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Conserved domains on  [gi|221040448|dbj|BAH11931|]
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unnamed protein product [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cobl pfam09469
Cordon-bleu ubiquitin-like domain; The Cordon-bleu protein domain is highly conserved among ...
 197-275 4.80e-41

Cordon-bleu ubiquitin-like domain; The Cordon-bleu protein domain is highly conserved among vertebrates. The sequence contains three repeated lysine, arginine, and proline-rich regions, the KKRAP motif. The exact function of the protein is unknown but it is thought to be involved in mid-brain neural tube closure. It is expressed specifically in the node. This domain has a ubiquitin-like fold.


:

Pssm-ID: 462810  Cd Length: 79  Bit Score: 145.42  E-value: 4.80e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221040448   197 EKTVRVVINFKKTQKTIVRVSPHASLQELAPIICSKCEFDPLHTLLLKDYQSQEPLDLTKSLNDLGLRELYAMDVNRAT 275
Cdd:pfam09469    1 EKTVRLVVNYKKTQKAVVRVSPHVPLQELLPIICSKCEFDPLHVLLLKDYISQEELDLTKSLNDLGIKELYAMDVNRES 79
WH2_Wc_Cobl cd21801
third Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wc) found in ...
 1182-1207 1.60e-09

third Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wc) found in protein Cordon-Bleu (Cobl) and similar proteins; This family contains the third tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2), called Wc, found in protein Cordon-Bleu (Cobl), a potent actin filament nucleator that plays an important role in the reorganization of the actin cytoskeleton. It regulates neuron morphogenesis and increases branching of axons and dendrites. It also modulates dendrite branching in Purkinje cells. Cobl binds to and sequesters actin monomers (G-actin). Cobl contains three tandem WH2 (or W) domains consisting of an N-terminal alpha helix and a C-terminal LRKV motif. The first two WH2 domains have the highest binding affinity for actin. They are functionally active in actin nucleation and polymerization. The model corresponds to the first WH2 domain.


:

Pssm-ID: 409199  Cd Length: 26  Bit Score: 53.85  E-value: 1.60e-09
                          10        20
                  ....*....|....*....|....*.
gi 221040448 1182 DPEQMRQSLLTAIRSGEAAAKLKRVT 1207
Cdd:cd21801     1 NPEQARQALLEAIRSGEGAARLKKVP 26
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 894-1131 2.19e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448  894 PEEPLPNLKPKPNLRTEHQVPSSVSSPDDAMVSPLKPAPKMTRDTGTAPFAPnleeinnilESKFKSRASNAQAKPSSFF 973
Cdd:PHA03247 2776 AAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP---------LPPPTSAQPTAPPPPPGPP 2846

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448  974 ---LQMQKRVS--GHYVTSAAAKSVHAAPNPAPKELTDKEAERDMLPSPE-QTLSPLSKMPHSVPQPLVEKTDDDVIGQA 1047
Cdd:PHA03247 2847 ppsLPLGGSVApgGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALPPDQPERPPQPQAPPPPQPQPQPPPP 2926

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448 1048 PAEASPPPIAPKPVTIPASQVSTQnlktlktfGAPRPySSSGPSPFALAVVKRSQSFSKERTESPSASalVQPPANTEEG 1127
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPA--------GAGEP-SGAVPQPWLGALVPGRVAVPRFRVPQPAPS--REAPASSTPP 2995


                  ....
gi 221040448 1128 KTHS 1131
Cdd:PHA03247 2996 LTGH 2999
 
Name Accession Description Interval E-value
Cobl pfam09469
Cordon-bleu ubiquitin-like domain; The Cordon-bleu protein domain is highly conserved among ...
 197-275 4.80e-41

Cordon-bleu ubiquitin-like domain; The Cordon-bleu protein domain is highly conserved among vertebrates. The sequence contains three repeated lysine, arginine, and proline-rich regions, the KKRAP motif. The exact function of the protein is unknown but it is thought to be involved in mid-brain neural tube closure. It is expressed specifically in the node. This domain has a ubiquitin-like fold.


