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Database: UniProt
Entry: A0A197JYF6_9FUNG
LinkDB: A0A197JYF6_9FUNG
Original site: A0A197JYF6_9FUNG 
ID   A0A197JYF6_9FUNG        Unreviewed;       500 AA.
AC   A0A197JYF6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=K457DRAFT_112118 {ECO:0000313|EMBL:OAQ29284.1};
OS   Linnemannia elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ29284.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ29284.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ29284.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA   Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA   Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA   Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA   Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA   Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT   the earliest lineages of terrestrial Fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00006388, ECO:0000256|RuleBase:RU367101}.
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DR   EMBL; KV442042; OAQ29284.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A197JYF6; -.
DR   STRING; 1314771.A0A197JYF6; -.
DR   OrthoDB; 130592at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000078512; 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; 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; 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; PF00400; WD40; 5.
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; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 3.
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:UP000078512};
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          245..281
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          296..337
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          349..381
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          382..423
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          465..500
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ   SEQUENCE   500 AA;  53881 MW;  22B966E302ECA29B CRC64;
     MFCAISGEAP EHPVVSKKSG QVYERRLIVK YIEDNGKDPV SGEDLSVDDL LDIKSTPGTV
     KPRPPAMTSI PSILSVLQNE WDSIMLETFT MKQQYQQVRQ ELSHALYQHD AACRVIARLM
     KERDAAREAL ANVEAHIGTK AASTESTGDV TMDDATSTGL SAEIREKLEA TTAVLSKTRK
     RKPNTTAEAI QTYTQRKVFP GLHAARSPGI SALDLDAKNG LVLTGGNDKN ALVFSQSEEK
     VVATLKGHSK KITHVSWAGR SEEAGQDMAL TASADQTVKI WTAGDKAYGY SAAHTLSGHS
     AEVTGLCVHP TKDYAATASM DSTWAFHDLE TGSTLMTARS DQVSNGYSSA AFHPDGLLFG
     TGTTDSAVKI WDVRTKDAVA SFEGHTGAVK TMTFSENGYL MAAAGENNEV SIWNLRTLEV
     IQKLKVADQG VINALAWDQS GTYLGVGGTD IRIFKVKTWQ ELANLTDNTA EITSLKFGPL
     GDYLVAGGLD RSLRVFGVAE
//
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