ID A0A225B310_9EURO Unreviewed; 1609 AA.
AC A0A225B310;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=UA08_02632 {ECO:0000313|EMBL:OKL62379.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL62379.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL62379.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL62379.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:OKL62379.1}.
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DR EMBL; LFMY01000003; OKL62379.1; -; Genomic_DNA.
DR RefSeq; XP_020122500.1; XM_020264696.1.
DR STRING; 1441469.A0A225B310; -.
DR GeneID; 31002387; -.
DR OrthoDB; 3573659at2759; -.
DR Proteomes; UP000214365; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR031101; Ctr9.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14027; RNA POLYMERASE-ASSOCIATED PROTEIN CTR9; 1.
DR PANTHER; PTHR14027:SF2; RNA POLYMERASE-ASSOCIATED PROTEIN CTR9 HOMOLOG; 1.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13174; TPR_6; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00563; PlsC; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000214365};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..263
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REPEAT 1210..1243
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1306..1333
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1429..1453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1502..1517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1565
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1609
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1609 AA; 182098 MW; FF70DF4B7E52A596 CRC64;
MSEIRHRAPT DPSGSSVLTE QTPLAESEKD AGLKHGLFMQ ILRSLLLATW FNGCCVCIVA
TQLIGSPLYF INKNYYYAYM AMTKQCFGIL VITITQWGSP TLVRVSGDAS VKGQMHITSD
GRLRTNFHDR LVFIANHQVY TDWLYLWWVS YTSRMHGHIF IILKESLKYI PLLGQGMMFY
GFIFMARKWE ADKPRLQHRL EKLKAQHSGP MSGSQGLDPM WLLIFPEGTN LSINTKNISN
KYGEKAGIAP LKHMILPRST GLFFCLQQLR GTVDWLYDCT IGYEGPPKGI YPDRYFTLRS
TYGQGRPPKS VNMYWRRWAV ADIPLDDQKE FEEWLLERWR EKDVLLEQFF ETGRFPTSLG
SSIDTHDIPA KQKAEASRGY IETEITLARW IEIAEIFAVL FQSCDHLDTH ITHAMAHFEN
GHANGFGDMA LNSETLPSAT RFSDIPSAID IPASTFDSEV EVSLEELPDD PTELCTLLEN
EKAAKNFWVI ISLAYAKQKQ LDHAVEILQK GLASVAHGAT KEKLGLLNWL CWLLMLKSRQ
SPRVAPDGNS SDVKTKDYYL QLATSTLNEA SRLNPAYTPL FLARGVLCLL RASLYPPRPV
RTGIPDNSER VETLRQALKC FEEASKASGG RNVMAHLGLA RAQYALGNYP DALLTYQTVL
TRMPGLTDPD PRIGIGCCLW QLGFKERARD AWERALSLNP TSKVANMLVG TYYLYGSSQR
PTNDPQFGEL YRISMTHTQS AIKLDRDYPM ACARFAGYKL TRKDYKTVEA LARKAIEQTD
VVSIASEGWY LLGRKAHYEG DASKASEYFN RSDQARGGGE SGFLPAKFGV VQMQVKSKDL
DGAKFRLEKI IQQTKSPECM ALLGALLAEE VFSAQASGSK DDKSADAAKA ISILEAVRSL
WKDPTKNISP DESVLIYLSR LYESSSPDKS MQCLSQLEDI QMEQIPDQDR PEENLQNGEL
KAALREYLPP QLLNNIGCFL YQSGKVAEAR DLFQSALNAC VKSEELEGEK ATDALITTVR
YNFARCLEAL DIPDEAKKVY ESLLERHSDY TEASARMTYI SLRQSPTDEG PKKMAKLYES
DSTNLEVRAL FGWYLSKSKK RVANLAEDHE QRHYKHTLQH FDKHDRYALT GMGNVHLLTA
RDMRRETDQD KEKRRKMYER AVEFFDKALQ LDPKNAYAAQ GIAIALVDDR KDYTGAVQIF
SKIRGAIKDA SVYINLGHAY AELKQFSRSI ECYETALSKD RARDAQILVC LGRVWWLKGK
HEKNLVAMKT ALDYANRALA VAPEQVHLEF NVAFVQNQIA LLVNSLPEMQ RTLQDLQEAA
EGLEKAIETF TRIAQVKNPP YPRESLEQRA NMGRNTISKQ LERSLQNQKE YEDKNALKLQ
QARAARDAEL KRREEEVRKA QELEMERKRQ LAEQRQRIVE ETQRLAAQRA EEQRAREAAE
LTTDSETGER QKRKKKSSSK RKKHRDDDDG VVSDGRSISV ARSDDEGETP APKRRRRLER
RGGAKEKPGK YKSTEYVDSD EELDDGAAVA NPAVTSVEDD AAAGDDDLFG DDNDIVEEDK
EEEEEEATVR EKGGRSRGGK RIVDDSDDED EPAVTKSGED EEMQDVDDE
//
