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Database: UniProt
Entry: D3TRT0_GLOMM
LinkDB: D3TRT0_GLOMM
Original site: D3TRT0_GLOMM 
ID   D3TRT0_GLOMM            Unreviewed;       314 AA.
AC   D3TRT0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   13-SEP-2023, entry version 48.
DE   RecName: Full=Cyclin-H {ECO:0000256|ARBA:ARBA00019496};
OS   Glossina morsitans morsitans (Savannah tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=37546 {ECO:0000313|EMBL:ADD20408.1};
RN   [1] {ECO:0000313|EMBL:ADD20408.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:ADD20408.1};
RX   PubMed=20353571; DOI=10.1186/1471-2164-11-213;
RA   Alves-Silva J., Ribeiro J.M., Van Den Abbeele J., Attardo G., Hao Z.,
RA   Haines L.R., Soares M.B., Berriman M., Aksoy S., Lehane M.J.;
RT   "An insight into the sialome of Glossina morsitans morsitans.";
RL   BMC Genomics 11:213-213(2010).
RN   [2] {ECO:0000313|EMBL:ADD20408.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:ADD20408.1};
RG   International Glossina Genome Initiative;
RA   da Silva J., Ribeiro J.M.C., Abbeele J.V., Attardo G., Hao Z., Haines L.R.,
RA   Soares M.B., Berriman M., Aksoy S., Lehane M.J.;
RL   Submitted (JAN-2010) 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; EZ424132; ADD20408.1; -; mRNA.
DR   AlphaFoldDB; D3TRT0; -.
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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   Kinase {ECO:0000313|EMBL:ADD20408.1};
KW   Transferase {ECO:0000313|EMBL:ADD20408.1}.
FT   DOMAIN          62..149
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
SQ   SEQUENCE   314 AA;  37041 MW;  257E0F704718495D CRC64;
     MFPLSSQKKY WTFNNEQHLN ELRKKQNEKF QETHGEAEAE DNKLDYFLDS SEERLLLKQY
     EIYLNDFCRR FEPIMPKCVV GTSFHYFKRF YLHNSPMDFH PKEILATCVY LACKVEEFNV
     SIGQFVNNIK GDRNKAMDII LSSEMLLMQH LNYYLTVHNP YRPIEGFLID IKTRSSLTNA
     ERLRQHIDDF IEKSFFTDAC LLYAPSQIAL AAVLHAASRE QENLDSYVTD ILFNGAREKL
     PLLVEAIRKI RLMVKQYEIP ARDKVKTIEK KLEKCRNQEN NPDSEIYKER MRKMFCDDDL
     EIDLQANSAA DMSV
//
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