ID A0A2K1JHL2_PHYPA Unreviewed; 437 AA.
AC A0A2K1JHL2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Amidohydrolase-related domain-containing protein {ECO:0000259|Pfam:PF01979};
GN ORFNames=PHYPA_018446 {ECO:0000313|EMBL:PNR41043.1};
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:PNR41043.1};
RN [1] {ECO:0000313|EMBL:PNR41043.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c14_13050V3.1,
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:PNR41043.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c14_13050V3.1,
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:Pp3c14_13050V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family.
CC {ECO:0000256|ARBA:ARBA00008829}.
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DR EMBL; ABEU02000014; PNR41043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1JHL2; -.
DR PaxDb; 3218-PP1S36_138V6-1; -.
DR EnsemblPlants; Pp3c14_13050V3.1; Pp3c14_13050V3.1; Pp3c14_13050.
DR EnsemblPlants; Pp3c14_13050V3.2; Pp3c14_13050V3.2; Pp3c14_13050.
DR Gramene; Pp3c14_13050V3.1; Pp3c14_13050V3.1; Pp3c14_13050.
DR Gramene; Pp3c14_13050V3.2; Pp3c14_13050V3.2; Pp3c14_13050.
DR InParanoid; A0A2K1JHL2; -.
DR OMA; HVHICGG; -.
DR OrthoDB; 5485094at2759; -.
DR Proteomes; UP000006727; Chromosome 14.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; IEA:InterPro.
DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IBA:GO_Central.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR010229; Pept_M38_dipep.
DR NCBIfam; TIGR01975; isoAsp_dipep; 1.
DR PANTHER; PTHR11647:SF97; AMIDOHYDROLASE-RELATED DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF001238; IadA; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..437
FT /note="Amidohydrolase-related domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033310782"
FT DOMAIN 92..414
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 437 AA; 46612 MW; 13DCDAD2EBBBCCD8 CRC64;
MEFLYSVTIF LLGLLCVPSV AHSAVNTCRD FSNGGEFPML LITNGQLYAP SPRGRAMILT
GGGSIISILP EDYPLGNLTG LPVRVVDAAG GFVVPGLIDI HAHVTGGGGE MGPASRTPEA
TVEELVASGI TTVVGILGTD CVSRSLENLR VKVAALQRQG ITAYMWSGCY RVPTPTLTGS
LIRDLQLIDE VIGAGEIAIS DHRSSWPTTQ ELLGLVTDAR VGGMLSGKAG IVHFHTGSAD
SLLQPLWDVV NASRGAIPLM HMIPTHVSNR GPALLKAAEE WVIKGGHVDF TSDQEDERVS
YDALMDWNKR IGNIALQRVS LSSDAFGSLP KFNSEGELVD YQVASPKANL NTIRRLVQKG
KWALEDALQF STTNPASFLT LELKGKLEAG ADADIVILSP EGLEVQNVIA RGKLLKTPSA
TCGRFEMTID LATNKVF
//
