ID A0A093Y658_9PEZI Unreviewed; 1107 AA.
AC A0A093Y658;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=V490_04344 {ECO:0000313|EMBL:KFX94444.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX94444.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFX94444.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX94444.1,
RC ECO:0000313|Proteomes:UP000029320};
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 -!- 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:KFX94444.1}.
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DR EMBL; JPJS01001199; KFX94444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093Y658; -.
DR STRING; 1437433.A0A093Y658; -.
DR HOGENOM; CLU_291047_0_0_1; -.
DR Proteomes; UP000029320; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
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 Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR22589:SF115; CARNITINE O-ACETYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029320};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 424..501
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT ACT_SITE 830
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 1107 AA; 122726 MW; 4FEE6A4D56EC1FC9 CRC64;
MASSTVKELE KAKNMDPVHD ATTAQMVFLF TGQGSQWYGM GRELISTKTV FGESIRKSDA
ILNSLCKSWA LLDELQRPED LSLIDEGHIA IPATTAIQIA LVDLLKSLDI LPNVVLGHST
GEISAAYAAG ILDHHDALTV AFCMGDVLRR RGLFDGRGGM LAVGLGEAGC QLYLDRLQDG
DASIACENSP WSTTVSGDYA AIKELESVLC GLNIFNRRLR VPAAYHSHQM KSVELEYLMA
IEAIGPSSPQ SIQFFSSVTG RREVDGFGPL YWARNAISAV AYSSALREII ASATKTSSSK
LLLVEIGPQP HLQRPTEECM GEASIKPFHM SYFPSLVRGK DAREALFDLA HGLSLRCSSA
DLRTLQKPGA IQDGTDDKIS RACNWRSRKM VPEIKNGMNL GVTDKHAHLV AIQEDLLLGL
AGDETLKAIC QGIADEILKL IGASRFDCQV DLPVSDYGLD SLLATKLAEW VNKEYALSFS
VAEILDSSSL FNLARSIEMS NSLGYSKFEE EVGGDHVLRD HNSLLLKPTV VAPLSKSLPR
LPLPDLKSTL ENYYRSIEAF GSDAELSATR KTIEDFRNSE DGRKLQGRLQ ARVNDPTRDC
WLADLYNGSN FLDRNGPLVP YSSFFYTHKL SNFQHTQAER AAIITAATLQ YKEDLESGAI
SPDVLHGQPS CTFLFKYLFN TTRKPRRGSD EMERFPGNDY IVVLRRGRAF VLPLYVNGTP
MALFQLEAVF EWILQNVDSE LLRVGILTSD ERTSWAKIRE NLKTLHPQNS QYLHTIEAAA
FLVCLDDASP STPSERAHHF HFGDGSNRWN DKSVQFAVCT NGVSGFIGDH SMLDAGTVLG
LNRFVTRAIL KHTYKPDTST QTIGDMSTYI KEVKLLTTPY IDLQIARVTH DFNANINNAN
HVFLVLSDFG DRLCRLHKYP PKSLFQLIVV LASKFHFGCP VPAFWETVSL GSFYKGRVEI
NQVITLPVLR FLDAAQDVAI PVSGRQQLLQ DAAKSHAASV MKAVRGRGVD RHITSLRQMV
EEGETVPALF TDPLYVRARP RKIMSHCHET GMEEKGFLLR DPQAIWVHYE ISDESVKFSI
TGLGDSPRQF CNFLEHAALV VRELVVA
//
