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Conserved domains on  [gi|61742829|ref|NP_001012977|]
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disrupted in schizophrenia 1 protein isoform S [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
329-488 2.28e-04

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829  329 LLRKWEPVLRDCLLRNRRQMEVISLRLKLQKLQEDAVE----NDDYDKAETLQQRLEDLEQEK--------------ISL 390
Cdd:COG4913  292 LLEAELEELRAELARLEAELERLEARLDALREELDELEaqirGNGGDRLEQLEREIERLERELeererrrarleallAAL 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829  391 HFQLPSRQPALSSflghLAAQVQAALRRGATQQASGDDthtplrmeprlleptAQDSLHVSITRrdwLLQEKQQLQKEIE 470
Cdd:COG4913  372 GLPLPASAEEFAA----LRAEAAALLEALEEELEALEE---------------ALAEAEAALRD---LRRELRELEAEIA 429
                        170
                 ....*....|....*...
gi 61742829  471 ALQARMFVLEAKDQQLRR 488
Cdd:COG4913  430 SLERRKSNIPARLLALRD 447
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
461-659 5.41e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 5.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829    461 EKQQLQKEIEALQARMFVLEAKDQQLRREIEEQEQQLQWQGCDLTPLvgQLSLGQLQEVSKALQDTLASAG--QIPFHAE 538
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL--EEDLHKLEEALNDLEARLSHSRipEIQAELS 801
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829    539 PPETIRS-LQERIKSLNLSLKEITTKVCMSEKFCSTLRKKVNDIETQLpALLEAKMHAISGNHFWTAKDLTE---EIRSL 614
Cdd:TIGR02169  802 KLEEEVSrIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI-KSIEKEIENLNGKKEELEEELEEleaALRDL 880
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 61742829    615 TSEREGLEGLLSKLLVLSSRNVKKLGSVKEDYNRLRREVEHQETA 659
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
 
Name Accession Description Interval E-value
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
329-488 2.28e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829  329 LLRKWEPVLRDCLLRNRRQMEVISLRLKLQKLQEDAVE----NDDYDKAETLQQRLEDLEQEK--------------ISL 390
Cdd:COG4913  292 LLEAELEELRAELARLEAELERLEARLDALREELDELEaqirGNGGDRLEQLEREIERLERELeererrrarleallAAL 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829  391 HFQLPSRQPALSSflghLAAQVQAALRRGATQQASGDDthtplrmeprlleptAQDSLHVSITRrdwLLQEKQQLQKEIE 470
Cdd:COG4913  372 GLPLPASAEEFAA----LRAEAAALLEALEEELEALEE---------------ALAEAEAALRD---LRRELRELEAEIA 429
                        170
                 ....*....|....*...
gi 61742829  471 ALQARMFVLEAKDQQLRR 488
Cdd:COG4913  430 SLERRKSNIPARLLALRD 447
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
461-659 5.41e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 5.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829    461 EKQQLQKEIEALQARMFVLEAKDQQLRREIEEQEQQLQWQGCDLTPLvgQLSLGQLQEVSKALQDTLASAG--QIPFHAE 538
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL--EEDLHKLEEALNDLEARLSHSRipEIQAELS 801
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829    539 PPETIRS-LQERIKSLNLSLKEITTKVCMSEKFCSTLRKKVNDIETQLpALLEAKMHAISGNHFWTAKDLTE---EIRSL 614
Cdd:TIGR02169  802 KLEEEVSrIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI-KSIEKEIENLNGKKEELEEELEEleaALRDL 880
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 61742829    615 TSEREGLEGLLSKLLVLSSRNVKKLGSVKEDYNRLRREVEHQETA 659
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
 
Name Accession Description Interval E-value
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
329-488 2.28e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829  329 LLRKWEPVLRDCLLRNRRQMEVISLRLKLQKLQEDAVE----NDDYDKAETLQQRLEDLEQEK--------------ISL 390
Cdd:COG4913  292 LLEAELEELRAELARLEAELERLEARLDALREELDELEaqirGNGGDRLEQLEREIERLERELeererrrarleallAAL 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829  391 HFQLPSRQPALSSflghLAAQVQAALRRGATQQASGDDthtplrmeprlleptAQDSLHVSITRrdwLLQEKQQLQKEIE 470
Cdd:COG4913  372 GLPLPASAEEFAA----LRAEAAALLEALEEELEALEE---------------ALAEAEAALRD---LRRELRELEAEIA 429
                        170
                 ....*....|....*...
gi 61742829  471 ALQARMFVLEAKDQQLRR 488
Cdd:COG4913  430 SLERRKSNIPARLLALRD 447
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
461-659 5.41e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 5.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829    461 EKQQLQKEIEALQARMFVLEAKDQQLRREIEEQEQQLQWQGCDLTPLvgQLSLGQLQEVSKALQDTLASAG--QIPFHAE 538
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL--EEDLHKLEEALNDLEARLSHSRipEIQAELS 801
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829    539 PPETIRS-LQERIKSLNLSLKEITTKVCMSEKFCSTLRKKVNDIETQLpALLEAKMHAISGNHFWTAKDLTE---EIRSL 614
Cdd:TIGR02169  802 KLEEEVSrIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI-KSIEKEIENLNGKKEELEEELEEleaALRDL 880
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 61742829    615 TSEREGLEGLLSKLLVLSSRNVKKLGSVKEDYNRLRREVEHQETA 659
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
337-488 9.74e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 9.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61742829 337 LRDCLLRNRRQMEviSLRLKLQKLQEDAVENDDYDKAETLQQRLEDLEQEKIslhfQLPSRQPALSSFLghlaAQVQAAL 416
Cdd:COG4717  93 LQEELEELEEELE--ELEAELEELREELEKLEKLLQLLPLYQELEALEAELA----ELPERLEELEERL----EELRELE 162
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61742829 417 RRGATQQASGDDTHTPLRMEPRLLEPTAQDSLHVSITRRDWLLQEKQQLQKEIEALQARmfvLEAKDQQLRR 488
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE---LEELEEELEQ 231
 
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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