ID A0A0F3GWF2_9BACT Unreviewed; 878 AA.
AC A0A0F3GWF2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:KJU84998.1};
DE EC=2.7.-.- {ECO:0000313|EMBL:KJU84998.1};
GN ORFNames=MBAV_002808 {ECO:0000313|EMBL:KJU84998.1};
OS Candidatus Magnetobacterium bavaricum.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Magnetobacterium.
OX NCBI_TaxID=29290 {ECO:0000313|EMBL:KJU84998.1, ECO:0000313|Proteomes:UP000033423};
RN [1] {ECO:0000313|EMBL:KJU84998.1, ECO:0000313|Proteomes:UP000033423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM-1 {ECO:0000313|EMBL:KJU84998.1};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJU84998.1}.
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DR EMBL; LACI01001200; KJU84998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F3GWF2; -.
DR PATRIC; fig|29290.4.peg.3717; -.
DR Proteomes; UP000033423; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR44129; WD REPEAT-CONTAINING PROTEIN POP1; 1.
DR PANTHER; PTHR44129:SF13; WD REPEAT-CONTAINING PROTEIN POP1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 4.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KJU84998.1};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Reference proteome {ECO:0000313|Proteomes:UP000033423};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KJU84998.1};
KW Transferase {ECO:0000313|EMBL:KJU84998.1};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 1..211
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 464..506
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 507..540
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 555..596
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 597..638
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 639..680
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 681..722
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ SEQUENCE 878 AA; 96240 MW; D58AF685321DAAD3 CRC64;
MAIQFAIGLH YAHEKGLVHQ DIKPANVMLS DNGIVKVTDF GLAKARALTD NKSVDMDISK
GALVSYGGMT PAYCSPEQAS SAERAMSARV SSARSNSALP VSAQQTIITP HTNSPFLEAG
LKPLSAKTDI WSWGVSILEI FVGGITWMTG SIADIALENY LGQGPEDNVI PRMPPEIIEI
LRRCFQKEPE DRPDSMLEIV EELKRIYHNI AGKPYPRTQY MVGRVTADGI NNRAISLLDL
NKTSGIDSLW KEALKTDPLH FESTYNLALY EWKNGAITEK DVMRRIKAIT TKRHMNWREY
HLLGNMYISY GNYSKAVDAL WKAVEPQRPA AAEIKDLALA LCAYGKAFTA TAGSKDPAAI
TLWKDVERQC RIIIDNIPDQ ERILNRGRLT PTATEKNRDC PGAETKATKS IDPHIVAAYT
LALTRQGRQR EACEFYTLYG TGMPSSMTEA FHRYLPGFEL LYTIEEHNGV VSSIAITPDG
TRVLSAGSDD KTLRIWDIEE GKCLTTLYGH TDWVTCVCVT SDGRFAISGS NDKTLRLWEI
GPSVENTTGR CVRVLSGSTD GITAVAVTRD SKYILAGSND GPLLLFNLAT GARLRTYEGH
GGRITSVAIT SDSFYAIVAG TDKKVFLYNI VTGKLLRTFT GHSGSVTSIA INSSGTLLLT
GSEDKTLRLY NISTAECVHT FIGHTGEVLC VALSADETLA ISGSKDETLC LWDIRSRQRT
VLFKKFEGPA LAVTPSAQRA VYGIWNGIKI LEIANRYSLS YAIAIPVSSV EAEEREAAFK
KEVECAKSLI QGNNIMEVPA IIKKATAVTS AECHQKTLNS VLVPISHRRM ALSSPPDRAY
LLSELTASAL MAPSCPVRYL TFHADEMFCL GNRDDISS
//