ID A9S238_PHYPA Unreviewed; 1115 AA.
AC A9S238;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PHYPA_010082 {ECO:0000313|EMBL:PNR50896.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR50896.1};
RN [1] {ECO:0000313|EMBL:PNR50896.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c7_7420V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR50896.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c7_7420V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c7_7420V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) 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};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; ABEU02000007; PNR50896.1; -; Genomic_DNA.
DR RefSeq; XP_001760452.1; XM_001760400.1.
DR AlphaFoldDB; A9S238; -.
DR STRING; 3218.A9S238; -.
DR PaxDb; 3218-PP1S42_181V6-1; -.
DR EnsemblPlants; Pp3c7_7420V3.1; Pp3c7_7420V3.1; Pp3c7_7420.
DR EnsemblPlants; Pp3c7_7420V3.2; Pp3c7_7420V3.2; Pp3c7_7420.
DR EnsemblPlants; Pp3c7_7420V3.4; Pp3c7_7420V3.4; Pp3c7_7420.
DR Gramene; Pp3c7_7420V3.1; Pp3c7_7420V3.1; Pp3c7_7420.
DR Gramene; Pp3c7_7420V3.2; Pp3c7_7420V3.2; Pp3c7_7420.
DR Gramene; Pp3c7_7420V3.4; Pp3c7_7420V3.4; Pp3c7_7420.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003532_0_1_1; -.
DR InParanoid; A9S238; -.
DR OMA; HTAHHRF; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000006727; Chromosome 7.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR CDD; cd00121; MATH; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 50..175
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 195..519
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1091..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 528..560
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1115 AA; 130359 MW; F1F768F1365072E2 CRC64;
MTVIAAPPEE DDDMLVPPQD FNDVIEPMEV VGQGEGVVTV ENQLVDDPQT GKFTWPIENL
SKINLRKHYS ETFTVGGYKW RVLLFPKGNN VDHLSIYLDV ADSAQLPYGW SRFAHFTLAV
VNQIDPKLTV KKDTQHQFNV RESDWGFTSF MPLHDLNDPS RGFVVNDTLI VEADVNVRKV
VDYWAYDSKK ETGFVGLKNQ GATCYMNSLL QTLYHLPYFR KAVYHMPTTE NDVPSNSIPL
ALQSLFYKIQ YSDTSVATKD LTKSFGWDTY DSFMQHDVQE LNRVLCEKLE DKMKGTAVEG
TIQQLFEGHH MNYIECINVD YKSTRKESFY DLQLDVKGCK DVYESFDKYV EVERLEGENK
YHAEQFGLQD AKKGVLFIDF PPVLQLQLKR FEYDFMRDTM VKINDRYEFP LQLDLDRENG
KYLSPDADRS VRNLYTLHSV LVHSGGVHGG HYYAFIRPTL SDQWFKFDDE RVTKEELKRA
LEEQYGGDEE LPQTNPCFNN TPFKFTKYSN AYMLVYIREA DKDKVVCNVD EKDIAEHLQI
RLKKEQEEKE RKRKEKAEAH LYTIIKVGRD EDLQNQIGKD IHFDLVDHEK VRSFRIQKQT
PFTQFKEEIA KQLGVPVECQ RFWLWAKRQN HTYRPNRPLT DQEEAQTVGH LKEASNKAHN
AELKLFLEVQ RLPGADSVPI PPPIKTKEDV LLFFKLYNPE KEELRYVGRS YVKASGRPAD
ILERLNEMAG FPPNEEIQLY EEIKFEPNVM CEHIDKKSTF RASQLEDGDI ICYQRALTRG
EEDVCRYPDV PSFLEYVRNR QNVHFRRLEK PKDDEFCLEL SKQHTYDDVV ERVAEKIGLE
DASKIRLTSH NCYSQQPKPQ PIKYRGVERL SDMLVHYNQT SDILYFETLD LPLPELQGLK
TLKVAFHNAK TEELSVHNIR LPKQSTVGDV VNELKGKVEL SSPRAELRIL EVFYHKIYKI
FPLNEKIENI NDQYWTLRAE EVPDEEKELG PQDRLIHVYH FTRDASQNHM VQNFGEPFFL
VVRESETLVE VKGRIQKKLL ISDEEFSKWK FAFLSLGRPE YLQDGDVVAA RFQKRDTYGA
WEHYLGLEHT DSAPKRSHTT NQNRHNFEKP VKIYN
//
