ID A0A094H2P8_9PEZI Unreviewed; 949 AA.
AC A0A094H2P8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN ORFNames=V502_08622 {ECO:0000313|EMBL:KFZ09615.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ09615.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ09615.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC also involved in DNA repair. {ECO:0000256|ARBA:ARBA00025178}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the EAF7 family.
CC {ECO:0000256|ARBA:ARBA00007117}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232}.
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:KFZ09615.1}.
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DR EMBL; JPKE01002935; KFZ09615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094H2P8; -.
DR STRING; 1420915.A0A094H2P8; -.
DR HOGENOM; CLU_013513_1_0_1; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000029308; Unassembled WGS sequence.
DR GO; GO:0043189; C:H4/H2A histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR InterPro; IPR012423; Eaf7/MRGBP.
DR PANTHER; PTHR22589:SF115; CARNITINE O-ACETYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF07904; Eaf7; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 374..924
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 29..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 665
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 949 AA; 106558 MW; 15BE5383D4B31B81 CRC64;
MQINSKFCAL SIHPTASDTF QIRLTLEMPP RKKTRGGGRI ASTPGHDDGD SMVVDTPEEE
ESPQKPAYDP LQDPWTDEQE TSLYKGIIRW KPAGMHKHFR MIALSEYLRN HGYKADVHTR
IPGIWEKLGR LYNLDLIDER ENTLDFAEDE TGEDKFLEFS LPEDEFGEMM WIRGQVSSEA
LSSPPQINAP PPDLPPPKKR RRGEAASNRA STVEDTDEAQ TSPPPPSSAT RPGRGRGGRR
GRGRGVGRGR ESSERQASKE TTAEPTDQEE VEETGDDGEE DEAETADETA EDGSPSPQPA
STRGRGKGSR GGGRGQVKSR RGRKRALRSG LQSMRTSRIV TPAMTRNNSS LPAGYKEDNS
KGPMLRYEES LPKLPVPTLE ETAARYVKSV HPLVSATEFE HTKKVVADFI QPGGIGEKLQ
KKLIARRENP KTANWIYEWW NDAAYLSYRD PVVPYVSYFY SHRDDRRRRD PSKRAAAITT
SALEFKKAVD SGTLEPEYMK KLPIAMDSYK WMFNCSRVAA KPADYPVKFN HEEHKYIAVV
RKNQFYKVFT EVDGQQLNTA ELEAQFRRIY EIAETVPAVG ALTSENRDIW TDAREVLLKA
HPANAKALEA IEAASFVVCL DDAAPVTLEE RAHQYWHGDG KNRWFDKPIQ FIINDNGTSG
FMGEHSMMDG TPTHRLNDYV NDVIFNNKLD FSATNVRSSL PEPAPVKFHV TKEVASEIHR
AEKDFADVIG QHELRVQAYQ GYGKGLIKKF KCSPDAYVQM IIQLAYFKMF GKNRGTYESA
ATRRFQLGRT ETCRTVSDDS VAFCKAISNA DNDSKTTVEL FRKAINSHLE YIAAASDGKG
VDRHLFGLKK LLAPGEELPA IYKDPAFSYS SKWFISSSQL SSEYFNGYGW SQVVDDGWGI
AYMINENSLQ FNVVSKGLGS ERMSFYLNEA AGDIRDLMLP TLEAPKAKL
//
