ID A0A0G4N991_9PEZI Unreviewed; 2015 AA.
AC A0A0G4N991;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=BN1708_008936 {ECO:0000313|EMBL:CRK42954.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK42954.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK42954.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK42954.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CVQH01027860; CRK42954.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4N991; -.
DR OrthoDB; 2718660at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd13952; 7tm_classB; 1.
DR CDD; cd09616; Peptidase_C12_UCH_L1_L3; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR045632; DUF6314.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR PANTHER; PTHR42970; PECTATE LYASE C-RELATED; 1.
DR PANTHER; PTHR42970:SF1; PECTATE LYASE C-RELATED; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF19834; DUF6314; 1.
DR Pfam; PF00743; FMO-like; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..2015
FT /note="ubiquitinyl hydrolase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002567725"
FT TRANSMEM 717..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 744..764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 792..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 817..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 868..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1054..1073
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 710..895
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 911..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2015 AA; 219655 MW; 0142C07C011A7F2E CRC64;
MKFSLQSLVG ALALLASAAD AQQLAFPGAE GFGRFATGGR TGSVYKVTNL NDSGAGSLRD
AVSEPNRIVV FDVGGVIDIN ARIVVSANVY IAGQTAPGDG ITVYGNGFSW SNAHNAITRY
IRIRMGRGGD SGKDAVTIAE GRNMIFDHVS VSWGRDENFS VSGSAVNITV QDTIIAQGLQ
THSCGGLMET EGGVSLFRNL YVDNNTRNPK VKGRNDFQNN VIYNWGVGAG YIAGDSAGPS
WVNIVNNYFV SGPSTGRSPF TRGNENFQAY VLNNYYDADR DGVLDGTPLC MTTNCYSPLV
FAPTPFPYPG PAKLLTPQES IEHVAARAGA SLRRDAVDKL LVSELRSYGK SGKLISDEAE
IGGVGEVAGG TAPVDTDGDG IPDAWERANG LNPNDAKDAF AIGAGGWTNL ENYVNSLVPG
THLLFSMSTM EKKRWVMLEN NPDVMNQLAA TLGLSSDLEF HDVYSLDDPE LLAHIPRPAL
ALLVIIPLTP AWDQSRRAED ADKEDYAGSG PDEPVVWFKQ TIGHACGSIG LLHSLINGPA
ADFIKPGSDL ADIRSRAIPL PMADRADLLY NSAPFERAHK SVEQAGDSQA DLTGEVEGGH
FVSFVKTGGK LWELEGSRKG PLDRGSLADD EDVLSPRALD NGIKRIIKLN ADGGGDNLSF
SCIALARRAA RAPPTLLVGH PSSLPSDQLV PRQYSGPEKM PLSGTQVTTI IALERTGASL
SLIGITLIFV SYYLFKRLRT IPNLFIVFAS VANIGASIAC LIGYDGILIG EASALCQAQA
FMLEMFMQSD PWWSLAMAVN VYLVFFFGAS PASFRQYLWV YCVICFGGPF IPAIVLLLAR
PNGQMMYGNA TLWCWINSDW SELRIYTYYL PIWICILCSI LIYFAVGYHV FHQRNQLRNL
TFSHIKDANE VSMSEDNRDS AEKVGGSSSA GPQAQRLTLT QNLTGRSEDW QVTAVTEVQI
TTGSPRPDRA IEIPTVPPAA LTDSPQIRSA GHAQSWHSSH ERVPSPVISH TRFETMISSN
PPPPPPRRSL LGYVKGGMQK FNAKLQGLDP VKLAYLRTSF IFAISILVTW TPSSINRVND
LVNPGQVSFG LNVATAIVLP LQGVWNAVIY FMTSWTTVKE EYHRLMHRRS VRRLDSRDDS
RGRSSRLNVF RGHRDNHFDP SRLERGKRPR SGQVSEYELA PPAKRVLVNL RSVEDPARSQ
NAGTITLQLG RTETEKTSCG LTCLTGLTAP DSSTDDLQPE HEDLSHRLPI SARKGVSHHS
NSYTIMAKNV CIIGAGPSGL VAAKTLLYNA PQGAFNVTVF DAQKRVGGLW PASPRDGGGA
VHPLMTTNQS RHTMHFSDCG WDDADGPQFP RAWMVGRYLE RYLARYPGAE VRLGWRVTRT
EALEGEDGRG GGWRVTARDG LGREEVGVFD RLVVATGFFG EPVLPRGITD GATVPVVHSS
RYRDLKGLLG KGAKGGKILV VGGQMSGVEI TGTIASHLSS AVNAPGTTSE LAGAEGYTIH
HLIQHPAWVF PLYTTPKPKL SAPPFLPVDL GSYNLNNRPK PLTNTQGHIS PETAKTVHGI
FQNIVGQDQS QCSESIAVKG DLTSEPPYLA MSEFYTEFVR SGLITASKGK LEAMESTTAI
VTPSGEKIED VAAVVLATGF DPSPCVSFLP DSVLRTLHHS PEHRDLPLAL GFHGTQHRDL
PTLGFVGFYR SPYWGVMEMQ ARFLAALWTP ENLAKPPSGL TAAVQSDACE KRILALREDP
RCSQFPFGDY AFIMQEMAAA LDMTMSPPVE PPMPTLPHNN LPMDILTPSR YLSPLADAQA
KEENAKVLQY SNDVATAALT SSRFVAHAVF RSLLGTWKLE RSLDSKLPSH PSGHFSGTAR
FLLRDATADG LQCASSSDSV APSVTDPGDP GQEYLYIEEG EFKASNGLVF QARRRYIWRY
DEKRDTISVW FVRTDDDKRA DYLFHEVEFE TKSATEESDE RASWRAKAGH LCIDDFYNVA
YEFAFAAVHL REWSIGYAVQ GPKKDYAIRG VYRRE
//