Pssm-ID: 462810  Cd Length: 79  Bit Score: 145.42  E-value: 4.80e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221040448   197 EKTVRVVINFKKTQKTIVRVSPHASLQELAPIICSKCEFDPLHTLLLKDYQSQEPLDLTKSLNDLGLRELYAMDVNRAT 275
Cdd:pfam09469    1 EKTVRLVVNYKKTQKAVVRVSPHVPLQELLPIICSKCEFDPLHVLLLKDYISQEELDLTKSLNDLGIKELYAMDVNRES 79
WH2_Wc_Cobl cd21801
third Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wc) found in ...
 1182-1207 1.60e-09

third Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wc) found in protein Cordon-Bleu (Cobl) and similar proteins; This family contains the third tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2), called Wc, found in protein Cordon-Bleu (Cobl), a potent actin filament nucleator that plays an important role in the reorganization of the actin cytoskeleton. It regulates neuron morphogenesis and increases branching of axons and dendrites. It also modulates dendrite branching in Purkinje cells. Cobl binds to and sequesters actin monomers (G-actin). Cobl contains three tandem WH2 (or W) domains consisting of an N-terminal alpha helix and a C-terminal LRKV motif. The first two WH2 domains have the highest binding affinity for actin. They are functionally active in actin nucleation and polymerization. The model corresponds to the first WH2 domain.


Pssm-ID: 409199  Cd Length: 26  Bit Score: 53.85  E-value: 1.60e-09
                          10        20
                  ....*....|....*....|....*.
gi 221040448 1182 DPEQMRQSLLTAIRSGEAAAKLKRVT 1207
Cdd:cd21801     1 NPEQARQALLEAIRSGEGAARLKKVP 26
PHA03247 PHA03247
large tegument protein UL36; Provisional
 894-1131 2.19e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448  894 PEEPLPNLKPKPNLRTEHQVPSSVSSPDDAMVSPLKPAPKMTRDTGTAPFAPnleeinnilESKFKSRASNAQAKPSSFF 973
Cdd:PHA03247 2776 AAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP---------LPPPTSAQPTAPPPPPGPP 2846

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448  974 ---LQMQKRVS--GHYVTSAAAKSVHAAPNPAPKELTDKEAERDMLPSPE-QTLSPLSKMPHSVPQPLVEKTDDDVIGQA 1047
Cdd:PHA03247 2847 ppsLPLGGSVApgGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALPPDQPERPPQPQAPPPPQPQPQPPPP 2926

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448 1048 PAEASPPPIAPKPVTIPASQVSTQnlktlktfGAPRPySSSGPSPFALAVVKRSQSFSKERTESPSASalVQPPANTEEG 1127
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPA--------GAGEP-SGAVPQPWLGALVPGRVAVPRFRVPQPAPS--REAPASSTPP 2995


                  ....
gi 221040448 1128 KTHS 1131
Cdd:PHA03247 2996 LTGH 2999
 
Name Accession Description Interval E-value
Cobl pfam09469
Cordon-bleu ubiquitin-like domain; The Cordon-bleu protein domain is highly conserved among ...
 197-275 4.80e-41

Cordon-bleu ubiquitin-like domain; The Cordon-bleu protein domain is highly conserved among vertebrates. The sequence contains three repeated lysine, arginine, and proline-rich regions, the KKRAP motif. The exact function of the protein is unknown but it is thought to be involved in mid-brain neural tube closure. It is expressed specifically in the node. This domain has a ubiquitin-like fold.


Pssm-ID: 462810  Cd Length: 79  Bit Score: 145.42  E-value: 4.80e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221040448   197 EKTVRVVINFKKTQKTIVRVSPHASLQELAPIICSKCEFDPLHTLLLKDYQSQEPLDLTKSLNDLGLRELYAMDVNRAT 275
Cdd:pfam09469    1 EKTVRLVVNYKKTQKAVVRVSPHVPLQELLPIICSKCEFDPLHVLLLKDYISQEELDLTKSLNDLGIKELYAMDVNRES 79
WH2_Wc_Cobl cd21801
third Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wc) found in ...
 1182-1207 1.60e-09

third Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wc) found in protein Cordon-Bleu (Cobl) and similar proteins; This family contains the third tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2), called Wc, found in protein Cordon-Bleu (Cobl), a potent actin filament nucleator that plays an important role in the reorganization of the actin cytoskeleton. It regulates neuron morphogenesis and increases branching of axons and dendrites. It also modulates dendrite branching in Purkinje cells. Cobl binds to and sequesters actin monomers (G-actin). Cobl contains three tandem WH2 (or W) domains consisting of an N-terminal alpha helix and a C-terminal LRKV motif. The first two WH2 domains have the highest binding affinity for actin. They are functionally active in actin nucleation and polymerization. The model corresponds to the first WH2 domain.


