UniProt: A0A131ZWV5

Database: UniProt
Entry: A0A131ZWV5_SARSC

LinkDB:  A0A131ZWV5_SARSC 
Original site:  A0A131ZWV5_SARSC

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (30)   
   InterPro (17)   
   Pfam (7)   
   PROSITE (2)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (37)   

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ID   A0A131ZWV5_SARSC        Unreviewed;      2087 AA.
AC   A0A131ZWV5;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Fatty acid synthase {ECO:0000256|ARBA:ARBA00018769};
DE            EC=2.3.1.85 {ECO:0000256|ARBA:ARBA00012873};
GN   ORFNames=QR98_0010060 {ECO:0000313|EMBL:KPM02590.1};
OS   Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC   Sarcoptidae; Sarcoptinae; Sarcoptes.
OX   NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM02590.1, ECO:0000313|Proteomes:UP000616769};
RN   [1] {ECO:0000313|EMBL:KPM02590.1, ECO:0000313|Proteomes:UP000616769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM02590.1};
RX   PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA   Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT   "Draft genome of the scabies mite.";
RL   Parasit. Vectors 8:585-585(2015).
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:KPM02590.1}.
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DR   EMBL; JXLN01002314; KPM02590.1; -; Genomic_DNA.
DR   VEuPathDB; VectorBase:SSCA006060; -.
DR   OrthoDB; 3080116at2759; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000616769; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08954; KR_1_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; 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; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR049391; FAS_pseudo-KR.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
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; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF7; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF21149; FAS_pseudo-KR; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 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; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857}.
FT   DOMAIN          25..456
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   2087 AA;  237118 MW;  FDB72D9D774D9F6D CRC64;
     MSSIEREESK QTQNSSNVFA NTLVNDEIVI SGIGGRYPES DSLDEFRDNL YNNVDMITSD
     DRRWPTGNLT KKIDQFGRFH VVCSSLDLYG MNHRMGKLKQ IDKFDASFFG IVPKVADEVD
     PPGRILLETT WEAIVDAGVN PQSLRGTNTG VYVGYTAVAM PDGVPQEAQD DQQSSKVESL
     LWFQGGSKAF YANRISFLYD LHGPSMSIDV ACASSMVCLD IAVTDLRLGK CDQAIVAGVS
     INLQPFTNHI YMINNIAAPD GRSKVWDQSA NGYVRGETVC SLFLQKRSDS KRIYATVLHT
     KTNIDGYKIT GMFFPSSESQ YDLMRDTYTE AGIDPLEVNY FESHGTGTKA GDPQEARAIL
     RAYCQNRKDR LPIGLLKSNI GHGEGASGVA SISKLCIVYE NKKIPANLNM QTIKSDIACM
     VPPLDPVTEN RDYEPGIVGI NSFGIGGVNA HALVKPNRKE FTDDSYKIID SVPRLINING
     RTKESIEYIF DFIRDNPKRV TREFLALLGD TVNSEPTIYS GGFPYRGTML IKTSPTSSNT
     YEFQTKLSKT DNVRRPICFF FSGMGSQWSS MAKSMISIEM FAESIQKCAN FLRPMQIDLH
     HILTSDDPEA LKEKIHHFVA ITSVQIALVD LFRAYGIKPD YIIGHSFGEI ACAYADGCLS
     LEQAIITSYW RGKSIKDANI EHGMMAAVGM SWEETKQKCP PNVYAACHNS IDSVTISGAY
     EPVNRFVKSL TEMKIFAKEV QCANIPFHSP LLNPAIKKMT EALRRVIPEP KPRSSKWIST
     SMPESEWLTE KAQRASADYF VNNLINPVYF HEGCQHLPEN CIVIELASHT LFSAIFKRSM
     PKANYVGLMR RNNPDNLDYY LSSLGELYRL GVSIDLKPLY PSVQWPVPRD TQSISSLIQW
     DHSRSFLVKS YPKYHCQATA ADFVQKFSLS NPDDQFLKDH AYDGQCYLPI SCYLLLAWRR
     LGVSLGKLWY QFPVQFENVT FEPLIPISNE NDCDEIELNV RILDPTDRFI ILYHNQIIAS
     GNIHSNEFYT EMNVRGYDFG PKFKQIQQIE FANFNRSKAL VRWDSNLITF VESMIQLSIS
     HTEKRLIYTV SKISSFKCDP REFYSKSSDT LASVIIDTNL RLVISEGLEM KGLQFRHQPL
     RDVMKNVKME TYGFVPFDDR KAIDQDDYEQ LQRYITDVQA LYKTIEKVLC DEQTSSMILD
     GKIQKLIDRT EFNEREILMQ ILIQYLRCLI DENQNLRNVG EEKMKRSILK RILMTENNQD
     IHLDLLNSCH KNCRMMRSTL EVDLKLSELG LQRIKSFIRL AESLGLSLIS NKSDSLTSTC
     LLFRKKINNI KPEMQSIVPI YFGSFDKWVN KLKQTFIEKK SRPKNENIWL LADDSHFNGI
     LGMINCLRQE PGGDRFRCIF SLNAPLPQPI DFKQNFYRKV MENDLAVNVW CDNQWGSYRL
     LDLHRNYNLR ETLDAYLDFG IKDNSMQLKW HHLMSANASP SRKQIKVHIN FSDLNDFHHR
     SDRFVDDQYE NHSLGSGFSG YRFDDGEKVM GLAQSKTIAS WIETDPNQLI AVPEEWTLVD
     GCATINALFM AWLGLVKRSQ LKQDETILIH PGTNAKGLMA IQLAKRENCR IIATIENESQ
     RQYLSENFGL SPANLISSRD TKFIDKILTL TSYKGVDVIF DSSSSELDLS LPILREHGRL
     IEIDRKFARK NPIHLKSTQH QINLSLMIDA KEFDSFVPPM MIEFREWFQD CAKKFIEPID
     SKVFDIDNLD GAFDAMHQED HIGKVILQIR NENNLSRKFS AIPTTRFSPK KCYVLVGGLG
     GLGLEVAHWM ATRGARKLVL VSRSGIKNEY QYVFVKRIEN LIRNTCEKAN PEVKICTSDP
     STIKGAEKLM NESQKLGPIG GIFHFATVLN DAFIEDQTPE SFKKVCAPKM DALCCLDTIT
     RQLCPELDYF VAFSSQSSSR GFIGQSNYGY ANSVMEHICE CRRNDGLPGQ AIEYGPIGDV
     GLWAKNEHID LTSIGMVIDT QRIPSCMEVL DRFLNRPEPI VATIVRHQDF KQNDGTSKAK
     DHIWQGIGIE LDSLPDNLTL GDVGMESILA VEMQQRIERE YEVNLGR
//

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