ID A0A166W4E4_9PEZI Unreviewed; 763 AA.
AC A0A166W4E4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Mov34/MPN/PAD-1 family protein {ECO:0000313|EMBL:KZL75302.1};
GN ORFNames=CT0861_04413 {ECO:0000313|EMBL:KZL75302.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL75302.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL75302.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL75302.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M67C family.
CC {ECO:0000256|ARBA:ARBA00010981}.
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:KZL75302.1}.
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DR EMBL; LFIV01000024; KZL75302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166W4E4; -.
DR STRING; 708197.A0A166W4E4; -.
DR OrthoDB; 5490729at2759; -.
DR Proteomes; UP000076552; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0061578; F:K63-linked deubiquitinase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR CDD; cd08066; MPN_AMSH_like; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR PANTHER; PTHR12947; AMSH-LIKE PROTEASE; 1.
DR PANTHER; PTHR12947:SF13; FI19924P1; 1.
DR Pfam; PF01398; JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR PROSITE; PS50249; MPN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT TRANSMEM 557..578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 664..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 693..711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 376..503
FT /note="MPN"
FT /evidence="ECO:0000259|PROSITE:PS50249"
FT REGION 175..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 86045 MW; AD1168C1F81B5BA8 CRC64;
MNGPSSPRPA RPMSIKEITN AAEDFEFRTT IPFKYWARSA DTLFQEATFA LQDRDIRKAY
QMLWRHSILV LQHLKTHPDA KLPENKALTK PLFNRQQKEV FGLLEELKPQ IDRDYNEWKL
MNASKTKVDD ETAKRPSSYD EFAARDPTLS GNAKILDAAD NQELAVSLAQ RDFKRRDAAR
RATRQAGVTE EEEQERRKGG RWEDWEHFGS PTTAATDDEE IRRQIEATRR RLDGTDGGRD
DSSFRHSQAS SYQSPAAPPR APPSYSYNYP SISRPRAVEW EATPLEPQRA YTPQLPQPPK
PPKEDFTILR QELDAAPPMR PGKEPLPSYE SVSTATLQHD VPELPAKEEV ATPSAKERLT
FRPAAYLENG DPIRPVFLPT QLRDRFLSIA SENTRKGLEM CGILCGRPVN NALFISCLLI
PEQKSTPDTC ETENESSMLD YCINEDLLMV GWIHTHPTQT CFMSSRDLHT QAGYQVMMPE
SIAIVCSPRH QPSYGIFRLT NPPGLTHILQ CTKSETFHQH SIDNLYTKAQ NPPGHVYHSD
KLDFYVKDLR PNRARACFAL SIPWLAWLDG FLLAYTLLRY ASYSKKTGKD AGLETEARLR
QGNHRDPFGT MAFPTNVLGI LITIVSGYAL VHSADSIPRL LKYEGKVKKA AEWSRTAEKQ
LWEIRYTVGT GFVGCLLSAV SGIAFSFFVP RGLGIVAVGW PALLAAGLTY GHQYMRSFWA
SKPKVPMMTD FNEAISDTMM VQDMMNPLAG AWGLVAVCKL VGL
//
