ID A0A177CV12_9PLEO Unreviewed; 431 AA.
AC A0A177CV12;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Acyltransferase 3 domain-containing protein {ECO:0000259|Pfam:PF01757};
GN ORFNames=CC84DRAFT_1133143 {ECO:0000313|EMBL:OAG11394.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG11394.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG11394.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG11394.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV441548; OAG11394.1; -; Genomic_DNA.
DR RefSeq; XP_018041759.1; XM_018175961.1.
DR AlphaFoldDB; A0A177CV12; -.
DR GeneID; 28759447; -.
DR InParanoid; A0A177CV12; -.
DR OrthoDB; 1951229at2759; -.
DR Proteomes; UP000077069; 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:SF128; ACYLTRANSFERASE 3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..336
FT /note="Acyltransferase 3"
FT /evidence="ECO:0000259|Pfam:PF01757"
FT REGION 402..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 48370 MW; 380CDD9CA8F7CA38 CRC64;
MVVSGHLCTA FVPWLHSPAN DPHTAPHLFQ LPFFRLAVGG RSAVALFFLI TGYVNSIGPI
GRSRAGNTDA AFNGIAKSAL ARSGRLVLPT MMATALTWFM ANINAYHMTK HVDSTWIRQG
WHRQEPTLGA AFSSLFKAEV DTWTVGWDDY DGTQWTLHLF LEGSMLVYMT MFATVLVKPK
ARFIVYAVLY LYFWQLGEGL AVGALKGLNI VFGMFVAELH NHYKDTATSV LPAPIPALMI
IAGMFMAGFP QDSPQNAHWS DSMAHFMQAI TVEKTDIRRY WDHIGAATVL LGIFFSRNAR
RVLTSPIFNF LGRVSFPVYL MHNTFIKSVL TWMVYLPSAM NPPRNEKGHQ MDLQRGSTTH
IFIAVAVFYY VLYRAAALWV QHIDPFCANL VNAATSWAYG ESQPRESRPI LQTIERRSSP
SREKPKLDSP V
//
