ID A0A1L9Q0W8_ASPVE Unreviewed; 2086 AA.
AC A0A1L9Q0W8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=ASPVEDRAFT_177948 {ECO:0000313|EMBL:OJJ07366.1};
OS Aspergillus versicolor CBS 583.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJJ07366.1, ECO:0000313|Proteomes:UP000184073};
RN [1] {ECO:0000313|Proteomes:UP000184073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV878137; OJJ07366.1; -; Genomic_DNA.
DR STRING; 1036611.A0A1L9Q0W8; -.
DR VEuPathDB; FungiDB:ASPVEDRAFT_177948; -.
DR OrthoDB; 2787863at2759; -.
DR Proteomes; UP000184073; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd05918; A_NRPS_SidN3_like; 1.
DR CDD; cd19542; CT_NRPS-like; 2.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 3.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 3.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45398; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR45398:SF1; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 3.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 6.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000184073}.
FT DOMAIN 28..104
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1557..1633
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2086 AA; 231102 MW; 615152D5F1A9106C CRC64;
MAVSTSQVPT DVLSLVHGQL DDRLQVGKDV PSILEQVQDA WASVLGIDPG KIRADDSFVS
LGGNLISALR CVEKCAALGI RVTVGDIFQS QTIAGLIENH APHESRLQGD LTKCVRLSPI
QELFLTANPV EYGQYNQTVV LRLNQPMTPE DILAAANSLV KRHAMLRARF TMSPDGEWTQ
MVTEETTQSF RCQHHQIASA VEIQDINACS SRSLNIHDGP LWIVSLMDES NGTGQYLSLI
VHQLVVDAGS WSVILADLKR LLESGTSPQG SSKPFLTWVS EQAQYAEANL LQRKALPASH
ISEAEQVNEY ECSGIPNTVD DSNLYSFTLD KSITNSLLGD ANNPLNTEPS EIIQGCILYA
FTQVFTDRPA PTIYVEGHGR EPWTDTIDLG STVGWFTTIS PTYIETAPDE ALTGLIMRTR
GSRRQLPANG WAYFTSRMLK QDGRKAFDAR RPFEILFRYT DITNLSYGTD SPFSVKSVHI
PGATSGGMQR LSLVEVNALA GSNGLVVDIR INKHMENQQR LQQWVGICEN TIKDAVVELN
VLCLKHKLSD YAVREERLRY LVENLLHGAA SIEDIYPCTP SQRGILLSQL RDPQQYYNRY
TVEVLPANGR PAVDPWQLAR AWKRVVARHA ALRTILVTVN NDDILDQLVL KDYAPEVPII
LEAGMTDFAQ GRKQDYSNRA DDLRPTTKAT IYVEPNGRVI LDMTISHMFV DATSLQVLMR
DLTLAYGGNL DLANRPLFKD FVLEIGEQSD KDQYWKRYLE GVKPCHILSN NTLLAAPLPS
THAKMQYIRM EQFLETRELK AFCARHGLLL TNILHVAWGL VIRCYTAMDN ICFSYTTSGR
ERAVPGIKDC VGLFVNVLIR RLTFDDEQPV LDVLQSTQKS FLESLAHQDC SFANIQHSAN
LVGQSIFDSS LSIHYHEAAE KKAVNPAIIL RRLDADGITE YPIVLNIAVD QEDVELILSY
WNTAMTRDFA TTIAQTYHQV IMEILQGQCR VGEIDILPPV SRNQIAKWNQ NVPQEFMGCV
HDLVDAHVVQ TPQATAVCSW DGCMTYKELD NMSTRLAADL VIHGVGPGVF VPVCLEKSKW
VPVAVLAVLK AGGAFLLLDL SVPQYRLREM CLSLEVSLVI VSGKSTALAP VLAPDWIVLS
ETYLGGDQDR CNTKVTNADI SPQSPAFVLF TSGSTGKPKA IVTEHRASCS QLADHGRIFR
LGPASRVLQF SSHSFDVACI DILSSLCTGA CLCIPSEEAR LNRLSEVAAS FGVTYMCTTP
SVARLLDQAM IPTLKTIVLA GEPACRNDIV TWGSRLIIGY GPAEGGIATV RSPVSLDQEI
TNIGKAIPGA RTWIVNGDNH NQLLPPGAAG ELLIEGPVLF RGYHNDPEKT QCNLISSPAW
SSLFDIPAHH RFYKTGDIVH YADDGSLVFQ GRRDDQVKLR GQRIELQEVQ HYVKQSFADV
DEAVADIIKP HGDVQQEALI CFVLPLDAEK RRVASQNHPQ MPFLPPSETF RTEARAAVAK
LQELVPQFMV PAIFLPLAYL PVTSSGKVDR KAIRKKAQGL TILDMEPYSV AQLTRRGPSG
QVEETLHAVA SSLLNQPPDS LGVDDDLFRR GLDSISLIRY VGLLKREGLQ LSVSDVFNHP
RISDLALLVK DVEPQSKGDS DGPRKGMIRF RALQGMAHSL KGPLRFEIPF DMATVVDILP
TTGFQREYLR GSHQAYFAIH LSGHPNLVRL QAALRAVLES HSSLRTSFVS VNDTIIQVVQ
HPFDFSVREI AAKDQDCKLD VHQVCREDVA VPVPCGRQYF QPFLIRETKD HSTLVLRLSH
AQYDGWSIPL LMRDISRCYC DDQLVPPPTF SDFMATRESL LNSPSTYETW ASILRGSSMT
FIPTSGLSES PNSDDQDAII ERQCTVSMRD SPAATVAILH KAAWCLVLAR WADTRDLVFG
QVVSGRNLPM DGIEELVGPC VNMIPVRIKL EDAWTVQDLL DTLLQQHIQS LEIEAVDLED
IVERSTAWPK GTCFGSVVQH QNIPGLDGPP FSLGELSGRL AIHAFNYLPA YPVIYSEPTG
DDQLTLRITA NSRLMDAETV SALLKDFKDI LIRLPSSLDQ IITALE
//