|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
107-415 |
4.05e-123 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 361.16 E-value: 4.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71011081 343 DSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALYVEIATYRKLLEGEESR 415
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
9-106 |
1.87e-13 |
|
Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.
Pssm-ID: 461414 [Multi-domain] Cd Length: 83 Bit Score: 65.49 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732 1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65
|
90
....*....|....*...
gi 71011081 89 LDFSLADAVNQEFLTTRT 106
Cdd:pfam04732 66 LDFSLADALNQEFKATRT 83
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-421 |
9.64e-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: 57.76 E-value: 9.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLK--GREPTRVAELYEEELRELRRQVEVLTNQRARVDVER 180
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 181 DNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADvdaatlaRIDLERRIESLNEEIAFLKK--------VHEEEIRELQA 252
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREaldelraeLTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYksKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 332
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 333 CEIDALKGTNDSLMRQMRELEDRFASeasgYQDNIARLEEEIRHLKDEMArhlREYQDLLNVKMALYVEIATYRKLLEGE 412
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR 973
|
....*....
gi 71011081 413 ESRINLPIQ 421
Cdd:TIGR02168 974 LKRLENKIK 982
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-404 |
8.20e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 111 ELQELNDRFANyiekvrfLEQQNAALAAEVNRLKGReptRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRL 190
Cdd:COG4913 618 ELAELEEELAE-------AEERLEALEAELDALQER---REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 191 KAkLQEEIqlkEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEeirelqaqlqeqqvqvEMDMSKPDL 270
Cdd:COG4913 688 AA-LEEQL---EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA----------------AEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 271 TAALRDIRAQYetIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAkqeMMEYRHQIQSYTCEIDALKGTNDSLMRQMR 350
Cdd:COG4913 748 RALLEERFAAA--LGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLD 822
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 71011081 351 ELEDrfaseasgyqDNIARLEEEIRHLKDEmarhlREYQDLLNVKMALYVEIAT 404
Cdd:COG4913 823 RLEE----------DGLPEYEERFKELLNE-----NSIEFVADLLSKLRRAIRE 861
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
107-415 |
4.05e-123 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 361.16 E-value: 4.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71011081 343 DSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALYVEIATYRKLLEGEESR 415
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
9-106 |
1.87e-13 |
|
Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.
Pssm-ID: 461414 [Multi-domain] Cd Length: 83 Bit Score: 65.49 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732 1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65
|
90
....*....|....*...
gi 71011081 89 LDFSLADAVNQEFLTTRT 106
Cdd:pfam04732 66 LDFSLADALNQEFKATRT 83
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-421 |
9.64e-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: 57.76 E-value: 9.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLK--GREPTRVAELYEEELRELRRQVEVLTNQRARVDVER 180
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 181 DNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADvdaatlaRIDLERRIESLNEEIAFLKK--------VHEEEIRELQA 252
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREaldelraeLTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYksKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 332
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 333 CEIDALKGTNDSLMRQMRELEDRFASeasgYQDNIARLEEEIRHLKDEMArhlREYQDLLNVKMALYVEIATYRKLLEGE 412
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR 973
|
....*....
gi 71011081 413 ESRINLPIQ 421
Cdd:TIGR02168 974 LKRLENKIK 982
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-404 |
8.20e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 111 ELQELNDRFANyiekvrfLEQQNAALAAEVNRLKGReptRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRL 190
Cdd:COG4913 618 ELAELEEELAE-------AEERLEALEAELDALQER---REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 191 KAkLQEEIqlkEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEeirelqaqlqeqqvqvEMDMSKPDL 270
Cdd:COG4913 688 AA-LEEQL---EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA----------------AEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 271 TAALRDIRAQYetIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAkqeMMEYRHQIQSYTCEIDALKGTNDSLMRQMR 350
Cdd:COG4913 748 RALLEERFAAA--LGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLD 822
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 71011081 351 ELEDrfaseasgyqDNIARLEEEIRHLKDEmarhlREYQDLLNVKMALYVEIAT 404
Cdd:COG4913 823 RLEE----------DGLPEYEERFKELLNE-----NSIEFVADLLSKLRRAIRE 861
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
165-415 |
3.36e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHE 244
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 245 EEIRELQaqlqeqqvqvemdmskpDLTAALRDIRAQYETIAAKNISEAEEwykskVSDLTQAANKNNDALRQAKQEMMEY 324
Cdd:COG1196 334 ELEEELE-----------------ELEEELEEAEEELEEAEAELAEAEEA-----LLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 325 RHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALYVEIAT 404
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250
....*....|.
