ID   I1BXD2_RHIO9            Unreviewed;       749 AA.
AC   I1BXD2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=RO3G_05567 {ECO:0000313|EMBL:EIE80862.1};
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:EIE80862.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE80862.1, 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).
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DR   EMBL; CH476735; EIE80862.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1BXD2; -.
DR   STRING; 246409.I1BXD2; -.
DR   VEuPathDB; FungiDB:RO3G_05567; -.
DR   eggNOG; KOG0379; Eukaryota.
DR   eggNOG; KOG4236; Eukaryota.
DR   InParanoid; I1BXD2; -.
DR   OMA; STQTWDT; -.
DR   OrthoDB; 1362104at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd00180; PKc; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR46093; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 5; 1.
DR   PANTHER; PTHR46093:SF17; MULTIPLE EGF-LIKE-DOMAINS 8; 1.
DR   Pfam; PF13418; Kelch_4; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        271..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          536..749
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          301..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   749 AA;  82236 MW;  10022591A9580A3B CRC64;
     MALGTIQQFS WSWSFPTTNF QASTAKVAGY SIVTVDNTIY TYGGVAVDNN GYPNTNAVQN
     TLSFLDAGSF QVSTGSNGIG LTDHTTCYLK KLNSLITFGG STTGSSTGVT DAVNIYNLSS
     KVWNVQGLST LTAPAARRLH TANCLDDFMI VFGGGTSQPF DSDIWILNAT SYPNMFWQRM
     SVANQTESPN PRMGHSSVLD SENNKLYIFG GWGVTGTNDS NMYVLDISHW SWTKVPTTGY
     AKNQVTTPSI PPLNTTATTA TSENHQNKAG IIAGATVGGV VFLALLALAL FFFKRRSRKE
     QEKDVTSSTH EDEQYVDKTS LPSDSYGRPP YRMSKAWSST SFAKHSEIGD YSDRVVTGVL
     EAVTDAGTVA ATHGSSRDSF RHSKTLLEIG PGQVPNEIIS QKPNEFSVLI RPKHDLQVDH
     HRAALDDEDW TLPDSPLSPV QYIQTSSKPS IGTNSTWDTT EARRKVVTHH HPSSSIMTNT
     PVAQTVHIQD EEQSRPELYN RMSPLDLLAS LGQHHHTESS GQSNSSGESF TILKSPSTSS
     SISDGLLTPI ISLLPKRYQI DPTLPPIIGP SNSILFANDN ITKMPVTIKL FGRREAWERE
     CRALTKLKSP WVVELVEVLT LQKKENEEEV KYVAVMERLS ETLNRKKNIM PQVVASHLLR
     ALAYCHNYRI AFCDLKPSNV MHVDGTWKLI DFEASRTIEE ECVGVMTPRY CAPEVAKATT
     YGLEGASGVV ATASVDLWSL GCLIYVSFQ
//