ID W6ZMB7_COCMI Unreviewed; 471 AA.
AC W6ZMB7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Pre-mRNA-processing factor 19 {ECO:0000256|RuleBase:RU367101};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367101};
GN ORFNames=COCMIDRAFT_97376 {ECO:0000313|EMBL:EUC44716.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC44716.1};
RN [1] {ECO:0000313|EMBL:EUC44716.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC44716.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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|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|ARBA:ARBA00006388, ECO:0000256|RuleBase:RU367101}.
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DR EMBL; KI963998; EUC44716.1; -; Genomic_DNA.
DR RefSeq; XP_007688738.1; XM_007690548.1.
DR AlphaFoldDB; W6ZMB7; -.
DR STRING; 930090.W6ZMB7; -.
DR GeneID; 19129047; -.
DR KEGG; bor:COCMIDRAFT_97376; -.
DR eggNOG; KOG0289; Eukaryota.
DR HOGENOM; CLU_023894_0_1_1; -.
DR OrthoDB; 130592at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054032; 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:0003755; F:peptidyl-prolyl cis-trans isomerase activity; 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; cd16656; RING-Ubox_PRP19; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR024977; Apc4-like_WD40_dom.
DR InterPro; IPR013915; Pre-mRNA_splic_Prp19.
DR InterPro; IPR038959; Prp19.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR43995; PRE-MRNA-PROCESSING FACTOR 19; 1.
DR PANTHER; PTHR43995:SF1; PRE-MRNA-PROCESSING FACTOR 19; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF08606; Prp19; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00504; Ubox; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367101};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367101};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU367101};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU367101};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367101};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728, 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 1..71
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 271..312
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 319..353
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ SEQUENCE 471 AA; 49959 MW; BAEBF5F959BFE63E CRC64;
MLCAISGEAP REPVASRKSG NVFEKRLIEA HIAEHHTDPV TGEDLATEDL IELKSPNVVT
PRAPNFTSIP AMLSAFQNEW DALVLETHTL KQHLAQTRQE LSTALYQNDA ATRVIARITK
ERDEAREALS NVTISGGAQG DAMQVDNQSL PQDLVKVVDD TQQELFGSRR KRAVPEGWAT
GEVITNYDLV KTTEAIYPGS SNIAVQEDGL VLFGGSDGTA GIYALAEGKV TQTFNAGSAI
TAAAWCGGRA VVGTSAGVAK IFEQGNEVAQ VGSHAGAVTS ISVHPSGKIL ATAGADKHYA
VHELTSFKTV SQVYVEAEIT CVAFHVDGML FFVGSSDGNI RIYDIKTGAA MAQLETGAPI
VDLKFAENGT WFAVAQQGST SVSVWDIRKQ TVIYTLESGS PVTCCEWDYS GMFLAIGGTG
SVSVQQFTKA TKSWAELVRK ALPVKDVAWS GKAESVVALT PEGGLAVLAA P
//
