ID G0SBG7_CHATD Unreviewed; 1873 AA.
AC G0SBG7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGS19547.1};
GN ORFNames=CTHT_0050210 {ECO:0000313|EMBL:EGS19547.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS19547.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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DR EMBL; GL988044; EGS19547.1; -; Genomic_DNA.
DR RefSeq; XP_006695369.1; XM_006695306.1.
DR STRING; 759272.G0SBG7; -.
DR GeneID; 18259059; -.
DR KEGG; cthr:CTHT_0050210; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OMA; THARAKV; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000008066; 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; 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; 3.40.50.720; 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; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; IPR020807; PKS_DH.
DR InterPro; IPR049552; PKS_DH_N.
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; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF13; POLYKETIDE SYNTHASE 1; 1.
DR Pfam; PF00698; Acyl_transf_1; 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 Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 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 SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1793..1870
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1768..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1873 AA; 209384 MW; 2CE0CCD24EEE8B7E CRC64;
MMNYDIYEDE GPMPVAIVGM SCRLPGGVSN PGELYRMLCR KRSAWSPVPE DRFTAGAFVH
PKPEIRGCFN SLGGYFLTDD INEFDAAFFD ITKKEADSMD PAQRILLECA YEAVENAGIP
KENLSGSRTG VFVGANYSEH RAANLRDIDN VPSFDATGNQ GAFMSGRISY IFNLKGPSMT
IDTACSSSLH ALHLAVQSIR AGESDQAIVG ASEIITHPDI WVSMSKLRLF IREGRTFAFD
HRATSGFARG EGAACVILKP LWAALEDNDH IFAVIKHTGV NHNGRTVGIV APSTEDQQAL
LDQVLKEAGI QPDEVGFFEA HGTGTKKGDP IEAEAIHRSI AHWRDPVDPL YIGSVKSNIG
HLEGASGLAS VIKVTLMLFY GFILPNADFE APNPEIPFKE YNMQVATTQK PWPAKKKYAF
INNFGFSGSN STAILEAAPM TRGLEIAGSD RYSPLRLFVL SANDETALKN SITKLGIWIE
QHAELYQTTM PRNLAYTLCQ RRSHMPWRVA VVASMCSEVA KALNSPEATP MRAPTEPPKI
AFVYTGQGAQ WWAMGRELLK THPVFYESIV RADDALTNVG CEFSILEELT RDKKDSKVGE
AHISQPICTA VQLALTNLLE AFGIIPVAVT GHSSGEICAA YRAGILSFED AMQAAYYRGQ
AVIEFKKRYP MLKGGMMAVG AGAHDLLCLI REVNESSYVE KVGVACQNSP ESTTLSGDVV
ALDQIAKILE RDGIFNRRLF VDVAYHSHHM KLIGDVYLEM ISHIPTPKAT WSETAFYSSL
KARKVGGREV GPEYWVDNLT QAVLFSDALQ RLCTEVQPNI LIEVGPHAAL KGPIMQILKT
LRSSSHGITY LPTLVRNEDA TRTVLELAGQ LYMRNWPLNF EEINHNREEA ERPEVIPTLY
TYPWTRQKYS HESRIDKAHR FKPFPRHDLL GVLADWSYEL NVCWRNFIST EHMPWLRECR
IDGRITYPVS CLVSMIIEAA TQDAEMNNML PARWTIEDFV LEKGVFLEDG EELEVLTQFE
PFDFVKRHEK QRHNTFYIAS YNASRGWTKH CYGRIVVDPW GYRDDLEWNL HLKDCERTEI
RTPLGGTLPE PQKGHESIYA WLKELGHEYP KAFHSIIDAE ITPRDDFIGG CNAQHTDIMG
NSLCTVHPAQ LEALFQAALV ASDNVEPCKG VVRQVLNFKR MVLRAYRWAM QPGEKFTVCA
SPRDWSDCNR DDERIDARFV SNDDWFCPAI SVDDIFVFGE QNPVVPKKKP VRELCFKYVW
EPYEDRPLGR LVYDTNDYIT IVVTDEKYRS NEEEELATEL KHDLMRYLDL EPDVCSFNEI
LLNSYNGHFI VLCDVTSPVL KHLNKEDFED VKKILTSAKS LLWVTRGAIG YPTLQYVESA
MALGLIRTAR SEIGLQACIF DLFPGVMDQN GLPWNKCHQD WAELLDPYIT VSQLRNVFLR
VFDENFNPAE PIDNEIFQGP EGDLMVQRIV SDDALNKYVA KPVIGAESFQ KGCTHLIIGA
GGLAKEVARF IGSAGAEHIV LVSRRSRPSK EMDHLVEQFV RDRGFYGARI GWAQCDVTDI
QQVRDLVAAL SASGWPPVGG VIHAAMVLKD VLIEDMQYED YISVIRPKVH GTHNLYQALC
WTRCSQKPPQ DFYWVSLSSA AGIVGSRGQA AYAAANTYLD AFADVLRQIG LPGKHINHVA
ASLDLTAVLG AGYLEKHENR KDEIIRNFGN ETISPREITV LLHAAQKGKT EAQVLTGLKL
HMGSNGQLPY YASDARFKYL VEACDQAAEN EDKSSKQREP TGAAFRKAKS DEEATTIAAQ
GIVDKLSEVL SMSAQDLDVS RNITSYGLDS LTAIELRNWI AKELRVNLQI LELLSSGTIT
DLAALIVQKS RSV
//
