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Conserved domains on  [gi|254675335|ref|NP_038667|]
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peripherin isoform 1 [Mus musculus]

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

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List of domain hits

 Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
100-442 6.20e-116

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 344.21  E-value: 6.20e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  100 NEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQ---EPARADQLCQQELRELRRELELLGRERDRVQVERDGL 176
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  177 AEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVqQVE 256
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQV-NVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  257 VEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKvrehwgnpggprvgrhwewrcasqpglsataqYADLSDAANR 336
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSK--------------------------------LEELQQAAAR 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  337 NHEALRQAKQEMNESRRQIQSLMCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQ 416
Cdd:pfam00038 208 NGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQ 287

                         330       340
                  ....*....|....*....|....*.
gi 254675335  417 ELLNVKMALDIEIATYRKLLEGEESR 442
Cdd:pfam00038 288 ELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 22-99 2.09e-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: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   22 TSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSGSPS--SSARLGSFRAPRAGALRLPSERLDFSMAEALNQEFLATRS 99
Cdd:pfam04732   4 SSYRRMFGDSSSSRPSYSSSSGSRSVSSRSYSRSSSSSpsSSSRRSSRSSSRSSYPSLAADSLDFSLADALNQEFKATRT 83
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
100-442 6.20e-116

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 344.21  E-value: 6.20e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  100 NEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQ---EPARADQLCQQELRELRRELELLGRERDRVQVERDGL 176
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  177 AEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVqQVE 256
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQV-NVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  257 VEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKvrehwgnpggprvgrhwewrcasqpglsataqYADLSDAANR 336
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSK--------------------------------LEELQQAAAR 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  337 NHEALRQAKQEMNESRRQIQSLMCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQ 416
Cdd:pfam00038 208 NGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQ 287

                         330       340
                  ....*....|....*....|....*.
gi 254675335  417 ELLNVKMALDIEIATYRKLLEGEESR 442
Cdd:pfam00038 288 ELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 22-99 2.09e-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: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   22 TSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSGSPS--SSARLGSFRAPRAGALRLPSERLDFSMAEALNQEFLATRS 99
Cdd:pfam04732   4 SSYRRMFGDSSSSRPSYSSSSGSRSVSSRSYSRSSSSSpsSSSRRSSRSSSRSSYPSLAADSLDFSLADALNQEFKATRT 83
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-424 4.72e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 4.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   102 KQELQELNDRFANFIEKVRFLEQQNAALRGELS---------QARGQEPARADQLCQQELRELRRELELLGRERDRVQVE 172
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEeleeeleqlRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   173 RDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIeflkKLHEEELRDLQVSVESQQV 252
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL----TLLNEEAANLRERLESLER 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   253 QQVEVEATVKpELTAALRDIRAQYENIAA--KNLQEAEEWYKSKVrEHWGNpggprvgrhwEWRCASQPGLSATAQYADL 330
Cdd:TIGR02168  832 RIAATERRLE-DLEEQIEELSEDIESLAAeiEELEELIEELESEL-EALLN----------ERASLEEALALLRSELEEL 899

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   331 SdaanrnhEALRQAKQEMNESRRQIQSLMCEVDGLRGTNEALLRQLRELEEQFA----LEAGGYQAGAARLEEELRQLKE 406
Cdd:TIGR02168  900 S-------EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysLTLEEAEALENKIEDDEEEARR 972

                          330
                   ....*....|....*...
gi 254675335   407 EMARHLREYQELLNVKMA 424
Cdd:TIGR02168  973 RLKRLENKIKELGPVNLA 990
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-437 4.98e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 4.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 160 ELLGRERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLEL---ERKIESLMDEIEFLKKLH 236
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIARL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 237 EEELRDLQVSVESQQVQQVEVEATVKpELTAALRDIRAQYENIAAKNLQEAEEWYKSKVREhwgnpggprvgrhwewrca 316
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELE-ELEEELEELEEELEEAEEELEEAEAELAEAEEAL------------------- 367

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 317 sqpgLSATAQYADLSDAANRNHEALRQAKQEMNESRRQIQSLMCEVDGLRGTNEALLRQLRELEEQFALEAggyqAGAAR 396
Cdd:COG1196  368 ----LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE----EEEEE 439

