ID Q0CA38_ASPTN Unreviewed; 1635 AA.
AC Q0CA38;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=ATEG_09446 {ECO:0000313|EMBL:EAU30583.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU30583.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CH476607; EAU30583.1; -; Genomic_DNA.
DR RefSeq; XP_001218068.1; XM_001218067.1.
DR STRING; 341663.Q0CA38; -.
DR EnsemblFungi; EAU30583; EAU30583; ATEG_09446.
DR GeneID; 4353860; -.
DR VEuPathDB; FungiDB:ATEG_09446; -.
DR eggNOG; KOG1505; Eukaryota.
DR eggNOG; KOG2002; Eukaryota.
DR HOGENOM; CLU_003008_1_0_1; -.
DR OMA; CFLAGEF; -.
DR OrthoDB; 3573659at2759; -.
DR Proteomes; UP000007963; 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; PF13174; TPR_6; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00563; PlsC; 1.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963};
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 43..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 133..265
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REPEAT 1257..1290
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1635
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1635 AA; 184740 MW; 71D15573160CDB71 CRC64;
MADNDARQRK PGASATQLMG ADGHPGAHQG EEPRLKHGIA MQLLRSLILA TWFNCCCVII
LATQLVGSPL YFVNKSYYYN YMAYTKQSFG LVITALTQWG CPTYVRVSGD KSVRGQVHLS
KDGRLKTQFP ERLVMIANHQ VYTDWIYLWW VAYTNSMHGR IFIILKESLK YIPIIGQGMM
FYGFIFMARK WLSDKPRLQH RLEKLKTRLS GSKSGSPEYD PMWLLIFPEG TNLSINTKRR
SDEYGTKQGF PPLKHEILPR STGLFFCLQQ LKGTVDWVYD CTVAYEGPPK GSYPDKYFTL
RSTYLQGRPP TSVNMYWRRF AVADIPLDDQ KDFDAWLRAR WTEKDQLLDE YFETGRFPTE
LTGTIETGEV TAEQKAAASA GYAEAHKPYG VLREAESHCG GADLGPEARR NKVSLASPSA
DSRLAAVATT RLSSRLSPGT SLFLVACLLS SLVILGIRAM ATLQNGYANG VNGDSLTTVN
SLANLRFSDI PSAIDIPAST LDSEVEVSLE GLPDDPTELC TLLENEKAAK NFWVIIALAY
AKQKQIDHAI DILNKGLASV AHGATKEKLG LLGWVCWLLM LKSRQAPRVA PEGELYTESK
TKDYYLQLAT STLNEASRLN PAFPPLFLAR GVLSLLRASL HPPRPVRPGT VDTSERVESL
RQALKCFDES SKAFGGRNVM AILGRARTQY MLGRYAEALE GYQKVLMRMP GLTDPDPRIG
IGCCLWQLGF KEQAKVAWER ALALNPDSKV ANILLAVYYL YDSSRHATTD PAFGSLYKMA
MTQYTQKAFK LDKEYPMTCA LFGGYFLLRK SYSTVETLAR KSIENTDVMQ IASDGWYLLG
RKAHYEGDLP RAAEFYNRSD QARGGGDKGY LPAKFGAVQM QVSNKDLDGA KFRLEKIIQQ
TKNAECMILL GALHAEEVFA AQKSGSKEDK SAEIKKAISL FESVRALWKD DGKKISPDES
VLVYLARLYE QTAPEKSMQC LVQLEEMQLA EIAADEYPEG IEDEEQIKDA MRVNLPPQLL
NNMGCFMYQN EKMDLARSLF QTALKACVRS KEKESDLDTD ALVTTISYNL GRSYEASDMP
DEAKKVYEGL LERHSDYTEA NARLTYIALR QSPTDEGPKR MAKLYEADST NLEVRALFGW
YLSKSKKRAA NLAEDHEQRH FKHTLQYYDK HDRYSLTGMG NVHLMTARDM RRDTDQDKEK
RRKMYERAVE FFDKALQLDP RNAYAAQGIA IALVDDKKDH GTAVHIFSKI RDTLRDASVY
LNLGHVYAEL RQYTRSIEHY ETALSKDRAR DAQILSCLGR VWLLKGKQEM SLSAMKTALD
YAQRAHSVAP AQIHLEFNVA FVQNQIASLA YSLPETQKTV QDVQEAADGL RQAVETFGRL
AQAKNPPYPA GALEQRANMG KTIIKQLERA LQSQKEYEEK NAAKLQQARE AREAEMRRRE
EEVRKAQEAE RERKQKIAEE RQQMIEEAQR LAAQRAEEER AREEAEMTTE EETGAKVKRS
KKKSSKRKKK RAEDDFISDG ETPARDEGSE AESGREAAPK KRRRLERRSG SKAQSKYKSS
EMVVDSDEEE DEAVATPAAA ESDHDQEMQQ DEEEEEVVQR RRNKVNRRVA DEEEDEDDLF
GDGGEKDTAM EDEEE
//