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Conserved domains on  [gi|2172663953|ref|NP_036765|]
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peripherin [Rattus norvegicus]

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

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List of domain hits

 Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
99-409 1.40e-119

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 352.30  E-value: 1.40e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  99 NEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQ---EPARADQLCQQELRELRRELELLGRERDRVQVERDGL 175
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 176 AEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQqVE 255
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVN-VE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 256 VEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGT 335
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2172663953 336 NEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESR 409
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 21-98 2.51e-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: 59.71  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  21 TSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSGSPS--SSARLGSFRAPRAGALRLPSERLDFSMAEALNQEFLATRS 98
Cdd:pfam04732   4 SSYRRMFGDSSSSRPSYSSSSGSRSVSSRSYSRSSSSSpsSSSRRSSRSSSRSSYPSLAADSLDFSLADALNQEFKATRT 83
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
99-409 1.40e-119

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 352.30  E-value: 1.40e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  99 NEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQ---EPARADQLCQQELRELRRELELLGRERDRVQVERDGL 175
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 176 AEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQqVE 255
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVN-VE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 256 VEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGT 335
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2172663953 336 NEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESR 409
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 21-98 2.51e-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: 59.71  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  21 TSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSGSPS--SSARLGSFRAPRAGALRLPSERLDFSMAEALNQEFLATRS 98
Cdd:pfam04732   4 SSYRRMFGDSSSSRPSYSSSSGSRSVSSRSYSRSSSSSpsSSSRRSSRSSSRSSYPSLAADSLDFSLADALNQEFKATRT 83
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 127-408 1.94e-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: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 127 ALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVL---- 202
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllae 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 203 ---FRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEatvkpELTAALRDIRAQYENIA 279
Cdd:COG1196   297 larLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-----EAEAELAEAEEALLEAE 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 280 AKNLQEAEEWYKSKYADLsdAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQA 359
Cdd:COG1196   372 AELAEAEEELEELAEELL--EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2172663953 360 GAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEES 408
Cdd:COG1196   450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-410 2.41e-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: 50.07  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  166 DRVQVERDGlAEDLGALKQRLEE-----ETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELR 240
Cdd:TIGR02169  201 ERLRREREK-AERYQALLKEKREyegyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  241 DLQVSVESQQVQQVEVEATVKPELTAALRDIRAqyeniAAKNLQEAEEWYKSKYADLsdaaNRNHEALRQAKQEMNESRR 320
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAE-----KERELEDAEERLAKLEAEI----DKLLAEIEELEREIEEERK 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  321 QIQSLTCEVDGLRGTNEALLRQLRELEEQFALeaggYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYR 400
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAE----TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426

                          250
                   ....*....|
gi 2172663953  401 KLLEGEESRI 410
Cdd:TIGR02169  427 AAIAGIEAKI 436
PTZ00121 PTZ00121
MAEBL; Provisional
 78-461 3.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953   78 SERLDFSMAEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRE 157
Cdd:PTZ00121  1459 AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  158 LELLGRERDRVQVERdglAEDLGALKQRLEEETRKREDAEHNLVLFRkdvddATLSRLELERKIESLMDEIEFLKKLHEE 237
Cdd:PTZ00121  1539 AKKAEEKKKADELKK---AEELKKAEEKKKAEEAKKAEEDKNMALRK-----AEEAKKAEEARIEEVMKLYEEEKKMKAE 1610

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  238 ELRDlqvsvesqqvqqvEVEATVKPELTAALRDIRAQYENIAAKnlqEAEEwyKSKYADLSDAANRNHEALRQAKQEMNE 317
Cdd:PTZ00121  1611 EAKK-------------AEEAKIKAEELKKAEEEKKKVEQLKKK---EAEE--KKKAEELKKAEEENKIKAAEEAKKAEE 1672

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  318 SRRQIQSLTCEVDGLRGTNEALLRQLREleeqfaleaggyqagaARLEEELRQLKEE---MARHLREYQELLNVKMAL-- 392
Cdd:PTZ00121  1673 DKKKAEEAKKAEEDEKKAAEALKKEAEE----------------AKKAEELKKKEAEekkKAEELKKAEEENKIKAEEak 1736

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  393 -----DIEIATYRKLLEGEESRIS-----VPVHSFASLSLKTTVPEVEPPQDSHSRKMVLIRTI-ETRDGEKVVTESQKE 461
Cdd:PTZ00121  1737 keaeeDKKKAEEAKKDEEEKKKIAhlkkeEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIkDIFDNFANIIEGGKE 1816
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
99-409 1.40e-119

