ID A0A1X2IJA6_9FUNG Unreviewed; 1138 AA.
AC A0A1X2IJA6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ORZ17403.1};
GN ORFNames=BCR42DRAFT_31460 {ECO:0000313|EMBL:ORZ17403.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ17403.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ17403.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ17403.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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:ORZ17403.1}.
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DR EMBL; MCGE01000010; ORZ17403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2IJA6; -.
DR STRING; 90262.A0A1X2IJA6; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000193560; Unassembled WGS sequence.
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; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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 SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000193560}.
FT DOMAIN 348..681
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 957..1088
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1007
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1138 AA; 126114 MW; 2CEA2FA32514D548 CRC64;
MNKNNNTTTT NTTTAVNTTS DIPKTPIPTM THSTSSSTML NNTPATTTQQ HMPSTRTTST
CLEDAQHALM MKTYSLVGYD YLETLTNELL AMTQAQTVII QQVITMDECN NITERLEQQG
IKVNMACLDD ASSVEHDGAP EEDLTHCLEL LDQQQQRKHK RKHPHQQNQP LDNDQLHNNQ
LLLTRACSST VSSVATSKYC VIPLALLHDT PPLKTLKEGV YITPNDQQPS FEVAKSATTA
TTKNDDDSRM TMMMDYCTES VADTFLPPHT SFVGIRLQGA NALPLGLLTV CHDKVKTPHW
FTETHQLLSF VATRTMRELA GIRDSERLVK ARNDATQDAE NKIKFLADMS HEIRTPMNAV
IALTDLLLQE KSSLNDEQIE HLDVIQTSGH HLLTVINDIL DISKINHDPK FKLENRRFSL
RKCIKDALNM ARHQASMSQL SKMVYVVEGP PDMDDNVPVQ HTIASLERLG MLPPMTSQYK
GKVLLPLIWN IDVDVPDYLM GDTMRLTQIL LNLCSNAVKF TKKGGIRVSI KRYVPTPLQA
NTNQQSKLKQ RYEAKLETIY TRTMQGNATK DGVGDGDGRA GAGASDNDDP TSNPEDDEPR
LEKTILEICV SDSGIGIPSD RLPRLFKSFS QIDISTARRY GGTGLGLAIS STLVNRMGGG
LWVESEEGVG SRFAMTLPMA IALGRTARTY GSESTTTSSF ITSPPSPSSS VSDGSGSVNS
GVFERTSDAS SSSHSYTNVL SPATYSSNNS NTSGYFPNVS QQHQQHQQQV NSLQQRLRSQ
SSWSLANARH HHFHHQQLLN ASSPPFESAS PDHSTTHPLS ALSSSPPNSN TNQHPPSVLT
HYSSSDAISQ TTRPSSSSDQ RRPLLRRENA ASQSNIHHHQ QHFERGPTPG VATDTRSPTS
PSPPRSGGRR LRAPSTNNTK SHYHHQQQQQ QQQQQQHHHH HKKTTAEESF ALTYPVKILL
AEDNVLNQKI AVSILKRLGY HDVVVTNNGK EALEVMRKIK FDVIFMDLYM PEMDGLEATR
EIISTRTKDT TTTSKRPPLL NVNDVYIIAL TASASNQDRQ ICIDAGMNDF ISKPFTMMEM
KAALKTCGTK RAKRRKQRKD DDDGDGDNHQ QSGSDTVMQP QEVEVEVVDA MVGVENAL
//
