ID R0M4C8_ANAPL Unreviewed; 1081 AA.
AC R0M4C8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7 {ECO:0000256|ARBA:ARBA00021393};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Ubiquitin thioesterase 7 {ECO:0000256|ARBA:ARBA00031508};
DE AltName: Full=Ubiquitin-specific-processing protease 7 {ECO:0000256|ARBA:ARBA00031500};
DE Flags: Fragment;
GN ORFNames=Anapl_03972 {ECO:0000313|EMBL:EOB08965.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOB08965.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(2013).
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 peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; KB742404; EOB08965.1; -; Genomic_DNA.
DR AlphaFoldDB; R0M4C8; -.
DR Proteomes; UP000296049; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03772; MATH_HAUSP; 1.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
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; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 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, ECO:0000313|EMBL:EOB08965.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000296049};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 42..169
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 188..495
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOB08965.1"
FT NON_TER 1081
FT /evidence="ECO:0000313|EMBL:EOB08965.1"
SQ SEQUENCE 1081 AA; 126040 MW; 443AA7322337A531 CRC64;
AGDADDPPRI TQNPVINGNV AMADGHNNTE EDMEDDTSWR SEATFQFTVE RFNRLSESVL
SPPCFVRNLP WKIMVMPRLY PDRPHQKSVG FFLQCNAESD STSWSCHAQA VLKIINYKDD
EKSFSRRISH LFFHKENDWG FSNFMAWSEV TDPEKGFIEE DKVTFEVYVQ ADAPHGVAWD
SKKHTGYVGL KNQGATCYMN SLLQTLFFTN QLRKAVYMMP TEGDDSSKSV PLALQRVFYE
LQHSDKPVGT KKLTKSFGWE TLDSFMQHDV QELCRVLLDN VENKMKGTCV EGTIPKLFRG
KMVSYIQCKH VDYRSERIED YYDIQLSIKG KKNIFESFID YVAVEQLDGD NKYDAGEHGL
QEAEKGVKFL TLPPVLHLQL MRFMYDPQTD QNIKINDRFE FPEQLPLDEF LQKTDPKDPA
NYILHAVLVH SGDNHGGHYV VYLNPKGDGK WCKFDDDVVS RCTKEEAIEH NYGGHDDDLS
VRHCTNAYML VYIRESKLSE VLQPVTDHDI PQQLVERLQE EKRIEAQKRK ERQEAHLYMQ
VQIVAEDQFC GHQGNDMYDE EKVKYTVFKV LKNSTLTEFV QNLSQTMGFP QDQIRLWPMQ
ARSNGTKRPA MLDNEADGNK TMIELSDNEN PWTIFLETVD PEMAATGATL PKFDKDHDVM
LFLKMYDPKT RSLNYCGHIY TPISCKIRDL LPVMCERAGF PQETNLILYE EVKPNLTERI
QDYDVSLDKA LDELMDGDII VFQKDDPEND NSELPTAKEY FRDLYHRVDV IFCDKTIPND
PGFVVTLSNR MNYFQARTLF VAKTVAQRLN TDPMLLQFFK SQGYRDGPGN PLRHNYEGTL
RDLLQFFKPR QPKKLYYQQL KMKITDFENR RSFKCIWLNS QFREEEITVY PDKHGCVRDL
LEECKKVVEL SEKGSGKLRL LEIVSYKIIG VHQEDELLEC LSPATSRTFR IEEIPLDQVD
IDKENEMLIT VAHFHKEVFG TFGIPFLLRI HQGEHFREVM KRIQTMLDIQ EKEFEKFKFA
IVMMGRHQYL NEDEYEVNLK DFEPQPGNMS HPRPWLGLDH FNKAPKRSRY TYLEKAIKIH
N
//
