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Q01917

- CDC2H_CRIFA

UniProt

Q01917 - CDC2H_CRIFA

Protein

Cell division control protein 2 homolog

Gene

CRK

Organism
Crithidia fasciculata
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    • Comment

    Functioni

    Probably involved in the control of the cell cycle.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.
    ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

    Enzyme regulationi

    Phosphorylation at Thr-17 or Tyr-18 inactivates the enzyme.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361ATPPROSITE-ProRule annotation
    Active sitei131 – 1311Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 219ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
    3. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.22. 1365.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell division control protein 2 homolog (EC:2.7.11.22, EC:2.7.11.23)
    Gene namesi
    Name:CRK
    OrganismiCrithidia fasciculata
    Taxonomic identifieri5656 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 474474Cell division control protein 2 homologPRO_0000085737Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171PhosphothreonineBy similarity
    Modified residuei18 – 181PhosphotyrosineBy similarity
    Modified residuei230 – 2301PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ01917.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 446440Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 3 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q01917-1 [UniParc]FASTAAdd to Basket

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    MSTLGRYRHV VKLGEGTYGM VYKGTEIQTG RVVAFKRMVV TSDDEGIPGA    50
    AIREICLLKE LRHNNVVELF EVLFDPPKIT MIFELCDCDL KRYMESRPQR 100
    LLDANTEMRP ILKQIFLGLE YLHGRCVVHR DMKPQNIFVN VRGPDFAAMT 150
    ALPSSPQQSM RVPHAGGTNG EAGRASANGN EHAPRPTAAE GSVSPWEEAA 200
    NTKDAPNQLI IKIGDFGLAR VEEIPVKKYS HEVVTLWYRS PDVLMSSALY 250
    SYPVDIWSMG AIFFEMATSK VLFSGRNEDE QLLRMFWLLG SPTKETWPSM 300
    MTYTGTMERL ERSSRAAAER QDLTVNGDVY VQQQQLQAQQ QQPQQGSSPS 350
    HSSSRAPDLL TQLAHKRFYH SESAMQQRRE SASSAANSYR LPVELWFDRP 400
    LFKEYMAATR CDVSVSPEGI DLLRRCLMYE PNQRITAAEA VHHPYLERVP 450
    VPTAGSLDVL ISSLMQTMET IHLL 474
    Length:474
    Mass (Da):53,473
    Last modified:July 1, 1993 - v1
    Checksum:i57CA1361E3651A9D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z12149 Genomic DNA. Translation: CAA78133.1.
    PIRiS26381.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z12149 Genomic DNA. Translation: CAA78133.1 .
    PIRi S26381.

    3D structure databases

    ProteinModelPortali Q01917.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 2.7.11.22. 1365.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 3 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Crithidia fasciculata CRK gene encodes a novel cdc2-related protein containing large inserts between highly conserved domains."
      Brown L.M., Hines J.C., Ray D.S.
      Nucleic Acids Res. 20:5451-5456(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiCDC2H_CRIFA
    AccessioniPrimary (citable) accession number: Q01917
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3