NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|129822|sp|P21807|]
View 

RecName: Full=Peripherin

Protein Classification

intermediate filament family protein( domain architecture ID 12057329)

intermediate filament family protein similar to desmin, a muscle-specific type III intermediate filament essential for proper muscular structure and function

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
93-403 1.10e-119

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 352.30  E-value: 1.10e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      93 NEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQ---EPARADQLCQQELRELRRELELLGRERDRVQVERDGL 169
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     170 AEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQqVE 249
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVN-VE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     250 VEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGT 329
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 129822     330 NEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESR 403
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
15-92 2.76e-11

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: 59.33  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      15 TSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSGSPS--SSARLGSFRAPRAGALRLPSERLDFSMAEALNQEFLATRS 92
Cdd:pfam04732   4 SSYRRMFGDSSSSRPSYSSSSGSRSVSSRSYSRSSSSSpsSSSRRSSRSSSRSSYPSLAADSLDFSLADALNQEFKATRT 83
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
93-403 1.10e-119

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 352.30  E-value: 1.10e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      93 NEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQ---EPARADQLCQQELRELRRELELLGRERDRVQVERDGL 169
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     170 AEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQqVE 249
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVN-VE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     250 VEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGT 329
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 129822     330 NEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESR 403
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
15-92 2.76e-11

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: 59.33  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      15 TSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSGSPS--SSARLGSFRAPRAGALRLPSERLDFSMAEALNQEFLATRS 92
Cdd:pfam04732   4 SSYRRMFGDSSSSRPSYSSSSGSRSVSSRSYSRSSSSSpsSSSRRSSRSSSRSSYPSLAADSLDFSLADALNQEFKATRT 83
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
121-402 1.67e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   121 ALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVL---- 196
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllae 296
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   197 ---FRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEatvkpELTAALRDIRAQYENIA 273
Cdd:COG1196 297 larLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-----EAEAELAEAEEALLEAE 371
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   274 AKNLQEAEEWYKSKYADLsdAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQA 353
Cdd:COG1196 372 AELAEAEEELEELAEELL--EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 129822   354 GAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEES 402
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
160-404 2.05e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 2.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      160 DRVQVERDGlAEDLGALKQRLEE-----ETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELR 234
Cdd:TIGR02169  201 ERLRREREK-AERYQALLKEKREyegyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      235 DLQVSVESQQVQQVEVEATVKPELTAALRDIRAqyeniAAKNLQEAEEWYKSKYADLsdaaNRNHEALRQAKQEMNESRR 314
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAE-----KERELEDAEERLAKLEAEI----DKLLAEIEELEREIEEERK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      315 QIQSLTCEVDGLRGTNEALLRQLRELEEQFALeaggYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYR 394
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAE----TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
                          250
                   ....*....|
gi 129822      395 KLLEGEESRI 404
Cdd:TIGR02169  427 AAIAGIEAKI 436
PTZ00121 PTZ00121
MAEBL; Provisional
72-455 2.99e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      72 SERLDFSMAEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRE 151
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     152 LELLGRERDRVQVERdglAEDLGALKQRLEEETRKREDAEHNLVLFRkdvddATLSRLELERKIESLMDEIEFLKKLHEE 231
Cdd:PTZ00121 1539 AKKAEEKKKADELKK---AEELKKAEEKKKAEEAKKAEEDKNMALRK-----AEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     232 ELRDlqvsvesqqvqqvEVEATVKPELTAALRDIRAQYENIAAKnlqEAEEwyKSKYADLSDAANRNHEALRQAKQEMNE 311
Cdd:PTZ00121 1611 EAKK-------------AEEAKIKAEELKKAEEEKKKVEQLKKK---EAEE--KKKAEELKKAEEENKIKAAEEAKKAEE 1672
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     312 SRRQIQSLTCEVDGLRGTNEALLRQLREleeqfaleaggyqagaARLEEELRQLKEE---MARHLREYQELLNVKMAL-- 386
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEE----------------AKKAEELKKKEAEekkKAEELKKAEEENKIKAEEak 1736
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     387 -----DIEIATYRKLLEGEESRIS-----VPVHSFASLSLKTTVPEVEPPQDSHSRKMVLIRTI-ETRDGEKVVTESQKE 455
Cdd:PTZ00121 1737 keaeeDKKKAEEAKKDEEEKKKIAhlkkeEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIkDIFDNFANIIEGGKE 1816
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
93-403 1.10e-119

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 352.30  E-value: 1.10e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      93 NEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQ---EPARADQLCQQELRELRRELELLGRERDRVQVERDGL 169
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     170 AEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQqVE 249
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVN-VE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     250 VEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGT 329
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 129822     330 NEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESR 403
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
15-92 2.76e-11

