GenomeNet

Database: UniProt
Entry: F2PR37_TRIEC
LinkDB: F2PR37_TRIEC
Original site: F2PR37_TRIEC 
ID   F2PR37_TRIEC            Unreviewed;       374 AA.
AC   F2PR37;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Pre-mRNA-processing factor 19 {ECO:0000256|RuleBase:RU367101};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU367101};
DE   Flags: Fragment;
GN   ORFNames=TEQG_03383 {ECO:0000313|EMBL:EGE04355.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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}.
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; DS995732; EGE04355.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2PR37; -.
DR   VEuPathDB; FungiDB:TEQG_03383; -.
DR   eggNOG; KOG0289; Eukaryota.
DR   HOGENOM; CLU_023894_0_1_1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009169; 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   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   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS51698; U_BOX; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
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..51
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REPEAT          222..256
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGE04355.1"
SQ   SEQUENCE   374 AA;  40234 MW;  387B4EC1DCEB5782 CRC64;
     GNVFEKRLVE EYISEHGKEP ITGEEHTVED LVELKSARIA RPRPPTLTSI PSLLGVFQEE
     WDALALETFT LRQTLAQTRQ ELSTALYQHD AAVRVIARLR KERDEARDAL SKISVGASRA
     PAAGDAMQVD STGLPEGVIS RIEETQEKLS KTRRKRPIPE DWATGEAIQE FKPSSPSEPL
     YPGGHSISLN SSGELALVGG TDGVAGVYSL PEKRVIFTDA ALSCVKFHPD GHLLAAGGTD
     GQIKIFDVKT GTSAATFDMS GPIKALYFSE NGTWLAAVTK DSSDISVWDL RKSAVVKVLE
     TGSRVDSISW DYTGQFLLAG GPNGITVQQY SKASKSWTEP LRSAVPSTAV AWSPSAQSIL
     SLNADGVIVS VSAQ
//
DBGET integrated database retrieval system