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 254675335 397 LEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLE 437
Cdd:COG1196  440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
100-442 6.20e-116

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 344.21  E-value: 6.20e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  100 NEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQ---EPARADQLCQQELRELRRELELLGRERDRVQVERDGL 176
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  177 AEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVqQVE 256
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQV-NVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  257 VEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKvrehwgnpggprvgrhwewrcasqpglsataqYADLSDAANR 336
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSK--------------------------------LEELQQAAAR 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  337 NHEALRQAKQEMNESRRQIQSLMCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQ 416
Cdd:pfam00038 208 NGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQ 287

                         330       340
                  ....*....|....*....|....*.
gi 254675335  417 ELLNVKMALDIEIATYRKLLEGEESR 442
Cdd:pfam00038 288 ELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 22-99 2.09e-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: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   22 TSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSGSPS--SSARLGSFRAPRAGALRLPSERLDFSMAEALNQEFLATRS 99
Cdd:pfam04732   4 SSYRRMFGDSSSSRPSYSSSSGSRSVSSRSYSRSSSSSpsSSSRRSSRSSSRSSYPSLAADSLDFSLADALNQEFKATRT 83
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-424 4.72e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 4.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   102 KQELQELNDRFANFIEKVRFLEQQNAALRGELS---------QARGQEPARADQLCQQELRELRRELELLGRERDRVQVE 172
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEeleeeleqlRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   173 RDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIeflkKLHEEELRDLQVSVESQQV 252
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL----TLLNEEAANLRERLESLER 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   253 QQVEVEATVKpELTAALRDIRAQYENIAA--KNLQEAEEWYKSKVrEHWGNpggprvgrhwEWRCASQPGLSATAQYADL 330
Cdd:TIGR02168  832 RIAATERRLE-DLEEQIEELSEDIESLAAeiEELEELIEELESEL-EALLN----------ERASLEEALALLRSELEEL 899

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   331 SdaanrnhEALRQAKQEMNESRRQIQSLMCEVDGLRGTNEALLRQLRELEEQFA----LEAGGYQAGAARLEEELRQLKE 406
Cdd:TIGR02168  900 S-------EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysLTLEEAEALENKIEDDEEEARR 972

                          330
                   ....*....|....*...
gi 254675335   407 EMARHLREYQELLNVKMA 424
Cdd:TIGR02168  973 RLKRLENKIKELGPVNLA 990
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-437 4.98e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 4.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 160 ELLGRERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLEL---ERKIESLMDEIEFLKKLH 236
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIARL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 237 EEELRDLQVSVESQQVQQVEVEATVKpELTAALRDIRAQYENIAAKNLQEAEEWYKSKVREhwgnpggprvgrhwewrca 316
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELE-ELEEELEELEEELEEAEEELEEAEAELAEAEEAL------------------- 367

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 317 sqpgLSATAQYADLSDAANRNHEALRQAKQEMNESRRQIQSLMCEVDGLRGTNEALLRQLRELEEQFALEAggyqAGAAR 396
Cdd:COG1196  368 ----LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE----EEEEE 439

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 254675335 397 LEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLE 437
Cdd:COG1196  440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 178-445 5.22e-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: 5.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   178 EDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEV 257
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   258 EAtVKPELTAALRDIRAQYENIAakNLQEAEEWYKSKVREHwgnpGGPRVGRHWEWRCASQPGLSATAQyaDLSDAANRN 337
Cdd:TIGR02169  754 EN-VKSELKELEARIEELEEDLH--KLEEALNDLEARLSHS----RIPEIQAELSKLEEEVSRIEARLR--EIEQKLNRL 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   338 HEALRQAKQEMNESRRQIQSLMCEVDGLRGTNEALLRQLRELEEQFAleagGYQAGAARLEEELRQLKEEMARHLREYQE 417
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE----ELEAALRDLESRLGDLKKERDELEAQLRE 900

                          250       260
                   ....*....|....*....|....*...
gi 254675335   418 LLNVKMALDIEIATYRKLLEGEESRISV 445
Cdd:TIGR02169  901 LERKIEELEAQIEKKRKRLSELKAKLEA 928
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 87-443 8.21e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 8.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  87 AEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRELELLGRER 166
Cdd:COG1196  307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 167 DRVQVERD--GLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQ 244
Cdd:COG1196  387 ELLEALRAaaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 245 VSVESQQVQQVEVEatvkpELTAALRDIRAQYEniAAKNLQEAEEWYKSKVREHWGNPGGPRVGRHWEWRCASQPGLSAT 324
Cdd:COG1196  467 ELLEEAALLEAALA-----ELLEELAEAAARLL--LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA 539