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 352.30  E-value: 1.40e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  99 NEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQ---EPARADQLCQQELRELRRELELLGRERDRVQVERDGL 175
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 176 AEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQqVE 255
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVN-VE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 256 VEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGT 335
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2172663953 336 NEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESR 409
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 21-98 2.51e-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: 59.71  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  21 TSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSGSPS--SSARLGSFRAPRAGALRLPSERLDFSMAEALNQEFLATRS 98
Cdd:pfam04732   4 SSYRRMFGDSSSSRPSYSSSSGSRSVSSRSYSRSSSSSpsSSSRRSSRSSSRSSYPSLAADSLDFSLADALNQEFKATRT 83
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 127-408 1.94e-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: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 127 ALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVL---- 202
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllae 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 203 ---FRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEatvkpELTAALRDIRAQYENIA 279
Cdd:COG1196   297 larLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-----EAEAELAEAEEALLEAE 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 280 AKNLQEAEEWYKSKYADLsdAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQA 359
Cdd:COG1196   372 AELAEAEEELEELAEELL--EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2172663953 360 GAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEES 408
Cdd:COG1196   450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 86-371 7.35e-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: 7.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  86 AEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLcqqelrelrrelellgrer 165
Cdd:COG1196   258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL------------------- 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 166 DRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQvs 245
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-- 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 246 VESQQVQQVEVEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSL 325
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2172663953 326 TCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQL 371
Cdd:COG1196   477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-409 8.15e-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: 8.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 159 ELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLEL---ERKIESLMDEIEFLKKLH 235
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIARL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 236 EEELRDLQVSVESQQVQQVEVEATVKpELTAALRDIRAQYENIAAK--NLQEAEEWYKSKYADLSDAANRNHEALRQAKQ 313
Cdd:COG1196   308 EERRRELEERLEELEEELAELEEELE-ELEEELEELEEELEEAEEEleEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 314 EMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALD 393
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                         250
                  ....*....|....*.
gi 2172663953 394 IEIATYRKLLEGEESR 409
Cdd:COG1196   467 ELLEEAALLEAALAEL 482
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 91-377 1.67e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  91 QEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARgqeparadqlcqQELRELRRELELLGRERDRVQV 170
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE------------LELEEAQAEEYELLAELARLEQ 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 171 ERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEiefLKKLHEEELRDLQVSVESQQ 250
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEE 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 251 VQQVEVEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVD 330
Cdd:COG1196   380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2172663953 331 GLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMAR 377
Cdd:COG1196   460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-410 2.41e-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: 50.07  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  166 DRVQVERDGlAEDLGALKQRLEE-----ETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELR 240
Cdd:TIGR02169  201 ERLRREREK-AERYQALLKEKREyegyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  241 DLQVSVESQQVQQVEVEATVKPELTAALRDIRAqyeniAAKNLQEAEEWYKSKYADLsdaaNRNHEALRQAKQEMNESRR 320
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAE-----KERELEDAEERLAKLEAEI----DKLLAEIEELEREIEEERK 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  321 QIQSLTCEVDGLRGTNEALLRQLRELEEQFALeaggYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYR 400
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAE----TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426

                          250
                   ....*....|
gi 2172663953  401 KLLEGEESRI 410
Cdd:TIGR02169  427 AAIAGIEAKI 436
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
166-397 3.68e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 166 DRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLElerkieslmdeieflkKLHEEELRDLQVS 245
Cdd:COG3206   164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA----------------KLLLQQLSELESQ 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 246 VESQQVQQVEVEA---TVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQI 322
Cdd:COG3206   228 LAEARAELAEAEArlaALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL 307

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2172663953 323 QSLTCEV-DGLRGTNEALLRQLRELEEQFAlEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIA 397
Cdd:COG3206   308 QQEAQRIlASLEAELEALQAREASLQAQLA-QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 177-434 5.37e-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: 5.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  177 EDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHE---EELRDLQVSVESQQVQQ 253
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEklkERLEELEEDLSSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  254 VEVEATVK------PELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTC 327
Cdd:TIGR02169  754 ENVKSELKeleariEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  328 EVDGLRGTNEALLRQLRELEEQFAL----------EAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIA 397
Cdd:TIGR02169  834 EIQELQEQRIDLKEQIKSIEKEIENlngkkeeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2172663953  398 TYRKLLEGEESRISVPVHSFASLSLKTTVPEVEPPQD 434
Cdd:TIGR02169  914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-391 5.98e-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: 5.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  102 QELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVER--------- 172
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelkalreal 805

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  173 DGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQ 252
Cdd:TIGR02168  806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  253 QveveatvkpeltAALRDIRAQYENIAAKNlqeaeewykskyADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGL 332
Cdd:TIGR02168  886 E------------EALALLRSELEELSEEL------------RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2172663953  333 RGTneallrqlreLEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMA 391
Cdd:TIGR02168  942 QER----------LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 133-410 7.35e-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: 7.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  133 SQARGQEPARADQLCQQEL-RELRRELELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDAT 211
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  212 LSRLELERKIESLMDEIEFLKKlhEEELRDLQVSVESQQVQQVEVE-ATVKPELTAALRDIRAQYENIAAKNLQEAEEwy 290
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEA--EIEELEERLEEAEEELAEAEAEiEELEAQIEQLKEELKALREALDELRAELTLL-- 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  291 KSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFAL---EAGGYQAGAARLEEE 367
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSE 895

