ID A0A1E3Q112_LIPST Unreviewed; 1019 AA.
AC A0A1E3Q112;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000256|PIRNR:PIRNR007860};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR007860};
GN ORFNames=LIPSTDRAFT_5299 {ECO:0000313|EMBL:ODQ71290.1};
OS Lipomyces starkeyi NRRL Y-11557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Lipomycetaceae; Lipomyces.
OX NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ71290.1, ECO:0000313|Proteomes:UP000094385};
RN [1] {ECO:0000313|EMBL:ODQ71290.1, ECO:0000313|Proteomes:UP000094385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ71290.1,
RC ECO:0000313|Proteomes:UP000094385};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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|PIRNR:PIRNR007860};
CC -!- SUBUNIT: Component of the homotypic vacuole fusion and vacuole protein
CC sorting (HOPS) complex. Component of the class C core vacuole/endosome
CC tethering (CORVET) complex. {ECO:0000256|PIRNR:PIRNR007860}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000256|PIRNR:PIRNR007860};
CC Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR007860};
CC Cytoplasmic side {ECO:0000256|PIRNR:PIRNR007860}.
CC -!- SIMILARITY: Belongs to the VPS11 family.
CC {ECO:0000256|ARBA:ARBA00007070, ECO:0000256|PIRNR:PIRNR007860}.
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DR EMBL; KV454298; ODQ71290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3Q112; -.
DR STRING; 675824.A0A1E3Q112; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000094385; Unassembled WGS sequence.
DR GO; GO:0033263; C:CORVET complex; IEA:UniProtKB-UniRule.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0030897; C:HOPS complex; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd16688; RING-H2_Vps11; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR016528; VPS11.
DR InterPro; IPR024763; VPS11_C.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23323:SF24; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG; 1.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF12451; VPS11_C; 1.
DR Pfam; PF17122; zf-C3H2C3; 1.
DR PIRSF; PIRSF007860; VPS11; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50236; CHCR; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR007860};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein transport {ECO:0000256|PIRNR:PIRNR007860};
KW Reference proteome {ECO:0000313|Proteomes:UP000094385};
KW Transferase {ECO:0000256|PIRNR:PIRNR007860};
KW Transport {ECO:0000256|PIRNR:PIRNR007860};
KW Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR007860};
KW Vacuole {ECO:0000256|PIRNR:PIRNR007860};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 927..964
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT COILED 884..918
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1019 AA; 113413 MW; 91498B0AE334742C CRC64;
MVLTAWRQFT FFDALPIRDP SVADDDGPLY SDPNVSAVCA GSGSLYLATN KGVVKIVSRS
LKLQVSFVAH DNGAAITYMT QLDGTPNLIT VAEIENAEPQ VRLWSLDKPD KKTTGPKCNA
SVTIHMKKIW EITSFAVSGD LSSIALGLAN GNVILIRGDL LNDKGLKQKV IFESSDPVTG
LAFYEASKTS FLYIATTTRI LTVFTSGKNQ GQPARVLEEK GCGSGCMALK KSTGEILVAR
DDAIYFYTPY GRGPCYMYDG PKDSIFVYKS YLVSVSLSAA SSDASVQSTL RRFVGSVPSR
DDPFDTTKFT ILDTENKFVA YTGQFVDGVK AIFAEWGDLY VLGGDGQLYR HQERDLQSKL
DILYQRNLYS LALTLAVNAG ADEKRVLVIY KKYGDYLYDK GEYDEAMVQY IKAIDGGEAS
QVIRKYLDSQ RIYNLTSYLE ELHNRGIATA DHTTLLLNCY AKLKDTEKLE TFIKSEGENL
KFDLDTAIQM CRQGGYFQQA AYLAEKHGQN DLVVDITLQD LGDYRSGLRF IRSLPPEDMY
YNLSRYGRVL LQYVPSETTS LFIDYFTGRY TVRKIANVGE FDPTATAVLG NEDQRPISPM
LGFQNYKNLI PYMAGSRPAS VLSGALGEPA PSIMSTITSN VGKLSSAMVG GVLPSGSESV
ANAPVTIDPR VFASDIAVPD YKIPKPRTAF ATFVDRPEEL IVFLEACIAH HRVVGGQASD
EADMCTTLFE MYLQRAEAST TEDEKHRWEE KSKVLITGFN APIDQSNVLL LSHLYSFRDG
RILVRERENL YIDIFRSSVA VNDTLGAIQT LHKYGDEEPE LYPLALSYFT SSPEVMAVAS
DELVQVLKKI EQEGLMAPLQ VIQALSVNAV ATVGIVRGYL SEIIEREKKE IETNRRLTES
YRQETKAKLD EIRELETEPR VFQSTRCASC GAPLDLPTVH FMCKHSYHRR CLNDVNEDTE
CPQCAPNNAT IRAIRRAQDD MADRHDLFKA ALEEGDDKFK VVSDFFGRGV MEQVEFLVE
//
