ID A0A1V4JTT3_PATFA Unreviewed; 321 AA.
AC A0A1V4JTT3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=Cyclin-H {ECO:0000256|ARBA:ARBA00019496};
GN Name=CCNH {ECO:0000313|EMBL:OPJ75608.1};
GN ORFNames=AV530_008823 {ECO:0000313|EMBL:OPJ75608.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ75608.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ75608.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ75608.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ75608.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates CDK7, the catalytic subunit of the CDK-activating
CC kinase (CAK) enzymatic complex. CAK activates the cyclin-associated
CC kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK
CC complexed to the core-TFIIH basal transcription factor activates RNA
CC polymerase II by serine phosphorylation of the repetitive C-terminal
CC domain (CTD) of its large subunit (POLR2A), allowing its escape from
CC the promoter and elongation of the transcripts. Involved in cell cycle
CC control and in RNA transcription by RNA polymerase II. Its expression
CC and activity are constant throughout the cell cycle.
CC {ECO:0000256|ARBA:ARBA00025343}.
CC -!- SUBUNIT: Associates primarily with CDK7 and MAT1 to form the CAK
CC complex. CAK can further associate with the core-TFIIH to form the
CC TFIIH basal transcription factor. {ECO:0000256|ARBA:ARBA00026042}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000256|ARBA:ARBA00008638}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ75608.1}.
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DR EMBL; LSYS01006186; OPJ75608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JTT3; -.
DR STRING; 372326.A0A1V4JTT3; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IEA:InterPro.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd20524; CYCLIN_CCNH_rpt1; 1.
DR CDD; cd20525; CYCLIN_CCNH_rpt2; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR031658; Cyclin_C_2.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR027081; CyclinH/Ccl1.
DR NCBIfam; TIGR00569; ccl1; 1.
DR PANTHER; PTHR10026; CYCLIN; 1.
DR PANTHER; PTHR10026:SF8; CYCLIN-H; 1.
DR Pfam; PF16899; Cyclin_C_2; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648}.
FT DOMAIN 62..152
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 283..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 321 AA; 37256 MW; 7AAC63E40306610E CRC64;
MYHSSTQRRN WTFRDEDELA RKRAEANRKF RSKAVATGKV QPTDPVLLEP HEELAICKYY
EKRLLDFCAV FKPAMPRSVV GTACMYFKRF YLNNSVMEYH PRIIMLTCAF LACKVDEFNV
SSVQFVGNLR ESPLGQEKAL EQILEYELLL IQQLNFHLIV HNPYRPFEGF LIDLKTRYPM
LENPEVLRKT ADDFLNRVAM TDAYLLFTPS QIALAAILSS GSRAGINMES YLSETLMLKE
NRTSLAELLD GVKCVKNLIK KYELPRPEEV AALKQKLEKC HSSELSLNTN PKKRKGYEDD
EYVTKKPKMD EEEWTDDDLL D
//
