ID T0KMX7_COLGC Unreviewed; 1951 AA.
AC T0KMX7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Vacuolar membrane protein {ECO:0000313|EMBL:EQB53394.1};
GN ORFNames=CGLO_06882 {ECO:0000313|EMBL:EQB53394.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB53394.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB53394.1}.
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DR EMBL; AMYD01001374; EQB53394.1; -; Genomic_DNA.
DR STRING; 1237896.T0KMX7; -.
DR eggNOG; KOG1977; Eukaryota.
DR eggNOG; KOG1978; Eukaryota.
DR eggNOG; KOG2114; Eukaryota.
DR HOGENOM; CLU_001877_0_0_1; -.
DR OMA; VAMAFQW; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006298; P:mismatch repair; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd16688; RING-H2_Vps11; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.1540.20; MutL, C-terminal domain, dimerisation subdomain; 1.
DR Gene3D; 3.30.1370.100; MutL, C-terminal domain, regulatory subdomain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR014790; MutL_C.
DR InterPro; IPR042120; MutL_C_dimsub.
DR InterPro; IPR042121; MutL_C_regsub.
DR InterPro; IPR037198; MutL_C_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR024763; VPS11_C.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
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; PF13589; HATPase_c_3; 1.
DR Pfam; PF08676; MutL_C; 1.
DR Pfam; PF12451; VPS11_C; 1.
DR Pfam; PF17122; zf-C3H2C3; 1.
DR SMART; SM00299; CLH; 1.
DR SMART; SM00853; MutL_C; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF118116; DNA mismatch repair protein MutL; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50236; CHCR; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1862..1896
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 404..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1951 AA; 216592 MW; A64ACA25CF2D4330 CRC64;
MSIKPLPEDV IRRIRSAATI TSLNAVVCGL IKNSFDAGAI RINITVDYSR GNCTVEDDGL
GILPIEFREA GGLGKLYHTS RHSSEGEAHG ANGNFLASLA ALSLLSITSH HHLHNSQNSL
TLHNAKVLAR NVPALREQRL LAFAHGTRVI VRDLFGSMAV RVKQRAVASE KAAVDKEWSR
LVHDLAALLL AWPSPVALYA RDTIHNNEIR FRPTSTSSKS VNFNLLGHSS LILAQSGLSG
GLDHVSWIPI GATRGKLTVD GCISLSPVAT RRAQFISFGV HPVANEHGTN VLYTEVNRVF
VNSGFAIEED VDMSLDQDEL LESLKGLANR NVRPKRGLDR WPMFHFRISS SSGVRPLLTS
SFEDLLEDRN RTLSDMIGLL KLVCFEFLKK YHFRPHKFND YLRRPGYEGK DEVNQSSGRP
GKRSRPVSTA SSRSNSATPT SRPDSPFDLW QRVKAGQVSA ATSKSGRSTP ISSTASPLAT
AASSVNDEEE RDLQPSLRFL DDSGNVLRRP FEDVPSISSP KKAAVPDQDS SSGSSPEEAG
QYRTTETGLA GSVQPQEASQ DSSQFPKFNT PFTSAFQRFK ENSAQPAKEP SDWFKGVLSK
WENPVFKPVQ PSVPRVDDTS LGGGDEDVRS TQATDAGCCH HTTMSDVKLT GRISKAALVG
AEVVSQVDAK FILVKLHREQ VSGRARPELQ RNSVLVLIDQ HAADERCRLE ALMQNYFEKA
DGSEQVVART QALDKPLQFE FSNKEHLLLR RYAHHLRRWG IVYKLGDQET NQWRHKSKQL
PKVEVLSLPP SMHERCKTDP KLLSEVLRNE IWKLEEGDRP TTRPFTAAKG IAGGDIDWVS
NFHGCPQGIL DLLHSRSCRS AIMFNDVLST DDCKDLVRRL GQCVFPFQCA HGRPSMVPLI
DMRNLNIHNE TSPHSCAAVA PARATAPKLP TAASLECEAP TTTDTQRRPQ HNSHRRPSDE
PLTPRDVAMA FQWKAFDFFD VAQIRLADDE TRAFFESNEI ASVCSGSDSL FLGSYDGFVR
IVGSSWKIVK SFQAHDVGTI THMRQIEGTS LLVTVAEDLS SEPVLKIWAL DKLVKKTNMP
TCLSTLNITN NKKQFPISAI DLLDNLTQVA VGFANGAVTL IRGDLINDLG AKQRTVHESE
EPVTGIELMT DVQGVTTLFI STTARILKLA ISRRGHSSPP KTVEDLGCNV DCMTVDKKTG
DVVVAREDAI YTYTLEGRGA PRAYESPKRL VSIYQDYVAL VCPPSSSTTD KPSDTMRRRF
GGGAADALFN ASTFVLLEPD LRVVGHTQSL ISPFKAIFQI WGDLFVLTQD GKVNRFHEKT
LQQRLEMLYQ RNMFPLAIEL AQKSKMDATQ QSGIFRRFGD HLYQKADYDG AMVQYIKAID
TTEPSQVIRK FLDTQRIHNL IQYLEQLHEH RKATADHTTL LLNCYAKLKD IDKLEAFIKS
PGDLKFDLET AISMCRQGGY YEQAAYLAKK HGETDLVVDI LIEDSKKYAD ALDFIWRQDP
EVAYPCLKKY ARVLIENCPK DATTLFIDYY TGKYRPRIHI IPIEDNEESV GAGGYVAGAA
NAVQNLSNFL PLPYMNTSSI ASPSTPGNQT KPINGDASLI MNPEDIPAPK YSPPRPRTAF
SSFIDHPDEF IVFLEACLKE PALEENDRTD LYTTLFEMYL HKSNEKKGDQ HKEEWENKAK
TLIEGQDIPM ESSNVLLLSH LSDFKDGTTL VKEQSGLLFD IFRSYTSAKD TRGAIKALRK
YGPEEPQLYP AALAYLTSDP RILEEAGPVE LSNVLGKIDR DGLMAPLQVI QTLVGQNGSS
AGGGVATMGM IKPYLHETID RERKEIAANR RRITAFRSET EHKRAELAEL GSKPAVFQSS
RCSVCTAQLD LPAVHFLCKH SFHQRCLRVE GECPQCATDN ATIRALRKTQ IETAGKHELF
KAELERSEDR FGTVAEWFGR GVMGAPNADT A
//
