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Conserved domains on  [gi|16950655|ref|NP_444284|]
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G1/S-specific cyclin-D1 [Homo sapiens]

Protein Classification

CYCLIN and Cyclin_C domain-containing protein (domain architecture ID 10444480)

CYCLIN and Cyclin_C domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cyclin_N pfam00134
Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Cyclin-0 (CCNO) ...
31-153 5.96e-37

Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Cyclin-0 (CCNO) is a Uracil-DNA glycosylase that is related to other cyclins. Cyclins contain two domains of similar all-alpha fold, of which this family corresponds with the N-terminal domain.


:

Pssm-ID: 306612  Cd Length: 127  Bit Score: 130.71  E-value: 5.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950655    31 MLKAEETCAPSVSYFKcVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVA 110
Cdd:pfam00134   6 LLELELKYLPPPDYMD-QQPELNPRMRAILIDWLVEVHEKFKLLPETLYLAVNYLDRFLSKQSVPKTKLQLVGITCLFIA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 16950655   111 SKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLA 153
Cdd:pfam00134  85 AKYEEIYPPTVKDFVYITDNAYTREEILRMERLILETLNFDLS 127
Cyclin_C pfam02984
Cyclin, C-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Human CCNO is a ...
156-269 4.40e-08

Cyclin, C-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Human CCNO is a Uracil-DNA glycosylase that is related to other cyclins. Cyclins contain two domains of similar all-alpha fold, of which this family corresponds with the C-terminal domain.


:

Pssm-ID: 308564  Cd Length: 120  Bit Score: 51.09  E-value: 4.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950655   156 TPHDFIEHFlSKMPEAEENKQIiRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSP-NNFLSYYrlTRFls 234
Cdd:pfam02984   2 TPLSFLRRF-SKAADYLHDKEL-RTLAKYLLELTLLDYDFLKYPPSLIAAAALYLARKTLGPSPPwTETLEHY--TGY-- 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 16950655   235 rvikcDPDCLRACQEQIEALLESSLRQAQQNMDPK 269
Cdd:pfam02984  76 -----SEEDLKPCVKLLLELLLNAPSSKLQAVRRK 105
 
Name Accession Description Interval E-value
Cyclin_N pfam00134
Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Cyclin-0 (CCNO) ...
31-153 5.96e-37

Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Cyclin-0 (CCNO) is a Uracil-DNA glycosylase that is related to other cyclins. Cyclins contain two domains of similar all-alpha fold, of which this family corresponds with the N-terminal domain.


Pssm-ID: 306612  Cd Length: 127  Bit Score: 130.71  E-value: 5.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950655    31 MLKAEETCAPSVSYFKcVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVA 110
Cdd:pfam00134   6 LLELELKYLPPPDYMD-QQPELNPRMRAILIDWLVEVHEKFKLLPETLYLAVNYLDRFLSKQSVPKTKLQLVGITCLFIA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 16950655   111 SKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLA 153
Cdd:pfam00134  85 AKYEEIYPPTVKDFVYITDNAYTREEILRMERLILETLNFDLS 127
CYCLIN cd00043
Cyclin box fold. Protein binding domain functioning in cell-cycle and transcription control. ...
56-131 1.39e-16

Cyclin box fold. Protein binding domain functioning in cell-cycle and transcription control. Present in cyclins, TFIIB and Retinoblastoma (RB).The cyclins consist of 8 classes of cell cycle regulators that regulate cyclin dependent kinases (CDKs). TFIIB is a transcription factor that binds the TATA box. Cyclins, TFIIB and RB contain 2 copies of the domain.


Pssm-ID: 238003  Cd Length: 88  Bit Score: 73.81  E-value: 1.39e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16950655  56 MRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEkLCIYTDNS 131
Cdd:cd00043   1 MRPTPLDFLRRVAKALGLSPETLTLAVNLLDRFLLDYSVLGRSPSLVAAAALYLAAKVEEIPPWLKD-LVHVTGYA 75
CYCLIN smart00385
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ...
62-132 3.79e-14

domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and TFIIB (twice) and Retinoblastoma (once). A protein recognition domain functioning in cell-cycle and transcription control.


Pssm-ID: 214641  Cd Length: 83  Bit Score: 66.85  E-value: 3.79e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16950655     62 TWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSI 132
Cdd:smart00385   1 DFLRRVCKALNLDPETLNLAVNLLDRFLSDYKFLKYSPSLIAAAALYLASKTEETPPWTKELVHYTGYFTE 71
COG5024 COG5024
Cyclin [Cell division and chromosome partitioning];
31-201 5.09e-13

Cyclin [Cell division and chromosome partitioning];


Pssm-ID: 227357  Cd Length: 440  Bit Score: 68.65  E-value: 5.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950655  31 MLKAEETCAPSVSYFKcVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVA 110
Cdd:COG5024 188 LLKLELIDLPNPNYLI-KQSLYEWSMRSILVDWLVEVHGKFGLLPETLFLAINIIDRFLSSRVVSLEKYQLVGISALFIA 266
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950655 111 SKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDfiehFLSKMPEAEENKQIIRKHAQTFVALCA 190
Cdd:COG5024 267 SKYEEVNCPSIKDLVYATDGAFTRDDIIRAERYMLEVLDFNISWPSPMS----FLRRISKASDYDIFSRTPAKFSSEISP 342
                       170
                ....*....|.
gi 16950655 191 TDVKFISNPPS 201
Cdd:COG5024 343 VDYKFIQISPS 353
Cyclin_C pfam02984
Cyclin, C-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Human CCNO is a ...
156-269 4.40e-08

Cyclin, C-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Human CCNO is a Uracil-DNA glycosylase that is related to other cyclins. Cyclins contain two domains of similar all-alpha fold, of which this family corresponds with the C-terminal domain.


