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Database: UniProt
Entry: A0A139HNI4_9PEZI
LinkDB: A0A139HNI4_9PEZI
Original site: A0A139HNI4_9PEZI 
ID   A0A139HNI4_9PEZI        Unreviewed;       259 AA.
AC   A0A139HNI4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=VPS37 C-terminal domain-containing protein {ECO:0000259|PROSITE:PS51314};
GN   ORFNames=AC578_9293 {ECO:0000313|EMBL:KXT03952.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT03952.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT03952.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT03952.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the VPS37 family.
CC       {ECO:0000256|ARBA:ARBA00007617}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT03952.1}.
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DR   EMBL; LFZN01000025; KXT03952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HNI4; -.
DR   STRING; 321146.A0A139HNI4; -.
DR   OrthoDB; 2732551at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
DR   GO; GO:0000813; C:ESCRT I complex; IEA:UniProt.
DR   GO; GO:0072666; P:establishment of protein localization to vacuole; IEA:UniProt.
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   InterPro; IPR037202; ESCRT_assembly_dom.
DR   InterPro; IPR009851; Mod_r.
DR   PANTHER; PTHR13678; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 37; 1.
DR   PANTHER; PTHR13678:SF2; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 37A; 1.
DR   Pfam; PF07200; Mod_r; 1.
DR   SUPFAM; SSF140111; Endosomal sorting complex assembly domain; 1.
DR   PROSITE; PS51314; VPS37_C; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          170..259
FT                   /note="VPS37 C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51314"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          138..213
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..32
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   259 AA;  29007 MW;  E5D1D7FC2BAB3AFA CRC64;
     MSYTPQPQPQ PYSPAPQSNC YSTPPAPPPK QASGTSTPAR GPPLPPPPPG QHQNEPSELD
     GGQHYYAQRQ QQQGPPQPSI PVIEGNWLPD TLKDKSVSDL QHILNTPTLQ NALLSNPSTT
     HPAVPASEAY LTPLITSNLQ IATQLEETEA KLTALRERTQ SRLLALRALE QQHRTKLNET
     ENALQEFSPM ALYQRLNASV QEQELMNRGL EESWLEEDNT ATDKETADFV RRVKEGRKTA
     FLRRERKGRW DEGRVGGWR
//
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