ID N6U2X2_DENPD Unreviewed; 501 AA.
AC N6U2X2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
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};
DE Flags: Fragment;
GN Name=109540173 {ECO:0000313|EnsemblMetazoa:ENN74961};
GN ORFNames=D910_09388 {ECO:0000313|EMBL:ERL92066.1}, YQE_08537
GN {ECO:0000313|EMBL:ENN74961.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ENN74961.1};
RN [1] {ECO:0000313|Proteomes:UP000019118, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
RN [2] {ECO:0000313|EnsemblMetazoa:ENN74961}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JAN-2017) to UniProtKB.
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, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
CC -!- SIMILARITY: Belongs to the WD repeat PRP19 family.
CC {ECO:0000256|ARBA:ARBA00006388, ECO:0000256|RuleBase:RU367101}.
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DR EMBL; APGK01044532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB741026; ENN74961.1; -; Genomic_DNA.
DR EMBL; KB632309; ERL92066.1; -; Genomic_DNA.
DR RefSeq; XP_019763964.1; XM_019908405.1.
DR AlphaFoldDB; N6U2X2; -.
DR STRING; 77166.N6U2X2; -.
DR EnsemblMetazoa; ENN74961; ENN74961; YQE_08537.
DR GeneID; 109540173; -.
DR KEGG; dpa:109540173; -.
DR HOGENOM; CLU_023894_1_1_1; -.
DR OMA; AHKTWEE; -.
DR OrthoDB; 130592at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000019118; Unassembled WGS sequence.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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; cd16656; RING-Ubox_PRP19; 1.
DR CDD; cd00200; WD40; 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; IPR020472; G-protein_beta_WD-40_rep.
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; IPR019775; WD40_repeat_CS.
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; PF08606; Prp19; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00504; Ubox; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 4.
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 Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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..72
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 257..298
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 342..383
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 384..425
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 467..501
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ENN74961.1"
SQ SEQUENCE 501 AA; 54973 MW; 581D6377D06017BB CRC64;
MALFCAISNE VPEHPVVSPS SGAVFERRII EKYIQENGVD PISGKELAVD ELIEIKTPPI
VKPKPPSATS IPATLKLLQD EWDAVMLYSF TQRQQLHTAR QELSHALYQH DAACRVIARL
NKEVTAAREA LATLKPQAGI TSVPQPAVAA EPSGIAAQPI EQAGMSVEVI QKLQEKATVL
TQERKKRGRT IPEDLATQEQ IRSFKNLASL IGLHSSSIPG ILALDVHSTD TSKVLTGGND
KNATVFNKDT EQVVAFLKGH TKKVTKVIYH TNEDIVLTAS PDSTIRIWHV PTSQTTLLLR
CHDGPVTGLS LHPTGDYVLS TSEDQHWAFS DINTGRLLTK VVDNSNVPLT TAQLHPDGLI
FGTGTADSQV KIWDLKEQSN VANFTGHSGA ITTISFSENG YYLATAADDA CVKLWDLRKL
KNFKTLQLDE GYQIRDLCFD QSGTYLAVAG TDVRVYLCKQ WQELKVFNDH TAAATGVRFG
KHARFIASTS MDRTLKLYGL D
//
