ID A0A094GPG2_9PEZI Unreviewed; 2024 AA.
AC A0A094GPG2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 37.
DE RecName: Full=Pre-mRNA-processing protein 45 {ECO:0000256|ARBA:ARBA00022160};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=V501_08990 {ECO:0000313|EMBL:KFZ04767.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ04767.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ04767.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
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 -!- 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 -!- SIMILARITY: Belongs to the SNW family. {ECO:0000256|ARBA:ARBA00010197}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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:KFZ04767.1}.
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DR EMBL; JPKD01002365; KFZ04767.1; -; Genomic_DNA.
DR STRING; 1420914.A0A094GPG2; -.
DR HOGENOM; CLU_001644_0_0_1; -.
DR Proteomes; UP000029315; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005681; C:spliceosomal complex; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR017862; SKI-int_prot_SKIP.
DR InterPro; IPR004015; SKI-int_prot_SKIP_SNW-dom.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR12096; NUCLEAR PROTEIN SKIP-RELATED; 1.
DR PANTHER; PTHR12096:SF0; SNW DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF02731; SKIP_SNW; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50866; GOLD; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000029315};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT TRANSMEM 1207..1229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1380..1406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..205
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 231..551
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 1236..1319
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REGION 1662..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1790..1874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1925..2024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1929..1943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1959..1984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2007..2024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2024 AA; 230223 MW; 344A45A1DAEDD027 CRC64;
MNQALDGETL SPTGMQVDGD EYVVEPQEGE PDDVAIINTD EDGEQAAALP TADNYEAMKA
VVLPRLIEDP EILADAVHTW NIERWTELGR KEHGPVFEAG GNPWRVLMFP SGNNVEHCSF
YLEQGFEEGK VPDDWYCCAQ FSLVLWNPND PSLYTSHTAH HRFTKEEGDW GFTRFVELRK
LFNVEWDSSG RPLVENEAAN MTAYVRVVKD ETGVLWHTFN NYDSKKETGY VGLKNQGATC
YLNSLLQSLY FTNAFRKAVY QIPTEDEENL ANSAYTLQRL FYQLQTSPTA VSTNELTKSF
GWETRHIFEQ QDVQELSRKL MERMEEKMKG TEAENVLPRL FCMKVKTYIS CINVDYESSR
VEDFWDIQLN VIGNKDIEES FKDYIGVEKM DGENQYFAGE VFKLQDANKG VIFQSFPEVL
HLQLKRFEYD MERDATMKTN DRYEFPETFD ASPYLAEDAD KSEPYIYQLH SVLVHSGDLN
AGHYYAFIKP TKDGCFYRCD DDKVIRATMR EVLEDNFGGE VDYVNGQVKP AFQKPPVIRQ
NSAYMLVYIR RSRLDQVLLP VTKEDTPEHL QKKLDEENAL REARRKEREE QHLYLNARVM
TDRTFKEHSS TDLTTFDVNE REPGCAKSFR VLRSSTIKDL ATRVGADIGQ DPRRIRFWFM
VNRQNKTVRP DQPITDVNQT VEQAHQKLSG TKTQEIRLWA EEAEEVDAAG EPIWPGLPSP
QANGSQKSDS ILLFLKWFDI DSQALRCIGH VYIGKERKVE DLVPLILHKM GWPDKLPSGD
RTQLKLYEEI KPQMIDPMKG KQTLKAAELQ DGDIICFQKA LGAKAAHELE KDAKNNRSLT
SLSSSVDFLS NANRSPSHPS APRPSDLIED AQQFYDYLLY RKIVHFLPYS KTAVDRQEVL
DIELSSKYSY DQIAAKVGEK INVDPTHLRF HTVNATTGAP KAPIKRSLNH TLHTILTPPY
TTFGNNNQRV DELYFEVLEM SLSELDTKKS LRIIWLSEGI TKDDTFDVLV PKSGNVTDLI
SGLIKKAKLD DEETAGPIRV YGIHNNKVYK EMSPEYSVAS ISEYITLVAE RIPEEDVNVD
PGHFIQAFHF QGEPNKPHGF PFKFSIQRDE KFSETRKRLE KRTGIKGKNF DKIKFAVVRR
SSYSKPTYLE DDDILWDVAT NDDDLLGLDH VDRTRLARNG AVDLFLNKPN SSHKLQARKL
NNHTMRLLVW ACGVLASLTP IVSATALTYK LNANEKACFF SSVEHSGAKI AFYFAVQAGG
SFDVDYEVVG PNEKIMMDGQ KERQGDFVFT ATEVGEYRFC FNNEMSTFAE KFVDFEITVE
NEERTSLPSK QGTSPEQTSA LEESIFKLSG QLSTITRNQK YFRTRENRNF STVRSTERRI
FNLSIIESLM MIAMAALQVF IVRFFFQGAR KGYNLKSKLT CPTLQQRAMA SLSSSLFKAL
PLPKYTGEEE TISQHAQQRG PRIVGAEALN ESQIVLKVTT QSSMLRYTRS DLTAQKSGPP
PYGRRAGWRP RGADDFGDGG AFPEIPVAQY PMDMGRKGQA TSNALAVQVD AEGKVKYDAI
ARRGHNDNRI VHASFKDLIP LRQRADAGDI NLSRPSEEEV AASTEKTKNA LAVLVSGAVA
AQKPKNVNVG ARKDPTYVRY TPANQMGDNT RKNDRIMKIV ERQQDPMEPP KFKHKKIPRG
PPSPPPPVMH SPPRKLTAED QEAWKIPPPV SNWKNPKGYT VPLDKRLAAD GRGLQDVTIN
DKFAQFAEAL FTADRHAREE VKQRAIMQQR LAEKEKEQKE DHLRMLAQKA REERTNAGAG
RRGSRDSRSR SRSYSGSESD YSGSDEDQEV REREKARQER HREEERKLRQ SRMGAERRVQ
MMAREQNRDI SEKVALGLAK PTQSTESMWD SRLFNQTSGF DTGFNEDQAY DKPLFAAQDA
ISSIYRPRQN MDDGEDEEAA GNEMSRIQKS SRFEVLGRGG FKGAEDAEER EGPVQFEKDT
GEDPFNVAEL ISEVEKGGSG KRYGIQADEP RASKRARMDD DDEA
//
