ID D7M4R8_ARALL Unreviewed; 1193 AA.
AC D7M4R8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 08-NOV-2023, entry version 54.
DE RecName: Full=CBM20 domain-containing protein {ECO:0000259|PROSITE:PS51166};
GN ORFNames=ARALYDRAFT_489476 {ECO:0000313|EMBL:EFH48471.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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DR EMBL; GL348718; EFH48471.1; -; Genomic_DNA.
DR RefSeq; XP_002872212.1; XM_002872166.1.
DR AlphaFoldDB; D7M4R8; -.
DR STRING; 81972.D7M4R8; -.
DR EnsemblPlants; fgenesh2_kg.6__2610__AT5G26570.1; fgenesh2_kg.6__2610__AT5G26570.1; fgenesh2_kg.6__2610__AT5G26570.1.
DR Gramene; fgenesh2_kg.6__2610__AT5G26570.1; fgenesh2_kg.6__2610__AT5G26570.1; fgenesh2_kg.6__2610__AT5G26570.1.
DR eggNOG; ENOG502QS3J; Eukaryota.
DR HOGENOM; CLU_012115_0_0_1; -.
DR OrthoDB; 19923at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0019200; F:carbohydrate kinase activity; IEA:EnsemblPlants.
DR GO; GO:0051752; F:phosphoglucan, water dikinase activity; IEA:EnsemblPlants.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005982; P:starch metabolic process; IEA:EnsemblPlants.
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:UP000008694}.
FT DOMAIN 65..165
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 807..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 130963 MW; 655D2447FB3E8861 CRC64;
MESIGSHCCS SPFTFITRNT SSLPKLVNFT RRVNLSHQSH RLRNSSSRLT CTATSSSTIE
EQRKKKDGSG TKVKLNVRLD YQVKFGEHVA MFGSAKEIGS WKKKSPLNWT ENGWVCELEL
DGGQVLEYKF VIVKDDGSLS WESGDNRVLK VPNSGNFSVV CHWDATRETL DLPQEVGIDD
GGGGDERDNH DVGDERVMGS ENGAQLQKST LGGQWQGKDA SFMRSNDHGN REVGRNWDTT
GLEGTALKMV EGDRNSKNWW RKLEMVREVI VGSVEKEERL KALIYSSIYL KWINTGQIPC
FEDGGHHRPN RHAEISRLIF RELEQICSKK DATAEEVLVA RKIHPCLPSF KAEFTAAVPL
TRIRDIAHRN DIPHDLKQEI KHTIQNKLHR NAGPEDLIAT EAMLQRITET PGKYSGDFVE
QFKIFHNELK DFFNAGSLTE QLDSMKISMD DRGLSALNLF FECKKRLDAS GESSNVLELI
KTMHSLASLR ETIIKELNSG LRNDAPDTAI AMRQKWRLCE IGLEDYFFVL LSRFLNALET
MGGADQLAKD VGSRNVSSWN DPLDALVLGV HQVGLSGWKQ EECLAIGNEL LAWRERDLLE
KEGEEDGKKI WAMRLKATLD RARRLTAEYS DLLLQIFPPN VEILGKALGI PENSVKTYTE
AEIRAGIIFQ ISKLCTVLLK AVRNSLGSEG WDVVVPGSTS GTLVQVESIV PGSLPSTGGG
PIILLVNKAD GDEEVSAANG NIAGVMLLQE LPHLSHLGVR ARQEKIVFVT CDDDDKVADI
RRLVGKFVRL EASPSYVNLI LSTEGKSRTS KSSANKKTDK NSLSKKKTDK KSLSTDDEES
KPGSSSSSSL LYSSKDIPSG GIIALADADV PTSGSKSAAC GLLSSLAEAS SKVHSEHGVP
ASFKVPTGVV IPFGSMELAL KQSNSEEKFA SLLEKLETAR PEGGELDDIC DQIHEVMKTL
QVPKETINSI SKAFPKDARL IVRSSANVED LAGMSAAGLY ESIPNVSPSD PLVFSNSVCQ
VWASLYTRRA VLSRRAAGIS QREASMAVLV QEMLSPDLSF VLHTVSPADP DSNLVEAEIA
PGLGETLASG TRGTPWRLAS GKLDGIVQTL AFANFSEELL VSGTGPADGK YVRLTVDYSK
KRLTVDSVFR QQLGQRLGSV GFFLERNFGC AQDVEGCLVG EDVYIVQSRP QPL
//
