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Database: UniProt
Entry: S2JF36_MUCC1
LinkDB: S2JF36_MUCC1
Original site: S2JF36_MUCC1 
ID   S2JF36_MUCC1            Unreviewed;       603 AA.
AC   S2JF36;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=HMPREF1544_04714 {ECO:0000313|EMBL:EPB88479.1};
OS   Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS   agent) (Calyptromyces circinelloides).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB88479.1, ECO:0000313|Proteomes:UP000014254};
RN   [1] {ECO:0000313|Proteomes:UP000014254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KE123950; EPB88479.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2JF36; -.
DR   STRING; 1220926.S2JF36; -.
DR   VEuPathDB; FungiDB:HMPREF1544_04714; -.
DR   eggNOG; KOG0590; Eukaryota.
DR   InParanoid; S2JF36; -.
DR   OMA; KHAIHQF; -.
DR   OrthoDB; 5318028at2759; -.
DR   Proteomes; UP000014254; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd13994; STKc_HAL4_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24343; SERINE/THREONINE KINASE; 1.
DR   PANTHER; PTHR24343:SF137; SERINE_THREONINE-PROTEIN KINASE RTK1-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EPB88479.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000014254};
KW   Transferase {ECO:0000313|EMBL:EPB88479.1}.
FT   DOMAIN          273..536
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..152
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   603 AA;  68077 MW;  B8233B50670367F7 CRC64;
     MSTNDVTVPS SLKHSAASSH HRPADSDAYT PDRRSTGSIY SSANNISSLS ERLREVDFES
     PAKIFQNKHA IHQFENVTPD ISAPGTPAIA PSTQFGYDSA ENNASSGAHT PRSQHSPSSA
     HTPRSASPEY AEDGAHRKHH HKHHHHHQHA SAKPSHPATE ASSATDYTSS SARPTSAIGS
     ATISRTSTPA QFVFKKPEYN SHYHHTHFHH LEKKDTIFHD LKRFFKKNQD KKKKKHLLDD
     TSSVRSSGSS VYSRQSDLSF ANEFNKNLEG RYGKWGEFVG KGSGGSVRII RRNTDGKTFA
     VKEFRKRAPG ENEKEYVKKV TAEFCIGSTL HNFNVIEALD IIQEGQSFYE IMEYAPNDLF
     NIVMSGKMTQ DEISCCWRQL LSGVKYLQSM GIAHRDLKLD NMVLDERGVV KIIDFGCATV
     IKYPFEDHVH LSKGICGSDP YIAPEQYTQK EYDARKTDLW SCGIIYICMT IRRFPWRLPR
     PEKDQSYSNF VQPNNIGAEK LFKLLPRYAR PIISRILLPD PEKRCLLEDV LDDTWVKSIE
     TCTPEQPAGN HPHHLLFEPS KEIMERGNII VLPAPKKEED SANNTPAVEK KKKTPDHHNR
     SKK
//
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