ID A0A1Q6YDR2_9CHLR Unreviewed; 782 AA.
AC A0A1Q6YDR2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=AUH05_13575 {ECO:0000313|EMBL:OLB36052.1};
OS Ktedonobacter sp. 13_2_20CM_53_11.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805233 {ECO:0000313|EMBL:OLB36052.1, ECO:0000313|Proteomes:UP000185646};
RN [1] {ECO:0000313|EMBL:OLB36052.1, ECO:0000313|Proteomes:UP000185646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLB36052.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNDA01000382; OLB36052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6YDR2; -.
DR Proteomes; UP000185646; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 5.
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; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44943; CELLULOSE SYNTHASE OPERON PROTEIN C; 1.
DR PANTHER; PTHR44943:SF4; TPR REPEAT-CONTAINING PROTEIN MJ0263; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00515; TPR_1; 3.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13432; TPR_16; 3.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 13.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50005; TPR; 11.
DR PROSITE; PS50293; TPR_REGION; 4.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT DOMAIN 48..307
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 374..407
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 408..441
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 442..475
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 476..509
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 510..543
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 544..577
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 578..611
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 612..645
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 646..679
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 680..713
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 714..747
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 762..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 782 AA; 87143 MW; 88E6583D7FD5FB69 CRC64;
MTTEELFCET CGAANPPTAH FCQYCASPLP FTHGTGDLPE QTLLIGRYQL LSRIGQGGMG
AVYKASDTRL DDRLVAIKEM SKAGLPAAGL EEAEAAFERE ARLLGKLLHP NLPRIHDHFT
ENDRSYLVMD FIDGETLEEY LDKRGHDPLP IERVLDWAEQ LCDVLSYLHN HQPPIIFRDL
KPANVMISES GHIFLIDFGI ARLFKPGQSH DTVALGSPGY AAPEQYGKAQ STPRSDLYSL
GALIHCLLTG DDPSERPFFF RPASQANPAV PHALEALLQR MLEMDAERRP ASAQEVLQAL
RADDAALHAQ PGLSNQYMTS ASRIGYSYGG ASTNTTPSGA DLLLEEAHTL YTQKRLNEAE
KVYTQALQLN NTNPLGWQGR GLTQGLLQRH TEALNSFDRA LQLDPSLVIS WNGKGTALST
LQRSQDALAA FDRALKLEPN NASSWNGKGA VLNALGRPKE ALDAFDMALR FDPHLAQAWN
NKGLVLRQQK RAQEALSAFD MALTYDKNIA TSWSGKASVL HDMGRLQEAL DCYQQAINCN
PQLVSAWNGK GSVLYDLGRY KQALQAFQEA LKLDKNYAPA CYGMGNVYYI QQKLKLALDM
FDRALRSDPN YARAWNRRGN VLNDMGQRVE ALKSYDQALR FDPRFASAWN GKAGVYAQLE
RYTEALHAYE NALRINPNFA QAWNGQGNTF YHLNNYAQAL AAYERAVKLN PQMASAWHNL
SLVLKRLKRN QEALDAAEEA IRLAPNDPDN WIRKAEALKS MRRSRDAKDA EKQALRLRGA
VR
//
