ID A0A2V1D7Y8_9PLEO Unreviewed; 1632 AA.
AC A0A2V1D7Y8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=KR-domain-containing protein {ECO:0000313|EMBL:PVH93269.1};
GN ORFNames=DM02DRAFT_697086 {ECO:0000313|EMBL:PVH93269.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVH93269.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVH93269.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVH93269.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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DR EMBL; KZ805602; PVH93269.1; -; Genomic_DNA.
DR STRING; 97972.A0A2V1D7Y8; -.
DR Proteomes; UP000244855; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR Gene3D; 3.30.70.3290; -; 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; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF49; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000244855};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1542..1619
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1632 AA; 180002 MW; 946473B93020F4C1 CRC64;
MKEVGEKYEA LLERIIASSC PKIPFYSTVL NTVIKEKGVL DSAYWRKNLE SPVLFNTTMK
ALLADHKSNN LFLEIGPHSA LAGPLRQILK KQQPEAIYIS TLSRGGDDTQ SLLTALGNLF
LKGIPVDLGP LNQGGKIATG LPSYPWNREE TFWEESRISR EWRMRKFPRH DLLGTQVVEG
SAMAPTWRNV LSLDDAPWIR DHMVNQDIVF PGAGYVAMAG EALRQVTGAE DFTVRNLTVK
AAMIVHEHIS TEIVSSLRPY RLTNSLDSTW YEFIVYSHNR SNWTKHCSGQ VTQGEADSKA
VSDAPSVVVD LPRKVSSARW YQAFSKVCIK YGPMFRGLHN LSAHPVDHRA VATVGNYVNP
DDSPYQLHPT TMDFALQLFS VAAYRAQPRE FVRMLLPSYF GEIYMKRPAS NTELKLSSDA
SVTARGAIRG DAFGTVGDQV VMKLRDVHLV PAADDSAADT DPHAGVRLQW KPDIAYLDAT
NLIRTKRSIQ SSFSIVQRLL LLCSIESTER LADLPPSAVA HLNKFRTWLS GHVQQAIDEG
YEGVDDASSL YTLSSAERLE LINETANQVA NSDSAPLGKA IMQVFENCVD IFTGKADALD
LLMQDEIMRK TYDLLAGFWD FSDFLGLLRH KKPNLKILEV GAGTGASTAV ILDSLLSGSG
ERTFQSYTYT DISAGFFVQA KERFKNVPGM EYSVLDVSKD PAKQGFELEA YDLVIATNVL
HATEYIGETL FNVRKLLQPE GKLILQELCS STKWFNFIVG VLPGWWLGDK KISLLSSSST
SSVAIRLSKS LVLQGYQVEF CSLADAPKPK QDIISILDLE GKPFLEKVPE DEFAFLQNFI
SGAISSGMLW LTKSAQMGTS EPQYAQILGL ARCVRNELSI DFATLEIDDV EDDNTFERVV
QVVGKFQTRN KDMDVGLDFE YAISKGVVHV PRYHWISVSN ELSSTKKTDA PKTLEIGKRG
ALKTLGWVER PQSKLIGDEM YIKIHAAGVN FKDVLIAMGI VDGNLNDGSG LGCECAGVVT
EVGPEATFNV GDRVAIVLIQ SACGGIGIAA IHICRMIGAE VFATVGSDEK VAYQMETFNI
PQNRIFNSRD SSFLPGIMRE TNGYGVDVVL NSLSGDLLHA SWKCLAEFGK MLEIGRRDFV
GQGNLPMDPF EANRIFYGVD LALYVEKRPL TFRSMLDRAM EWCSQGLIHP IRPVKSFDAH
EIEDALRSMQ GGQHIGKFVI KFPDDHTKLP ASRGTNRIFL RPDVSYLLVG GLGGLGLSVS
TWMVEHGARH FIYLSRSGDK GKKDAAFAHE MQVAGCTVEI TAGSVINKAD VQKVIAQAKY
PIAGILQMSM VLNDASFPIM THEEWQNAVL PKIDGTWNLH EVFASQPLDF FVLFSSFAGL
VGHMGQSNYA SANTFLDAFA QFRHSQGLPA SVLDISVIED VGWVSQEPAR LERMKSTAAY
CLKEKDLLDA LGLAIYKSTP HNQEAKTGVA GYVNESQIGI GLRTTMPIAL DANRCIWKRD
IRMSQYQNLE DSSVESSNSS NDGLRQFLAS VTANPEILHE DASITSLAEE IGATLYSFLM
KPIEELDITE PLASLGLDSL VAIELRNWSR QKLGVELNVL QIMGASSIKK LGQTAAQGLL
VKLGVVVKEN GH
//
