ID S7MGE2_MYOBR Unreviewed; 1609 AA.
AC S7MGE2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=D623_10031039 {ECO:0000313|EMBL:EPQ02916.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ02916.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(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};
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DR EMBL; KE161298; EPQ02916.1; -; Genomic_DNA.
DR RefSeq; XP_005858612.1; XM_005858550.2.
DR MEROPS; C19.044; -.
DR GeneID; 102250276; -.
DR KEGG; myb:102250276; -.
DR CTD; 84669; -.
DR eggNOG; KOG0044; Eukaryota.
DR eggNOG; KOG1870; Eukaryota.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 3.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF76; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 32; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR PRINTS; PR00450; RECOVERIN.
DR SMART; SM00695; DUSP; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000313|EMBL:EPQ02916.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT DOMAIN 228..263
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 264..299
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 369..586
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 735..1572
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1323..1432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1609 AA; 182047 MW; 33EA08998EFB4C6E CRC64;
MGAKESRIGF LSYEEALRRV TDVELKRLKD AFKRTCGLSY YMGQHCFIKE VLGDGVPPKV
AEVIYCSFGG TSKGLHFNNL IVGLVLLTRG KDEEKAKYIF SLFASESGSY VTREEMERML
HVVDGKVPDT LRKCFSEGEK VNYEKFRNWL LLNKEAFTFS RWLLSGGVYV TLTDDSDTPT
FYQTLAGVTH LEESDIIDLE KRYWLLKAQS RTGRFDLETF GPLVSPPIRP SLSEGLFNAF
DENRDNHIDF KEISCGLSAC CRGPLAERQK FCFKVFDVDR DGVLSRVELR DMVVALLEVW
KDNRTDDIPE LHTDLSDIVE GILSAHDTTK MGHLTLEDYQ IWSVKNVLAN EFLNLLFQVC
HIVLGLRPAT PEEEGQIIRG WLERESRYGL QPGHNWFIIS MQWWQQWKDY VKYDASPVVI
EPSSVLNGGK YSFGIAVHSI EQSEDRIGGG SLSYVNTTEE KFSDNISTAS EASETAGSGF
LYSATPGADM CFARQHNILD SNNQCFLGAN GNILLHLNPQ KPGAIDNQPL VTQEPVKATS
LTLEGGRLKR TPQLIHGRDY EMVPEPVWRA LYHWYGANLA LPRPVIKNSK TEIPELELFP
RYLLFLRQQP ATRTQQSNIW VNMGNVPSPN APLKRVLAYT GCFSRMQTIK EIHEYLSQRL
RIKEEDMRLW LYNSENYLTL LDDEDHRLEY LKIQDEQHLV IEVRNKDMSW PEEMSFIANS
SKIDRHKVPT EKGATGLSNL GNTCFMNSSI QCVSNTQPLT QYFISGRHLY ELNRTNPIGM
KGHMAKCYGD LVQELWSGTQ KNIAPLKLRW TIAKYAPRFN GFQQQDSQEL LAFLLDGLHE
DLNRVHEKPY VELKDSNGRP DWEVAAEAWD NHLRRNRSIV VDLFHGQLRS QVKCKTCGHI
SVRFDPFNFL SLPLPMDSYM HLEITVIKLD GTTPVRYGLR LNMDEKYTGL KKQLSDLCGL
KSEQILLAEV HGSNIKNFPQ DNQKVRLSVS GYLCAFEIPI PGSPVSASSP ILTDISSSPS
TNGMLTLTTN GDLPRPIFIP NGMPNTVVPC GTEKSFTNGM VNGHMPSLPD NPFTGYIIAV
HRKMMRTELY FLSSQKNRPS LFGMPLIVPC TVHTRKKDLY DSVWIQVSRL ASPLPPQEAS
NHAQDCDDSM GYQYPFTLRV VQKDGNSCAW CPWYRFCRGC KIDCGEDKAF IGNAYIAVDW
DPTALHLRYQ TSQERVVDEH ESVEQSRRAQ AEPINLDNCL RAFTSEEELG ENEMYYCSKC
KTHCLATKKL DLWRLPPVLI IHLKRFQFVN GRWIKSQKIV KFPRESFDPS AFLVPRNPAL
CQQKPLTPQG DDFCETRVPT GEVKKMDAQN SAGEEDMRLS KSPSSLSANI ISSPKGSPSS
SRKGGASCPS SKNSSPNSSP RTLGRSKGRL RLPQIGSKNK LTSSKENLDA SKENGTVHVC
ELADALSQGH MLGGSQPELV TPQDHEVALA NGFLYEHEAY GSVCGNGYSN GQLENHSEED
STDDQRRDIR VNPIYNLYAI SCHSGILGGG HYVTYAKNPN SKWYCYNDSS CKELHPDEID
TDSAYILFYE QKGIDYAQFL PKVDGKKMAD TSSMDEDFES DYKKYCVLQ
//