Pssm-ID: 308564  Cd Length: 120  Bit Score: 51.09  E-value: 4.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950655   156 TPHDFIEHFlSKMPEAEENKQIiRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSP-NNFLSYYrlTRFls 234
Cdd:pfam02984   2 TPLSFLRRF-SKAADYLHDKEL-RTLAKYLLELTLLDYDFLKYPPSLIAAAALYLARKTLGPSPPwTETLEHY--TGY-- 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 16950655   235 rvikcDPDCLRACQEQIEALLESSLRQAQQNMDPK 269
Cdd:pfam02984  76 -----SEEDLKPCVKLLLELLLNAPSSKLQAVRRK 105
 
Name Accession Description Interval E-value
Cyclin_N pfam00134
Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Cyclin-0 (CCNO) ...
31-153 5.96e-37

Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Cyclin-0 (CCNO) is a Uracil-DNA glycosylase that is related to other cyclins. Cyclins contain two domains of similar all-alpha fold, of which this family corresponds with the N-terminal domain.


Pssm-ID: 306612  Cd Length: 127  Bit Score: 130.71  E-value: 5.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950655    31 MLKAEETCAPSVSYFKcVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVA 110
Cdd:pfam00134   6 LLELELKYLPPPDYMD-QQPELNPRMRAILIDWLVEVHEKFKLLPETLYLAVNYLDRFLSKQSVPKTKLQLVGITCLFIA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 16950655   111 SKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLA 153
Cdd:pfam00134  85 AKYEEIYPPTVKDFVYITDNAYTREEILRMERLILETLNFDLS 127
CYCLIN cd00043
Cyclin box fold. Protein binding domain functioning in cell-cycle and transcription control. ...
56-131 1.39e-16

Cyclin box fold. Protein binding domain functioning in cell-cycle and transcription control. Present in cyclins, TFIIB and Retinoblastoma (RB).The cyclins consist of 8 classes of cell cycle regulators that regulate cyclin dependent kinases (CDKs). TFIIB is a transcription factor that binds the TATA box. Cyclins, TFIIB and RB contain 2 copies of the domain.


Pssm-ID: 238003  Cd Length: 88  Bit Score: 73.81  E-value: 1.39e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16950655  56 MRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEkLCIYTDNS 131
Cdd:cd00043   1 MRPTPLDFLRRVAKALGLSPETLTLAVNLLDRFLLDYSVLGRSPSLVAAAALYLAAKVEEIPPWLKD-LVHVTGYA 75
CYCLIN smart00385
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ...
62-132 3.79e-14

domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and TFIIB (twice) and Retinoblastoma (once). A protein recognition domain functioning in cell-cycle and transcription control.


Pssm-ID: 214641  Cd Length: 83  Bit Score: 66.85  E-value: 3.79e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16950655     62 TWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSI 132
Cdd:smart00385   1 DFLRRVCKALNLDPETLNLAVNLLDRFLSDYKFLKYSPSLIAAAALYLASKTEETPPWTKELVHYTGYFTE 71
COG5024 COG5024
Cyclin [Cell division and chromosome partitioning];
31-201 5.09e-13

Cyclin [Cell division and chromosome partitioning];


Pssm-ID: 227357  Cd Length: 440  Bit Score: 68.65  E-value: 5.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950655  31 MLKAEETCAPSVSYFKcVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVA 110
Cdd:COG5024 188 LLKLELIDLPNPNYLI-KQSLYEWSMRSILVDWLVEVHGKFGLLPETLFLAINIIDRFLSSRVVSLEKYQLVGISALFIA 266
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950655 111 SKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDfiehFLSKMPEAEENKQIIRKHAQTFVALCA 190
Cdd:COG5024 267 SKYEEVNCPSIKDLVYATDGAFTRDDIIRAERYMLEVLDFNISWPSPMS----FLRRISKASDYDIFSRTPAKFSSEISP 342
                       170
                ....*....|.
gi 16950655 191 TDVKFISNPPS 201
Cdd:COG5024 343 VDYKFIQISPS 353
Cyclin_C pfam02984
Cyclin, C-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Human CCNO is a ...
156-269 4.40e-08

Cyclin, C-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Human CCNO is a Uracil-DNA glycosylase that is related to other cyclins. Cyclins contain two domains of similar all-alpha fold, of which this family corresponds with the C-terminal domain.


Pssm-ID: 308564  Cd Length: 120  Bit Score: 51.09  E-value: 4.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950655   156 TPHDFIEHFlSKMPEAEENKQIiRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSP-NNFLSYYrlTRFls 234
Cdd:pfam02984   2 TPLSFLRRF-SKAADYLHDKEL-RTLAKYLLELTLLDYDFLKYPPSLIAAAALYLARKTLGPSPPwTETLEHY--TGY-- 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 16950655   235 rvikcDPDCLRACQEQIEALLESSLRQAQQNMDPK 269
Cdd:pfam02984  76 -----SEEDLKPCVKLLLELLLNAPSSKLQAVRRK 105
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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