ID A0A2G5VA86_9PELO Unreviewed; 780 AA.
AC A0A2G5VA86;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PIC48571.1};
GN Name=Cni-cpt-1 {ECO:0000313|EMBL:PIC48571.1};
GN Synonyms=Cnig_chr_II.g7491 {ECO:0000313|EMBL:PIC48571.1};
GN ORFNames=B9Z55_007491 {ECO:0000313|EMBL:PIC48571.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC48571.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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:PIC48571.1}.
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DR EMBL; PDUG01000002; PIC48571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5VA86; -.
DR STRING; 1611254.A0A2G5VA86; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000230233; Chromosome ii.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR Gene3D; 6.10.250.1760; -; 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 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; IPR032476; CPT_N.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR22589:SF31; CARNITINE O-PALMITOYLTRANSFERASE; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF16484; CPT_N; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003801};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..47
FT /note="Carnitine O-palmitoyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16484"
FT DOMAIN 175..759
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 474
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 780 AA; 89438 MW; B5F369934BA60E6D CRC64;
MAEARSAAAL SFAVTHDGVS VSYDQELLRD IWHGISRSYK RRTGRFRNDF MNGMFPANSW
TLGLVVGAVA VFSVIKHDLS FGIFPFIQNY IVHYVFGDGY LGQSISIAVA GALLWLIFVQ
LLRLSIKTLL EYKGWMYESP GKPVSKATKL WLGVLHIISK AGPMLHSFQG ALPRLPLPKL
DDTVRKHLLS MKPILNDEEY QELEFLSERF RKGVGRRLQR YLTLKSWFSS NYVTDWWEEF
VYMRQRSPIM INSNYYGFDT LNEHPTTNQA SRAANLTYTS LQFRRMVDRQ EVSPFSISPR
TKVPFCTMQY ERLFNTCRVP GEEVDRLLHW DDAKHVAVYC RGVWFKLIVH NGKRLLEACE
LQHQYDTILA HSYEPSEGEM HLASLTAGER ADWAKTRRAH FRSGVNKTSL NDIERAAFVV
ILDDEETHYD PEDPSKLDHW AHNLLHGKAH DRWFDKSFNL IISKNGHVGI NTEHSWGDAA
VMAHFTEWSL LQDIVFIGYD ADGRCKGEAK EKLTPERLKW DIPTPALEQI RKSMEVANAL
IADVEMSLLV WTDYGKGFAK KLKVSPDAFL QMTLQYTYFK NQNKFSLTYE ASMTRLFREG
RTETVRSCTV QSSDFVRSML DASKTPQERL QLLRKACDKH QELYRDAMCG QGVDRHLFAL
YVIKRYLEEE SPFFDNIFPP TYLLSTSQTP MNQCEADAKG LSDDVRLRLI TAGGGFGPVA
DRGYGVSYIV AGENTLSFHI SSKRSADNTS SREFREELKR SLSDMKKLAE ALEAPPKKVQ
//