ID A0A177BW29_9PLEO Unreviewed; 895 AA.
AC A0A177BW29;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Putative polyketide synthase PksJ {ECO:0000313|EMBL:OAF98539.1};
GN ORFNames=CC84DRAFT_1238472 {ECO:0000313|EMBL:OAF98539.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAF98539.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAF98539.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAF98539.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV441567; OAF98539.1; -; Genomic_DNA.
DR RefSeq; XP_018028905.1; XM_018183941.1.
DR AlphaFoldDB; A0A177BW29; -.
DR STRING; 1460663.A0A177BW29; -.
DR GeneID; 28767427; -.
DR InParanoid; A0A177BW29; -.
DR OrthoDB; 3149897at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
DR PANTHER; PTHR24096:SF428; DIDEMETHYLASTERRIQUINONE D SYNTHETASE TDIA-RELATED; 1.
DR PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT DOMAIN 532..609
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 895 AA; 99575 MW; 241EA141E1892056 CRC64;
MYILNNTNHP ERLSYRELRD EATVNANALK HHGVCAGQIT LVHFQSHREN MIWFWASILA
SCVPALSTPL VNNHEGRLSH FSHLHKMLLD PLVITSKELL RTDFAQNTVL RCVAAETLET
PTPPKPSIEQ LTQESTSLHD VAALMLTSGS TGSAKAVCLK HEQILAACRG KLSHMPLAPK
DTVLNWIGLD HVGSLTELHL TAMVAGCDQI QVATADIITD PLLFLRLLSK HKVARTFAPN
FMLAKLQQTL DSAAASDTSG IDLSHLRYLI SGGEPNGVET CVQISTHLQK LGAPTPNIIT
PGFGMTETCA GSIYSRDCPN VDVASRTEFT ALGTCIPGID MRVSEGGLEV RGPIVFQRYF
NNPEATKAAF TDDGWFRTGD TATIDASSVL RLVGRSKDLL IVNGVKYLPH ELEMAIEQAE
IAGVALSCVV CFAYRPADAT TEHIQIVYER AYDTQDIEAR MRALQGIIRT VASFTGAQPR
VLPLSPGILE RSTLGKLSRA KVRASLLKGD YRGEIDINTE ALQMYREQHA RQPDSITEKR
LIKVFRDLEL GSLDMGIDTP ILDTGVTSVD LIRLKRVAQD TFDIKDIPLI TIMTYTTIRT
LATAIEVLQG SQAQRTTSYD PIITLQPNGD KTPLFLVHPG IGEMLVFLGL VQYFPDRPIH
AMRARGLNEG EQPFTSQDEI VTEYHRALKA KQSQGPYALA GYSYGSMLAF EIAKLLEKNG
DIVQFLGSFN LPPHIKTRMR TLDWTAGMVH IAHFCSIITE QRSEELMLEL RPLPHEQQVA
LLLAESNPKR CAELALTQAG LHNWTDVSWS LQRIGWDYEP SSDVSHMDIF YCQPLKTVAK
NRVEYRKNHL NRWVNFIRND LKFWEVDGEH YTMIGPEHVP KFQQTLKMAL AARGL
//
