ID A0A094BJA5_9PEZI Unreviewed; 1999 AA.
AC A0A094BJA5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, 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=V492_05012 {ECO:0000313|EMBL:KFY10437.1};
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:KFY10437.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY10437.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY10437.1,
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 -!- 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:KFY10437.1}.
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DR EMBL; JPJU01001713; KFY10437.1; -; Genomic_DNA.
DR STRING; 1420902.A0A094BJA5; -.
DR HOGENOM; CLU_001644_0_0_1; -.
DR Proteomes; UP000029299; 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; 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:UP000029299};
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 1182..1204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1355..1381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..204
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 230..550
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 1211..1294
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REGION 1637..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1765..1833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1900..1999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1765..1788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1904..1918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1934..1959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1982..1999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1999 AA; 227231 MW; 004B20FDCC4330E7 CRC64;
MNQALDEEAL SPTGMQVDGD EYVVEPQGGE PDDVAIINTD DDGGQAALPT ADDFEAMKSV
VLPRLIEDPE ILAEAVHTWH IERWTELSRK EHGPVFEAGG NPWRVLFFPS GNNVEHCSFY
LEQGFEEGKV PDDWYCCAQF SLVLWNPNDP SLYTSHTAHH RFTKDEGDWG FTRFVELRKL
FNVEWDSSGR PLVENEAANM TAYVRVVKDE TGVLWHTFNN YDSKKETGYV GLKNQGATCY
LNSLLQSLYF TNAFRKAVYQ IPTEDEENLA NSAYTLQRLF YQLQTSPTAV STNELTKSFG
WETRHIFEQQ DVQELSRKLM ERMEEKMKGT EAENVLPRLF CMKVKTYISC INVDYESSRV
EDFWDIQLNV IGNKDIEESF KDYIGVEKMD GENQYFAGEV FKLQDANKGV IFQSFPEVLH
LQLKRFEYDM ERDATMKTND RYEFPETFDA SPYLAEDADK SEPYIYQLHS VLVHSGDLNA
GHYYAFIKPT KDGCFYRCDD DKVIRATMRE VLEDNFGGEV DYVNGQAKPA FQKPPVIRQN
SAYMLVYIRR SRLDQVLLPV TKDDTPSHLQ KKLDEENALR EARRKEREEQ HLYLNARVMT
DRTFQEHTST DLTTFDAHER EPGCAKSFRV LRSSTIKDLA ARVGADIAQD PRRIRFWFMV
NRQNKTVRPD QPITDINQTI EQAHQKLSGT KTQEIRLWAE EADEVDANGD PVWPGLSAQQ
TNGSAKSDSI LLFLKWFDVD NQALKCIGHT YIGKERKVED LVPLILNKMG WPEKLPSGDR
TQLKLYEARD KTTNDRPNEG KANPESSRIA RWGYYLLPKS VNSKNKISSS ADAPNNATIA
SSTPHPSDWI EDAQQFYDYL LYRKIVHFLP YSKTAVDRQE VLDIEMSSKY SYDQIAAKVG
DKINVDPTHL RFHTVNATTG APKVPVKRSL NHTLQTILTP PYTTFGNNNQ KVDELYFEVL
EMSLSELDTK KNLRVIWLSE GISKEEIFDI LVPKNGNVTD LISGLIKKAK LDDEETAGPI
RVYGIHNNKV YKEMSSEYTV ASISEYITLV AERIPEEDVD VDPRNFIQAF HFQGEPNKPH
GIPFKFSIRR DEKFSDTRKR LEKRTGIKGK NFDKIKFAVV KRSSYAKPTY LEDDDILWDA
ATNDDDLLGL DHIDRTRLAR NGAVDLFLKR QARKVNDLTM RLSVWACGLL ASLSPLVSAT
ALTYKLSANE KACFFSSVEH SGAKIAFYFA VQAGGSFDVD YEVVGPNEKI VMDGQKERQG
DFVFTATEVG EYRFCFNNEM STFAEKFVDF EITVENEERT SLPSKQGTSP EQTSALEESI
FKLSGQLSTI TRNQKYFRTR ENRNFSTVRS TERRIFNLSV VESLMMIAMA MLQVFIVRFF
FQGARKGYNL KSKLNWSTLQ QRAMASISSS LSSALPLPKY TGEEETISQH AQQRGPRIVG
AEALNESQIV LKVTTQVGVF QYNDPNLASQ KSGPPPYGRR AGWRPRGADD FGDGGAFPEI
PVAQYPMDMG RKGQATSNAL AVQVDAEGKV KYDAIARRGH NDNRIVHASF KDLIPLRQRA
DAGDIDLSRP SEEEVAAATE KTKNALAVLV SGAVAAQKPK NVNVGARKDP TYVRYTPANQ
MGDNTKKNDR IMKIVERQQD PMEPPKFKHK KIPRGPPSPP PPVMHSPPRK LTAEDQEAWK
IPPPVSNWKN PKGYTVPLDK RLAADGRGLQ DVTINDKFAQ FAEALFTADR HAREEVKQRA
IMQQRLAEKE KEQKEDHLRM LAQKAREERT NAGAGRRGSR DSRSRSRSYS GSESDYSASG
EDEEIRERQK ARQEKHREEE RKLRQSRMGA ERRVQMMARE QNRDISEKVA LGLAKPTQST
ESMWDSRLFN QTSGFDTGFN EDQAYDKPLF AAQDAISSIY RPRQNMDDGD DEEAAGNEMS
RIQKSSRFEV LGRGGFKGAE DAEEREGPVQ FEKDSGDDPF NVADLISEVE KGGSGKRYGI
QTDEPRASKR AKMDDDDEA
//