ID I2H9K8_TETBL Unreviewed; 1462 AA.
AC I2H9K8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=TBLA0J00600 {ECO:0000313|EMBL:CCH63060.1};
GN ORFNames=TBLA_0J00600 {ECO:0000313|EMBL:CCH63060.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH63060.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH63060.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE806325; CCH63060.1; -; Genomic_DNA.
DR RefSeq; XP_004182579.1; XM_004182531.1.
DR STRING; 1071380.I2H9K8; -.
DR GeneID; 14498243; -.
DR KEGG; tbl:TBLA_0J00600; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_7_1_1; -.
DR InParanoid; I2H9K8; -.
DR OMA; PELEYIN; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000002866; Chromosome 10.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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 Reference proteome {ECO:0000313|Proteomes:UP000002866}.
FT DOMAIN 105..205
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 414..1218
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1462 AA; 167452 MW; 6A79B1613919DDDD CRC64;
MDPEDNDSME NNNISTPLVM ENTPSTKNQP EQAEDDQPTE NNNNIPNDID HSINHNTYSD
NLIDDPVDVE LIDESTAKDN NNVNNSDRLD LNAATIYNNN VTNRSVLEEQ RQIVDDLLDE
FKKTAQEGSR VFIIPQTWYV NFLNADLAEN LDPINTKLIC KDFDNFIFKD YNRFPYVSIP
QSVFEKFFEW YGLAANSQPI EAFLIWDNEN NTLVTEFNRL SFRLHHLTLS NQSQGTTSNS
YHYHNMRERN NVVYFSASRF HTVKQLTARA LDVFLQTEKQ FDNDTTNLKV WVVSNNKNKP
RPDKAKNSNN STSIVDDDIA DIDEEAGNDD ASVSNSVSSV DDPILSTTYR INPRQFIEFG
SKIRLTREHF ETILKDCDFP LEDFVIEVKP KGKQHHWLSN YFKYNYLVPS TGTLGLVNLG
NTCYMNSALQ CLIHLPKFNE YFLLNGYQKE INLDNPIGYQ GNVANAFGKL IHKLFEERII
DNESEKSSFS INSFSPTNFK STVGYCNSMF SGYLQQDSQE FLAFILDGLH EDLNRILKKP
FVEKPSLPEN SNYKDYKVIK KLADDTWEAH LKRNDSIVTD LFVGMYKSTL QCPDCHNVSV
TFDPYNDLTL PLPVETIWNK VIKIFPSNSP PCSLEVELEK TSTYNDLKEY ISRNTGIAAS
DLFGFEIFSN TFYSNYEAPG SNGQFLPLQE LIADSDDVIF YEIPDRENNI VIPILNMKID
KGFRSPRLFG VPFFITLTNE EASNPGFVRY IIEKYYTMLS GGFIEFPLFS SFDGDTNISQ
LPELSKKYPD IDFTLLEDFL KYSNPDESSK VNQYFDIRIS KGLNNVTTMK SNTGLFDNSY
VWTPSSSQQY GNAKDIKEFL HPVIRDIYDY ASLFQSENLS DEPHDIELPE FNTDFNQLVN
NSNNVINNNV ANDIPSKNSH TPSIHSSEQP DLQLDSLLAD LTENIQTNVS ELDKNFKISN
NEISTNNTNP TTLDNINIDS SVPNDLQINM EDIDIDNALD IPERVDSTEN YSKQILFNHD
VILCQWDDSR INTVFYDEQR FTNWEKPAVL KNTELEKKRE EQIFEKEKTI LLDDCLRLFS
KPEILGLQDS WYCPTCKDHR QATKQIELWN TPDILLIHLK RFENQRSFSD KIDAVVNFPI
TDLDLTPHIV CTDQEKSNIY DLIAVDNHYG GLGGGHYTAY VKNFVDQKWY YFDDSRVSLA
DPQRSISGSA YLLFYVRRSS ENPIKHQTLD KILEESRNKY SEELEELRAK QDLLYETNRT
DTESESESES ELETNSDSDS RTDSDDLQTD ASPEEKNKLL EEKGLKEINT ISDDLQGDYI
ELANDSDTGE KMNSNNSDMD VDTDDAPIEK TSDNLEDNPQ NSHDFSVNPT RSENYCHESL
EVGQTTKLED TDRSEDNTGR RKLRLLNRNY GNCIDSTSSS NGSNSDHELL ANDASSVTGS
ISGQLKKDEP IIAKSPESGE EF
//
