ID A0A135VJB0_9ARCH Unreviewed; 1238 AA.
AC A0A135VJB0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AM324_00720 {ECO:0000313|EMBL:KXH72757.1};
OS Candidatus Thorarchaeota archaeon SMTZ1-83.
OC Archaea; Asgard group; Candidatus Thorarchaeota.
OX NCBI_TaxID=1706445 {ECO:0000313|EMBL:KXH72757.1, ECO:0000313|Proteomes:UP000070043};
RN [1] {ECO:0000313|EMBL:KXH72757.1, ECO:0000313|Proteomes:UP000070043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMTZ1-83 {ECO:0000313|EMBL:KXH72757.1};
RX PubMed=26824177;
RA Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT phylum with pathways for acetogenesis and sulfur reduction.";
RL ISME J. 0:0-0(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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:KXH72757.1}.
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DR EMBL; LRSK01000204; KXH72757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135VJB0; -.
DR Proteomes; UP000070043; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 7.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 8.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR NCBIfam; TIGR00229; sensory_box; 8.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 6.
DR SMART; SM00091; PAS; 8.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 8.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 7.
PE 4: Predicted;
FT DOMAIN 17..78
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 128..198
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 203..254
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 255..326
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 329..381
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 382..421
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 629..703
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 708..758
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 779..831
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 886..960
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 965..1015
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1033..1237
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1238 AA; 139203 MW; 3AAC5CDA445E85AE CRC64;
MQSEPWTETI SSGVLCDLMS EGFLVVDESF TVRYVNEPFA AMIGFSKEEI KGRSVPELVH
AASRRQIEDS LTESSNKTLS GLVIDWATRS GNQVTTSVRL GSFADSERNT RWGFVLTSEQ
TQQTLSEDEA RYRLVYENLA DGVFRTDQDG TILMSTAKGA EIFGYTVEEL EGKSFTMLLH
PDDMPAILHA FAESRDRMET VPGGIEARGV RKDGSTIHFH TTNSVLIKGG EFQGYQSLIR
DVTIRKEAEE ALRESEELYR GLIDTSPDAI TLTDLEGNLV FVNDQVLRLH RASSREELMG
ISAFDLIAEE DHERAMENLK RTLAEGSIRN VRYTMLRRDG SRFPAELSAA VVRDAKGNPK
SFIGIVRDVT DQVEALADLR ESEERFALFA ENIPGPVFIK DEDSNMLYAN SFMRGRFGIE
EWSGKNTIEL FPEELAAAMI EDDRRTLKEG PTQILQRVPD KDGVIHSYRT SKFPIRREGK
PTLLGGVAFD VTQIDRAETA LRESEEQYRT TLLAIGDPIH VVDSDLRVVL SNPVLENWIE
ELGFDPDILG KRLPEIFPFL PNNVLDEYEM VFENKETLVS EERTLIAGRE IFTEVTKIPI
VRKGEVEQVL TIIRDVSEAR TAELALKGSE TKYKQLVEQY TQGVAIVRGP PLSIPFANRA
FGTILDMIPD DIMNLTSDQI QELIHPDDYE ELTSRFADLL EGDPAGNAPK EFRVVRPSGE
VRFVAVLGRR VEYEGQYVIQ MAIEDVTERL RAERELRKSE ERYRSLVENL LQGLAIIQDG
TYMYVNPAFA ETLGYSVEEL LEFTEDDVWG IIHPDDRGEL QRRNETLAIG GEISPRHRFR
YLREDGSVRY VESFVQQIEY EGRPALQVMD IDVTGQMMSE KALRESEAKY RQLVEQSPLG
VLIVKGLPIE IAFANNAMVE MTGHSLEDLL SLSAQDIERL VHPDDFKPLI EMFANILSGE
PPLEAPVALR VIRSDGKMLW VEAVGHKILF EDDIAIQATI VDITERVVAE RERKRAEMEL
KTAADTSMLY LDLLGHDTRN KLQAIQMSIE LLQFDETRPE AFGVIDRIMD LVQSAEALID
KAHATRGLLT APLEPTSLKD ALVAAVGALK FKHDNVEVRV DYQVDEAIVK ADEYVGHLFT
NVLENAILHN PAEIKNVWVS LKEEGAGFEV SIADDGAGIG DAMKGAIFDQ DRRYGGLGLH
QAKRILAKYG GRIEVLDRIE GEPEKGALFR LWFPGSIS
//
