ID   MAT1_XENLA              Reviewed;         309 AA.
AC   P51951; Q5D081;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=CDK-activating kinase assembly factor MAT1;
DE   AltName: Full=CDK7/cyclin-H assembly factor;
DE   AltName: Full=Menage a trois;
DE   AltName: Full=RING finger protein MAT1;
GN   Name=mnat1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyte;
RX   PubMed=7588631; DOI=10.1002/j.1460-2075.1995.tb00185.x;
RA   Devault A., Martinez A.-M., Fesquet D., Labbe J.-C., Morin N.,
RA   Tassan J.-P., Nigg E.A., Cavadore J.-C., Doree M.;
RT   "MAT1 ('menage a trois') a new RING finger protein subunit stabilizing
RT   cyclin H-cdk7 complexes in starfish and Xenopus CAK.";
RL   EMBO J. 14:5027-5036(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Stabilizes the cyclin H-CDK7 complex to form a functional
CC       CDK-activating kinase (CAK) enzymatic complex.
CC   -!- SUBUNIT: Associates with CDK7 and cyclin H.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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DR   EMBL; U29667; AAC59726.1; -; mRNA.
DR   EMBL; BC054267; AAH54267.1; -; mRNA.
DR   RefSeq; NP_001080361.1; NM_001086892.2.
DR   AlphaFoldDB; P51951; -.
DR   SMR; P51951; -.
DR   PRIDE; P51951; -.
DR   DNASU; 380053; -.
DR   GeneID; 380053; -.
DR   KEGG; xla:380053; -.
DR   CTD; 380053; -.
DR   Xenbase; XB-GENE-876269; mnat1.L.
DR   OMA; FSGLFWH; -.
DR   OrthoDB; 1454155at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 380053; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; IEA:InterPro.
DR   GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR015877; Cdk-activating_kinase_MAT1_cen.
DR   InterPro; IPR004575; MAT1/Tfb3.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12683:SF13; PTHR12683:SF13; 1.
DR   Pfam; PF06391; MAT1; 1.
DR   Pfam; PF17121; zf-C3HC4_5; 1.
DR   PIRSF; PIRSF003338; MAT1_metazoa; 1.
DR   TIGRFAMs; TIGR00570; cdk7; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Metal-binding; Nucleus; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..309
FT                   /note="CDK-activating kinase assembly factor MAT1"
FT                   /id="PRO_0000055935"
FT   DOMAIN          142..161
FT                   /note="UIM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   ZN_FING         6..50
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   309 AA;  36047 MW;  E4E39084E17C7E04 CRC64;
     MDDQGCPRCK TTKYRNPSLK LMVNVCGHTL CESCVELLFV RGSGSCQECD TPLRKSNFKV
     QLFEDPTIDK EVEIRKKILK IYNKREEDFP SLREYNDFLE EIEEIVLNLT NNVDLDNTRR
     KIDMYQKENK DTIQRNKIKM TREQEELEEA LEMEKHENEQ RRLHLQKEEQ FQQMMKRKNK
     QELLDQLETS HLPASILLAQ HKGKSVQAEM QVEKPRSFKT DTFSTGIKKG HHIASVPVTK
     IEEALYQYQP IHIETYGPQV PHIEMLGRQG YLNHVRAAAP QDLAGGYVSS LACHRALQDA
     FSGLFWQTH