ID G4UDT2_NEUT9 Unreviewed; 684 AA.
AC G4UDT2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Acyltransferase 3 domain-containing protein {ECO:0000259|Pfam:PF01757};
GN ORFNames=NEUTE2DRAFT_56258 {ECO:0000313|EMBL:EGZ74937.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ74937.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ74937.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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DR EMBL; GL891107; EGZ74937.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UDT2; -.
DR STRING; 510952.G4UDT2; -.
DR eggNOG; ENOG502RYMZ; Eukaryota.
DR HOGENOM; CLU_005679_13_5_1; -.
DR OMA; GAYEWTR; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR PANTHER; PTHR23028; ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR23028:SF53; O-ACYLTRANSFERASE HOMOLOG; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 138..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 641..663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..377
FT /note="Acyltransferase 3"
FT /evidence="ECO:0000259|Pfam:PF01757"
FT REGION 23..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 684 AA; 77088 MW; F3D9684B12DBC8E4 CRC64;
MNHTYAEETS SVGLKLNTDK AFLPDIEPNS GHEEQEVGSA PQHQRRRHST IFGWLPRVNI
GFFSRNPRHR ISHLIPPIRP LLLRSACFLL PSFLQSRIRR RRPFCSASPE NQKKRDKERH
DEEPRTLSPT AYLDGMRGIA AFSVFLCHYF YTCFVIAEGW GSGGSNYNFL KLPIIRLFYS
GPPMVCIFFV ISGYAISLKP LKLIHSASCS SGSSTTAHAD ERNYSKLFET LSSLVFRRGL
RLFLPPAIST FLIVLLLRLG AYEWNREFAS DENFLRNVQE IHYERFQSAT EQFVDWTYAM
LNFVHLWDWD AFAGSTGIDV HLWTIPVEFR ASMVLFLTIL GTARLNRGVR RGVVLGWCGF
AFLWERWEMC LFWMGMVLAE SDLIREVEAR QEKEGRVQGG FAERNGGEGV LPVVEPVLAR
KGDVMPQQRR HPQRHPQETT ARGPDISSDM TIVGSGDETS HESHQPPTPS PPTTAVAGRS
LPAGITLFPT LLLVISLYLL SQPDINSHLT PGWITLTSLI PHWWTEHYRF YQSIGAVLFV
YSVSRYPSSS DSRSGSSSHP PSVAGSCSPN TGPTTAVPIF SSILNPKTLF ESSIARHLGK
TSYAIYLVHG PVLHTLGYTM MKFTWTRVTG TETNEQYVTG FVLASLAVIP LVIWVADVFW
RGVDEPVVRL ARRLEQRVVV GIGE
//
