ID A0A068SEB3_9FUNG Unreviewed; 1081 AA.
AC A0A068SEB3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Protein {ECO:0000313|EMBL:CDH60698.1};
GN ORFNames=LCOR_11478.1 {ECO:0000313|EMBL:CDH60698.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH60698.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH60698.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the VPS18 family.
CC {ECO:0000256|ARBA:ARBA00010454}.
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:CDH60698.1}.
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DR EMBL; CBTN010000102; CDH60698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068SEB3; -.
DR STRING; 1263082.A0A068SEB3; -.
DR VEuPathDB; FungiDB:LCOR_11478.1; -.
DR OrthoDB; 22879at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; 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; cd16462; RING-H2_Pep3p-like; 1.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR007810; Pep3_Vps18.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23323:SF26; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 18 HOMOLOG; 1.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF05131; Pep3_Vps18; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50236; CHCR; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 62..487
FT /note="Pep3/Vps18/deep orange beta-propeller"
FT /evidence="ECO:0000259|Pfam:PF05131"
FT COILED 894..935
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1081 AA; 123825 MW; FB1E7549ED9DA13E CRC64;
MSLIDDFNES TEASLAPVPA SFGDVYAAPN GYGTGFEGGG DNVRLETGYV SVSNGFGQAD
VPIFALNYVQ FQLPAPLVDM AVSNNILVMA LETFRILRID LDHSLEVEEI EITRKASDGK
ISKVFFDPTG RHLIITTDHG ENFYLYEKWR RTKQLSKLKG VTISSVAWNK QATLTDPSTR
EILIGTTNGL IYETCLEPTD EFFRREEKYF KQIYSMHEST MPITGLYFEQ FPVNNRKYFA
MATTPTRIYQ FVGYVGPSTN SNGSRSSPGF GESEDNRAAE KALFEAMFSN YDVNPGFQEL
PGELPYSELH FFSRFHELQQ QGVAQTFAWL TGPGIYHGDL VFGSQGVGDS VIDNVQLLQY
PATPSEDETG KLVTEIPISV ALTEFHFILL YKDRVRAVCQ LNDQIVYEEH IPINDGEIML
GMAVDDIKRT FWIYTTQTIY ELSIENEERD VWKLYLEKGQ YDTALQYCKD PGQKDKVYTA
QARDYFSLRR YQMSARYFAE STVPFEEVAL KFVEKNERDA LRTYLNNKLE RFRKKDRTQK
TILATWLVEL YLSKMNELED LMSSVHCTTT TTNGDAATTT TTATTANGTT TTTAATAVHH
NDSMYYKEQL AEIRDEFHLF LKTYCNILHK PTTYKLISSH GRNDELLDYA ALIEDYERVI
SHWIVEKDWE KALEVLAKQA NPDIFYKFSP VLMENAPYET VNVWMRQPNL NPRQLIPSLL
RYDHKRISDK VTQNQAIRYL SHVVTTLRNT DPAIHNLLLT LYATQPTPDE TALLTFLKNE
GRDMHYNLDY ALRLCTQNGR TQSCVHIYSQ MGLYEEAVNL ALKYHDLELA RINADKPEDD
DALRKKLWLS IAKHVVHENN DIKTAMEFLQ QSDLLKIEDI LPFFPDFVLI DDFKEEICNA
LEEYNIHIEE LKAEMDEATK SSESIRLDIR ELKNRFALVN AVEKCYICSF PLLTRQFYIF
PCQHAFHADC LMDQTSQFLS VRQIRRLRYI REQLSKDLGR GKKGKSNTAR GEVISAHEAA
ASMTEVHGDP RSTMTQSELL REELDEIVAG ECALCGDIMI RSIDQPFIGD DETEEVASWA
V
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