ID A0A2K1J155_PHYPA Unreviewed; 1148 AA.
AC A0A2K1J155;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=CBM20 domain-containing protein {ECO:0000259|PROSITE:PS51166};
GN ORFNames=PHYPA_023156 {ECO:0000313|EMBL:PNR35257.1};
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:PNR35257.1};
RN [1] {ECO:0000313|EMBL:PNR35257.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004
RC {ECO:0000313|EnsemblPlants:PAC:32982499.CDS.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:PNR35257.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004
RC {ECO:0000313|EnsemblPlants:PAC:32982499.CDS.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:PAC:32982499.CDS.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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DR EMBL; ABEU02000018; PNR35257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1J155; -.
DR STRING; 3218.A0A2K1J155; -.
DR PaxDb; 3218-PP1S3_320V6-1; -.
DR EnsemblPlants; Pp3c18_14870V3.1; PAC:32982499.CDS.1; Pp3c18_14870.
DR EnsemblPlants; Pp3c18_14870V3.2; PAC:32982500.CDS.1; Pp3c18_14870.
DR EnsemblPlants; Pp3c18_14870V3.3; PAC:32982501.CDS.1; Pp3c18_14870.
DR EnsemblPlants; Pp3c18_14870V3.4; PAC:32982502.CDS.1; Pp3c18_14870.
DR EnsemblPlants; Pp3c18_14870V3.5; PAC:32982503.CDS.1; Pp3c18_14870.
DR Gramene; Pp3c18_14870V3.1; PAC:32982499.CDS.1; Pp3c18_14870.
DR Gramene; Pp3c18_14870V3.2; PAC:32982500.CDS.1; Pp3c18_14870.
DR Gramene; Pp3c18_14870V3.3; PAC:32982501.CDS.1; Pp3c18_14870.
DR Gramene; Pp3c18_14870V3.4; PAC:32982502.CDS.1; Pp3c18_14870.
DR Gramene; Pp3c18_14870V3.5; PAC:32982503.CDS.1; Pp3c18_14870.
DR InParanoid; A0A2K1J155; -.
DR OMA; WRLCEIS; -.
DR OrthoDB; 19923at2759; -.
DR Proteomes; UP000006727; Chromosome 18.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR CDD; cd05818; CBM20_water_dikinase; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034848; CBM20_water_dikinase.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR47453; PHOSPHOGLUCAN, WATER DIKINASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47453:SF1; PHOSPHOGLUCAN, WATER DIKINASE, CHLOROPLASTIC; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006727}.
FT DOMAIN 51..149
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 151..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 125501 MW; E2F039A73C01DF7B CRC64;
MAGSSAMQCG QLGQMGLRRI SFQGLRKAAV TQSKVKGRRV GAGNMRSVLS VRCGEKVKVR
VRLDHQVQFG ETHAILGSAK SIGAWQEKVP MTWTEAGWVV DLEGDSGETV EYKHIIVTHD
GGVIWEEGPN RTISLPDEGD FELVTHWGCT QEDPQFQGGR SPKSHGSDNG HAGKAEEQTE
GKAESSKVEE AVREMSTSFV KEWQGASVKD RKERSGKWDT TGLGGPTLQI VEGDKSASNW
WRKLDVVRDL LSGEAGKKDR LKALINAAVY LKWINTGQIV CYEDGQHYRP NKHAEISRRI
FVELERISGQ KDVDLKELLV IQKIHPCLPA FKAEFTASVP LTRIRDIAHR NDIPHDLKQE
IKHTIQNKLH RSAGPEDLVA TENMLARITR NPGQYNEAFV KEFQIFYAEL KDFFNAGGLT
EQLEGLRQSI DDEGQVILDH FLASKGKLDQ LNSSDTAKIT ESVLDTLHAL TCIRERLLEG
LVSGLRNDAS DAAIAMRQKW RLSELGLEDY SFVLLSRLIN AFESEGGASW LAEEAKSGRV
GKWTPALTSL AMAVQQLGLS GLQKEECVAI KNELLAWSAT SARTNDTKAW ALRLKATIDR
VRRVAENYTD TVLQLYPDFV EKLGNALGIP ENSVRTYTEA DIRASVVFQV AKLCSFLLKA
IRTTAGGDGF DVIMPGRARG TLLEVDRIVP GTLPTSATGP IILLVKQADG DEEVKAAGSN
VAGVILLHEL PHLSHLGVRA RQEKIVFVTC DDEERSANLR TLLNKPVEIV ASPESVHVEF
RDALSPQKQD KQESVSEPKS QQKDTITVTK QSVVVRSPPG TVLNLSEATT ENAGSKAAAC
GELAVLVEQA KKVSAAFLVP RGKVIPFGAM EDTLENSGSS SKFKTLLEKV ETASLEGGEL
DKVCNELQVL IAAQRPAQSI LDKLSADGFP KETRLIVRSS ANVEDLAGMS GAGLYESIPN
VRLSEPDVFG KAVAQVWASL YTRRAVLSRR VAGVPQKEAS MAVLVQELLS PELSFVLHTV
SPIDQDKNVV QAEIAVGLGE TLASGTRGTP WRLAANKFDG TVKTLAFANF SEQMMVKGGA
NVADGSVVKA VVDYSNQRLS VDTEYRQQIG QYLATVGFFL EKHFGVPQDV EGCVIGKDVY
IVQARPQP
//
