UniProt: A0A1H7VDG1

Database: UniProt
Entry: A0A1H7VDG1_STIAU

LinkDB:  A0A1H7VDG1_STIAU 
Original site:  A0A1H7VDG1_STIAU

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Ontology (3)   
   GO (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (29)   
   InterPro (16)   
   Pfam (7)   
   PROSITE (2)   
   SMART (4)   
All databases (34)   

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ID   A0A1H7VDG1_STIAU        Unreviewed;      1363 AA.
AC   A0A1H7VDG1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:SEM07094.1};
GN   ORFNames=SAMN05444354_11146 {ECO:0000313|EMBL:SEM07094.1};
OS   Stigmatella aurantiaca.
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=41 {ECO:0000313|EMBL:SEM07094.1, ECO:0000313|Proteomes:UP000182719};
RN   [1] {ECO:0000313|Proteomes:UP000182719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17044 {ECO:0000313|Proteomes:UP000182719};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOAP01000011; SEM07094.1; -; Genomic_DNA.
DR   RefSeq; WP_075008322.1; NZ_FOAP01000011.1.
DR   OrthoDB; 9808564at2; -.
DR   Proteomes; UP000182719; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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; 3.10.129.110; 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; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 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; 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; 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; 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   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182719};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SEM07094.1}.
FT   DOMAIN          22..444
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1275..1352
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          444..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1363 AA;  147676 MW;  E059854BB8B849BF CRC64;
     MTIRRKSALA SRFARKLQRH ATEPIAVVGM SCRFPNAPHL EAYRRLFSDG MEVRKEIPPE
     RFDLDAYYSP VAGTPGAIST RHGGFIQDID RFDAGFFRLT PREVEAMDPQ HRLLLELAWE
     AFESAGMPPA VLSGSQTGVY VGIATFDYLE LTDIHSPDGY TNTGLSHSAA VGRVSYFFDL
     KGPCEAIDTA CSGSLVAVHN ACQSLRAREV DCALAGGVNA LIAPYGFMGF SQAGMMAPDG
     RCKTFDARAD GYGRSEGSGM VVLKRLSDAR RDRDIIHALI TGSAVNHDGR SQGFTAPNGL
     AQREVVQRAW KMGGYGPGDI DCVEVHGTGT ALGDPQELLA LGAVFREREA AANRVVVSSA
     KTNVGHLEAA AGIAGLIKLV LMVRDAEIFP HLHLQRTNPN IDLGSLPLQV PTERRPWRTH
     GSRRVGGVSS FGFSGTNAHV LVESVSEEEA SEATEGAEAG DGASLGEGAS PAEPPAPPLP
     LRPVQIVPLS ARTRPALTEL AGRWSRHTRE SLGDELADLA FTAATGRHHF EHRAAVVASS
     RRELEAALDA LRHGREDKNL LRGNVRPRMQ PKVGFLFTGQ GSQYAGMGRG LYEQEPVFRE
     ALEACAQGLK GQLPKGLLEV MFAGPEERTI HETQYAQPAL FSVQYALSRL WESWGVRPYA
     VVGHSVGEFA AACVAGVLEL KDALELVAAR GRLMQALPSK GSMVSVQAPV EKVREAMEAA
     GGGQVSIAAQ NGPRSTVMSG EKQAVQEVVG RLEREGYKGQ ALTVSHAFHS AQMEPMLEEF
     ERVARPVVAR PARCKLISNV TGQAFQAGQA PDAAYWRKHV REPVLFEQGM RAMAELGVST
     FLEIGPHPTL IPLARASLTS PSAEGEEQPW LWSLTRDGDD TRRMVESAAA LYAHGVELNW
     AGFHERRLAK KALLPTYPFE RKRHWLVPSN SQSKKAPKQA KGHPLLGRRL QSPLAGAQFE
     GLLSSESPAY LSGHRIYGLT VFPATGYVEM ALAALRAVVG SFPCELENVL FERALILPED
     SQRRVQLLLM PVSRENGEER FRFEIHSQPF LGDGEEEQRL PWLLHARGEA RCDTSGQAQP
     SPSLEGTGSV EFKLEGESEL APADFYRLLT ERGMGYTGPF RSITTLRKGP HGSGVAMARV
     ALPAEESPGA SPVSARHVAH PALLDGCFQA IGAALTTRFA AGNAIKMAYL PVAIERVRLR
     QPLGNEASAR VEVSLGKGLE YSAALSVFAA DGSPALEIVG LRMQGVERSR MREAASERQD
     GADILHQLVE ASPVKRWDLM VSFLANQVAD IMGVESSEIS GGLMYFELGM SSLGSVELQY
     RLQKNLRCEL PKNLVIDYES TESLAAHLLT QTFGNGSFER GQS
//

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