ID A0A151MBW5_ALLMI Unreviewed; 1286 AA.
AC A0A151MBW5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=USP47 {ECO:0000313|EMBL:KYO22017.1};
GN ORFNames=Y1Q_0000646 {ECO:0000313|EMBL:KYO22017.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO22017.1};
RN [1] {ECO:0000313|EMBL:KYO22017.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO22017.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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 -!- 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:KYO22017.1}.
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DR EMBL; AKHW03006283; KYO22017.1; -; Genomic_DNA.
DR Proteomes; UP000050525; Unassembled WGS sequence.
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 CDD; cd17039; Ubl_ubiquitin_like; 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|EMBL:KYO22017.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525}.
FT DOMAIN 168..544
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 108..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 558..585
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 412..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1286 AA; 147009 MW; FE203459A830DBE0 CRC64;
MVPSEESQLV PKEIESAADE PRVLCIIQDT TNSKTVNERV TLNLPASTPL RRLFEDVASK
VGYVNGTFDL VWGNGVSVAD MTPLEQSSDK SILDAGFEPG KKNFLHLTDK DGEQPHIMSQ
ESSSTDDGTQ DRFIGPLPRE GSVGCTSDYV SQNYSYSSIL SKSETGYVGL VNQAMTCYLN
SLLQTLFMTP EFRNALYKWE FEESEEDPVT SIPYQLQRLF VLLQTSKKRA IETTDVTRSF
GWDSSEAWQQ HDVQELCRVM FDALEQKWKQ TEQADLINQL YQGKLKDYVR CLECGYESWR
IDTYLDIPLV IRPYGSNQAF ASVEEALHAF IQPEILDGPN QYFCERCKKK CDARKGLRFL
HFPYLLTLQL KRFDFDYTTM HRIKLNDRMT FPEELDMGTF IDVEDEKSPQ TESCTDSGAE
NEGSCHSDQM SNDFSNDDGV DEGICLETNS GAERISKVGS EKNSLLYELF SVMVHSGSAA
GGHYYACIKS FSDDQWYSFN DQHVSKITQE DIKKTYGGSS GSRGYYSSAF ASSTNAYMLI
YRLKDSTRNA KFLEAHEYPE HIKQLVQKER ELEEQEKRQR EIERNTCKIK LFCMHPVKQI
MMENKLEVHK DKTLKEAVEI AYKIMDLEEA VPLDCCRLVK YDEFHDYLER SYEGEEDTPM
GILLGGVKST YMFDLLLETK RPDQVFQCYK PGEVMVKVHV VDLKTESVAP PISVRAYLNQ
TVTEFKQLIS KATHLPAETM RVVLERCYND LRLLNVANKT LKAEGFFRSN KVFVESSESL
DCHMTYTDSQ LWKLLDRHAN TIRLYVSLPE QSPGSQFKRT VYQKASGDSA SAEHRELENQ
IQISDPENFQ SEERSDSDVN NDRSTSSVDS DILSSSHSSD TLCNVENAPV PLANGLDSHS
ITSSRRSKAN EGKKDTWDTA EEDSGTDSEY DESGKSRGEA QYMFFKAEPC AADEGSGEGQ
KWLMVHVDKR ITLSAFKQHL EPFVGVPSSH FKVFRVYASN QEFESVRLNE TLSSFSDDNK
ITIRLGRALK KGEYRVKVYQ LLVNETEPCK FLLDAVFAKG MTVRQSKEEL LPQLREQCGL
DLTIDRFRLR KKTWKNPGTV FLDYHIYEED INISSNWEVF LEILDGAEKM KSMSQLAVLS
RRWRPSAMKL DSFQEVVLES SSVDELKEKL SEISGIPLEN IEFAKGRGTF PCDISVLEIH
QDLDWNPKVS TLNVWPLYIC DDGAVIFYRD KTEELMELTD EQRNELMKKE SSRLQKTGHR
VTYSPRKEKA LKIYLDGAPN KDLTQD
//
