ID X0BL33_FUSOX Unreviewed; 1632 AA.
AC X0BL33;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=FOQG_12825 {ECO:0000313|EMBL:EXK82860.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK82860.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK82860.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK82860.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH658409; EXK82860.1; -; Genomic_DNA.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_003997_0_0_1; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF10; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 3.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 897..919
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1071..1095
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1128..1152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1380..1403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1432..1459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 742..819
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1321..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1632 AA; 179656 MW; C7D759BD5309C735 CRC64;
MAVKQSQQFR SLVALNLDRA ELLAAIPTSQ QHSIFSLYTL CHLLEELPGS WPVFQLIKTY
TRLYTQLPED AKTNSNHELS SLIEQTSALV KSSYTSFAQF IGYDDKPALR APTDEDVITH
RELRQFVDNF QLPADASDKK PVVSIALPNG PLLAATCIAV TTYYTASPIN PAAGAEQFRA
DILQARADFI LTTKDEYEKL QLDARWVSDN NIQIFIMDWT RDEGISLRTV DGEAVPTGST
QRVANKADDI GLILFTSGTS GTKKVVPLTA HSIVAGVAFV IESWGLTATD ICLNMMPLYH
VGGLVRNIFA PIFSGGSTVC CPSFDANLFW DVAETIQPTW YYASPSMHSI IIAEATARPK
ALRKSRIRLA CNAAGGLLPS LAYQLRDTFN CVVLPSYGMT ECMPISTPPL DYRLDREGTS
GISTGPELTI LDWSEQNVTN GTVGRICVRG EPVFPGYLKP DGTYDKSPFN EHGWFDTGDL
GYMDDDGYLY ITGRSKEVIN RGGELISPFE VENAIMTASR ASESAIYGRV SQALAFSASH
DVLQEVVAIV LVTPPNVPRV DMRTLHGALK SSLQQAKWPV LITYMNDVPK NNNKVLRIKL
GQRLGLPSVS DDTPYMSRHW DAVCPPADTP LSEAIQCSPC SVDYTKLASH IQTIVPDLDV
FCLPSTHDGS PEAVLAPKAE ATVDSDIASS IRHQLASIID NYMIPTEIHL MPRPFQKDSS
GNIDVEVLHA ELEQLQMASM NELAASTEGL VTKAFAEVLS IPPADIPRDA DFFSLGGDSL
RAGRLLSTLR AEFSISLPIT AVFNGGTVTS IAAHIDKMLH SKTDVSDQPS AIVGCTETCS
STNPFLMILQ LFPLVIFYPL RRAVQWTIFF VTLAHSQKLP TNHSLPGRFL NLTVSMLIAR
IIMGFVSPIV GIICKWLIIG RYRAGLYPMW GMYHTRWWLV QKIVAICGKG FFDANEMTER
IYCRLMGAKI GRNVKLEGAA LGEWDLIEVG DDCNLTKCIC RPFAAEGNTS MYLGRITIGS
NCSVGMSSIV APGTNMPPDT CLGFNSSSWE MQDASEEYRD QLPSEKPKPH WVLNLLFTMP
LKLIGLFLSA VPWMAGLVGM VTTQGQTVNH KAPLRSSVDW FTQPNRIAYH YLALALGCLF
GPFFLFGFVI LVKSVLDCIF GKLKANSRNT VDIWRANLIK MLLPEGKLHR MTSLFGQHYE
ATSIALRMLG AKIGERVYWP GTGPSIGDYH LIDVGNDVVF GSRSHLVTSD GIGSEKVTIQ
DRAMIADRVC LLPGVTVGER TTMGSGALTK RNGNYVSDGT YVGSKAGDAV CLSTGSDTKV
SRSHIRNMQS EDTLTNEKER PDTQPSITSG SDTEGSDGKG DWAQHLSPFG RAFYLKLAPY
HVLGPFAIFC YSGFFTVFTA VYWDVPSVSS IQFVGIMFRS SFPRGMNVWF DLVAIFLTML
AGIAVLSTIQ SVLALVIIIG SKWLLMGRRT AGNYDWDKSP YCQRWQIFLG IERLRRHCYK
GNGILNLLTG THWMVIYFKL MGAKIGKDCA LFVNGTPSLM FTEPDLITLG DRVVVDDASV
VAHINTRGKF DLNRVEIGDR CVLRTGSRLL SGAQMKSDSC LLEHTLIMGG DIVEERRTMQ
GWPAEEFSGK RI
//
