ID A8PZV4_MALGO Unreviewed; 502 AA.
AC A8PZV4;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Pre-mRNA-processing factor 19 {ECO:0000256|ARBA:ARBA00015618, ECO:0000256|RuleBase:RU367101};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|RuleBase:RU367101};
GN ORFNames=MGL_1953 {ECO:0000313|EMBL:EDP43740.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP43740.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP43740.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC -!- FUNCTION: Ubiquitin-protein ligase which is mainly involved pre-mRNA
CC splicing and DNA repair. Required for pre-mRNA splicing as component of
CC the spliceosome. {ECO:0000256|RuleBase:RU367101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU367101};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367101}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU367101}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU367101}.
CC -!- SIMILARITY: Belongs to the WD repeat PRP19 family.
CC {ECO:0000256|RuleBase:RU367101}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP43740.1}.
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DR EMBL; AAYY01000006; EDP43740.1; -; Genomic_DNA.
DR RefSeq; XP_001730954.1; XM_001730902.1.
DR AlphaFoldDB; A8PZV4; -.
DR STRING; 425265.A8PZV4; -.
DR GeneID; 5855261; -.
DR KEGG; mgl:MGL_1953; -.
DR VEuPathDB; FungiDB:MGL_1953; -.
DR InParanoid; A8PZV4; -.
DR OMA; AHKTWEE; -.
DR OrthoDB; 130592at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0000974; C:Prp19 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR013915; Pre-mRNA_splic_Prp19.
DR InterPro; IPR038959; Prp19.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR43995; PRE-MRNA-PROCESSING FACTOR 19; 1.
DR PANTHER; PTHR43995:SF1; PRE-MRNA-PROCESSING FACTOR 19; 1.
DR Pfam; PF08606; Prp19; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367101};
KW DNA repair {ECO:0000256|RuleBase:RU367101};
KW mRNA processing {ECO:0000256|RuleBase:RU367101};
KW mRNA splicing {ECO:0000256|RuleBase:RU367101};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367101};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Spliceosome {ECO:0000256|RuleBase:RU367101};
KW Transferase {ECO:0000256|RuleBase:RU367101};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU367101};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 32..97
FT /note="Pre-mRNA-splicing factor 19"
FT /evidence="ECO:0000259|Pfam:PF08606"
FT REPEAT 354..386
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 387..429
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 104..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 53302 MW; C98E448304F36A31 CRC64;
MQDPVTGEEL TREDLITLQQ SPRIAFPRPP THSSVPSLLT ALQNEYDAMV YETVALRKQY
DSVRQDLANA LYTNDASMRV IARLMKERND AREALASIHT SLGVPTTTSI SSSSTTTTST
APGSATQDVD MTVQGDEQVL PRSLPPAVME QVDATASQLS SERRARIKRG ASAPYPTPAT
ASSMEEREAI NAAHRASSPG ILALDISANG SLVLTGGQDK SVHVVDRASG QVTAKLQGHS
KPITAAVFSG RSNPAVGDAA LEAPMPAFAV SASADGSVRT WRRTENDSYE LAHVLETYDA
PVTGVDVHPT DSLVGSASRD GSWAIHSLEN GERLMHVPAP AASDDQGTGY VYESFAFHPD
GQLAATGTAD GAIRIWDIKQ GEQSAVFRGH EGNVHTLSFS QNGYLLVAAS RDASHAKVWD
LRKLDVTRTI ETAGSGIESV RLDASAQLLA VVGRDVRVFG GKSFELCATW DAASCTCAQW
SPSDGALLVG SLDRSVRVFV SS
//
