ID A0A093ZVD3_9PEZI Unreviewed; 1456 AA.
AC A0A093ZVD3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Ubiquitin-like protease family profile domain-containing protein {ECO:0000259|PROSITE:PS50600};
GN ORFNames=V492_02287 {ECO:0000313|EMBL:KFY15000.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY15000.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY15000.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY15000.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family.
CC {ECO:0000256|ARBA:ARBA00005234}.
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:KFY15000.1}.
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DR EMBL; JPJU01000673; KFY15000.1; -; Genomic_DNA.
DR STRING; 1420902.A0A093ZVD3; -.
DR HOGENOM; CLU_243309_0_0_1; -.
DR Proteomes; UP000029299; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019783; F:ubiquitin-like protein peptidase activity; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02979; PHOX_C; 1.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF7; P-HYDROXYBENZOATE-M-HYDROXYLASE; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF02902; Peptidase_C48; 1.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029299}.
FT DOMAIN 1244..1414
FT /note="Ubiquitin-like protease family profile"
FT /evidence="ECO:0000259|PROSITE:PS50600"
FT REGION 691..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 966..993
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1173..1200
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 803..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1456 AA; 163168 MW; 79BF5155612F93FF CRC64;
MANNVAPNDP VPASSVELYD IVIVGAGPVG LLLSTCLARW GYKIKHIDNR PEPTKTGRAD
GIQPRSLDLL KNMGLKPEIM SHKPAKVFEV AFWDPTSAQD GIHRTGTWAS CPSFIDARYP
FTTLLHQGHI ERAFISDLEK NGVTVQRPWT ITGFKTDADS DPTYPVEVNI SHIDGKAKET
VRAKYLFGGE GARSFIRDQL KIQITHKDPI AHVWGVMDGV VQTDFPDIKM KCTIHSEHGS
IMVIPREDNM VRLYIQIASS TDKNWNPRRT ATEEEVQAAA KKIMAPYNIT WERVEWFSVY
PIGQGIASKY TLDHRVFLGG DSCHTHSPKA GQGMNTAFLD AQNIAWKIHH VESGFADRRI
LETYESERKL VAENLLNFDA KYAALFSQRP PAAHDVKAAS EGATSNAGEE NIFIKTFKES
CEFTSGYGVA YMPNPLNWSP DHPAKSPLIH PEGTTLRTGR ILINANVTRA VDANVVHLEQ
EIPLNGSFRI YVFAGEQAVT RKALHDFGAN LEKKGSFYSS YRRADKTSIS YHERHNPESL
FFTLCTIFAS KRADIEVSRD LPMTLARYRD NIYADDIWDQ RVPNATAAAH AKMGLDQKKG
GVVVVRPDGY VGVVVSLVEG SGTVDALNEY FAAFCTKKLA TTAQRFKNVL DTGSPMEWEP
THRSNPAWQP PMSGRIAVAN ERDHPHWVPP IPGAFINTPP RRNEVGLRSA DRKRSAEGAQ
FEYRPQYVEE SGIQPFADGH SKMTLRSIIT AVCWFAGATW ETAQWTYKRA RQVQVTEIQR
VAADGYISIK RRAAEVVRPS APTVEQITHQ SRSQPPPRES LSQRPRNPRG IRQEPSNISA
SAPSRSRKPS REHTVPRNTT DAEASSLISP PESPRMAAMS LPETQKSKVG KHARVNDISP
SEDEFEEMMY QEARARELRE AKRLEERRIE EARRPKSLDE MIAAQKQRQT HNEKKIEESA
EELALKKAQQ IARVKAQREA RELSEQIARE MEMARSSARR RALLAGTVAG TVTRPWVPLL
SPQPSEDEVK DKAADEAKVE ANDEAKDEAK DEAKDEVKDE AKDEVKDEAK DNAETLARQP
ARSALRRNRQ QEAQDETVPS VQLPIPSSGE GQRARNGGFI DYFLLPEVYE EKEVLEAKIE
GGLKNLALES STEHLHWKSE EDEKRKKAID DYNRMVAEEL AKAHEEAEKL ARELAEEEAA
REPHTGRRRL QTKLVQLSED WHTTINQAMS RGENVALATS LDGTQLTKRD FVTVLGQEAW
LNDNIINSYV DVVVEHANRK AGRNQRDKTP KVVAQSSFFY KKIRDDGPQS VSRWMRRKRA
AGRNLLEVET MLIPVNNSAH WTMIVVSPKA RTIEYLDSFG GSKDVFIRNT KAWLAVELGS
AWNESDWRVL DTKSARQFNG FDCGVFAVTN AECVAGGVTT TSYDGDDMAM QRRRIAAVLL
NGGFSGGLEA AEDIDM
//
