ID Q0CV01_ASPTN Unreviewed; 928 AA.
AC Q0CV01;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000256|PIRNR:PIRNR007860};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR007860};
GN ORFNames=ATEG_02483 {ECO:0000313|EMBL:EAU37445.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU37445.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476596; EAU37445.1; -; Genomic_DNA.
DR RefSeq; XP_001211661.1; XM_001211661.1.
DR AlphaFoldDB; Q0CV01; -.
DR STRING; 341663.Q0CV01; -.
DR EnsemblFungi; EAU37445; EAU37445; ATEG_02483.
DR GeneID; 4316592; -.
DR VEuPathDB; FungiDB:ATEG_02483; -.
DR eggNOG; KOG2114; Eukaryota.
DR HOGENOM; CLU_001287_0_0_1; -.
DR OMA; ENECPAC; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000007963; 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; IPR019734; TPR_repeat.
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 SMART; SM00299; CLH; 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; PS50005; TPR; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
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:UP000007963};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
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 REPEAT 352..385
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 837..874
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 928 AA; 103827 MW; 04F7C3BAC36139CD CRC64;
MALTSADVSS LCTGSANLFL GTTDGFVHII SSGFKIVRSF KASDTGSIVH VKQIEGSAFL
VTISEDLLNE PVLKVWALDT TEKKTGAPRC LSTTSIQNAR RLFPVTAFGA LPDLSQVAVG
FGNGSVAVIR GDLIHDRGAR QRVVFESEEP VTGLEMQSGS AGTLYISTTN RILALAISGR
VQGQPARVLE DTGCAVGCMA LDDFTGDVLV AREDAIYTYG PHGRGPSYAF ESNKSSLTIF
KDYIALVCPP KVRSPNGGSL ENLPIDGMFN TTTFTLLDTD LKFIAHSESV ASSVKRVFME
WGDLFLLTTD GKIFRYREKS LQQKLEILYQ RNLYILAINL AQKKGVDTLQ QNAIYRKYGD
FLYQKGDYDT AMQQYLRAID NTEPSQIIRK YLDTQRIHNL IEYLEELHDH DKATVDHTTL
LLNCYAKLKD TSKLDAFIKA PGELKFDLET AIAMCRQGGY YEQAAYLATK YGENDMVVDI
LVEDSKKYAE AVEYIWRLDP ELAYDNLMKY ARVLLSNCPQ KTTELFIEYY KGQYKPRTEV
ELPPEPQTQS GSNLQSLAAF LPLSLINSSA GAKSEAVEPQ STQEDKVDHA VSQYQPPKPR
TAFSAFVGHP QEFITFLEAL INKETLKEED KVDLYTTLFE MYLDASSRQK DSAEKQEWEN
KAKKLIEGKD IPISTSSVLL LSDLSGFREG STLVREQEGL RSDIFRSFTS AKDTRGAIKA
LKKYGPEEPQ LYIDALTYFA SSPAILEEAG EELDVVLKRI HDDGLMSPLQ VIQALSNNAV
VTMGRVKKYL SENIERERKE ISSNRRLIKS YSTETEKKRQ ELEQLGSKPV VFQARRCMSC
GGALDLPTVH FLCKHSFHQR CLNKVDEDAE CPVCAPENST IKAIRRRQVE SADQHELFKG
ELQRSKDRFG TVSEFFGRGV MRPQSTME
//
