ID A0A0D2SBP2_GOSRA Unreviewed; 770 AA.
AC A0A0D2SBP2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Aminoglycoside phosphotransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=B456_005G061800 {ECO:0000313|EMBL:KJB28675.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB28675.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB28675.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CM001744; KJB28675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2SBP2; -.
DR EnsemblPlants; KJB28675; KJB28675; B456_005G061800.
DR Gramene; KJB28675; KJB28675; B456_005G061800.
DR OMA; LHGGHFE; -.
DR Proteomes; UP000032304; Chromosome 5.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd05154; ACAD10_11_N-like; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR041726; ACAD10_11_N.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304}.
FT DOMAIN 43..271
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT DOMAIN 555..656
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 668..762
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 377..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 85868 MW; C385DF97829703C8 CRC64;
MANRTGDLVE AVQEAHKIDV KALFGYASAN VPGFPLSPSK FNLSQFGHGQ SNPTYLMEVE
TGSGTVKRYV LRKKPPGKLL QSAHAVEREF QVLKALGDNT NVPVPKVFCL CNDPTVIGTA
FYIMEYLEGR IFVDPSLPGV PPERRRAIYQ ATAKVLASLH SANIDAIGLG SYGRRDNYCK
RQIERWFKQY LASTSEGKPE RYPKMFELVD WLRKNIPPED ASGATGGLVH GDFRVDNVVF
HPTEDRVIGI LDWELSTIGN QMCDVAYSCM PYITQAGLGS DELVKGFEII GIPEGIPTQA
EFLAEYCLES GKAWPVSEWK FYVAFSLFRG ASIYTGVYNR WLMGNASGGK RAEHAGRHAK
SLVDSALDFI SKKTVLPEQP PSVSRGSRQY GTENKAQGLP EGSGRFVPSK KIQELRNKLI
QFMEVHIYPL ENEFNKLARS DLRWTVHPEE ERLKELAKKE GLWNLWIPFD SAARAKELIF
NGSAHCTHDR LLGAGLSNLE YGYLCEIMGR SLWAPQIFNC GAPDTGNMEV LLRYGTKEQL
NEWLVPLLEG KIRSAFAMTE PQVASSDATN IECSIKRQGD SYIINGTKWW TSGAMDPRCR
ILILMGKTDF TAPKHKQQSM ILVDIKTPGI CVKRPLTVFG FDDAPHGHAE VSFENVRVPA
KNILLGEGRG FEIAQGRLGP GRLHHCMRLI GTAERGMQLM AERALNRKTF GKYIAQHGSF
LSDFAKCRIE LEQTRLLVLE AADQLDRLGN KKARGTIAMA KVADIFSCSY
//
