ID A0A1Y2GS21_9FUNG Unreviewed; 1364 AA.
AC A0A1Y2GS21;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=BCR41DRAFT_28657 {ECO:0000313|EMBL:ORZ20948.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ20948.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ20948.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ20948.1,
RC ECO:0000313|Proteomes:UP000193648};
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:ORZ20948.1}.
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DR EMBL; MCFF01000012; ORZ20948.1; -; Genomic_DNA.
DR STRING; 64571.A0A1Y2GS21; -.
DR InParanoid; A0A1Y2GS21; -.
DR OrthoDB; 1662268at2759; -.
DR Proteomes; UP000193648; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR23257:SF779; SERINE_THREONINE-PROTEIN KINASE WNK4; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000193648}.
FT DOMAIN 522..781
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 921..955
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..376
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1364 AA; 152669 MW; DAEE9A7ECE68FEEA CRC64;
MSSTTLSRRS GIRAPSGSGR PRSRPSSSST NVDPANNEKQ QQQRHSYSAS SGSESDLLVP
PAPPPTQQLL FTEEPQEMTK EEERELTRGE ARGEREEKVR GEEEVEKDKN IHTRLLNDDM
FTRAYKPSFY SEPLGGSTNY DNGFIDYITI GNSNSSNTRN NTRPDSVTDG YNISSNHNSN
SNNSDNDNDS GNTEKAKSKF ISPPSSLSPS SPSSPPPPYS QTPRVKTPRP NTVHQDTLIG
NGNIYSFHEH NFPMPPRSRS PNPQTNPQTA LHQQLEQQQK PSPSSIPPHS PLQEQGAGVV
NQALSRSEIP PRRDSIWLGP PDETGTVDSG STVPAFHPGQ RELDYFCLSR VREEDEDGDK
EQEQEEEEEE EEEKEERKTD DREIIVVVKD FAERTRNDNP WDDAGYEQQP VKKFQLRDPS
TPNFRHAQAQ AQTLMHGHSL QRQSDQQSFP IPPVRPRVRQ GRRPRTPPSP IDAFHNEDDA
GGDNFKQYTN ELETQETLKR ERTRILQRTV VSSYRQINYK DITNVQPLKK GGFGEIHTAE
WSRLKVVLKR ALADGIEQFE QELEILKRVH DYDFIVPFYG VTMDPIANVR CMVMKHCANG
NLCQFLEKNH TTLTWAERYR LSIEITKGLE FLHKSGFYHR DLHSGNILLD DKRTAMLCDF
GLSRSVNKTR TMDMTATVGV ASFLAPERFP AERPVYSAAC DIYSLGVIFW HITSGRIPFA
NRLGAGTGVA LLLRQLMEGL REEIEPDTPV EYRNLLTQCW DVNPSERPPI DMIIAVLQTL
MAEPSEPVHL QQQHGGYPYH HPHHRPVAAG FTVPSSTTSA ALPVPPELDT KMASLERASN
TLNKMVFDIT DPTMRETVDY IHRMRRRFRE QRMPKQPYSL SNPPTVPIYL CPLVGDIEGF
EYHLSVHDKS YNPINESSEQ TGDTALHLAC LFLESPLDTI KVLVELGADI NLENLQGYTP
LMILVSSNTQ YCYEALKYLV MRGARIPAYI RNPITPLGNA QTYAKDIVNE SRQLQMDNSV
KYAKQAKVNS ITHNNSSSNN RKQRGGNRFY AQGRPLIHVV AAMQDDYRIL DCLCEAGLDP
AITFGGENAL VAAAAHLKIK NMEWLLNNDL DISSQKMITR ATKVVRLLHA PVPTSPTDIG
GFNVYGHGTM YITANHKRGG ASGPGTSSDV IIKGSTWGRL DPKEFPEDIR ELGQYSWAGA
AYKGRQGTDQ FNKDMIGPVL QLLEQWSGHR LNEARKQVAT KLMKAHRAAV AAMAAVAAVA
SNNATTNATP PILPRSPSPM RIDTVSASHH HHHNSPRPSS PFAAPSSLVS PGESVPYIPP
PPANLNPGRG SSNINNGSSR HHSLRKNQRH LIDHVLRAKA PVRY
//
