ID A0A194VAT0_9PEZI Unreviewed; 1481 AA.
AC A0A194VAT0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Putative ubiquitin carboxyl-terminal hydrolase 3 {ECO:0000313|EMBL:KUI61132.1};
GN ORFNames=VP1G_08348 {ECO:0000313|EMBL:KUI61132.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI61132.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; KN714768; KUI61132.1; -; Genomic_DNA.
DR STRING; 694573.A0A194VAT0; -.
DR OrthoDB; 294001at2759; -.
DR Proteomes; UP000078576; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd02257; Peptidase_C19; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR48083:SF28; ACYL-COA DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10880); 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme {ECO:0000256|ARBA:ARBA00022617};
KW Hydrolase {ECO:0000313|EMBL:KUI61132.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000078576}.
FT DOMAIN 5..82
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1028..1398
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 515..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1481 AA; 162193 MW; 7DEA11B7D45749B4 CRC64;
MAAPIKTFTR EQVTKEGSTE DQVLFIIDSK VYDVSDFLDA HPGGEAVLRQ VAGTDATEAF
YNLHRHEVLT GKYAELAIGT IEGEKPQVVN PGPGELSKVP YAEPLWLTPQ FKNPYYNDSH
RRLQKAIRKF TDLYVTPEAQ AKEKDGTFIS QELIDRMSKA GILHMRLGPG KHLQSAPPLL
GGAVKPEEFD YFHDLIVGQE MVRASARGFQ DGNMAGMTIG LTAVLNYAND EAFKKKIADE
VFSGKKKICL AITEAFAGSD VARLRTTAKK TADGKHYIVN GTKKWITNGV FSDYFVTGVQ
TDKGLSVLLI ERGEGVETKL IKTSYSTAAG TTFITFDNVK VPVENLLGKE NQGIYVILSN
FNHERWTMCC GTVRFSRTII EETLKWAHQR LVFGKRLIDQ PVIRLKLAKM IALVESHQSW
LETITYQMCN MSYASQSKHL GGPIGLLKMS CTRMAHEIAD EAVQIWGGRG LTQSGMGRVI
DNFNRGYKFD AILGGAEEVL GDLGTDESIQ VRISSSRASG ARRIASTHNT NPKTRVTPAS
VPGPPPRGGR GRGQHYNSHH SQGHFQQQFT QYSPNIYNPY ATPYNNAFAY ASPQYIPPQY
GQNGALPQAY AHHAYQPQFY THQQQLPPQQ FFNTNPLVPH YPGPQSPSFS IPFQPPPQPM
VSVPPPDVVP IPPPVPPTLP TTPASHHSLQ HTPIPIAQSV YQPPEVPVAN VLSPRPTIAQ
EPVPVSDTHV KTPEPPAAVS TPTASTSASR DLPSSPEFSP INPRPETIAH RLPWTTHPDE
PWPKSKKPKR KKKVLPKDAQ GVAMRSAKAA PLEASAVTVE GQTSHGQDAS EDPVAAADLQ
DDSSLTEKTT STVDAATDTL TTSTPESTVQ PPTPSPQKTS SGATPTKPPK TTPRHVAPAV
PVLPVLPKDG AMTNNNSAVS KDKATEKPDD ESKTSTEAPE APEQPKEEEN TAQPAAVTSW
SALFKRASAS KPAATGTPPP NGTAVSDKPR PVAEGTTVVA KPNSATLADM LKTYEVRTND
KIYFIEPRAL KNRGTDCYMN SVLQVLVFCM PFFNFLQQVR SNVVHSFNNT SQTPLIDVMI
DFMAEFRAIT SADDLDQLRR KLKKEDYQPN SDSFLPDMVY NCIRKLSGFA TVWPGSQHDA
QEFLMLLLDG LDDECKKMII SPANTAPDSH ASSQGDDIND DGAWTEVGHR QRHAVTTISG
DTPVPNPISK IFDTGFRLEL RVPGSKDSVR IEPHKCIPLA IGDPSVKDVV DALRLFTAPE
TVEMGNAQGA QVNGKMQRSM HVLPPVLTLF FKRDKKVGNE FQKIWKSVGY PLELELPAEV
LSRQLRNEIV AGGRELPKYK LFGVVYHHGH SVTSGHYTVD VCRQDDQEWI RFDDTQITRI
SGEDVVAGGM EEPPAKSTGS NKAETANGSS SNRFAAMEEY DAGDNDGNWK QVGQGANGTK
KYSSVVNGSS SGTSTPKGKP TKNNFKDNNK VAYVLFYQLM N
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