ID I2H0Q9_TETBL Unreviewed; 576 AA.
AC I2H0Q9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=UEV domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=TBLA0C01460 {ECO:0000313|EMBL:CCH59961.1};
GN ORFNames=TBLA_0C01460 {ECO:0000313|EMBL:CCH59961.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH59961.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH59961.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV
CC subfamily. {ECO:0000256|ARBA:ARBA00009594}.
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DR EMBL; HE806318; CCH59961.1; -; Genomic_DNA.
DR RefSeq; XP_004179480.1; XM_004179432.1.
DR AlphaFoldDB; I2H0Q9; -.
DR STRING; 1071380.I2H0Q9; -.
DR GeneID; 14494941; -.
DR KEGG; tbl:TBLA_0C01460; -.
DR eggNOG; KOG2391; Eukaryota.
DR HOGENOM; CLU_046554_0_0_1; -.
DR InParanoid; I2H0Q9; -.
DR OrthoDB; 37962at2759; -.
DR Proteomes; UP000002866; Chromosome 3.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-KW.
DR GO; GO:0072666; P:establishment of protein localization to vacuole; IEA:UniProt.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:UniProt.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR Gene3D; 6.10.140.820; -; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR017916; SB_dom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR008883; UEV_N.
DR PANTHER; PTHR23306:SF3; TUMOR SUPPRESSOR PROTEIN 101; 1.
DR PANTHER; PTHR23306; TUMOR SUSCEPTIBILITY GENE 101 PROTEIN-RELATED; 1.
DR Pfam; PF05743; UEV; 1.
DR Pfam; PF09454; Vps23_core; 1.
DR SUPFAM; SSF140111; Endosomal sorting complex assembly domain; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS51312; SB; 1.
DR PROSITE; PS51322; UEV; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..150
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT DOMAIN 513..576
FT /note="SB"
FT /evidence="ECO:0000259|PROSITE:PS51312"
FT REGION 154..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 65527 MW; 13DD5C009556BE0E CRC64;
MLLTIVQHIY ISCLRQIYKD AKATFHDSMV VLSEFKQLRP RTRVFTNSEG SSELLLCIYG
EPVPESSIQT PVLIWVPQNY PAEPPNVFLD LEKLQNARIR ISNHIDSNGR IFLPILNKWD
YRTSTLQSLL IELIHTIYST TLVDPVISVS PDKFNSSRPM GNQPVQSPPL PPLPSKKLLE
QQSQSIQNDS INNDQRDNNT FQIPSSYKQN EIHDSSNNEN NYQKFESTPS ISPSITDISS
QQTTGSDTSI HLSKHMVDTS IDHQCMERTQ YNVDNSFNPH FNHPNNSNQY IRNNSNLSHS
SYNTNSINIP LESSSMKSPQ LPPKPYFNSR INSNNSSINQ AVQTKPSLIS PSANTVPLNT
NNTTTVKSDI HILPINQNIN ARNKPPLKPP APPSIDILTS YDNNKDTGDP RYKDAINQLQ
NTLNSLDITA SNNLESQVIN RKKAMESALL QFENMYKYEC DVLKNTDDQI NQKLHDIESQ
EIILDKEIQK VDLFKEKNNE DLLDPNTLAS AETIAINQLY ELVATDYALT DSIQLLSRLL
SREIITLEIF VKKNRELARK QFLTRVHINK ITQYLV
//
