ID A0A2Y9RF14_TRIMA Unreviewed; 1375 AA.
AC A0A2Y9RF14;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 47 {ECO:0000256|ARBA:ARBA00026136};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme 47 {ECO:0000256|ARBA:ARBA00030277};
DE AltName: Full=Ubiquitin thioesterase 47 {ECO:0000256|ARBA:ARBA00029910};
DE AltName: Full=Ubiquitin-specific-processing protease 47 {ECO:0000256|ARBA:ARBA00032453};
GN Name=LOC101351646 {ECO:0000313|RefSeq:XP_023593017.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023593017.1};
RN [1] {ECO:0000313|RefSeq:XP_023593017.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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};
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DR RefSeq; XP_023593017.1; XM_023737249.1.
DR STRING; 127582.A0A2Y9RF14; -.
DR InParanoid; A0A2Y9RF14; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; 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; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR045578; USP47_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF702; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 47; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF19718; USP47_C; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|RefSeq:XP_023593017.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480}.
FT DOMAIN 188..564
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 425..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 578..605
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 432..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1375 AA; 157661 MW; 4C1B794E82670CF4 CRC64;
MGPGEENQLV PKEDVFWRCR QNIFDEMKKK FLQIENAAEE PRVLCIIQDT TNSKTVNERI
TLNLPASTPL RKLFEDVANK VGYVNGTFDL VWGNGINTAD MTPLDHTSDK SLLDASFEPG
RKNFLHLTDR DGEQPQILLE DSSAVDDNVH DRFIGPLPRE CSVGSTSDYV SQSYSYSSIL
NKSETGYVGL VNQAMTCYLN SLLQTLFMTP EFRNALYKWE FEESEEDPVT SIPYQLQRLF
VLLQTSKKRA IETTDVTRSF GWDSSEAWQQ HDVQELCRVM FDALEQKWKQ TEQADLINEL
YQGKLKDYVR CLECGYEGWR IDTYLDIPLV IRPYGSSQAF ASVEEALHAF IQPEILDGPN
QYFCERCKKK CDARKGLRFL HFPYLLTLQL KRFDFDYTTM HRIKLNDRMT FPEELDMSTF
IDVEDEKSPQ TESCTDSGAE NEGSCHSDQM SNDFSNDDGV DEGICLESNS GNEKISKPGL
EKNSLIYELF SVMVHSGSAA GGHYYACIKS FSDEQWYSFN DQHVSRITQE DIKKTHGGSS
GSRGYYSSAF ASSTNAYMLI YRLKDPVRNA KFLEVDEYPE HIKNLVQKER ELEEQEKRQR
EIERNTCKIK LFCLHPVKQV MMENKLEVHK DKTLKEAVEM AYKMMYLEDI LPLDCCRLVK
YDEFHDYLER SYEGEEDTPM GLLLGGVKST YMFDLLLETR KPDQVFQSYK PGEVMVKVHV
VDLKAESVAA PVTVRAYLNQ TITEFKQLIS KAIHLPAETM RIVLERCYND LRLLSVPSKT
LKAEGFFRSN KVFVESSETL DYQMAFTDSH LWKLLDRHAN TIRLFVLLPE QSPGSYSKRT
AYQKAGGDSG NVDDDCERVK GPVRSLKSVE AILEESTEKL KSLSLQQQQD GDNGDSSKST
ETSDFENIES PLNERDSSAS VDNRELEPHI QTSDPENFQS EERSDSDVNN DRSTSSVDSD
ILSSSHSSDT LCNADNAQIP LANGLDSHSI TSSRRTKANE GKKETWDTAE EDSGTDSEYD
ESGKSRGETQ YMYFKAEPYA ADEGSGEGHK WLMVHVDKRI TLAAFKQHLE PFVGVLSSHF
KVFRVYASNQ EFESVRLNET LSSFSDDNKI TIRLGRALKK GEYRVKVYQL LVNEQEPCKF
LLDAVFAKGM TVRQSKEELI PQLREQCGLE LSIDRFRLRK KTWKNPGTVF LDYHIYEEDI
NISSNWEVFL EVLDGVEKMK SMSQLAVLSR RWRPSEMRLD PFQEVVLESS SVDELREKLS
EISGIPLEDI EFAKGRGTFP CDISVLDIHQ DLDWNPKVST LNVWPLYICD DGAVIFYRDK
TEELMELTDE QRNELMKKES SRLQKTGHRV TYSPRKEKAL KIYLDGAPNK DLTQD
//
