ID I1CGN5_RHIO9 Unreviewed; 1265 AA.
AC I1CGN5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=RO3G_12326 {ECO:0000313|EMBL:EIE87615.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE87615.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE87615.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00000780};
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DR EMBL; CH476741; EIE87615.1; -; Genomic_DNA.
DR AlphaFoldDB; I1CGN5; -.
DR STRING; 246409.I1CGN5; -.
DR VEuPathDB; FungiDB:RO3G_12326; -.
DR eggNOG; KOG1474; Eukaryota.
DR InParanoid; I1CGN5; -.
DR OMA; NLPHMAQ; -.
DR OrthoDB; 1366536at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd04369; Bromodomain; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR037800; GCN5.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR45750; GH11602P; 1.
DR PANTHER; PTHR45750:SF3; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT DOMAIN 489..558
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 759..1205
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 11..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1265 AA; 143269 MW; 11A07836AA9DB557 CRC64;
MQMLWKLQSL DSLMPANDND APESFNEFNQ STSTDFPDSD ELVEKLFLES MAMQQQADIQ
NEANQDVSSD NLLLESLLNA TKDDNDMTTS SPSETANVPE KRPSSPSFDE QNDRSQAIRP
KLLPAPSSLP IVSQQQQPSS GYFNASPIQL QRPIQEANIT PNSTTTSTTN NSNNNHLTMS
TNSPIPVTTS TSTPTTTTTP YQKSHESVPS APLVPISLSA TPTLTTVRLP LPNNTRSSMT
MPPPNTLPSS MLFRQLTTPL PTSSNPTSMT NGGNPLTTPM PSGGPMLPGF MRMNTGSPVS
VRKPIPPRPQ LRIHISKRKE VDPSFYDDPK DPMKPDLDVS SLRRLTVATL RTLGVYLSLE
ELPEVQIEDP LPTDSQQVLP VAAMQLITTM VLGTSGDKEV SQTLGSQISN GDLVALQRMI
VAGLRSKNIV IHTVLTDQSL PASKTDTSPE QTLLTTNQFA DLSQVKYEPP HNVTRLFLRL
YRFIINMLLS TPDCWPFIQP VPASAFVYHQ EIKQPMDLQT IEENVWAGKY TKFARFEKDI
RLIWKNARAF HNNTGTIPKH ADCLEKLFNK IVVDIKKQIS TNRKQQQVAG SHDFKFDPAN
TLPEESDFSY PPLEQVFSEQ STVYAISALS PLEPKGRKPV GLTDEKLLYL QLNGPFFQAV
EQMKSDPKSN HSIVPRFYIA KNRTLLRQIR SQGVLAIFYN TKTSRVKSTK LIRIETDMIL
AYPASDLFDI DQINEYTEDF APKAWIHLRP LRVVQHMVFE VNEAIERDYF KRMFATSKMS
VDSKGGHSMT KKLLKKVVRQ ILGLPDLPEP LEEAAPSSAS SSLSPAVDTP TGRLVDIKSL
IRTKSYPRIR RKTQEEEAMD ADEGSDDEKA SGTTPKYDKS TTSDYPQEIS NLQRLGQKEI
THDVWKRLFQ VCASKGIMIR NISDHGHINW HIPSSEGFFK RVYFLQDTVV QVFRQMTMYQ
RITEVACLMQ EVEKSTAYGP STGNIKYDVI YQMLVCMKTI HEAGLAHRDL SEVNIMVNTV
EGQYLEDGSE KVCLYLIDFG KAVFCQPQDV RDWFVDVPRA EWEYDGDVVP ETKEELDTWC
ETLPWVKGKP DHGYRMYRSI QTLPKTRSDN QVLPWLIHPQ AEDMYSIGVM IWKVFTDTEP
WRGILDTDLQ GLRYVAQDDY RIQRALEGEV HGELSRQLLL KCLRTRPQDR ETARDILDWI
SQEPIKEGLI GEWKMYSSDT RSARRAKTFY GFEEEDDEDK KKPRKKANTM SKRGRPKAQK
ELFLN
//
