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Conserved domains on  [gi|1800417185|ref|NP_001364959|]
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coiled-coil domain-containing protein 78 isoform 3 [Homo sapiens]

Protein Classification

DUF4472 domain-containing protein( domain architecture ID 10631677)

DUF4472 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF4472 pfam14739
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ...
56-165 1.12e-31

Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members also carry Kinesin-motor domains at their N-terminus, Kinesin, pfam00225.


:

Pssm-ID: 464291 [Multi-domain]  Cd Length: 107  Bit Score: 117.02  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185  56 EQQLQISKELVDIQITTHHLHEQHEAEIFQLKSEILRLESRVLELELRGDGtsqgcAVPVESDPRHPRAAAQELRHKAQV 135
Cdd:pfam14739   3 EEKLQISKALVDLQIENNKLREQYEAEKFELKNKLLNLENRVLELELRLEK-----AAEEIQDLRERLRELEDDRRELAE 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 1800417185 136 PGHSDDHRFQVQPKNTMNPENEQHRLGSGL 165
Cdd:pfam14739  78 EFVALKKNYQALSKELEAEVAKNQELSLEL 107
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
156-313 5.94e-05

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: 45.68  E-value: 5.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185  156 NEQHRLGSGLQgevkwaLEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAEN-ARLQL 234
Cdd:COG4913    272 AELEYLRAALR------LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLER 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185  235 QLKKLKDEYVLRLQHCAwQAVEHADGAGQAPATTA-----LRTFLEATLEDIRAAHRSREQQLARAARsyhkRLVDLSRR 309
Cdd:COG4913    346 EIERLERELEERERRRA-RLEALLAALGLPLPASAeefaaLRAEAAALLEALEEELEALEEALAEAEA----ALRDLRRE 420

                   ....
gi 1800417185  310 HEEL 313
Cdd:COG4913    421 LREL 424
 
Name Accession Description Interval E-value
DUF4472 pfam14739
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ...
56-165 1.12e-31

Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members also carry Kinesin-motor domains at their N-terminus, Kinesin, pfam00225.


Pssm-ID: 464291 [Multi-domain]  Cd Length: 107  Bit Score: 117.02  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185  56 EQQLQISKELVDIQITTHHLHEQHEAEIFQLKSEILRLESRVLELELRGDGtsqgcAVPVESDPRHPRAAAQELRHKAQV 135
Cdd:pfam14739   3 EEKLQISKALVDLQIENNKLREQYEAEKFELKNKLLNLENRVLELELRLEK-----AAEEIQDLRERLRELEDDRRELAE 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 1800417185 136 PGHSDDHRFQVQPKNTMNPENEQHRLGSGL 165
Cdd:pfam14739  78 EFVALKKNYQALSKELEAEVAKNQELSLEL 107
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
156-313 5.94e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 5.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185  156 NEQHRLGSGLQgevkwaLEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAEN-ARLQL 234
Cdd:COG4913    272 AELEYLRAALR------LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLER 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185  235 QLKKLKDEYVLRLQHCAwQAVEHADGAGQAPATTA-----LRTFLEATLEDIRAAHRSREQQLARAARsyhkRLVDLSRR 309
Cdd:COG4913    346 EIERLERELEERERRRA-RLEALLAALGLPLPASAeefaaLRAEAAALLEALEEELEALEEALAEAEA----ALRDLRRE 420

                   ....
gi 1800417185  310 HEEL 313
Cdd:COG4913    421 LREL 424
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-313 8.46e-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: 8.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185   80 EAEIFQLKSEILRLESRVLELELRGDGTSQGCAVPVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQH 159
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185  160 RLgsglQGEVKWalEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKL 239
Cdd:TIGR02168  777 LA----EAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800417185  240 KDEyVLRLQHcawqavEHAD-GAGQAPATTALRTFLE--ATLEDIRAAHRSREQQLARAARSYHKRLVDLSRRHEEL 313
Cdd:TIGR02168  851 SED-IESLAA------EIEElEELIEELESELEALLNerASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
 
Name Accession Description Interval E-value
DUF4472 pfam14739
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ...
56-165 1.12e-31

Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members also carry Kinesin-motor domains at their N-terminus, Kinesin, pfam00225.


Pssm-ID: 464291 [Multi-domain]  Cd Length: 107  Bit Score: 117.02  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185  56 EQQLQISKELVDIQITTHHLHEQHEAEIFQLKSEILRLESRVLELELRGDGtsqgcAVPVESDPRHPRAAAQELRHKAQV 135
Cdd:pfam14739   3 EEKLQISKALVDLQIENNKLREQYEAEKFELKNKLLNLENRVLELELRLEK-----AAEEIQDLRERLRELEDDRRELAE 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 1800417185 136 PGHSDDHRFQVQPKNTMNPENEQHRLGSGL 165
Cdd:pfam14739  78 EFVALKKNYQALSKELEAEVAKNQELSLEL 107
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
156-313 5.94e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 5.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185  156 NEQHRLGSGLQgevkwaLEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAEN-ARLQL 234
Cdd:COG4913    272 AELEYLRAALR------LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLER 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185  235 QLKKLKDEYVLRLQHCAwQAVEHADGAGQAPATTA-----LRTFLEATLEDIRAAHRSREQQLARAARsyhkRLVDLSRR 309
Cdd:COG4913    346 EIERLERELEERERRRA-RLEALLAALGLPLPASAeefaaLRAEAAALLEALEEELEALEEALAEAEA----ALRDLRRE 420

                   ....
gi 1800417185  310 HEEL 313
Cdd:COG4913    421 LREL 424
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-313 8.46e-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: 8.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185   80 EAEIFQLKSEILRLESRVLELELRGDGTSQGCAVPVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQH 159
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185  160 RLgsglQGEVKWalEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKL 239
Cdd:TIGR02168  777 LA----EAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800417185  240 KDEyVLRLQHcawqavEHAD-GAGQAPATTALRTFLE--ATLEDIRAAHRSREQQLARAARSYHKRLVDLSRRHEEL 313
Cdd:TIGR02168  851 SED-IESLAA------EIEElEELIEELESELEALLNerASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
51-314 3.78e-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: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185  51 LALNKEQQLQISKELVDIQITTHHL-HEQHEAEIFQLKSEILRLESRVLELELRGDgtsqgcavpvesdprhpRAAAQEL 129
Cdd:COG1196   229 LLLLKLRELEAELEELEAELEELEAeLEELEAELAELEAELEELRLELEELELELE-----------------EAQAEEY 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185 130 RHKAQVPghsddhrfqvQPKNTMNPENEQHRLGSGLQGEVKWALEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLA 209
Cdd:COG1196   292 ELLAELA----------RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417185 210 TQAvvlcscqGQLRQAEAENARLQLQLKKLKDEYVLRLQHCAWQAVEHADGAGQAPATTALRTFLEATLEDIRAAHRSRE 289
Cdd:COG1196   362 EAE-------EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
                         250       260
                  ....*....|....*....|....*
gi 1800417185 290 QQLARAARSYHKRLVDLSRRHEELL 314
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEE 459
 
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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