ID A0A1Q9CPU0_SYMMI Unreviewed; 2929 AA.
AC A0A1Q9CPU0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=phosphatidylinositol N-acetylglucosaminyltransferase {ECO:0000256|ARBA:ARBA00012420};
DE EC=2.4.1.198 {ECO:0000256|ARBA:ARBA00012420};
DE AltName: Full=GlcNAc-PI synthesis protein {ECO:0000256|ARBA:ARBA00032160};
GN Name=Piga {ECO:0000313|EMBL:OLP84944.1};
GN ORFNames=AK812_SmicGene34120 {ECO:0000313|EMBL:OLP84944.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP84944.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP84944.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP84944.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
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:OLP84944.1}.
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DR EMBL; LSRX01001005; OLP84944.1; -; Genomic_DNA.
DR OrthoDB; 24420at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03796; GT4_PIG-A-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR039507; PIG-A/GPI3.
DR InterPro; IPR013234; PIGA_GPI_anchor_biosynthesis.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45871; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL BIOSYNTHETIC PROTEIN; 1.
DR PANTHER; PTHR45871:SF1; PHOSPHATIDYLINOSITOL N-ACETYLGLUCOSAMINYLTRANSFERASE SUBUNIT A; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF08288; PIGA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 362..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 482..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 551..591
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 103..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2644..2672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2644..2663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2929 AA; 324095 MW; C43D2C8231F944B7 CRC64;
MNGLDKLKPL PSRKSSGCCE CSLPFHFGVL RGLEELGLHS CRCRRLKSFR LVVGWRSFAG
YLFWVGQGPP ERSGSHGGMA GRSQVAAVAR TISAVRTAFA WRHSSTGTHG RRTPSEADAK
KRPRRRRGEA LRFDLARPYT RQEKAEVRDE IAEALSTLPE RPPKDVQESI DPAELRLKSK
VALLCDLRPD AGPVEVAQVL RRTRDCYEAA EREAKEECGR GISLQFRRWA AQESGLAAVL
RRTLQLRRML APQALADGAC LALALLPATD SNAAEALLEA LAPHAVSDMS ASSFTRSASA
LLGGGVSAGP PSLSRPRENS GAAEETLLSR VSSRRQVDSQ SVQRRLRDEA VEQLMQRFTP
KIICLCFVGL FGIAVASFAL VIVFWRAFFA ALAYGSLPCD QPMLRYYMVF SILIGRISEQ
LSAKASRYMQ VRGMSTRSVW VSTTLTSLIP GWITMTWGYT LIQGSSTCRT TNPHLFFDTR
TYVYFQIAAS LAYLLLGIPL ILFAHRFLLA IRSLNSGEGV RGCAAMIKDL PKIPSDSPEL
QDPEDGSIME CSICLVSFSS LTVVRTPCKH YFCEPCLTKW CKAHVTCPLC KSLVADPGPL
SADSSEVAVR RDLPPVLGAA NAVGGLPGAS GLLCALLAEL AEMGPMLQEQ ELFEVLDVLG
