ID   A0A0L7R8R8_9HYME        Unreviewed;      1086 AA.
AC   A0A0L7R8R8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Vacuolar protein sorting-associated protein 11 homolog {ECO:0000256|PIRNR:PIRNR007860};
GN   ORFNames=WH47_00147 {ECO:0000313|EMBL:KOC67277.1};
OS   Habropoda laboriosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Habropoda.
OX   NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC67277.1, ECO:0000313|Proteomes:UP000053825};
RN   [1] {ECO:0000313|EMBL:KOC67277.1, ECO:0000313|Proteomes:UP000053825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0110345459 {ECO:0000313|EMBL:KOC67277.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Habropoda laboriosa.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004492}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004492}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004492}.
CC   -!- SIMILARITY: Belongs to the VPS11 family.
CC       {ECO:0000256|ARBA:ARBA00007070, ECO:0000256|PIRNR:PIRNR007860}.
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DR   EMBL; KQ414631; KOC67277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L7R8R8; -.
DR   STRING; 597456.A0A0L7R8R8; -.
DR   Proteomes; UP000053825; Unassembled WGS sequence.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0099023; C:vesicle tethering complex; IEA:UniProt.
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; cd16688; RING-H2_Vps11; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR016528; VPS11.
DR   InterPro; IPR024763; VPS11_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
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; PF13923; zf-C3HC4_2; 1.
DR   PIRSF; PIRSF007860; VPS11; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50236; CHCR; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          822..860
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          945..1086
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        975..1001
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1010..1034
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1043..1063
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1064..1086
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1086 AA;  124104 MW;  97340EF7A6744D55 CRC64;
     MAFLEWKRFN FFDLKKEVDD GKVAQALGEA QVTAATSGNG NLVFGDNTGN VHLVNRKYDV
     TTFRAYEITL TLAQQVQHST FLFTIGEDEK GCNPTIKVWN LAKLDKQGSP TCVRISRAIP
     SYKAVPATAL CVHTNLTLMA VGFADGSIML YRGDLTRERK NKIKVLKDTN DSITGLAIRS
     TSKQNHLFVA TPNSVFLYNI TVKDKEFKFP LDTDMGCEKN CSILADSMQD NHFMIGRNDA
     IYCYTPDGRG PCYAVRGQKI MLEWFRNYLV IIAKEAANDP RTTTTISAKP RQAFTYFTIE
     PIPPGVDKHI ITVLDIQNKL TVFSASTLFV QAVLSEWGGF FILNGNSKLY LLDEIDLQTK
     LFLLFKKNLY DISIRIAKNQ QYDAEGLVDI FRQYGDHLYS KGDHNGAIEQ YIKTIGKLEP
     WYIIRKFLDS QHIDNLTTYL EALHKAGHAT EDHTTLLLNC YTKLNHTDKL KEFIMTKDRE
     IDFDVEIAIK VCRLASPEDA LLLAQKHGRH EWYLRIQIED KHEYEKALEY MATLEFEEAE
     SIMKKYGDIL IKNVPNESTQ FLKTLCTNYR PSNKLLIDQK TIDGLIDKAN PEDFIHLFLN
     NSEHLVEFLE HLVNTNTKWS TQVYNTLIEH YLHVWSALDS EAKAEYEQRI IRLLQSSEAC
     YDKDQILILC YQHNFSRGLL YLYEKSELYQ EILWYHLQNG NSEQVLATCK RFGHQDPNLW
     VQALWNVARN KEAPTKLLTD ILANIAQERL LSPLMVIDAI STSLSCTLGD VRTYLYNVLR
     TEHEQTQADI ELTEKYRADT QKMREQIESI KNSTIIFQGS RCSACQDQLE LPSVHFMCQH
     SYHQRCFQDF SENDNECPAC LPTNKQFLDI IRAQEQAKDL DETFHSLLDR AEDPFSLVAD
     YFGRGVFKKL TVITDKSLSS SSMKFAEPKL NYGPGAEAKL RLAEGKNTTL VKPETRRPYN
     NLPTAADDRL RSFSKPDQSS SLEANISATG SGISSPRENL RKTSPVRIRE ARILNSTTPK
     SSPIQKSFVP PKTPTVPSNR IKIDDYNESK NPFFKKESDD STNPFKKNTN PFNTSTNPFD
     DDDSIP
//