Pssm-ID: 409199  Cd Length: 26  Bit Score: 53.85  E-value: 1.60e-09
                          10        20
                  ....*....|....*....|....*.
gi 221040448 1182 DPEQMRQSLLTAIRSGEAAAKLKRVT 1207
Cdd:cd21801     1 NPEQARQALLEAIRSGEGAARLKKVP 26
PHA03247 PHA03247
large tegument protein UL36; Provisional
 894-1131 2.19e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448  894 PEEPLPNLKPKPNLRTEHQVPSSVSSPDDAMVSPLKPAPKMTRDTGTAPFAPnleeinnilESKFKSRASNAQAKPSSFF 973
Cdd:PHA03247 2776 AAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP---------LPPPTSAQPTAPPPPPGPP 2846

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448  974 ---LQMQKRVS--GHYVTSAAAKSVHAAPNPAPKELTDKEAERDMLPSPE-QTLSPLSKMPHSVPQPLVEKTDDDVIGQA 1047
Cdd:PHA03247 2847 ppsLPLGGSVApgGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALPPDQPERPPQPQAPPPPQPQPQPPPP 2926

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448 1048 PAEASPPPIAPKPVTIPASQVSTQnlktlktfGAPRPySSSGPSPFALAVVKRSQSFSKERTESPSASalVQPPANTEEG 1127
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPA--------GAGEP-SGAVPQPWLGALVPGRVAVPRFRVPQPAPS--REAPASSTPP 2995


                  ....
gi 221040448 1128 KTHS 1131
Cdd:PHA03247 2996 LTGH 2999
PHA03247 PHA03247
large tegument protein UL36; Provisional
 880-1122 2.85e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448  880 ETAIQTEDSAISESPEEPLPNLKPKPNLRTEHQVPSSVSSPDDAMVSPLKPAPKMtrdtgtapfAPNLEEINNILESKFK 959
Cdd:PHA03247 2579 EPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSP---------AANEPDPHPPPTVPPP 2649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448  960 SRASNAQAKPssfflqmqkRVSGHYVTSAAAKSVHA-AP--NPAPKELTDKEAERDMLPSPeqtlSPLSKMPHSVPQPLV 1036
Cdd:PHA03247 2650 ERPRDDPAPG---------RVSRPRRARRLGRAAQAsSPpqRPRRRAARPTVGSLTSLADP----PPPPPTPEPAPHALV 2716

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448 1037 EKTDDDVIGQAPAEASP-PPIAPKPVTIPASQVS----TQNLKTLKTFGAPRPYSSSGPS--PFALAVVKRSQSFSKERT 1109
Cdd:PHA03247 2717 SATPLPPGPAAARQASPaLPAAPAPPAVPAGPATpggpARPARPPTTAGPPAPAPPAAPAagPPRRLTRPAVASLSESRE 2796

                         250
                  ....*....|...
gi 221040448 1110 ESPSASALVQPPA 1122
Cdd:PHA03247 2797 SLPSPWDPADPPA 2809
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
1004-1213 7.55e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 40.53  E-value: 7.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448 1004 LTDKEAERDMLPSPEQTLSPLSKMPHSVPQPLVeKTDDDVIgQAPAEASPPPIAPKPVTIPAsqVSTQNLKTLKTFGAPR 1083
Cdd:PRK14971  362 LTQKGDDASGGRGPKQHIKPVFTQPAAAPQPSA-AAAASPS-PSQSSAAAQPSAPQSATQPA--GTPPTVSVDPPAAVPV 437

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221040448 1084 PYSSSGP--SPFALAVVKRSQSFSKERTESPSASALVQPPANTEEGKTHSV-----NKFVDIPQL--------GVSDKEN 1148
Cdd:PRK14971  438 NPPSTAPqaVRPAQFKEEKKIPVSKVSSLGPSTLRPIQEKAEQATGNIKEAptgtqKEIFTEEDLqyywqefaGTRPQEE 517

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221040448 1149 NSAHNEQNSQIPTPTDGPSFTVMRQSSLtfQSSDPEQMRQSLLTAIRSGEAAAKLK---RVTIPSNTI 1213
Cdd:PRK14971  518 KALKETMINCRPKLLNGTTFEVAVDNEL--QEKELTNLIPDLLGFLRGRLKNSKITmtvRVSEPTEVN 583
 
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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