SHVGEVGPAI VEDFVESLRY VWPLCGSRTL IKALLALGQE RDARKKERDA RKKAEAAAKA
AQQEKEMVAG TWWHRISDLQ SKKTNIQNDN IVRSTSLAEV WCPKKAKRAI PTSAASAASS
ANLKGISVSL LGGPPGQLKR AHLLPNSLNC ALVWDTIVKS MIRVPQQDSW TAIVGMLGEE
NIATLSLRNA SFNFLALDGE GDLLDSNPQI MILPVLSKQN VIDWAGEAYN AVFIAGTPDA
YKKAGSYECT PRATTQHVEQ AFQTFETVAS TLVALYSTDT FERMVTLGGK TYGKPDASMQ
AQCRVFQQSV QRNGLYVPCP GEDLRFPYIA FSENMPGPDV KQPWTPGSGH CAPHPLLLLA
RSLNSWANMR AGNDTKMRFV PACMPPLEAE FDEVEWDFFE TLHRFQMEDR LCRGSPPAQQ
ANALDVKTCR LILAELEARS EFIGRADREA LLLLLALHKS AFDRTAVALG LPHPLYDEAA
KKLLKELSKD AAAQISALPM ENLSRPVLAM AQLGSMSRRA LHSLDERLKS GRLLSLSPAA
FVSLAYATRL VRGPVPREEL RLPLCLAFGA LLHGMEPKQV ASCIESLKGY SYKAYRHVFE
AAYARLASAL ESQAAGLGDQ RPWAILTPAE AAAAIKSFPE LKFEDSRLLL RMLRALSPSS
AQSSPRRLAS PESDGGAAYP PTEPVLQLHQ PMGMLGRMGM VELVDILEAF GQQGLIGCGA
VADAIVARYG ANGGRLSRRN TARALWALAQ LGERETELVE LLVAELEGWE VQDPHGTDLR
PRPALVALWS LCALNLVPRA AASVDWLLTF LCRETAATHV LGIRSQALLL FASLDAVRLV
VPGVAARHLQ ALQASHSPVA EQVLLEVGRP LRSPQELLSL PGSPEPKLLQ SPEDQELLSL
ADSGAIEEGA TDTTDCGGRS LLDELAIRWE MARRKQESEG LSKAKQLLGS VLAALNTAQL
LRAAPHPLGR LAAETARGSG GFELRWPAGC YDVDWGHPFF RLGILVLSQP DFVLEASAGS
TWMTPRLRAS PRLRVQQLRE EGWRLVLLRA AAVDAWIVPF SEDPDLFSAK LQARVVRANA
LYPLEVRALK KRLRRSMRDE VPGSELREQI VQQVLQQLDF IFPDGLVSGA GSVGQQEVAS
SAVQLEQGKK DRQHSPSAAE ECVVVVTDLE IDRAKKFQHI SALCKEGTSY SDIEERDDRS
GGGLPPETDH LFQVPCILSL LEELLEASGR SPTFLALDLR SMEISRILPE LSSRGYEHFK
DLLEMRSLEH FVLHAAMAGP TRLCLTGQLR SRNGVADLEQ VLRRFASFDV FAVVPSQDCA
RACEVLAPLR AQVYVWRDVD TCGRLLHRYM RRPPPAGPAL AASLRDLVTH SQAKVREVSM
TKEGMDRSLN ICMVSDFFHP GLGGVEMHIY QLSECLIQRG HKVIVVTHFR GTRQGVRYMR
NGLKVYYLPF LPFHDNCTFP TFLSFFPLIR KVLIRERIDI VHGHQATSNL AHECVLHART
MGYHTVYTDH SLFGFADAAC IHVNKLLKFF LTNVEHCICV SHTNRENLVL RASLNPANVS
VIPNAVDTRR FTPDTSKRAP RPAVTVVVVS RLTYRKGVDL LVGAVPEICR RNRDVRWVIG
GSGPKRLLLE EMIERDNLHD RVELLGSVPH EDVRKVLVRG DIFLNTSLTE AFCIAIVEAA
ACGLMVVSTN VGGIPEVLPP HMTRLAAPCV DDIVQALEDA LGSLPLPEAA ATFHEEVRGM
YSWLDIAERT EKVYRKVVKL PRVCLRQRLL RFLRVGPVSG KLFLLLAALD TLLFWCLKWF
HPVEEVESAV DVPRFPGSGS PERFRVSYWR VARMRLDLRI AIFPKDVAVF GEENTIWAYA
IPDRQWIAMP DRFAMGPPRL MDAYFTTYRW MLDKRSWQHY DPRVRTACAR RGHLQVEPPT
ESGKLGEHRL RAFGKLWPCP EHSARGLAYP GQRQWQWSQS KDEGGTIFQG TIFQGTLSQG
IQGTFTAHSQ PRSSSSSSTL LRPAATGEDR YKTPAMPSTF KFPTNISKYE VDWSAIEVEQ
YPVQDDMKMF VQALASSAKF KISGGVLLEH NPSWDRGVEA TAETMRRYYY LVSSDLALKD
PPLPTKSERS LFWSHGTDVG SFWFMLRNRE MFPMNAHGVS QFGCNIFYAL GHEVCGGEED
EYNIARVLYN TSKSAKKLAS IIVGGKAWGS LRKVYGGSFE TARVATEEDQ VLKDSNAKAY
CVTRNRYSRY SFNYIAFEQL AQPPSTARGL INQYLRAANI KPPGRQTLF
//
