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Database: UniProt
Entry: A0A091PIY4_HALAL
LinkDB: A0A091PIY4_HALAL
Original site: A0A091PIY4_HALAL 
ID   A0A091PIY4_HALAL        Unreviewed;       242 AA.
AC   A0A091PIY4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Cyclin-H {ECO:0000256|ARBA:ARBA00019496};
DE   Flags: Fragment;
GN   ORFNames=N329_12804 {ECO:0000313|EMBL:KFQ07173.1};
OS   Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Haliaeetus.
OX   NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ07173.1, ECO:0000313|Proteomes:UP000054379};
RN   [1] {ECO:0000313|EMBL:KFQ07173.1, ECO:0000313|Proteomes:UP000054379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ07173.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KK659366; KFQ07173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091PIY4; -.
DR   Proteomes; UP000054379; 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; 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   SUPFAM; SSF47954; Cyclin-like; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054379}.
FT   DOMAIN          2..78
FT                   /note="Cyclin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00134"
FT   DOMAIN          82..180
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16899"
FT   REGION          210..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ07173.1"
FT   NON_TER         242
FT                   /evidence="ECO:0000313|EMBL:KFQ07173.1"
SQ   SEQUENCE   242 AA;  27882 MW;  3233E86F84CB1EED CRC64;
     GTASMYFKRF YLNNSVMEYH PRIIMLTCAF LACKVDEFNV SSAQFVGNLR ESPLGQEKAL
     EQILEYELLL IQQLNFHLIV HNPYRPFEGF LIDLKTRYPM LENPEVLRKA ADDFLNRVAL
     TDAYLLFPPS QIALTAILSS GSRAGINMES YLSESLMLKE NRISLAKLLD GMKCMKNLIK
     KYELPRPEEV AALKQKLEKC HSLELSLNTN PKKRKGYEDD EYVTKKPKTD EEEWTDDDLA
     DS
//
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