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2172663953  368 LRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRI 410
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 182-421 1.27e-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: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  182 LKQRLEEETRKREDAEHNLvlfrKDVDDAtlsRLELERKIESLMDEIEFLKKLHE--EELRDLQVSVESQQVQQVEVEAT 259
Cdd:TIGR02168  170 YKERRKETERKLERTRENL----DRLEDI---LNELERQLKSLERQAEKAERYKElkAELRELELALLVLRLEELREELE 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  260 VKPELTAALRDIRAQYENiAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEAL 339
Cdd:TIGR02168  243 ELQEELKEAEEELEELTA-ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  340 LRQLRELEEQfaleAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRISVPVHSFAS 419
Cdd:TIGR02168  322 EAQLEELESK----LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397


                   ..
gi 2172663953  420 LS 421
Cdd:TIGR02168  398 LN 399
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
215-411 1.84e-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: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  215 LELERKIESLmDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQYENIAAKnLQEAEEwyksKY 294
Cdd:COG4913    245 EDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE-LERLEA----RL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  295 ADLSDAANRNHEALRQAK-QEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKE 373
Cdd:COG4913    319 DALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2172663953  374 EMARHLREYQELLNVKMALDIEIATYRKLLEGEESRIS 411
Cdd:COG4913    399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
115-398 3.48e-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: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  115 IEKVRFLEQQNAALRGELSQARGQEpARADQLCQQELRELRRELELLGRERDRVQVerDGLAEDLGALKQRLEEEtrkrE 194
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERL-EALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAELEAELERL----D 681

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  195 DAEHNLVLFRKDVDDATLSRLELERKIESLMDEIeflkKLHEEELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQ 274
Cdd:COG4913    682 ASSDDLAALEEQLEELEAELEELEEELDELKGEI----GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  275 YenIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAkqeMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQfalea 354
Cdd:COG4913    758 A--LGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLDRLEED----- 827

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2172663953  355 ggyqaGAARLEEELRQLKEEmarhlREYQELLNVKMALDIEIAT 398
Cdd:COG4913    828 -----GLPEYEERFKELLNE-----NSIEFVADLLSKLRRAIRE 861
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 263-409 3.96e-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: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 263 ELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQ 342
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 343 LRELEEQFALEA---GGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESR 409
Cdd:COG1196   297 LARLEQDIARLEerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
313-410 6.72e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 313 QEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQfaleaggyqagAARLEEELRQLKEEMARHLREYQELlnvkMAL 392
Cdd:COG2433   406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDER-----------IERLERELSEARSEERREIRKDREI----SRL 470

                          90
                  ....*....|....*...
gi 2172663953 393 DIEIATYRKLLEGEESRI 410
Cdd:COG2433   471 DREIERLERELEEERERI 488
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 148-377 8.57e-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: 8.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 148 QQELRELRRELELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDdatlsrlELERKIESLMDE 227
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 228 IEFLKKLHEEELRDLQvsvesQQVQQVEVEATVKPE-LTAALRdiRAQYENIAAKNLQEAEEWYKSKYADLsdaaNRNHE 306
Cdd:COG4942    99 LEAQKEELAELLRALY-----RLGRQPPLALLLSPEdFLDAVR--RLQYLKYLAPARREQAEELRADLAEL----AALRA 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2172663953 307 ALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMAR 377
Cdd:COG4942   168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 75-350 1.19e-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: 41.58  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953   75 RLPSERLDFSMAEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQA---RGQEPARADQLCQQEL 151
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAeaeIEELEAQIEQLKEELK 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  152 RELRRELELLGRERD------RVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESL- 224
Cdd:TIGR02168  800 ALREALDELRAELTLlneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALl 879

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  225 --MDEIEFLKKLHEEELRDLqvsveSQQVQQVEVEATVKPELTAALRDIRAQYENIAAK---NLQEAEEWYKSKYADLSD 299
Cdd:TIGR02168  880 neRASLEEALALLRSELEEL-----SEELRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERLSEEYSLTLE 954

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2172663953  300 AANRNHEALrqaKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQF 350
Cdd:TIGR02168  955 EAEALENKI---EDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERY 1002
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
198-410 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 2172663953  198 HNLVLFRKDVDDATLSRLEL----ERKIESLMDEIEFLkklhEEELRDLQVSVESQQVQQveveatvkpeltAALRDIRA 273
Cdd:COG4913    585 GNGTRHEKDDRRRIRSRYVLgfdnRAKLAALEAELAEL----EEELAEAEERLEALEAEL------------DALQERRE 648

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  274 QYENIAA-----KNLQEAEEWYKSKYADLsDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEE 348
Cdd:COG4913    649 ALQRLAEyswdeIDVASAEREIAELEAEL-ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2172663953  349 QFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRI 410
Cdd:COG4913    728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 95-324 2.15e-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: 40.13  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  95 ATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLcQQELRELRRELELLGRERDRVQVERDG 174
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-RALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 175 LAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKlHEEELRDLQVSVESQQVQQV 254
Cdd:COG4942    99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELE 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953 255 EVEATVKPELTAALRDIRAQYENIAAknLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQS 324
Cdd:COG4942   178 ALLAELEEERAALEALKAERQKLLAR--LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 282-473 3.00e-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: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  282 NLQEAEEWY-KSK-YADLSD----AANRNHEALRQAKQEMNESRRQIQSLTCE--VDGLRGTNEALLRQLRELEEQFALE 353
Cdd:TIGR01612 1484 NINELKEHIdKSKgCKDEADknakAIEKNKELFEQYKKDVTELLNKYSALAIKnkFAKTKKDSEIIIKEIKDAHKKFILE 1563

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  354 AGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALD------IEIATYRK-----LLEGE--ESRISvpvhsfaSL 420
Cdd:TIGR01612 1564 AEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLEnfenkfLKISDIKKkindcLKETEsiEKKIS-------SF 1636

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2172663953  421 SLKTTVPEVEPPQDSHSrkmVLIRTIETRDGEKVVTESQKEQHSELDkSSIHS 473
Cdd:TIGR01612 1637 SIDSQDTELKENGDNLN---SLQEFLESLKDQKKNIEDKKKELDELD-SEIEK 1685
PTZ00121 PTZ00121
MAEBL; Provisional
 78-461 3.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953   78 SERLDFSMAEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRE 157
Cdd:PTZ00121  1459 AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  158 LELLGRERDRVQVERdglAEDLGALKQRLEEETRKREDAEHNLVLFRkdvddATLSRLELERKIESLMDEIEFLKKLHEE 237
Cdd:PTZ00121  1539 AKKAEEKKKADELKK---AEELKKAEEKKKAEEAKKAEEDKNMALRK-----AEEAKKAEEARIEEVMKLYEEEKKMKAE 1610

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  238 ELRDlqvsvesqqvqqvEVEATVKPELTAALRDIRAQYENIAAKnlqEAEEwyKSKYADLSDAANRNHEALRQAKQEMNE 317
Cdd:PTZ00121  1611 EAKK-------------AEEAKIKAEELKKAEEEKKKVEQLKKK---EAEE--KKKAEELKKAEEENKIKAAEEAKKAEE 1672

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  318 SRRQIQSLTCEVDGLRGTNEALLRQLREleeqfaleaggyqagaARLEEELRQLKEE---MARHLREYQELLNVKMAL-- 392
Cdd:PTZ00121  1673 DKKKAEEAKKAEEDEKKAAEALKKEAEE----------------AKKAEELKKKEAEekkKAEELKKAEEENKIKAEEak 1736

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  393 -----DIEIATYRKLLEGEESRIS-----VPVHSFASLSLKTTVPEVEPPQDSHSRKMVLIRTI-ETRDGEKVVTESQKE 461
Cdd:PTZ00121  1737 keaeeDKKKAEEAKKDEEEKKKIAhlkkeEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIkDIFDNFANIIEGGKE 1816
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 157-410 4.27e-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: 39.65  E-value: 4.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  157 ELELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKlHE 236
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER-QL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  237 EELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQyeNIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMN 316
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESL--EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  317 ESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFA-LEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIE 395
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476

                          250
                   ....*....|....*
gi 2172663953  396 IATYRKLLEGEESRI 410
Cdd:TIGR02168  477 LDAAERELAQLQARL 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 79-371 7.02e-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: 7.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953   79 ERLDFSMAEALNQEF-LATRSNEKQE-LQELNDRFANFIEKVRFLEQQNAALRGELSQargqeparadqlCQQELRELRR 156
Cdd:TIGR02168  242 EELQEELKEAEEELEeLTAELQELEEkLEELRLEVSELEEEIEELQKELYALANEISR------------LEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  157 ELELLGRERDRVQVERDGLAEDLGALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKK--- 233
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkva 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  234 --LHEEELRDLQVSVESQQVQQVEVEATvkpELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQA 311
Cdd:TIGR02168  390 qlELQIASLNNEIERLEARLERLEDRRE---RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663953  312 KQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEeqfaleagGYQAGAARLEEELRQL 371
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.
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