ID A0A2L0F1Y3_SORCE Unreviewed; 2101 AA.
AC A0A2L0F1Y3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=SOCE26_070690 {ECO:0000313|EMBL:AUX45575.1};
OS Sorangium cellulosum (Polyangium cellulosum).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=56 {ECO:0000313|EMBL:AUX45575.1, ECO:0000313|Proteomes:UP000238348};
RN [1] {ECO:0000313|EMBL:AUX45575.1, ECO:0000313|Proteomes:UP000238348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce26 {ECO:0000313|EMBL:AUX45575.1,
RC ECO:0000313|Proteomes:UP000238348};
RA Zaburannyi N., Bunk B., Overmann J., Mueller R.;
RT "Sorangium comparison.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CP012673; AUX45575.1; -; Genomic_DNA.
DR OrthoDB; 9757540at2; -.
DR Proteomes; UP000238348; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 3.40.50.980; -; 4.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020459; AMP-binding.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013217; Methyltransf_12.
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 NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 2.
DR PRINTS; PR00154; AMPBINDING.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 513..588
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1989..2064
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2063..2101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2081..2101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2101 AA; 230524 MW; D359F323B301E0DA CRC64;
MFEAHANRCP GAVAVVADDE QISYGALNAR ANRLAHHLMA LGVGPEMRVG LCVERSIDMI
VGALGILKAG GAYVPLDPAY PRDRLRFFLE DAGAPLLVTH RPRTAALPQG NAAVVDLDEH
LGAIGARSAE NPARNVSPEN LAYVVYTSGS TGKPKGVMIP HAALANCIEA LREAYELGAD
DRVLQFASLC FDVSAEEIYT CLAAGATLVL RSELMLQSTS TFLQRCAAHG VTVLNLPTSY
WHDLAADLRK ESAALPPSLR LVIIGGERAL PARLAAWREH VGPRPRLLNA YGPTEATITA
MIADLSTSPA EGPISVGAPI RNVSALILDG AMHRAGLGEL GELYLGGAGL ARGYLGRPEL
TAARFIADPF SRETGARLYR TGDLARLLPD GSAEIVGRAD DQVKHRGYRI ELGEIESALC
AHPRVRQAAA ILREDAPGDR RLVAHVALGP GVHEPRSAAE ELRAFVRQRL PDYMVPSSFV
LQEALPLSPS GKVDRAALRA PDRTGDDERG SAPPRTAVEK VLEGVFAAVL GLGQVGVHEN
FFELGGHSLL ATQVIARVRD VYRIEIPIRC LFESPTIEAL AKVVEAARNQ EHGAGLPMIQ
RAPRDRPLPV SHAQRRLWLV DRMTPDHAFY NVPQAVRRIL GPLDVTALER ALGEIMHRHE
ALRTTFAWSG GELVQVIHPH HGFSLPRVDL RGIERSARER TVLALIAEDI RRPFDLTAGP
LVRASLLELR EDEHVLLLTL HHITCDNWSL GVLFLELMSL YDAFARGLGS PLPALPIQYA
DYAVWQRAWL EGPARSAQLA YWRRELDGLP VLELPADHPR KAVPTHRGGA APVSIPKHLA
DTLARFSQRQ GVTSFMTLLA AYFTLLARYT GADDIPIGVA IANRRQRELE GLIGFFVNTL
VLRGDLSGEP TFRELVGRVR DVALRGYTNQ DLPFDELVDE LQPHRDPSRH PLFQVGFTHF
NDPLPTMELP GLELLPEELH NGTSKLDLLL LLAEAPDGIH GSLEYSAELF EPETAQRMVR
HFLVLLESIA QEPDRSIWSL PLLPADEEEL VTRVWNRTSR EYSDAACIHH LVEAQASRSA
DALAVVFEGE SLTYGELDTR ANQTAHLLLS LGVGPGSLVG IWLERSPEIV VAILAVWKAG
GAYVPLDPRY PRERLEFMLQ DARVPLVLTQ RQLAEAIPRG DVPVVCLDEE AGAIARNADT
PPETRVTPDD LAYVIYTSGS TGRPKGVLIE HRGVCNLAES LRRIFGLGPS DRLLQFASMS
FDASVAKIVM ALTAGATLYL ASREAQMPGR ALLALLRERE IEIAVLPPSV LAALPFEQLP
ALRTLVVAGE ACPPELVATW GRGRRFWNAY GPTEATVCAT AGECVDASRK PPIGRPIDNT
RLYILDRHRK PVPIGVPGEI YIGGVGVARG YLNLPELTEE RFIRDPFSDA PRARVYRTGD
LGRYLPDGSI EFLGRVDQQV KLRGFRVETG EVESILGLHP AVRSASVVLH EDASGQQRLV
AYVVLGARAA DTLESAAWDD EQVTAWKALY DEDHRRMSEP EDPTFNISEW NSSYTGQPIP
EEEMRAWRDH TVARIRALEP RKVLEIGCGT GLLLFPVAPH CEGYLGTDFS SEVLEYLGRQ
LARLEAPLPQ VSLERRAADD LGDLTPGAFD TVVVNSVVQY FPSVAYLTRV LEGAARAVRR
GGRIFVGDVR SLPLHHAYCA SVELHRAMAA LGRAALRTLA RQRMTQEEEL VIDPAFFEAL
RERIPRISGV EILLKRGRHH NELTKFRYDV VLHIEASSAP ERRAPDTFWI EWTRDWTPER
IRRKLEETRS GGLGIRGVPD ARVYADMTLV EWLTRDRGPL NAGEMRAALA ESTSAAVDPE
EMWALCDGMP FTASVRSSGG GAAGRFDVAF TRDETGTTVP WPAARGAPLG RHAAAPLASY
ANDPLQGKLT QKLVPELRRF LQAKVPSYMV PSAFIVLDAQ PLSPTGKVDR RALARREGVH
HVSTATFAPP RTKLQRDIAD VWQRVLHLDA VGVNDNFFDL GGNSLLTAQV QAKLREALGR
DVALVDLFQY PTVSALADFL ARDPRARAPG RPSAGPRSSP EDMIARHEAR AQARRTHREN
S
//