ID A0A226MBM2_CALSU Unreviewed; 1851 AA.
AC A0A226MBM2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OXB52631.1};
GN ORFNames=ASZ78_013773 {ECO:0000313|EMBL:OXB52631.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB52631.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB52631.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB52631.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB52631.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC Evidence={ECO:0000256|ARBA:ARBA00023404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC Evidence={ECO:0000256|ARBA:ARBA00023404};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
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:OXB52631.1}.
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DR EMBL; MCFN01002462; OXB52631.1; -; Genomic_DNA.
DR STRING; 9009.A0A226MBM2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000198323; Unassembled WGS sequence.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000198323};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..177
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1754..1829
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1851 AA; 205265 MW; D35B84B681B85FFE CRC64;
MEDYSKIWGV INISAVNQNG RSITPITRPS QIEQEKLLRS IYGSRVDPSV VQYIEAHGTG
TAVGDPTEAE GLGNVVCKNR PSQVPTLRIG SVKGNIGHTE SAAGAAGLIK VLLMMHHGKI
VPSLHYSKEM SSIDTEKLNL AVPTEVEPWE DSGEYGRVAG INCFGFGGTN AHVVVRQVKQ
PGPLPAFKRP LELIVLSAAS AKSLQMTMAD TAEQLSTRNC ITLPSLAYTS ACRRSHANYR
YRKAFVANSL QHLQQEVMSA ASTESAVSKV EPQLVFVFCG NGVTLKEFSE ALLSSEPVFR
DKCKEIEALF QKHAPISLLP ARGRSSKELL NPELSQPMLF TLQVALASLL KYWGIKPVAA
VGHSVGEVAA AHFAGYLSLA DAVKVIYHRS RLQAKTAQGR MLVVGNIPVQ EIAEHLRPYS
GRVCIAAFNS PVTCTLSGNP DDVDLVQKDL AQAFSQRNIF LHVLNVPAAY HSPSMDVILG
ELEQSIEPLE EQKGDVEVIS TLTGAAASAN DFTRGKFWAQ HTREPVAFTR AIETAARDRE
NVVFVEISPH RVLQRNIKET LGKVTKVLSS LQSDAEYQAL FNLVGHLFEL GYNPNWQHIY
DGYQSVPVTI PRYQFDRKKV VTSLDTNQLV NQRDINSSHP LIYVLNSDNT EYGCLLSQDT
TSYIYEHKNN GVALVPGAFY VELGLACVMS CSRPKAPLSA CQMSISFSAP CVLTQSSQVL
TIKLSPQKAG TAFEILSSSD AVYASGQVRK VPEGFVEEST ISFQEVYHRC TSVISTEEVY
EALSRVGFQY GSVFRQLRDV HYCQDLKEAI TSIKVNKETL REMYSYCIHP VLLDCFMQMT
AVMISSTLQS RAGFPSGIGS LVVLRPLEEE MMIYMRTSKA IGSCLELCGC FMDKHGSVLV
ELKRVTITFM KQASSRDNEF MFENKWSEVS PSQSIGHLEA MPRVLVFADK FGVAEQLRKY
LHPDSRYVRY EDWESLLEVP REHKMKAEVE DYDEVLFLWG IQRVNEEFPS KAVDQLSKCC
EAYRQVIVAL REKGSHCSIR VISYRTTERN VDHINCGFAL HGMTRTCVVE VPEITFQIID
LSSSSSLDIS ALSDVLVKYG GKDYPEVCIS QGRIYASEIK RTPFVDENYT QHVRSLQNSE
TFTLYTADPY SAKDLSAELC TSTATQLENQ SVEIQVDKIC IHSEDYFPIS VSSRNFGNAL
YWNSQAVDKH RLLALDFSGT VTAVGTDVRK VKVGDHVVSC YPAAASSRIQ VPGTICLNVK
KFPCFQTVPC VSYFIIAWEI LNQRLPKGKR GRTLGIISTE PSSVLCRVLS AAAEEMGWKT
VLARPSPDML QYINACSALV VLPPVGRLSR EDLAHMCCLK DVVIVCGHQQ SECIQNISGL
DHENIIFHIL ILSSIFQKAS LKELQKAVHV WISSLDMKRF RHLPASVFQQ TENLERLQSV
VSSFTCKSVP LAVLRKQKDI TVVSDIPLYE SEKKIFKQNA VYVVAGGLTG LGFETVKFIA
ANGGGCIAIL SRKIPSQEKQ EEMKALRQKY EGSKIVFVQC DITLTNDVEK AFQIIVKSFA
GCPIKGVFQS AVVLHDGRLE VLKFADFQKV LSPKVAGTLN LHWATRGQQL DYFVCYSSVT
SFLGNSTQAN YAAANSFLDV FCLYRRNCGL SGQSINWGAL NLGILLNQNH IQNILESKGI
DILQVHEIHE YLKKSLLLNN PQQAVVKLNV KTLISHVFIR IISLKSRFYS LMLEEFGSKL
DTAEESHDPD TALVKSEDYI TSLMADLTGS NPDELTMNTP LSSLGIDSML AMTIQNRIFQ
ERKVDISLLK LLDPHTTLSS LVVLLGETTK ADGVVDKNMS AVASAEHESW L
//