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: 59.33  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      15 TSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSGSPS--SSARLGSFRAPRAGALRLPSERLDFSMAEALNQEFLATRS 92
Cdd:pfam04732   4 SSYRRMFGDSSSSRPSYSSSSGSRSVSSRSYSRSSSSSpsSSSRRSSRSSSRSSYPSLAADSLDFSLADALNQEFKATRT 83
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
121-402 1.67e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   121 ALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVL---- 196
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllae 296
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   197 ---FRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEatvkpELTAALRDIRAQYENIA 273
Cdd:COG1196 297 larLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-----EAEAELAEAEEALLEAE 371
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   274 AKNLQEAEEWYKSKYADLsdAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQA 353
Cdd:COG1196 372 AELAEAEEELEELAEELL--EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 129822   354 GAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEES 402
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
80-365 6.26e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 6.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822    80 AEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLcqqelrelrrelellgrer 159
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL------------------- 318
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   160 DRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQvs 239
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-- 396
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   240 VESQQVQQVEVEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSL 319
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 129822   320 TCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQL 365
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
153-403 7.50e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 7.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   153 ELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLEL---ERKIESLMDEIEFLKKLH 229
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIARL 307
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   230 EEELRDLQVSVESQQVQQVEVEATVKpELTAALRDIRAQYENIAAK--NLQEAEEWYKSKYADLSDAANRNHEALRQAKQ 307
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELE-ELEEELEELEEELEEAEEEleEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   308 EMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALD 387
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
                       250
                ....*....|....*.
gi 129822   388 IEIATYRKLLEGEESR 403
Cdd:COG1196 467 ELLEEAALLEAALAEL 482
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
85-371 1.35e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822    85 QEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARgqeparadqlcqQELRELRRELELLGRERDRVQV 164
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE------------LELEEAQAEEYELLAELARLEQ 302
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   165 ERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEflkKLHEEELRDLQVSVESQQ 244
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA---EAEEALLEAEAELAEAEE 379
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   245 VQQVEVEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVD 324
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 129822   325 GLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMAR 371
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
160-404 2.05e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 2.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      160 DRVQVERDGlAEDLGALKQRLEE-----ETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELR 234
Cdd:TIGR02169  201 ERLRREREK-AERYQALLKEKREyegyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      235 DLQVSVESQQVQQVEVEATVKPELTAALRDIRAqyeniAAKNLQEAEEWYKSKYADLsdaaNRNHEALRQAKQEMNESRR 314
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAE-----KERELEDAEERLAKLEAEI----DKLLAEIEELEREIEEERK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      315 QIQSLTCEVDGLRGTNEALLRQLRELEEQFALeaggYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYR 394
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAE----TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
                          250
                   ....*....|
gi 129822      395 KLLEGEESRI 404
Cdd:TIGR02169  427 AAIAGIEAKI 436
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
160-391 2.68e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 2.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   160 DRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLElerkieslmdeieflkKLHEEELRDLQVS 239
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA----------------KLLLQQLSELESQ 227
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   240 VESQQVQQVEVEA---TVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQI 316
Cdd:COG3206 228 LAEARAELAEAEArlaALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL 307
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 129822   317 QSLTCEV-DGLRGTNEALLRQLRELEEQFAlEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIA 391
Cdd:COG3206 308 QQEAQRIlASLEAELEALQAREASLQAQLA-QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
171-428 4.86e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.30  E-value: 4.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      171 EDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHE---EELRDLQVSVESQQVQQ 247
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEklkERLEELEEDLSSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      248 VEVEATVK------PELTAALRDIRAQYENIAAK-----------NLQEAEEWYKSKYADLSD---AANRNHEALRQAKQ 307
Cdd:TIGR02169  754 ENVKSELKeleariEELEEDLHKLEEALNDLEARlshsripeiqaELSKLEEEVSRIEARLREieqKLNRLTLEKEYLEK 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      308 EMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFAleagGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALD 387
Cdd:TIGR02169  834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE----ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 129822      388 IEIATYRKLLEGEESRISVPVHSFASLSLKTTVPEVEPPQD 428
