ID U7PQD3_SPOS1 Unreviewed; 2823 AA.
AC U7PQD3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1624_06909 {ECO:0000313|EMBL:ERS96700.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS96700.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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DR EMBL; KI440849; ERS96700.1; -; Genomic_DNA.
DR STRING; 1391915.U7PQD3; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000018087; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR013154; ADH-like_N.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 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; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018087};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..442
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2736..2814
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 478..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1393..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1818..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..515
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1818..1857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2823 AA; 297867 MW; 5581083CBB23F2B4 CRC64;
MASPADPVPP VAIIGLGGRF PGEATDPLKL YDMCAAGADA WTEVPASRFN HAAFYHPDQA
RNGATNVTGG FYLRDDVAFF DAPFFGITQT EAASLDPQQR LLLECSYEAL ENAGLALADV
AGSDMGVFVG SFCFDWAKMT LRDPDAIPLY HATGTGQAML ANRLSYFFNL HGPSVTLDTA
CSSSLVALHQ ACQALRAGEC STALVAGVNC SLCHDSLASM SSMGFLSAAG RSFTYDSRAA
GYGRGEGVAA LVLRRVDAAV AAGNSVRAVV RNTGVNQDGR TPGITFPSGA AQAALIRRVY
AQAGLDLADT SYVEAHGTGT QAGDPIEARA LAETFGAVRK EADGPLVVGC IKTNIGHLEG
ASGAAGLIKT VLMLERETLL PNCDFREAND KIPLADWHLT VPTRVQLWRD ALGTTTKTPA
VLRASINGFG YGGTNAHVIV ESAADFLRAR GIDGGRYAFS HGRPATRHLP DPIVHEHDRH
STLDVPSVAP SDAPDAPDAP SRSPSPSPTP SSPDSDGTPP TTNGAVSPTS ETHKPDDAAL
PVPQLFVLSA HDAAAGKAQA AQLADYLASA ADPRLLSDLA YTLSTRRSAL PWKAAVAAAS
ASQLAAALRD SSLRFHHTPA QAPPRVGFVF TGQGAQWFAM GRELAATSAV FRASLDRSAA
ILASSTMQAD WSLHDELLRR DAATTRVNEP AVSQPLCTVL QVALVDLLRS WGVAPAAVVG
HSSGEIGAAY AAGLLSQEAA VAAAYFRVPL DSAAADACRG GMVALACDEA TTRGLLAGLR
RGTAVIACYN SPQSFTVSGD DAAIEELAAA CTAAGVRHRT LVVGFAYHSH RMAAAAEAYR
ALLQANETVV GAFADPVTTT DSERAVEMYS SVTGRKLQPG ALTLDYWVEN LVSPVRFTEA
LTALCYEAQT EMAADTAAAP PKARVDVLVE VGPHAALAGP IRQILQTEAP LSKIGVLSML
RRGQDATATA QQLACALVER GVAVDVAAAN ADARLEGSAS STASPPSTAS PPSTALPLVD
LPPYPWNHST AYWAEPRDSI RYRQRTHGRH DLLGAPVRFG SPLEPRWRQW IRTAETPWVR
DHRVQGLVVY PAAGYISMAI EAVRQVATAQ GATAAIASYE LRDVSLGQAL IVPEGRDEVE
ALVSLRPQTE SAMDNSTVWH EFFVYSCASS ATTATPMGAP LTETWAEHCR GRIAVRWAEE
GEKDKDKDNN VTDHAALAAA RARHDAAQRQ RTRDACTRDV DLAALYDHCT AIGLEYGPTF
ANLTAARAGA ATPADPTHYI AGTVVLPDVA AVMPAHHHSP LVVHPGTLDA CLHGIMAFRD
LLQAAIMPVF FAHISIDAAL ERVAAGDALD VYLGVQQSGF RNLDIHLTAY GGTDADAPLI
RMDGLRMTSL AGSMPAGGGG GSSGNSSGNP PKTYFQAEWR PDPAFLSSAQ FDDLCAHLMP
AEAESAALRR LDQGAFYMAD AAVAQVPPDS VPALSTKGRK LYASLRRQRD AVLALHDAQP
SATAKAAPVH ADDIASWPNA SPAERAALLD ALAATGAEGR LLAAVAARMH EIVLGTADPL
EVTMQGDVLG QYYAHNPRMA RQYQQAAVYV DLLAHKNPHM RILEIGAGTG GATLPLLHAL
GGGADGRNTL PRFASYDVTD ISSGFFEAVQ AKTQPWASLL RFRRLDIERD PVAQGVAAGA
YDLVVAANVL HATRNMARTV RHARRLLRPG GTLLLIELVR VPQQRVSTAA VGNIFGIFDG
WWVAEEPHRQ DSPLLAETHW DAVLKEQGFS GLDAAVWETP DVATHQGTTM ISTAVYQGGG
DADGAEGVSD VETTTIENTE TETTEAPETT KTTEAPETTK TTTESTNTVT ETEPNADTPL
PDDTPLLVTD DAANKPWLAS LAKALAVALP LSPGTDLPVY TLDDLPTITD RHVCVVYQTD
PQTLGPQTPA SMDKMRALFL RPAGTSGGRV LWLTRGASDG ASAPDFALVQ GLLRTLRVEL
GGRLVHLDLD VDTGSPAADQ DPSIQTVARV YAKSFGRATD IATDGRPADV ELELAVRGRH
ATVHIPRYDE ARAPSDYVAA RTGRRIAVPA SPVQPGRHLQ LMVGQPGLLD SLYFDDDADA
DADLPDDHVE IAVRAAGLNF HDVMVAMGQI ETRALGRECA GVVRRVGRAV TAVRVGDRVA
APADGTFATT VRCAAWRAQV LPDSLSFAAA AALPIVLCTA LHAVRITQLA AGETVLIHAA
SGGLGQALVQ LCQQRGAVVY ATVGTPAKKQ LLVDQYGLDP AHIFSSRDDG FADAVRQATG
GAGVDVVFNV LAGELLRASW RCVAAFGRFV ELGKRDLGRN GRLDMAPFAR NVTFVAVDLV
ALLAERPRYG AALWADSMDL VRQGVARAPA PLTTYAYADA VAALRTMQAG RHVGKLVLVP
QTSTSTNGVP TAPVMSPRVP PVRLRADASY LLVGGLGGIG RALAARMVHA LGARHLILLS
RGDVVTDVAA AAVADLRGRG GARVHVASNC DVGRDDQLAA ALAAAQAAGF PPVRGVVHLG
LVMESALFQD MSSAAWNHSL WPKVAGTWNL HRQLPQAPGA LDFFVLLSSM VGTIGNPSQA
AYGAASTFQD AFARYRRRRG LPATTLDLGM VTGIGYVAEH GQVQQTLRSQ GFEEISGDEC
LALVESAMLQ GDEDPDHDHG HAWSANYVTG LGLGRYAGGD PARAIYQDPR FAMARRMALH
AADAHADADN VPGAGAGDTP TRSLREAVRQ AASLADVVAV LAAALRAKIT ALLMLAAEDD
LDPHKPLSQY GLDSLIAVEL RNWVSSEMEA TVPVLEFLGS RTTQSLSDFI ARQSRLVKKE
LLE
//
