ID A0A1C7NIL9_9FUNG Unreviewed; 2404 AA.
AC A0A1C7NIL9;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=mak2_0 {ECO:0000313|EMBL:OBZ88971.1};
GN ORFNames=A0J61_02979 {ECO:0000313|EMBL:OBZ88971.1};
OS Choanephora cucurbitarum.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC Choanephora.
OX NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ88971.1, ECO:0000313|Proteomes:UP000093000};
RN [1] {ECO:0000313|EMBL:OBZ88971.1, ECO:0000313|Proteomes:UP000093000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ88971.1,
RC ECO:0000313|Proteomes:UP000093000};
RA Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT "Choanephora cucurbitarum.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OBZ88971.1}.
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DR EMBL; LUGH01000121; OBZ88971.1; -; Genomic_DNA.
DR STRING; 101091.A0A1C7NIL9; -.
DR InParanoid; A0A1C7NIL9; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000093000; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OBZ88971.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000093000};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 8..378
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1838..2063
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2252..2375
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 841..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2377..2404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2304
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2404 AA; 268954 MW; 09BAC1C80387F448 CRC64;
MSNSGSTGSL TDSTGHSIFG DILQIPNYHF KAAPIPSLAH GENVDIVFGY RISNKKPVVA
KVSPNSLRLE REYYIMKRLY QLGDGSSFLV RPLEYIHLPS GLTIVIYADE GQNYLEYNKR
HSEDSIILHR NVHSDKASSI SSENSINFYE ERRRAQNKPT FDNDLVQPLP SAGLPAILNG
GPAFDLGTFL RFAIKCTDCL EFIHRNNVVH GEIRLSAFQW TGEDSARVKV WNFGSGSRSL
ENYLTSEGWR KTATNKESMG LLQNLLVYMS PEQTGRTTYI PDHRTDIYSL GIVFYVLLTG
KSPFEGGPLE ILNGILSRKI PLIHETQLEV PEVLARIVEK MTHKSPEDRY SSAYGIRADL
KECLKRLRFA SESAHEVIES FPLAERDVAS VFTLPKAIYG RQGTIVELTY IIQRVAGVYK
SIRNRREKSH STTSTLPTIT SENFHISNAS VSEGSLSDRL STNDTNSIAG GTVGAGTKSN
ASPSYCSGFD GSDISSGNGR VQSSKQGVEI VSLSGPGGAG KSTLCNAVQN IARQHGYVAT
TKFDSRHQVP YSCILKSLSQ ILQQILSESE DEIHAFYDHL KSHLGAQFCK IESLADLVPE
LRPLLDPVDS EDSEEPINQI HLDNVETRIR FHTLFVEVFR ALTQWRMVTL FLDDVHLADD
PSLELVESMI ASKVKILLFV CYRDQEVTDT LNRLLSNEFA IFHNVNVGAL DFDSLVDYIS
DALHRPLDIN RDSILPLAEI VYKKTRGNAF YTSQLLVTLE KKKLIFFNWE ENEWDYSLSD
IHQAIMTREE AGRDAELDIS FLVNRLKELP LDGQRLLKWA SFVGDTFSWN TVKYLMVHSD
PESEFSDTDT NSTSGSTVSR RQIDEADSSS QLISDSLHPL IKFSQHTSYS NSSVPSTSST
STSVTGKSTL KSPSGRLTRD PINGLQAALQ EGYILPLESD EFKWSHDRYS QAAMELANPK
NREKIHFKIA KYLLHAEDQV DNFLIADHLL KCISLIKELE HRACYRDVLF EAGNKARASG
AHKMAFTYYN SAISLLDSCA WEDDQYARTH YLYTNAVALS WIVGEYDITE RYLEIIFSHT
TDPLDRVTAH RIQHKYFFSR QMHSEGAVAL RTCLAELEME DFDFDNTQSQ MKKEYDTAVN
MIAKIGIQEL TKIGPCDDPR LKAIMSVLEE MLTAAYWLGN KLEMNYLALK MIQISIREGW
CSSSGVAFQF LSLCACEYFE DYGYSEEVGN AGVVIAEKFG GFSEKGRALC LYNIFSTMWK
YHIKDSIPQF RQALRYCLSA GDRIYGSFSH LHVATTMLYT GYRLSDVLIE AESCYDDCHA
WSSSADTNVL IMSIIRCVKA LQGHTFSENP KEVFDGDDGF NDSHFIAESC KQSANPRVPL
NWYETFRMIP LVLYGHYDYA IALGYCVVNG IGDHPGHRHT RIACAYHSLA LLEKVRTEKD
IMTQEEIDVY LERVEANQDI LRPWAENAAT NYQYFYTLIE AEKAAIAPND ISKAIRLYED
AIDQARKNNY YFELCICHEY AGAFYARMGL KNTAFGMIKK AISLYVNHGS YGKARHLSTK
YNALLADYDD GRIESHDTGV QTDPFPFLGP QNTWSTSSLG VVNTSLNEPL ISEVIPPVTT
EQTLLTLDIL DMASILKSSQ VISSEVKFDS LLKSMMSIIL ENSGADCGAI IVKEEKYGVC
AYGSQLDGAM TFDPPRILSE NDNLVSSRII HHTINTNESI FIHNVEQDAR FAVGPWYDRV
GGKSVICMPI IHKSALAGCL FLEGSSGIFT QRHITVLSLL CQQMGISITN AFLFKSVQRV
TMANMRMIEM QKKALEDARK SKEAAVRATR LREIFLANMS HEIRTPFSGF YGMISLLAET
ELDPEQRDLV KTAKESCEIL LQIIDDLLNF SKLQAGKVTL DLAPVVIEDL IADVVEMLIA
MAIQKNINIA YVVADDVPNV VMADGNRLRQ VLINLLGNAI KFTHEGEIRI KCSLDTTKKT
KNKDQVSLLF EVIDTGIGIS DEQRKVLFEP FSQVDGSTTR KYGGTGLGLS ICLQLVELMS
GSINVSSVPG KGSDFYFSVC VSKLGSQSLK SKAIQAEESF NERNALIRCI SNLKVIVISK
YAATIDSIRF LLPGMQVDGA IQIEEFRKLV KQTTYDVIIV GLYMNPEHTS TAHSSAWLEE
ASKINKDGLI IITNYPAVGA VNGKSGLIED ISDQKLSCKA IRIAVPLRRT KLQRTIGEIL
NKKMPVLVNN NVKTKPASLI TDEERAIYSN MNILIAEDNP VAQKLLLKQL TRLGFQVVCA
NNGLEAINIW SSHPQGYFTM AFFDHHMPKC DGVAAAKRIR EIEISEQRAT RLPIVALTAD
VQESAKHICM NAGMDGYLTK PLNQKVLAES LRTYCQSPTN SSSTTHPETH QSPPLVSELI
TTKE
//