gi 71011081 405 YRKLLEGEESR 415
Cdd:COG1196 472 AALLEAALAEL 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
166-469 |
6.82e-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: 45.44 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 166 VEVLTNQRARVDVERDNLL--DDLQRLKAKLQEEIQL--KEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAflkk 241
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAEryQALLKEKREYEGYELLkeKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE---- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 242 vheeeirelqaqlqeqqvqvemdmskpdltAALRDIRAQYETIAAKNISEAEEwYKSKVSDLTQAANKNNDALRQAKQEM 321
Cdd:TIGR02169 269 ------------------------------EIEQLLEELNKKIKDLGEEEQLR-VKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 322 MEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASeasgyqdniarLEEEIRHLKDEMARHLREYQDLLNVKMALYVE 401
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK-----------LTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71011081 402 IATYRKLLEGEESRINLPIQTYSALNFRETSPEQRGSEVHTKktvmIKTIETRDGEVVSEATQQQHEV 469
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA----IAGIEAKINELEEEKEDKALEI 450
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
103-393 |
8.36e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAelyeeelrelrrQVEVLTNQRARVDVERDN 182
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNA------------QVKELREEAQELREKRDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 183 LLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARID---LERRIESLneEIAFLKKVH--EEEIRelqaqlqeq 257
Cdd:COG1340 69 LNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERL--EWRQQTEVLspEEEKE--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 258 qvqvemdmskpdLTAALRDIRAQYETIaaknisEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDA 337
Cdd:COG1340 138 ------------LVEKIKELEKELEKA------KKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 71011081 338 LKGTNDSLMRQMRELedrfASEASGYQDNIARLEEEIrhlkDEMARHLREYQDLLN 393
Cdd:COG1340 200 LYKEADELRKEADEL----HKEIVEAQEKADELHEEI----IELQKELRELRKELK 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
88-373 |
1.68e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 88 LLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREptrvaelyeeelRELRRQVE 167
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE------------YELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 168 VLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEI 247
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 248 RELQAQLQEQQvqvemdmskpDLTAALRDIRAQYETIAAKNISEAEEwykskVSDLTQAANKNNDALRQAKQEMMEYRHQ 327
Cdd:COG1196 379 EELEELAEELL----------EALRAAAELAAQLEELEEAEEALLER-----LERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 71011081 328 IQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEE 373
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-418 |
2.03e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHE 244
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 245 EEIRELQAQLQEQQVQVEmdmSKPDLTAALRDIRAQYETIAAKNISEAEEWY--KSKVSDLTQAANKNNDALRQAKQEMM 322
Cdd:TIGR02168 320 ELEAQLEELESKLDELAE---ELAELEEKLEELKEELESLEAELEELEAELEelESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 323 EYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFAS-EASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALYVE 401
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250
....*....|....*..
gi 71011081 402 IATYRKLLEGEESRINL 418
Cdd:TIGR02168 477 LDAAERELAQLQARLDS 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
165-393 |
2.82e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLAR--IDLERRIESLNEEIAFLKKV 242
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 243 HEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETiAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMM 322
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE-LQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71011081 323 EYRHQIQSYTCEIDALkgtNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLK----DEMARHLREYQDLLN 393
Cdd:COG4913 770 NLEERIDALRARLNRA---EEELERAMRAFNREWPAETADLDADLESLPEYLALLDrleeDGLPEYEERFKELLN 841
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
162-383 |
3.02e-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: 39.75 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 162 LRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDaatlariDLERRIESLNEEIAFLKK 241
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 242 VHEEEIRelQAQLQEQQVQVEMDMSKPDLTAALRdiRAQYETIAAKNISEAEEWYKSKVSDLTQaankNNDALRQAKQEM 321
Cdd:COG4942 105 ELAELLR--ALYRLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAELAA----LRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71011081 322 MEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMAR 383
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
172-361 |
3.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 172 QRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARID-LERRIESLNEEIAflkkvheeeiREL 250
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELE----------ERE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 251 QAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKniseaeewYKSKVSDLTQAANKNNDALRQAKQEmmeyRHQIQS 330
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA--------LEEELEALEEALAEAEAALRDLRRE----LRELEA 426
|
170 180 190
....*....|....*....|....*....|.
gi 71011081 331 ytcEIDALKGTNDSLMRQMRELEDRFASEAS 361
Cdd:COG4913 427 ---EIASLERRKSNIPARLLALRDALAEALG 454
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
108-423 |
3.55e-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: 40.05 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 108 EKVELQELNDRfanyIEKvrfLEQQNAALAAEVNRLKGR--EPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLD 185
Cdd:TIGR02169 672 EPAELQRLRER----LEG---LKRELSSLQSELRRIENRldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 186 DLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRI------------ESLNEEI-----------AFLKKV 242
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsripeiqaelSKLEEEVsriearlreieQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 243 HEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAA--KNISEAEEWYKSKVSDLTQAANKNNDALRQAKQE 320
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 321 MMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEAS---------GYQDNIARLEEEIRHLKDEMARHLREYQDL 391
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsleDVQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
330 340 350
....*....|....*....|....*....|..
gi 71011081 392 LnvkmALYVEIATYRKLLEGEESRINLPIQTY 423
Cdd:TIGR02169 985 L----KRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-241 |
3.71e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 111 ELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGReptrVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRL 190
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQ----IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71011081 191 K----------AKLQEEI-QLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKK 241
Cdd:COG4913 372 GlplpasaeefAALRAEAaALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
170-407 |
4.32e-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: 39.36 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 170 TNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKvHEEEIRE 249
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 250 LQAQLQEQQVQVemdmskpdLTAALRDIRAQYETI--AAKNISEAEEWYKSkVSDLTQAANKNNDALRQAKQEMMEYRHQ 327
Cdd:COG4942 98 ELEAQKEELAEL--------LRALYRLGRQPPLALllSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 328 IQSytcEIDALKGTNDSLMRQMRELEdrfaSEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALYVEIATYRK 407
Cdd:COG4942 169 LEA---ERAELEALLAELEEERAALE----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
174-286 |
5.20e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.29 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011081 174 ARVDVERDNLLDDLQRLKAKLqeeIQLKEEAEnnlaAFRADVDAATLARID-LERRIESLNEEIAFLKKVHEEEIRELQA 252
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRL---EQLEIEKE----ALKKEQDEASFERLAeLRDELAELEEELEALKARWEAEKELIEE 472
|
90 100 110
....*....|....*....|....*....|....
gi 71011081 253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAA 286
Cdd:COG0542 473 IQELKEELEQRYGKIPELEKELAELEEELAELAP 506
|
|
| |
