ID A0A2K1JDC7_PHYPA Unreviewed; 1107 AA.
AC A0A2K1JDC7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PHYPA_019801 {ECO:0000313|EMBL:PNR39523.1};
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:PNR39523.1};
RN [1] {ECO:0000313|EMBL:PNR39523.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c15_15710V3.1,
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:PNR39523.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c15_15710V3.1,
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:Pp3c15_15710V3.1}
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; ABEU02000015; PNR39523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1JDC7; -.
DR STRING; 3218.A0A2K1JDC7; -.
DR PaxDb; 3218-PP1S104_2V6-1; -.
DR EnsemblPlants; Pp3c15_15710V3.1; Pp3c15_15710V3.1; Pp3c15_15710.
DR EnsemblPlants; Pp3c15_15710V3.3; Pp3c15_15710V3.3; Pp3c15_15710.
DR Gramene; Pp3c15_15710V3.1; Pp3c15_15710V3.1; Pp3c15_15710.
DR Gramene; Pp3c15_15710V3.3; Pp3c15_15710V3.3; Pp3c15_15710.
DR InParanoid; A0A2K1JDC7; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000006727; Chromosome 15.
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 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 44..169
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 189..513
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1087..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1107 AA; 129429 MW; D550BC83FB6E830F CRC64;
MAPPLDEDEN MVVPPQDLND GIEPMEGHGE SVATVENQPV DDHIGKFTWT LTNFGKLSVR
KHYSDPFVVG GYKWRVLLFP RGNNVDQLSI YLDVADSNQL PSGWTRFAHF NLAVLNQYEP
KMSVRKDTQH QFNARESDWG FTSFMPLHEL YDLSKGFLVN DTLVIEADVN APKMVDYWSH
DSKKETGFVG LKNQGATCYM NSLLQTLYHI PYFRKAVYHM PTTENDAPSS SIPLALQSLF
YKMQYSDTCV ATKDLTKSFG WDTYESFMQH DVQELNRVLC EKLENKMKGT AVEGTIQNLF
EGHHMNYIEC INVDFKSTRK ESYYDLQLDV KGCKNIYDSF DKYVEIEKME GENKYQADQF
GLQDAKKGVL FIDFPPVLQL QLKRFEYDYM RDSMVKVNDR YEFPLQLDLD KYDGKYLSPD
ADRSVRNLYS LHSVLVHSGG VQGGHYYAFI RPTLTNQWYK FDDEHVTKEE TKRALEDQYG
GEEELPAQNP AYNQPAFKFT KYSNAYMLVY IRDSDKDKVI CNVDEKDIAE HLQIRLKKEQ
GEKERKRKDK AEAHLYTVLK IARDEDLSNQ IGKQQFFDLV DHDSVKSYRI NQEVPFKQFK
EDVAKEIGIP ASCQRYWLWA RRQNHTYRPN KPLTEQEEME TVGKLKDASN KTHNAELRLW
LEVNYQEGIP APVPERTKED VLLFFKLYSP EREELRFVGR LFVKANGRPV DILEKLNQMA
GFAANEEIRL YEEIKFDPTV MCEHIDKKST FRGSQLENGD IICYQKARTK EEEAKFNYPD
VPSFLEYVCN RQIVHFRRLE KPKEDEFCLE LSKQHTYDDV VEKVAKKLGL EDPSKLRLTS
HNCYSQQPKP QPIKYRGVER LSDMLGHYNQ ISDILYFETL DLPLPELQGL KTLKITFHNS
KTEEVSTHNV RLPKQSTVGD VINELKTKVE LSSPKAELRI LEVFYHKIYK VFPLNEKIEN
INDQYWKLRA EEIPDEEKEL GPQERVIHVY HFLRDAAQNQ MQVENFGEPF FLKVKESETL
ASIKARIQNK LQIPDDEFSK YKFAFLSLGR PDYLRDDDVV ASRFQKKDSY GAWEYYLGLE
HIDSAPKRAH QTNQGRHSFE KPVKIYN
//
