ID L8WPE2_THACA Unreviewed; 1071 AA.
AC L8WPE2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Phosphatidylglycerol/phosphatidylinositol transfer protein {ECO:0000256|ARBA:ARBA00016056};
GN ORFNames=AG1IA_06116 {ECO:0000313|EMBL:ELU39835.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU39835.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU39835.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELU39835.1}.
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DR EMBL; AFRT01001600; ELU39835.1; -; Genomic_DNA.
DR AlphaFoldDB; L8WPE2; -.
DR STRING; 983506.L8WPE2; -.
DR HOGENOM; CLU_287604_0_0_1; -.
DR Proteomes; UP000011668; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd01908; YafJ; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR006616; DM9_repeat.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR003172; ML_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR43187; GLUTAMINE AMIDOTRANSFERASE DUG3-RELATED; 1.
DR PANTHER; PTHR43187:SF1; GLUTAMINE AMIDOTRANSFERASE DUG3-RELATED; 1.
DR Pfam; PF11901; DM9; 1.
DR Pfam; PF02221; E1_DerP2_DerF2; 1.
DR Pfam; PF13522; GATase_6; 1.
DR SMART; SM00696; DM9; 1.
DR SMART; SM00737; ML; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000011668}.
FT DOMAIN 216..819
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 50..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..147
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 117811 MW; 014F4BB4727EDFFB CRC64;
MVRKWIPDTQ FNRGAVVRFN NLFYRSSVSH TSGPGREPTE APQLWAALNN ESAPPAAPDP
PQSYENPPPM YVHPESGAST TTVNSIPPPP PHVPGYGFYT YLPAGHHPTQ YHLPSGYRPL
YNAPQAPYLH APKPQHPIRP PDPDVKLPLP VTQAQSQSRS DRASPDYVLP MPFPFSRFIE
GPTHPAYRTL AHAMRALETN EAVLREEMKG EIDAVCCVGG FGLWAYRHGE PGEDVKRRVY
AELQSDDDTG REAWLKAARA RTKRYCEPGA IRPAIRWVLV EPHPEAENMT PAALERHALQ
HGSFPRIPDD ALQTGTEVSG TGLYSARAWH AGGVHLGKAG KHLQAGGASL SYGSIEHELS
SFEVLVGDVA SVRWIEGSQL ASQLAAGVIP VEGGREAHGG AILIAQAPYE GGWHPGKAAI
GEDHACVGFG GGEFWAINDL WLQLSLPSSR QYNIQSRLST EAHPFARRIH GRLDKQMGYR
KQLLDDILNR PENSIVKQVK EHYLPGLFPH KSAEEDKKQE AESAIRNADG TGVAFYNKTM
QDYGEAKCRM PQIYKTIIAP TNDVNFQSLC RNTSSRTVFA HVRMATSEVQ QFNSHPFAFG
RHIFMHNGSV ANFSSIRRDL CAKLSTRAYN NIKGSTDSEH LAALYMTHLG DDWTVQYGLE
NMKRALERAI ADIIALQRKL PDATTPLAAS SLNVCTTDGE ELLAFRFRNS EVEQPPSLYY
STSAGVTLNR KYPGHPNYFK WEDPGDAATG LVGPDELRPE AYGNHVIVAS EPTTKVWNFS
KPAHELTEFS RMRANGNGFP KTRRSWSIFP GERTGSSASV ISVDWPPRLL PSATTYLTTP
AHLHSRIMYF PKVALLAASL SPFAASALSF TRPDLVLNGE SPIFTQMPSD GVQIKSIEVS
PDPPKPGQDL TVTVIATADQ PIEGAYADVT VKLGLIKLLN KRFDICEEAR NANATIQCPV
QKGDHTVVQT VALPKEIPRG MLSPANQPDI ETNSDVQKIS PVSNLMLISC LATTCGRLAT
IFHPPERHNR PSATHASILT KLHKQDLVAI PSVHSTPGSV PTRLDHEIMR F
//
