ID B8B3E4_ORYSI Unreviewed; 1325 AA.
AC B8B3E4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 13-SEP-2023, entry version 65.
DE RecName: Full=Major facilitator superfamily (MFS) profile domain-containing protein {ECO:0000259|PROSITE:PS50850};
GN ORFNames=OsI_23296 {ECO:0000313|EMBL:EEC80776.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000313|EMBL:EEC80776.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EEC80776.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|ARBA:ARBA00010755}.
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DR EMBL; CM000131; EEC80776.1; -; Genomic_DNA.
DR STRING; 39946.B8B3E4; -.
DR EnsemblPlants; BGIOSGA021082-TA; BGIOSGA021082-PA; BGIOSGA021082.
DR Gramene; BGIOSGA021082-TA; BGIOSGA021082-PA; BGIOSGA021082.
DR HOGENOM; CLU_259548_0_0_1; -.
DR Proteomes; UP000007015; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR CDD; cd17324; MFS_NepI_like; 1.
DR CDD; cd13579; PBP2_Bug_NagM; 1.
DR Gene3D; 3.40.190.150; Bordetella uptake gene, domain 1; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR HAMAP; MF_00006; Arg_succ_lyase; 1.
DR InterPro; IPR029419; Arg_succ_lyase_C.
DR InterPro; IPR009049; Argininosuccinate_lyase.
DR InterPro; IPR005064; BUG.
DR InterPro; IPR042100; Bug_dom1.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF03401; TctC; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007015};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 397..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 936..954
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..994
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1001..1021
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1027..1049
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1061..1082
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1088..1110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1139..1158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1178..1198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1205..1224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1230..1251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1263..1284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1290..1311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 932..1316
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT REGION 904..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1325 AA; 140407 MW; 9AC27D2F0B012FBB CRC64;
MSDLVKRYTS SVFFDKRLWQ ADIAGSLAHA EMLAAQGIIG AQDHAAIQRG MATITQEIES
GAFEWKLDLE DVHLNIEARL TQLVGDAGKR LHTGRSRNDQ VATDVRLWLR GEIDLIADLL
KELQVALVDV AEQNVDVILP GFTHLQVAQP VSFAHHMLAY VEMFARDAER MQDVRRRTNV
LPLGSAALAG TTYPLDRERV ARTLGMEGVC QNSLDAVSDR DFAIEFTAAA SLCMVHVSRL
SEELIIWMSQ NFGFIRIADR FTTGSSIMPQ KKNPDVPELA RGKTGRVEAG ITVNPQAMEQ
AAQKGYATAT DLADYLVKKG LPFRDAHETV AHAVKAATSH GVDLSELPLT VLQGFHPAIE
KDVFDALSLR GSLNARNTLG GTAPAQPLAM TLSRRRLLSH ASLAGAALAA GLPLAARAQA
GRTLRILVGF PPGGGSDAIA RLLADKLKDV LGVPVVVENR PGAGGQIAAQ VLKTSPLDGS
TVFLTHDHTI SILPQVVKHP GFDPAHDFIG VGGVATFVNA FAVSGGTPAR SFDEYVAWVK
SQGGKSAVGI PAPASTPEFL VKLLGERYRL DLVSAPYRGS APMIGDMLGN QIAAGVGSVP
DFLENHKAGK IRIVAVLGDR RQAALPDVPT FGELGLKGFE DLPYYGFYAP AGTPAKAVQQ
FSDALAKVLA RADVREQLVA MGLTRQSAAP AGAGVVGRQC GHERLFHQRL HRERDRVGEG
RAQHGGIEAP LQQCRGERHR IRFHQAQLHL GEGMAERPDA GRDQGIECRG AGKTQLQLAG
LAAGRPPGRL QCLGGLHRQG LHPFQEGPAG LRQLGAMGNT MEERGADLGF QVADLQAQRR
LPDAQPRCGP GEVAFLGHGE KVADVSQFHA AIYRTYGLMV CHILDRWSRA SYIDLRHLPQ
SMASSSAPPA SSSSIPPGSA PASDWVRRGT PEYRRAGLAM FLLGLASFSL IYSVQPLLPA
FASDFGVSPA ESSLALSLTT GWLAFAIVLA GAFSQALGRR GLMCASMALA ALLQIGAALA
PTWHGLLVAR ALEGLVLGGV PAVAMAWLAE EIEPAALART MGLYVGGTAF GGMVGRVGMG
LVTEFTSWRL ALGGLGLLCL VAAAGFLRLL PPSRRFERRP GINARFHLRA WAGHLRNPGL
LRIYAIGFLL TSVFVTVFNY ATFRVSGAPY HLGQTQASLI FLAFGFGIVS SSVAGALADR
FGRHRLLAAG FALMLAGVGL TLFAPLAAVV AGIALVTTGF FIGHAVASGS VGPQAVEAKG
HAASLYLLFY YLGSSVTGSV GGWFWQHGGW PAVAGLTGGI ALAGLGATVA LGRAARVRPA
AWAHG
//
