ID A0A2G4SVK4_RHIZD Unreviewed; 694 AA.
AC A0A2G4SVK4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=RHIMIDRAFT_292096 {ECO:0000313|EMBL:PHZ12800.1};
OS Rhizopus microsporus ATCC 52813.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ12800.1, ECO:0000313|Proteomes:UP000242254};
RN [1] {ECO:0000313|EMBL:PHZ12800.1, ECO:0000313|Proteomes:UP000242254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ12800.1,
RC ECO:0000313|Proteomes:UP000242254};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR EMBL; KZ303849; PHZ12800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4SVK4; -.
DR STRING; 1340429.A0A2G4SVK4; -.
DR OrthoDB; 5475340at2759; -.
DR Proteomes; UP000242254; 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 Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 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; PTHR24346:SF93; KP78A-RELATED; 1.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 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:PHZ12800.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000242254};
KW Transferase {ECO:0000313|EMBL:PHZ12800.1}.
FT DOMAIN 34..301
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 694 AA; 80294 MW; 5EFBACC7A81F9A0B CRC64;
MSHVSHSVPP VQFSDRTVRR SRSRHQVQQI GNYVIYKKTL GSGSMGTVKL AESLSPKDHQ
LYAVKIMPKI NLDLPVNGNS KDPKDTPRER EQRTVREMAI MHLLRHPNIC QLKEWIIHGD
HYYMFLEYIE GGQLLDYIIG HGKLREKLAR KFARQIASAL DYCHRNSIVH RDLKIENILL
TNNEEIKIID FGLSNIYSPR KLLNTFCGSL YFAAPELLQA KNYTGPEVDV WSFGVVLYVL
VCGRVPFDDT SLPALHEKIK AGQVEYPDHL SRECVDLLSK ILVVDPRKRE TLSNVIRHPW
MNKGYDELVS NHLPHRQPLH KIDRQVVQGM QGFGLGLPEE IEHKLEQIIR SPEYQYAAKQ
IDQNYQGNHN NTESSQQQQQ QQQQHNSLTR WRRTVSIRRT ASSLHSKPRD DPQSLPAMYD
PLISIYYLVK ERRDFDEKIR LLESEGYQSP VQLGRSASTS LSKSTKESNS YLTRRKTERV
APSHTRQVFQ QHNEEDWAAP TNHSTTVQKN SSKSSSNLLK RSKSAAKRLG AMLPTRGGSH
ESIEDGSLKQ KTMNILRSNS VAHRNKENNN SNSTGRFVEE TEVTIPPNIS TYPKSLFNFN
RRHLFKVTAK EMIEYVERVL RWKNIFYKQE EPFVFKCEIQ DEAIEKEHVV FSLMIYQARW
ANGRLGIKLL ENENTKTVSI YHEILNELNS LINK
//
