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Conserved domains on  [gi|578827969|ref|XP_006720906|]
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coiled-coil domain-containing protein 78 isoform X18 [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 5.76e-33

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: 120.87  E-value: 5.76e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969   56 EQQLQISKELVDIQITTHHLHEQHEAEIFQLKSEILRLESRVLELELRGDGtsqgcAVPVESDPRHPRAAAQELRHKAQV 135
Cdd:pfam14739   3 EEKLQISKALVDLQIENNKLREQYEAEKFELKNKLLNLENRVLELELRLEK-----AAEEIQDLRERLRELEDDRRELAE 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 578827969  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 1.80e-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: 47.60  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969  156 NEQHRLGSGLQgevkwaLEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAEN-ARLQL 234
Cdd:COG4913   272 AELEYLRAALR------LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLER 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969  235 QLKKLKDEYVLRLQHCAwQAVEHADGAGQAPATTA-----LRTFLEATLEDIRAAHRSREQQLARAARsyhkRLVDLSRR 309
Cdd:COG4913   346 EIERLERELEERERRRA-RLEALLAALGLPLPASAeefaaLRAEAAALLEALEEELEALEEALAEAEA----ALRDLRRE 420

                  ....
gi 578827969  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 5.76e-33

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: 120.87  E-value: 5.76e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969   56 EQQLQISKELVDIQITTHHLHEQHEAEIFQLKSEILRLESRVLELELRGDGtsqgcAVPVESDPRHPRAAAQELRHKAQV 135
Cdd:pfam14739   3 EEKLQISKALVDLQIENNKLREQYEAEKFELKNKLLNLENRVLELELRLEK-----AAEEIQDLRERLRELEDDRRELAE 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 578827969  136 PGHSDDHRFQVQPKNTMNPENEQHRLGSGL 165
Cdd:pfam14739  78 EFVALKKNYQALSKELEAEVAKNQELSLEL 107
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
156-313 1.80e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969  156 NEQHRLGSGLQgevkwaLEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAEN-ARLQL 234
Cdd:COG4913   272 AELEYLRAALR------LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLER 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969  235 QLKKLKDEYVLRLQHCAwQAVEHADGAGQAPATTA-----LRTFLEATLEDIRAAHRSREQQLARAARsyhkRLVDLSRR 309
Cdd:COG4913   346 EIERLERELEERERRRA-RLEALLAALGLPLPASAeefaaLRAEAAALLEALEEELEALEEALAEAEA----ALRDLRRE 420

                  ....
gi 578827969  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 2.18e-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: 47.36  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969    80 EAEIFQLKSEILRLESRVLELELRGDGTSQGCAVPVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQH 159
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969   160 RLgsglQGEVKWalEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKL 239
Cdd:TIGR02168  777 LA----EAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578827969   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 5.76e-33

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: 120.87  E-value: 5.76e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969   56 EQQLQISKELVDIQITTHHLHEQHEAEIFQLKSEILRLESRVLELELRGDGtsqgcAVPVESDPRHPRAAAQELRHKAQV 135
Cdd:pfam14739   3 EEKLQISKALVDLQIENNKLREQYEAEKFELKNKLLNLENRVLELELRLEK-----AAEEIQDLRERLRELEDDRRELAE 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 578827969  136 PGHSDDHRFQVQPKNTMNPENEQHRLGSGL 165
Cdd:pfam14739  78 EFVALKKNYQALSKELEAEVAKNQELSLEL 107
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
156-313 1.80e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969  156 NEQHRLGSGLQgevkwaLEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAEN-ARLQL 234
Cdd:COG4913   272 AELEYLRAALR------LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLER 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969  235 QLKKLKDEYVLRLQHCAwQAVEHADGAGQAPATTA-----LRTFLEATLEDIRAAHRSREQQLARAARsyhkRLVDLSRR 309
Cdd:COG4913   346 EIERLERELEERERRRA-RLEALLAALGLPLPASAeefaaLRAEAAALLEALEEELEALEEALAEAEA----ALRDLRRE 420

                  ....
gi 578827969  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 2.18e-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: 47.36  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969    80 EAEIFQLKSEILRLESRVLELELRGDGTSQGCAVPVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQH 159
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969   160 RLgsglQGEVKWalEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKL 239
Cdd:TIGR02168  777 LA----EAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578827969   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 8.60e-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: 8.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969  51 LALNKEQQLQISKELVDIQITTHHL-HEQHEAEIFQLKSEILRLESRVLELELRGDgtsqgcavpvesdprhpRAAAQEL 129
Cdd:COG1196  229 LLLLKLRELEAELEELEAELEELEAeLEELEAELAELEAELEELRLELEELELELE-----------------EAQAEEY 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969 130 RHKAQVPghsddhrfqvQPKNTMNPENEQHRLGSGLQGEVKWALEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLA 209
Cdd:COG1196  292 ELLAELA----------RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969 210 TQAvvlcscqGQLRQAEAENARLQLQLKKLKDEYVLRLQHCAWQAVEHADGAGQAPATTALRTFLEATLEDIRAAHRSRE 289
Cdd:COG1196  362 EAE-------EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
                        250       260
                 ....*....|....*....|....*
gi 578827969 290 QQLARAARSYHKRLVDLSRRHEELL 314
Cdd:COG1196  435 EEEEEEEEALEEAAEEEAELEEEEE 459
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
114-401 6.76e-03

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 39.07  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969  114 PVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQHRLGSGLQGEVKWALEHQEARQQALVTRVATLGRQ 193
Cdd:COG1020     3 AAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969  194 LQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKLKDEYVLRLQHCAWQAVEHADGAGQAPATTALRTF 273
Cdd:COG1020    83 VQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578827969  274 LEATLEDIRAAHRSREQQLARAARSYHkrlvDLSRRHEELLVAYRAPGnpQAIFDIASLDLEPLPVPLVTDFShredqhg 353
Cdd:COG1020   163 LAELLRLYLAAYAGAPLPLPPLPIQYA----DYALWQREWLQGEELAR--QLAYWRQQLAGLPPLLELPTDRP------- 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578827969  354 gpgallsspkkRPGGASQGGTSEPQGLDAASWaqihQKLRDFSRSTQV 401
Cdd:COG1020   230 -----------RPAVQSYRGARVSFRLPAELT----AALRALARRHGV 262
 
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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