ID U9SI45_RHIID Unreviewed; 1363 AA.
AC U9SI45;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERZ94751.1};
GN ORFNames=GLOINDRAFT_14308 {ECO:0000313|EMBL:ERZ94751.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:ERZ94751.1};
RN [1] {ECO:0000313|EMBL:ERZ94751.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM 197198 {ECO:0000313|EMBL:ERZ94751.1};
RG DOE Joint Genome Institute;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei-dit-Frey N., Gianinazzi-Pearson V.,
RA Gilbert B., Handa Y., Hijri M., Kaul R., Kawaguchi M., Krajinski F.,
RA Lammers P., Lapierre D., Masclaux F.G., Murat C., Morin E., Ndikumana S.,
RA Pagni M., Petitpierre D., Requena N., Rosikiewicz P., Riley R., Saito K.,
RA San Clemente H., Shapiro H., van Tuinen D., Becard G., Bonfante P.,
RA Paszkowski U., Shachar-Hill Y., Young J.P., Sanders I.R., Henrissat B.,
RA Rensing S.A., Grigoriev I.V., Corradi N., Roux C., Martin F.;
RT "The genome of an arbuscular mycorrhizal fungus provides insights into the
RT evolution of the oldest plant symbiosis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the YSP2 family.
CC {ECO:0000256|ARBA:ARBA00006582}.
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DR EMBL; KI301773; ERZ94751.1; -; Genomic_DNA.
DR TCDB; 9.B.198.1.4; the membrane-anchored lipid-binding protein (lam) family.
DR eggNOG; ENOG502QU87; Eukaryota.
DR HOGENOM; CLU_256846_0_0_1; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR031968; VASt.
DR PANTHER; PTHR23319:SF4; AT22714P-RELATED; 1.
DR PANTHER; PTHR23319; UNCHARACTERIZED; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF16016; VASt; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51778; VAST; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 90..191
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 635..801
FT /note="VASt"
FT /evidence="ECO:0000259|PROSITE:PS51778"
FT REGION 194..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..829
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1363 AA; 154937 MW; 0243DF491F96FD90 CRC64;
MHEASLIVHK GSENQLERLK GWLSENKKTC ESQNPLLQDL RKKLEEEAIN SNKPRRNLTK
YTDGGMTIHP NSDALQITRP PSPASMSNET PAKQGYLFMR TNGKNTWVRK YFYLKDGIFW
WTSVGHGKNR SVIEESERIG VLLCEVRMDT FHDRRFCFEV FYGAKQTTYI LQAETETELK
DWISAFENAK RHAFRSSNDS SSSTASVNPN KETEDEQHVS ITNEGDHNTN KPSSSNSAEG
YKIDGNSTSD LKITPSLVSP PPPLETKRNN SNLLTKKRAT SVSNLPNSKP QLAHHNYSNV
SSKGSMTPPT NNNAVTTSSL TTQSSSNEKS STSANQQNFW GTLNWAMPAV NLIMNTGNAQ
EDEEADGDGT ISKRNGSGPV GSGVDGSIVE YPHNLLLHNV QLHILFSCAT EAEYALDIFN
CAWYKDNMLF KGRAYITQDK LYFYSTVMSV INMFWISWRD IKSIVYKTTD TQQIVEFIDN
TNNQNYIIKT YLDTKGVFYE KTHTVWRLST GEKPVSLQHI FDAVWKLESG PKNEEKKDTV
SEKNTEQKDE NSTIDEKPLE KTEVKDQKSG DLDDDHKDLI AHDRISVNDA HEGDNKIPNT
PRTPSMIIIP SPEDDLPSNI PSPKDPIECQ CPDHPEKIEV EHEFPVSAKK LFDMMFDEKS
TIWSRLHKKK GNTLLHSGPW VMDNGERKRE FKFIIPVNNP MAKVKESNCI ETQICKKRDD
YLVLSQTNAL DIPYNDSFIP MIKFCITYIS KTSCKLNCYI GIKWLKSPMV KPLIRKATMA
GLSETVTDIM SLVNADIAQR KLLDPSSPRS HPASSLRRRS HSHRHHKPRT KLISGEELQT
AGTSANKVSG GPPNEQKRSK KANLLTMENL IGLLDKSISA FIEIVTNLSS IRIVGIILTL
SLLFNIYLLM GTGYNAPSII ATGNFRTNAT PPAVYIRDIE EYVLNTSSKA LKGVDPTSYK
QFLSTRIARP PYPWLLHFHR RMSDEISFAR KKVAILRYDL LLTFRLINSI DRRLSESEYV
NWLLDERAKC NKARWMLLKD DSLSEEIKVN ERDDSELNSS YDNEKHGFNN RYKSEYKSII
KYCSDVKKQL DYHMSLKVLI LGAGYGTRLQ RDLLNDTSRK YSHLLGISKA LLPLGDKDAL
ITHWIDTLME SNIDIKTSLY IVTNSTAYSS FISWAETHNI PTNNIINDGT TSNENRLGAV
EDIYFTIKKF SSSLQNSNLL IIGGDTLFLK DFNFKKLYEK FNLINSNDDD DEACLVTTYK
VNDDVVSKFG ILELNENNQL VLVLFLHNKS LELLKEFLEE SKNNPNHTLE DRDASGKFLA
WVINNNKFKF FAENVQGRID VGGLQSYIDA NKYFDDQKDN KPY
//
