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Database: UniProt
Entry: A0A162P4V7_9CRUS
LinkDB: A0A162P4V7_9CRUS
Original site: A0A162P4V7_9CRUS 
ID   A0A162P4V7_9CRUS        Unreviewed;       328 AA.
AC   A0A162P4V7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   RecName: Full=Cyclin-H {ECO:0000256|ARBA:ARBA00019496};
GN   Name=EOG090X080D {ECO:0000313|EMBL:SVE83132.1};
GN   ORFNames=APZ42_015053 {ECO:0000313|EMBL:KZS18522.1};
OS   Daphnia magna.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS18522.1, ECO:0000313|Proteomes:UP000076858};
RN   [1] {ECO:0000313|EMBL:KZS18522.1, ECO:0000313|Proteomes:UP000076858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinb3 {ECO:0000313|EMBL:KZS18522.1,
RC   ECO:0000313|Proteomes:UP000076858};
RC   TISSUE=Complete organism {ECO:0000313|EMBL:KZS18522.1};
RA   Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT   "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SVE83132.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FI-XINB3 {ECO:0000313|EMBL:SVE83132.1};
RA   Cornetti L.;
RL   Submitted (AUG-2018) 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; LRGB01000512; KZS18522.1; -; Genomic_DNA.
DR   EMBL; LR013513; SVE83132.1; -; mRNA.
DR   AlphaFoldDB; A0A162P4V7; -.
DR   STRING; 35525.A0A162P4V7; -.
DR   EnsemblMetazoa; XM_032939118.2; XP_032795009.1; LOC116931527.
DR   EnsemblMetazoa; XM_032939127.2; XP_032795018.1; LOC116931527.
DR   OrthoDB; 5481790at2759; -.
DR   Proteomes; UP000076858; 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   2: Evidence at transcript level;
KW   Cyclin {ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076858}.
FT   DOMAIN          62..149
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          284..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   328 AA;  38105 MW;  3190529FB6206AA7 CRC64;
     MFATSTQRHF WMFKDETDVS NARLSANIKY ISSRGRNMTV IEREAHFLNV IEEKSLIMSY
     EYQLRDFCRK FHPPMPRYVI GTALHYLKRF YVNNSVMDYP PKEILVTCVY LACKVEEFNV
     SMDQFVGNLK GDREKAAAII LNNELLLMQQ LDYQLTVHNP FRPLEGLMID MKTRFPTFSD
     PERLRPGIDE FLEQVFYTDA ILIYSPSQIS LAAIIHSAST SKENVDEYIT KILFSEDQKR
     LLNLIEAVKK IRVMVRNVQL PHRDTIKALE KKLALCCNPD NNSESPAFKK RMKQSFDEEE
     SFEDGQYPSA SSDQVRSMLM GLSEMGKI
//
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