Cdd:TIGR02169  910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
96-385 5.51e-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: 5.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822       96 QELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVER--------- 166
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelkalreal 805
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      167 DGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQ 246
Cdd:TIGR02168  806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      247 QveveatvkpeltAALRDIRAQYENIAAKNlqeaeewykskyADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGL 326
Cdd:TIGR02168  886 E------------EALALLRSELEELSEEL------------RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 129822      327 RGTneallrqlreLEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMA 385
Cdd:TIGR02168  942 QER----------LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
127-404 6.72e-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: 45.43  E-value: 6.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      127 SQARGQEPARADQLCQQEL-RELRRELELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDAT 205
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      206 LSRLELERKIESLMDEIEFLKKlhEEELRDLQVSVESQQVQQVEVE-ATVKPELTAALRDIRAQYENIAAKNLQEAEEwy 284
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEA--EIEELEERLEEAEEELAEAEAEiEELEAQIEQLKEELKALREALDELRAELTLL-- 815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      285 KSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFAL---EAGGYQAGAARLEEE 361
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSE 895
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 129822      362 LRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRI 404
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
176-415 1.15e-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: 44.66  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      176 LKQRLEEETRKREDAEHNLvlfrKDVDDAtlsRLELERKIESLMDEIEFLKKLHE--EELRDLQVSVESQQVQQVEVEAT 253
Cdd:TIGR02168  170 YKERRKETERKLERTRENL----DRLEDI---LNELERQLKSLERQAEKAERYKElkAELRELELALLVLRLEELREELE 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      254 VKPELTAALRDIRAQYENiAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEAL 333
Cdd:TIGR02168  243 ELQEELKEAEEELEELTA-ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      334 LRQLRELEEQfaleAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRISVPVHSFAS 413
Cdd:TIGR02168  322 EAQLEELESK----LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                   ..
gi 129822      414 LS 415
Cdd:TIGR02168  398 LN 399
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
209-405 1.90e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822    209 LELERKIESLmDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQYENIAAKnLQEAEEwyksKY 288
Cdd:COG4913  245 EDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE-LERLEA----RL 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822    289 ADLSDAANRNHEALRQAK-QEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKE 367
Cdd:COG4913  319 DALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 129822    368 EMARHLREYQELLNVKMALDIEIATYRKLLEGEESRIS 405
Cdd:COG4913  399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
109-392 3.44e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822    109 IEKVRFLEQQNAALRGELSQARGQEpARADQLCQQELRELRRELELLGRERDRVQVerDGLAEDLGALKQRLEEEtrkrE 188
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERL-EALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAELEAELERL----D 681
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822    189 DAEHNLVLFRKDVDDATLSRLELERKIESLMDEIeflkKLHEEELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQ 268
Cdd:COG4913  682 ASSDDLAALEEQLEELEAELEELEEELDELKGEI----GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822    269 YenIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAkqeMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQfalea 348
Cdd:COG4913  758 A--LGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLDRLEED----- 827
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 129822    349 ggyqaGAARLEEELRQLKEEmarhlREYQELLNVKMALDIEIAT 392
Cdd:COG4913  828 -----GLPEYEERFKELLNE-----NSIEFVADLLSKLRRAIRE 861
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
257-403 3.63e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   257 ELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQ 336
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   337 LRELEEQFALEA---GGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESR 403
Cdd:COG1196 297 LARLEQDIARLEerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
307-404 5.85e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.54  E-value: 5.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   307 QEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQfaleaggyqagAARLEEELRQLKEEMARHLREYQELlnvkMAL 386
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDER-----------IERLERELSEARSEERREIRKDREI----SRL 470
                        90
                ....*....|....*...
gi 129822   387 DIEIATYRKLLEGEESRI 404
Cdd:COG2433 471 DREIERLERELEEERERI 488
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
142-371 7.06e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 7.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   142 QQELRELRRELELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDdatlsrlELERKIESLMDE 221
Cdd:COG4942  26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAELRAE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   222 IEFLKKLHEEELRDLQvsvesQQVQQVEVEATVKPE-LTAALRdiRAQYENIAAKNLQEAEEWYKSKYADLsdaaNRNHE 300
Cdd:COG4942  99 LEAQKEELAELLRALY-----RLGRQPPLALLLSPEdFLDAVR--RLQYLKYLAPARREQAEELRADLAEL----AALRA 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 129822   301 ALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMAR 371
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
69-344 9.90e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 9.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822       69 RLPSERLDFSMAEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQA---RGQEPARADQLCQQEL 145
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAeaeIEELEAQIEQLKEELK 799
