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Database: UniProt
Entry: K1WDG9_MARBU
LinkDB: K1WDG9_MARBU
Original site: K1WDG9_MARBU 
ID   K1WDG9_MARBU            Unreviewed;       659 AA.
AC   K1WDG9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Vps52/Sac2 family protein {ECO:0000313|EMBL:EKD15465.1};
GN   ORFNames=MBM_06681 {ECO:0000313|EMBL:EKD15465.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD15465.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD15465.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD15465.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- SIMILARITY: Belongs to the VPS52 family.
CC       {ECO:0000256|ARBA:ARBA00008180}.
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DR   EMBL; JH921442; EKD15465.1; -; Genomic_DNA.
DR   RefSeq; XP_007294570.1; XM_007294508.1.
DR   AlphaFoldDB; K1WDG9; -.
DR   STRING; 1072389.K1WDG9; -.
DR   GeneID; 18762616; -.
DR   KEGG; mbe:MBM_06681; -.
DR   eggNOG; KOG1961; Eukaryota.
DR   HOGENOM; CLU_010797_1_0_1; -.
DR   InParanoid; K1WDG9; -.
DR   OMA; IHVVMVE; -.
DR   OrthoDB; 2723231at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007258; Vps52.
DR   InterPro; IPR048361; Vps52_C.
DR   InterPro; IPR048319; Vps52_CC.
DR   PANTHER; PTHR14190; SUPPRESSOR OF ACTIN MUTATIONS 2/VACUOLAR PROTEIN SORTING 52; 1.
DR   PANTHER; PTHR14190:SF7; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 52 HOMOLOG; 1.
DR   Pfam; PF20655; Vps52_C; 1.
DR   Pfam; PF04129; Vps52_CC; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          153..320
FT                   /note="Vps52 coiled-coil"
FT                   /evidence="ECO:0000259|Pfam:PF04129"
FT   DOMAIN          337..653
FT                   /note="Vps52 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20655"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   659 AA;  73912 MW;  B3501E2C98072AC2 CRC64;
     MSFSPIPRRP SHLGPAPASA VPTRPVFNPR SSSLSIHSSD STTSLLASAR RPNGSALKNS
     QKAPGATDPL TVLDILLGSE APELDLVQAQ AQDHLGKDAV GDTYAHEWEW ESELDFEGRS
     LRELLAPQSP YSEEELLHPP TRTVEEFEQD EAKFEHLHHS IRDCDDVLNS VEMNLTSFRN
     DLAAVSAEIE TLQARSTALS VRLENRKIVE NGLGPIVEEI SVSPAVVRKI VEGAIDEAWV
     RALAEVEKRS KAMDLKSKEN RNIKGIKDLE PLLGNLIDKA LERIRDFMVA QIKSLRSPNI
     NAQIIQQQNL IKYKDLYAFL YKHHPQLAEQ IGQAYMNTMR WYFLNQFTRY VKALEKIKLH
     AIDKHDVLGG DDGSRKSNLL SSAKPTASHD AFNLGRRIDM LRTSNQTALS SFLAEEEKST
     HYMEVVFRNF NLALVDNASA EYSFLTAFFA PSLSYAAISR HFNYIFEPTF SLGNNLTKSL
     IHETFDCLGL LLCVRLNQHF AFELQRRKIP AVDGYINGTN MLLWPRFQVI MDQHCESVRT
     VTNGVSTRKP SASEQARQSA APHFMTQRFG QFMAGILSLS TEAGDDEPVS ASLMRLRSEI
     EAFLTKTSKA IGDARKRERF LYNNYSLILT IVGDVEGKLA LEQQEHLQGL KSAFGEVAR
//
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