ID   MAT1_MARGL              Reviewed;         324 AA.
AC   P51950;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
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;
OS   Marthasterias glacialis (Spiny starfish).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC   Forcipulatacea; Forcipulatida; Asteriidae; Marthasterias.
OX   NCBI_TaxID=7609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
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).
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.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U29666; AAC46933.1; -; mRNA.
DR   PIR; S60118; S60118.
DR   AlphaFoldDB; P51950; -.
DR   SMR; P51950; -.
DR   PRIDE; P51950; -.
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; 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   SMART; SM00184; RING; 1.
DR   TIGRFAMs; TIGR00570; cdk7; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Direct protein sequencing; Metal-binding;
KW   Nucleus; Zinc; Zinc-finger.
FT   CHAIN           1..324
FT                   /note="CDK-activating kinase assembly factor MAT1"
FT                   /id="PRO_0000055934"
FT   ZN_FING         7..51
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   324 AA;  37432 MW;  69FBDFC7502C27F1 CRC64;
     MMEEQACPRC KSTKYRNPSL KLLVNVCGHT LCENCVEILF VRGSGSCPSC NTPLRRNQFR
     VQEFEDAYVE KEVDIRKRIL KDFNKQEEEF PALKDYNDYL EEIETIIFNL ANGTELEATK
     RKVDQYRKNN RESIMKNRSK QSSDQAYLEA LLQQENEDEE EKKQQLQFME RQTKNQKKRD
     KEALIDELIH SNMPADHVIA SHTANVEMQE APVFKLPKKT TFSTGIKVGF GYQDTFLPIP
     KQEEILFTYE EETYETYGPS APSTDELDTQ RYNKHVRPAS PQGIAGGYSQ NLACLRALQE
     AFSGLLYFPS QHKNTDDSSS METS