ID A0A158NNI3_ATTCE Unreviewed; 1324 AA.
AC A0A158NNI3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=Ubiquitin thioesterase 47 {ECO:0000256|ARBA:ARBA00029910};
DE AltName: Full=Ubiquitin-specific-processing protease 47 {ECO:0000256|ARBA:ARBA00032453};
GN Name=105622281 {ECO:0000313|EnsemblMetazoa:XP_012059091.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012059091.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012059091.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) 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 EMBL; ADTU01021606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012059091.1; XM_012203701.1.
DR STRING; 12957.A0A158NNI3; -.
DR EnsemblMetazoa; XM_012203701.1; XP_012059091.1; LOC105622281.
DR GeneID; 105622281; -.
DR KEGG; acep:105622281; -.
DR eggNOG; KOG4598; Eukaryota.
DR InParanoid; A0A158NNI3; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000005205; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000005205}.
FT DOMAIN 180..584
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 461..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1324 AA; 153282 MW; C5391E4C5CF8BEAF CRC64;
MPCRAASCCI MVCKAGEKTQ VCVVQFNMPY EANHKLCTSD KFSLHVSTRV KDLYNYIEEH
YHMQPDSFRL LLRTPSCTLI DLSELKDKTM EQVGVDFSVD SSSPETKNTL FVVHPTEPFV
IDMATSRRKM DYHHSPPFNV TGAPSLHPRW TEENIVREDV RDGREEVNFR TFIKTETSYV
GLVNQAMTCY LNSLLQALYM TPEFRNALYN WEYIDSSEKD EALSIPYQLQ KLFLNLQTST
RSAVETTSLT KSFGWDSTEA WQQHDIQELC RVMFDALEQK FKNTEQADLI NRLYEGKMTD
YVKCLECGTE KSREDTFLDI PLPVRPFGSN VAYNSVEEAI RAFVQYETLE GANQYHCEKC
NKKCDAHKGL KFTKFPYLLT LHLKRFDFDY KTFHRIKLND KVTFPYVLNL NSFISSTTSQ
ESPGGEEDIG LGIKCDDSST TDSGTLDDDC APCDNSLSNS NHSASHDQDD DEGIDMSNGP
STSSCITHNH ENEKNRSAYM LGKGPYTYEL FSIMIHSGSA SGGHYYAYIK DFRTQEWLCF
NDQSVTQITD DDIHKTYGGG PSRAYYSGAY SSSTNAYMLM YRQIDRARNA LPMQTEDFPQ
HIQELLKKMK ESEDNDRKNR EKMSIPRLKV YCHHPVEGKL MNVKLFVMPD ITWTEATEKA
YKKFGLENVV SLDQCRLVSY EHNTDLIECS YDDREHESVG NIWRFSRRFD LLLEIRRKDQ
KFETYLPGGV ATKVFVIDVT REEVIDGPID IRGLLSQSVK EYKQTVGKII SMDPKQMKVI
LRKFPEIRPV ENDDSDLQTE GFYNANKVFI STMYDIDNGK PFQESTVHRI IENFRHVISL
HIQLPDTSKE TLEELNIPLL DDKYEEKEKS VTSGPLKLFN ESDWDVNLKC NETLKGARTN
EDATIRNISP QLGEAEEWNT PEQSNSEDSS LSDSDKTLVG DVPEGVDIAP LSHDCGSISW
DSRAISNRYD CNIGVRRNYK ISKRFEIENW DIDDDSDYYF RATQYTDSTQ QNLLKVLVDK
RMRLSTLKKD LEPFVGVPVE YFKIFRLSNS GESECNCLME QLSSYEDGER LNVKLGRALR
NGEFKVKLYQ LLIDSTEPYK FLCEWIVSRD MTVGHAKKEI LAEIKRKYDI DIPYEKCRLR
KKYYKTASKV FLNEQKFEDL QFHSQFEMIV QELSDKEIVT DTNQIVLFVR RWLPAKLQLG
QFQEIVMDNR TVEELKKKLS SISDIPEEHI DIAKGKGSFP CDNSVLRIQN EHDWNEHHDS
LFFYNFEDGA VFLYRDNREK PKQLNADEVM EIAFKENSRL TPLSTTSSYS PRRERALKIY
LDTE
//