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 325 AQYADLSDAANRNHEALRQAKQEMNESRRQIQSlmcevdglRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQl 404
Cdd:COG1196  540 LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG--------RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE- 610

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 254675335 405 kEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRI 443
Cdd:COG1196  611 -ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 87-289 1.34e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  87 AEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELS---QARGQEPARADQLcQQELRELRRELELLG 163
Cdd:COG1196  258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleERRRELEERLEEL-EEELAELEEELEELE 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 164 RERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDL 243
Cdd:COG1196  337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 254675335 244 QvSVESQQVQQVEVEATVKPELTAALRDIRAQYENIAAKNLQEAEE 289
Cdd:COG1196  417 E-RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
218-430 1.64e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 218 LERKIESLMDEIEFLKK---LHEEELRDLQVSVES--QQVQQVEVEATVKPeLTAALRDIRAQYENIAAKnLQEAEEWYK 292
Cdd:COG3206  166 LELRREEARKALEFLEEqlpELRKELEEAEAALEEfrQKNGLVDLSEEAKL-LLQQLSELESQLAEARAE-LAEAEARLA 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 293 SKVREHWGNPGG-PRVGRHWEWRCASQPGLSATAQYADLSDAANRNHEALRQAKQEMNESRRQIQSLMCEV-DGLRGTNE 370
Cdd:COG3206  244 ALRAQLGSGPDAlPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELE 323

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 371 ALLRQLRELEEQFAlEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIA 430
Cdd:COG3206  324 ALQAREASLQAQLA-QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
346-443 6.93e-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: 6.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 346 QEMNESRRQIQSLMCEVDGLRGTNEALLRQLRELEEQfaleaggyqagAARLEEELRQLKEEMARHLREYQELlnvkMAL 425
Cdd:COG2433  406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDER-----------IERLERELSEARSEERREIRKDREI----SRL 470

                         90
                 ....*....|....*...
gi 254675335 426 DIEIATYRKLLEGEESRI 443
Cdd:COG2433  471 DREIERLERELEEERERI 488
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 167-443 1.21e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   167 DRVQVERDGlAEDLAALKQRLEE-----ETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELR 241
Cdd:TIGR02169  201 ERLRREREK-AERYQALLKEKREyegyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   242 DLQVSVESQQVQQVEVEATVKPELTAALRDIRAqyeniAAKNLQEAEEwykskvrehwgnpggprvgrhwewrcasqpgl 321
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAE-----KERELEDAEE-------------------------------- 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   322 sATAQYADLSDAANRNHEALRQAKQEMNESRRQIQSlmcEVDGLRGTNEALLRQLRELEEQFALeaggYQAGAARLEEEL 401
Cdd:TIGR02169  323 -RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE---EYAELKEELEDLRAELEEVDKEFAE----TRDELKDYREKL 394

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 254675335   402 RQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRI 443
Cdd:TIGR02169  395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 172-434 1.83e-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: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 172 ERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLkklhEEELRDLQVSVESQQ 251
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIAELR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 252 VQQVEVEATVKPELTAALRDIRAQYENIaaknLQEAEEWYKSKVREHWgnpggprvgrhwewrcasqpglsataqYADLS 331
Cdd:COG4942   97 AELEAQKEELAELLRALYRLGRQPPLAL----LLSPEDFLDAVRRLQY---------------------------LKYLA 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 332 DAANRNHEALRQAKQEMNESRRQIQSLMCEVDGLRGTNEALLRQLRELEEQfaleaggYQAGAARLEEELRQLKEEMARH 411
Cdd:COG4942  146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE-------RQKLLARLEKELAELAAELAEL 218