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      146 RELRRELELLGRERD------RVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESL- 218
Cdd:TIGR02168  800 ALREALDELRAELTLlneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALl 879
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      219 --MDEIEFLKKLHEEELRDLqvsveSQQVQQVEVEATVKPELTAALRDIRAQYENIAAK---NLQEAEEWYKSKYADLSD 293
Cdd:TIGR02168  880 neRASLEEALALLRSELEEL-----SEELRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERLSEEYSLTLE 954
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 129822      294 AANRNHEALrqaKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQF 344
Cdd:TIGR02168  955 EAEALENKI---EDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERY 1002
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
192-404 1.28e-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: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822    192 HNLVLFRKDVDDATLSRLEL----ERKIESLMDEIEFLkklhEEELRDLQVSVESQQVQQveveatvkpeltAALRDIRA 267
Cdd:COG4913  585 GNGTRHEKDDRRRIRSRYVLgfdnRAKLAALEAELAEL----EEELAEAEERLEALEAEL------------DALQERRE 648
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822    268 QYENIAA-----KNLQEAEEWYKSKYADLsDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEE 342
Cdd:COG4913  649 ALQRLAEyswdeIDVASAEREIAELEAEL-ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 129822    343 QFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRI 404
Cdd:COG4913  728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
89-318 1.88e-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: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822    89 ATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLcQQELRELRRELELLGRERDRVQVERDG 168
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-RALEQELAALEAELAELEKEIAELRAE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   169 LAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKlHEEELRDLQVSVESQQVQQV 248
Cdd:COG4942  99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELE 177
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822   249 EVEATVKPELtAALRDIRAQYENIAAKnLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQS 318
Cdd:COG4942 178 ALLAELEEER-AALEALKAERQKLLAR-LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
PTZ00121 PTZ00121
MAEBL; Provisional
72-455 2.99e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      72 SERLDFSMAEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRE 151
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     152 LELLGRERDRVQVERdglAEDLGALKQRLEEETRKREDAEHNLVLFRkdvddATLSRLELERKIESLMDEIEFLKKLHEE 231
Cdd:PTZ00121 1539 AKKAEEKKKADELKK---AEELKKAEEKKKAEEAKKAEEDKNMALRK-----AEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     232 ELRDlqvsvesqqvqqvEVEATVKPELTAALRDIRAQYENIAAKnlqEAEEwyKSKYADLSDAANRNHEALRQAKQEMNE 311
Cdd:PTZ00121 1611 EAKK-------------AEEAKIKAEELKKAEEEKKKVEQLKKK---EAEE--KKKAEELKKAEEENKIKAAEEAKKAEE 1672
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     312 SRRQIQSLTCEVDGLRGTNEALLRQLREleeqfaleaggyqagaARLEEELRQLKEE---MARHLREYQELLNVKMAL-- 386
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEE----------------AKKAEELKKKEAEekkKAEELKKAEEENKIKAEEak 1736
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822     387 -----DIEIATYRKLLEGEESRIS-----VPVHSFASLSLKTTVPEVEPPQDSHSRKMVLIRTI-ETRDGEKVVTESQKE 455
Cdd:PTZ00121 1737 keaeeDKKKAEEAKKDEEEKKKIAhlkkeEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIkDIFDNFANIIEGGKE 1816
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
276-467 3.13e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.42  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      276 NLQEAEEWY-KSK-YADLSD----AANRNHEALRQAKQEMNESRRQIQSLTCE--VDGLRGTNEALLRQLRELEEQFALE 347
Cdd:TIGR01612 1484 NINELKEHIdKSKgCKDEADknakAIEKNKELFEQYKKDVTELLNKYSALAIKnkFAKTKKDSEIIIKEIKDAHKKFILE 1563
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      348 AGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALD------IEIATYRK-----LLEGE--ESRISvpvhsfaSL 414
Cdd:TIGR01612 1564 AEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLEnfenkfLKISDIKKkindcLKETEsiEKKIS-------SF 1636
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 129822      415 SLKTTVPEVEPPQDSHSrkmVLIRTIETRDGEKVVTESQKEQHSELDkSSIHS 467
Cdd:TIGR01612 1637 SIDSQDTELKENGDNLN---SLQEFLESLKDQKKNIEDKKKELDELD-SEIEK 1685
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
151-404 3.91e-03

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: 40.04  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      151 ELELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKlHE 230
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER-QL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      231 EELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQyeNIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMN 310
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESL--EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      311 ESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFA-LEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIE 389
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
                          250
                   ....*....|....*
gi 129822      390 IATYRKLLEGEESRI 404
Cdd:TIGR02168  477 LDAAERELAQLQARL 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
73-365 6.22e-03

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: 39.27  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822       73 ERLDFSMAEALNQEF-LATRSNEKQE-LQELNDRFANFIEKVRFLEQQNAALRGELSQargqeparadqlCQQELRELRR 150
Cdd:TIGR02168  242 EELQEELKEAEEELEeLTAELQELEEkLEELRLEVSELEEEIEELQKELYALANEISR------------LEQQKQILRE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      151 ELELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKK--- 227
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkva 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      228 --LHEEELRDLQVSVESQQVQQVEVEATvkpELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQA 305
Cdd:TIGR02168  390 qlELQIASLNNEIERLEARLERLEDRRE---RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 129822      306 KQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEeqfaleagGYQAGAARLEEELRQL 365
Cdd:TIGR02168  467 REELEEAEQALDAAERELAQLQARLDSLERLQENLE--------GFSEGVKALLKNQSGL 518
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH