ID M7BIB4_CHEMY Unreviewed; 2239 AA.
AC M7BIB4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Acyl carrier protein {ECO:0000256|RuleBase:RU000722};
GN ORFNames=UY3_05909 {ECO:0000313|EMBL:EMP36929.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP36929.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis. {ECO:0000256|RuleBase:RU000722}.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000256|ARBA:ARBA00010930}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KB523472; EMP36929.1; -; Genomic_DNA.
DR STRING; 8469.M7BIB4; -.
DR eggNOG; ENOG502QRAP; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_01217; Acyl_carrier; 1.
DR InterPro; IPR003231; ACP.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR042417; PALB2.
DR InterPro; IPR031920; PALB2_WD40.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR14662; PARTNER AND LOCALIZER OF BRCA2; 1.
DR PANTHER; PTHR14662:SF2; PARTNER AND LOCALIZER OF BRCA2; 1.
DR Pfam; PF16756; PALB2_WD40; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU000722};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU000722};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450,
KW ECO:0000256|RuleBase:RU000722};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2124..2147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1151..1226
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1934..2051
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 2076..2116
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 54..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1457..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1664..1738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1773..1859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..36
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1550..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2239 AA; 240539 MW; A97D7BAD956CAEC6 CRC64;
MKENPGSYLD RLKEKLAFLK REYSKTFNRL QRAQRAERVK NYVKKTVAEQ NQLLRQEETE
NNTTELMDKQ SPNDDDKSGI YMLQTNTCSD SGTEKKMSVT FKLEPEFFNN EVNLQESSLA
ESTNSDQENI LSGLMRSVTE ENQSQLSRSR MTLVSEGRES ACEVPPISVG ETLEDQMGST
EEPGSPVFKG RNTISNTKNK IQKAPKLVIV REEKGLTPQD PQVGDFQEMP EENVFLSVPK
PLSCMSMGGN NIQQPVSPCA EDICDSYEPL PQCLVVDMPV SLQNIENTGK ELACIENQMD
QEELCRAFDL TADNQPSPAG RSNPSTSESR PHKERNHNET KSSSPLNTDS LLDNVEEPLR
NQEAQTEAGS PVLEKTPPAA ESALSSCTMI EGLLFPVEYY VRTTRRMSNC QRKVDLEAVI
LSQLGRSRKG LRSKHKQINS NSDQLYQETA RSDLQAGGTP FPFLGGESDP VSSNSSQKSL
PPSDESCTSS GSLSQKTVIS MKQAKGKSWR RGRGRWGSTC RPALNGSQAH PETSDLTVLK
ENSHLLSNGS QPGKENCEGD PERSPTGKTR VLVPAAGEAT ETEMTDITWP TETDLPDVSQ
TFSKCHQPPL EHTQNPLQGN NFLNPWDEAF SSPTRDLEAN VNVSQAGKQP VEHIRNQCVQ
KACRAEQLPT VKESLLQHDL PSSSVKRKVR QGSKGKRGRS QQMDLESPTP LSHLGLDPMA
FDPPFHFQNE MLSVKWLPSK LDIKDFHLPD EEFGLLKFEK LQSCTVKQLE PFVPSGSEHW
LQSAGDTVAL GDMRLKQVNT EGMSLENSFI SPSKTMSPKL PHLEGQLHKK GLSPSELLLT
PASSVSAGAI NQLESQIPTS AFPVLGATPA VLSLVHNEAL PDTLSVLPLQ VKTNLFKEPA
SHVVDGRECN NSTGTLHSDS CRTGSDCRSD EAVPLKEYQQ PGSGSKECCG AENKLTAEEL
AVVLSDSLRA RSLQLASKLK IPVIQIVPLP DVSNLVCVAL GDLEIGEIRL LLCSSEDGSL
KQSLVKTGNI KAVLGLTNRR LVSSSGTLQD QQIEIISVSE AGRSNERQTL MPPEETILAF
AEVEGIRDAL VGTTAVNSLV VWNLKTGQIL KKMHVGYSYP ASICHRAYSD SVSGTLQLCR
HYSDLPPLTL ESIKERVLYV LKLYDKVDPE KLTVTAHFMK DLGLDSLDQV EIIMAMEDEF
GFEIPDTEAE KLMCPQEIVD YIADKKDVGT TRLRAKKASS DYIFSSEIQH GGAGSLQERG
SCGGIIDVIS AANGTIHLPA AKGPLAPTGT CTWVVAALPS EEVRVEIKAL EAAAHPNLSV
RFEGDDGAQH FGGGMRGLGT AHREAAVTTE LDFTDLGLGA RLPSPTEGSG TLPRGQTEPA
MRTAAPAPCD SLETSQTPAL QLDGRESLTW RLGGKAQPAT ETSGTPMRTP GSSLTETLAT
TAHSAPGLHS SMRRMVPLGS PRPGEDLGHT LAEAGSEESP GRRGVDGVPE NMDLSLSTDT
RIEGDPRAAS WAESFPGTSP DKTPSVFAGT PRPLGNLTAP APSPGSAQPP APAEQLSTGS
SVSHPTAPGH ENGSLSERAL EPRLSTPAPA LERLFRTPTW LPETPAARTR VPGTGEPRST
VTAAPGTAVS VGMSSQPPVS CTHGAKQPSL APSPVMAVTS QEGVFPGASS GEAVPHGPGT
VQATTPLGFQ PSPASQHDRA HHPPATLQRG STALSPTEPP DPPGTRLSSP FSLEKDISGS
PAALGLAELG VATTQSPSWD TATTNASVAT PSLASASWRG GTERLGQRAT TPPAWAAQAG
AEPGNSSQAT DTRTPSGAGR SFLSINTGAL FSPTPPTPEL ILTAESAGSP AGSRSPWPPL
AATPRAWGAD VTDPVSSART NVPFASTQLR AAMPPVTPGP AGATDGQPLP VTTKGAHGRA
QSVFVVEDQP PLLKATRLRM PCELALDMEF VGAFRTPGSQ AHRSLVQSFN ETVAPLFTAV
PGFQSLEVTR IRKGSVVLEY DALFAAERLR GPVQGLGALL NRTVLSGAAR SGLRIASAIV
LWNVVLERQL DLCTALFSCH AGFECISSGA GNASCTSVCH RDYCKNHGIC THPRAHEPVC
QCPIGSDYWF MGPRCDYKVT QQSLLGVACG VLLTVALLGL AIACLVVRRF KALLLEARVD
QTKSSYRRFC RLDDVSAQYW SQPWLASANS LDNPAFSNSE ELLHLQMLDH SCCSCKDDTM
IPDRYEQQTT PISTVCRPR
//