                        250       260
                 ....*....|....*....|...
gi 254675335 412 LREYQELLNVKMALDIEIATYRK 434
Cdd:COG4942  219 QQEAEELEALIARLEAEAAAAAE 241
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-404 2.89e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  92 QEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQL----------------CQQELREL 155
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaqaeeyellaelarLEQDIARL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 156 RRELELLGRERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKL 235
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 236 HEEELRDLQvsVESQQVQQVEVEATVKPELTAALRDIRAQYENIAAKNLQEAEEwykskvrehwgnpggprvgrhwewrc 315
Cdd:COG1196  388 LLEALRAAA--ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE-------------------------- 439

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 316 ASQPGLSATAQYADLSDAANRNHEALRQAKQEMNESRRQIQSLmcevdgLRGTNEALLRQLRELEEQFALEAGGYQAGAA 395
Cdd:COG1196  440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL------LEELAEAAARLLLLLEAEADYEGFLEGVKAA 513


                 ....*....
gi 254675335 396 RLEEELRQL 404
Cdd:COG1196  514 LLLAGLRGL 522
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
323-444 4.43e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  323 ATAQYADLSDAANRNHEALRQAKQEMNES--------RRQIQSLMCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGA 394
Cdd:COG4913   307 LEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 254675335  395 ARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRIS 444
Cdd:COG4913   387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 134-443 5.07e-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: 5.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   134 SQARGQEPARADQLCQQEL-RELRRELELLGRERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDAT 212
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   213 LSRLELERKIESLMDEIEFLK--------KLHEEELRDLQVSVESQQVQQ-VEVEATVKPELTAALRDIRAQY--ENIAA 281
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEaeieeleeRLEEAEEELAEAEAEIEELEAqIEQLKEELKALREALDELRAELtlLNEEA 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   282 KNLQEAEEWYKSKVREhwgnPGGPRVGRHWEWRCASQPGLSATAQYADLSDAANRNHEAL-------RQAKQEMNESRRQ 354
Cdd:TIGR02168  820 ANLRERLESLERRIAA----TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELeallnerASLEEALALLRSE 895

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335   355 IQSLMCEVDGLRGTNEALLRQLRELEEQFAleagGYQAGAARLEEELRQLKEEMArhlREYQELLNVKMALDIEIATYRK 434
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREKLA----QLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEE 968


                   ....*....
gi 254675335   435 LLEGEESRI 443
Cdd:TIGR02168  969 EARRRLKRL 977
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
178-412 5.93e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  178 EDLAALKQRLEEETRKREDAEHnLVLFRKDVDDATLSRLELERKIESLMDEIEFLK-KLHEEELRDLQVSVESQQVQQVE 256
Cdd:COG4913   235 DDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELER 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335  257 VEATVKpELTAALRDIRAQYENIAAKNLQEAEEWYKSKVREHwgnpggprvgRHWEWRCASQPGLSATAQYADLSDAA-- 334
Cdd:COG4913   314 LEARLD-ALREELDELEAQIRGNGGDRLEQLEREIERLEREL----------EERERRRARLEALLAALGLPLPASAEef 382

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675335  335 NRNHEALRQAKQEMNESRRQIQSlmcEVDGLRGTNEALLRQLRELEEQFAleagGYQAGAARLEEELRQLKEEMARHL 412
Cdd:COG4913   383 AALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIA----SLERRKSNIPARLLALRDALAEAL 453
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 103-281 6.48e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 6.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 103 QELQELNDRFANFIEKVRFLEQQNAALRGELSQARGqepARADQLCQQELRELRRELELLGRERDRVQVERDGLAEDLAA 182
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKT---ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 183 LKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEATVK 262
Cdd:COG1579   94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173

                        170
                 ....*....|....*....
gi 254675335 263 PELTAALRDIRAQYENIAA 281
Cdd:COG1579  174 PELLALYERIRKRKNGLAV 192
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 168-281 7.12e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.29  E-value: 7.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675335 168 RVQVERDGLAEDLAALKQRLEEETRKREDAEhnlvlfrKDVDDATLSRL-ELERKIESLMDEIEFLKKLHEEELRDLQVS 246
Cdd:COG0542  401 RVRMEIDSKPEELDELERRLEQLEIEKEALK-------KEQDEASFERLaELRDELAELEEELEALKARWEAEKELIEEI 473

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 254675335 247 VESQqvQQVEVEATVKPELTAALRDIRAQYENIAA 281
Cdd:COG0542  474 QELK--EELEQRYGKIPELEKELAELEEELAELAP 506
 
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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