEELEELTaelqeleeklEELRLEVSELEEEIEElqk 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 431 --------ISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELD 502
Cdd:TIGR02168 289 elyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217314697 503 VSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAILNDTKLTDINQ 548
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-509 |
1.09e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 239 QEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEELQQGLSQAKRDVQEQm 318
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK- 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 319 avlmQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEdfilpdttealrelvlKYREDIINVRTAADHVEEKLKAEILF 398
Cdd:PTZ00121 1391 ----KKADEAKKKAEEDKKKADELKKAAAAKKKADEAK----------------KKAEEKKKADEAKKKAEEAKKADEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 399 LK--EQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEEQLKKE 476
Cdd:PTZ00121 1451 KKaeEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
250 260 270
....*....|....*....|....*....|....*
gi 2217314697 477 TAAKATVEQLMFEEKNKAQRLQT--ELDVSEQVQR 509
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKaeELKKAEEKKK 1565
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
124-347 |
1.41e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 124 LDESDFGPLvgADSVSENFDTASLGSLQMpsgfmltKDQERAIKAMTPEQEETASLLSSVTQGMESAYVSPSGYRLVSET 203
Cdd:COG4913 218 LEEPDTFEA--ADALVEHFDDLERAHEAL-------EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 204 EWNLLQKEVHNAGNKLGRRcdmcsnyEKQLQGIQIQEAETRDQVKKLQLMLRQAN----DQLEKTMKDKQELEDFIKQSS 279
Cdd:COG4913 289 RLELLEAELEELRAELARL-------EAELERLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217314697 280 EDSSHQISALVLRAQASEILLEELQ-------QGLSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHS 347
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRaeaaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
230-418 |
2.45e-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: 40.52 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 230 EKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEELQQGLSQ 309
Cdd:COG4942 54 LKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 310 AKRDVQeQMAVLMQSREQVSEELVRLQKDNDSLQgkhslhVSLQQAEdfilpDTTEALRELVLKYREDIINVRTAADHVE 389
Cdd:COG4942 134 AVRRLQ-YLKYLAPARREQAEELRADLAELAALR------AELEAER-----AELEALLAELEEERAALEALKAERQKLL 201
|
170 180
....*....|....*....|....*....
gi 2217314697 390 EKLKAEILFLKEQIQAEQCLKENLEETLQ 418
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
224-526 |
3.47e-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: 40.49 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 224 DMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEdsshQISALVLRAQASEILLEEL 303
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKE----QNKRLWDRDTGNSITIDHL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 304 QQGLSQAKRDVQEQMAVLM----QSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDFI-------------------- 359
Cdd:pfam15921 418 RRELDDRNMEVQRLEALLKamksECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLrkvveeltakkmtlessert 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 360 LPDTTEALRE---LVLKYREDIINVRTAAD-----------------HVEEKLKAEILFLKEQIQAEQCLKENLEETLQL 419
Cdd:pfam15921 498 VSDLTASLQEkerAIEATNAEITKLRSRVDlklqelqhlknegdhlrNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 420 -----------EIENCKEEiASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISL----EEQLKKETAAKATVE 484
Cdd:pfam15921 578 vgqhgrtagamQVEKAQLE-KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERD 656
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2217314697 485 QLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIR 526
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
314-542 |
6.27e-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: 39.67 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 314 VQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDFILPDTTEALRelvlKYREDIINVRTAADHVEEKLK 393
Cdd:TIGR02169 182 VEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE----RQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 394 AEILFLKEQI-QAEQCLKENLEETLQL---EIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISL 469
Cdd:TIGR02169 258 EEISELEKRLeEIEQLLEELNKKIKDLgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217314697 470 EEQLKKE-TAAKATVEQLMFEEKNKAQRLQTEL----DVSEQVQRDFVKLSQtLQVQLER-IRQADSLERIRAILNDTK 542
Cdd:TIGR02169 338 IEELEREiEEERKRRDKLTEEYAELKEELEDLRaeleEVDKEFAETRDELKD-YREKLEKlKREINELKRELDRLQEEL 415
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
238-478 |
6.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 238 IQEAETRDQVKKLQLMLrqanDQLEKTMKDKQELEDFIKQSSEdsshQISALVLRAQASEILLEELQQGLSQAKRDVQEQ 317
Cdd:PRK03918 141 LESDESREKVVRQILGL----DDYENAYKNLGEVIKEIKRRIE----RLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 318 MAVLMQSREQ---VSEELVRLQKDNDSLQGKHSLHVSLQQ---AEDFILPDTTEALRELVLKYREDIINVRTAADHVEEK 391
Cdd:PRK03918 213 SSELPELREElekLEKEVKELEELKEEIEELEKELESLEGskrKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 392 LKAEIL--FLKEQIQAEQCLKENLEeTLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISL 469
Cdd:PRK03918 293 EEYIKLseFYEEYLDELREIEKRLS-RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK 371
|
250
....*....|.
gi 2217314697 470 E--EQLKKETA 478
Cdd:PRK03918 372 EelERLKKRLT 382
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
393-502 |
9.35e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 38.76 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217314697 393 KAEILFLKEQIQA--EQCLKENLeetlqLEIENCKEEIASISSLKAELERIKVEKG--QLESTLREKSQQLESLQEIKI- 467
Cdd:PRK05771 8 KVLIVTLKSYKDEvlEALHELGV-----VHIEDLKEELSNERLRKLRSLLTKLSEAldKLRSYLPKLNPLREEKKKVSVk 82
|
90 100 110
....*....|....*....|....*....|....*
gi 2217314697 468 SLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELD 502
Cdd:PRK05771 83 SLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
|
| |
