ID A0A5N6RM93_9ROSI Unreviewed; 2841 AA.
AC A0A5N6RM93;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FH972_018423 {ECO:0000313|EMBL:KAE8100531.1};
OS Carpinus fangiana.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Betulaceae; Carpinus.
OX NCBI_TaxID=176857 {ECO:0000313|EMBL:KAE8100531.1, ECO:0000313|Proteomes:UP000327013};
RN [1] {ECO:0000313|EMBL:KAE8100531.1, ECO:0000313|Proteomes:UP000327013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cfa_2016G {ECO:0000313|EMBL:KAE8100531.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAE8100531.1};
RA Yang X., Wang Z., Zhang L., Hao G., Liu J., Yang Y.;
RT "A chromosomal-level reference genome of Carpinus fangiana (Coryloideae,
RT Betulaceae).";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM017327; KAE8100531.1; -; Genomic_DNA.
DR OrthoDB; 3247158at2759; -.
DR Proteomes; UP000327013; Chromosome 7.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR CDD; cd00293; USP-like; 1.
DR FunFam; 3.30.200.20:FF:000268; probable receptor-like serine/threonine-protein kinase At5g57670; 1.
DR FunFam; 3.40.50.620:FF:000177; probable receptor-like serine/threonine-protein kinase At5g57670; 1.
DR FunFam; 1.10.510.10:FF:000284; Putative receptor-like serine/threonine-protein kinase; 1.
DR FunFam; 4.10.1000.10:FF:000008; zinc finger CCCH domain-containing protein 3; 1.
DR FunFam; 4.10.1000.10:FF:000022; Zinc finger CCCH domain-containing protein 7; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR006016; UspA.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR46156; CCCH ZINGC FINGER; 1.
DR PANTHER; PTHR46156:SF1; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00582; Usp; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00356; ZnF_C3H1; 5.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000327013};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 417..688
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 2603..2632
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 2658..2684
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 2707..2735
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 2603..2632
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 2658..2684
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 2707..2735
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 998..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1705..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1806..1827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2073..2095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2121..2141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2176..2220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2488..2513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2525..2552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2724..2755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1709..1726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2190..2208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2525..2538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2728..2744
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2841 AA; 313386 MW; 5EE5123D07D92961 CRC64;
MLQAGVPGEA EALGDSGGRT VVVGVKLDSP SRELLTWALV KVSQPGDLVV ALHVLGNDEI
VDRDGKSSLL SLVKAFDSVL AVYEGFCNLK QVDLKLKICR GTSVRKILVR EAKAYSAAKI
IVGTARSHHK IRSSTSVAKY CAKKLSKDCW VLAVNNGKVV FKREGSPTTI GHSKGTEDHR
RNRLLSLIHG TLSKNTKVLN EGNASVSLKE RFEERSCQDF EQGLAKAALD CRESASKEKC
SICAPNSELP DNYCDQSAEE SCGDGGEDKS LAIVPVQKEE ASSSSISLLI KELPELKPGW
PLLHRAILPD RKVSERFSVR QISVVQWALR LPSRHFSCTT ISDLKQISYD HGEDQSSNLD
AESGAIVPVG TETLAAPPSP EHCPRRLPKE LEGLHEKYSS TCRLFLYQEL LSATSNFLPE
NLIGKGGSSQ VYRGCLPDGK ELAVKILKPS DEVLKEFVLE IEIITTLHHK NIISLLGFCF
EDGNLLLVYD FLSRGSLEEN LHGHRKDPLA FSWSERYKVA VGVAEALEYL HSGCAQPVIH
RDVKSSNILL SDDFEPQLCD FGLAKWAPTS SSHITCTDVA GTFGYLAPEY FMYGKVNDKI
DVYAFGVVLL ELLSGRKPIS NDYPKGQESL VMWAKPILNG GKASQLLDPS LGDKYNQDQM
ERMVLAATLC IRRSPRARPQ MSIVSKLLHG DCEITKWAKL QVNALEEYDV LDGEACPRSN
LQSHLNLALL EVDDSLSISS IEQSVSLEDY LKGSAIGKGE EGRSQKPLVF PPIKNWASMK
FAISYAHTLQ DFAQSHRIDD RPRNRLPEPD QSRRVDIWDP HSVLPDTNRP AARPYYPPLD
FDLDRNDGHQ HQRLFDRPVN KFRQDSQGTS RVRIEFSDGF DPKQKDEKLV WGHGDENYHR
RGHLLSDSDS VRRDFGFVSN SRDVESNLVG YDHRHGSVRD NEAYGSFRIG GGHDGRASRD
IGDLLYEMGS KETGDCEGVR IGSAKREYYG LEVGRYDHNR GNREGSHEYN RTPRKQVQKK
SAFLRIQMAR PNNRNRESEQ LHYSGYFDKG NFGSFRGKDQ LYLDHGMEEG EEHERERSPV
ELDVSFKSNS LVAKAIVTPS DMNLTPRNEK IRKVSDGDCS NSYLSKLSEG TVNLDGFTCV
ANKASNSERD LKQPEEKVMK SDIGNVCDGS SQPCSSRTSV SVGKSKVERS PKGLVLDKDG
ATNVGSGKTT APKFVKKKKI VKKIVKKVIN PQSRLSSSQK TKKCDETAKA GCSTHSPPGA
PDSGKGVPLL EHIVTSDGMA SRHNVALQPC LDKVNVLPEN DMADRSPLTA LSHDCGINVE
SGRVCVTKIK RNWKSSTSAL GSLSCEENRI NESPVNADNS VHSLRSISNS DNDFKPRNEI
TFSEIGRVKD VSKQLNHNGL LLSLENDAEK EATKTVLSLE DNVNSRLLSS EEIKIHEDIS
NTYSSPHYTN NKLGFENCID KSQENTASDI GIMDTIKKQP CINQFSTSLE NSISEGIHQA
LIGSSAIVGL SSSEKTEICK DLVYAECSNH GRDTWNSDNG CSSLEEKYTV CNSGTINYTS
KHPFSGRIPI SIENCAIERD PIDMVTVRAS EVNTRKIKKR RKTRTQLDFS DSTNIHTNSV
NDAVSPANAL DAPLGFSLKG LSPTEVAVSG VGSLDIGLLP GKDGISVLHA NSSADGFSGV
KLTMNSDVNS YLDGTLPRCK KNREVSATDL ASSRPTVSET NERPTGTSIS CAEVFLTNND
DLAQPEEEVN VSSIHNLSTS GLMACPSGTT VLLENTLGGR SSEAVGETRD TDDGLKLLQL
GVESFSNAED PDAQSSFPSG LGSEQKENGT PLIAVDINQN DTMDIETSDG EKMDAQAAED
QVLIHGETPW CKITSEPQSP DLGQRFSSTD IESDYLLVKD DLPSVSNNPS FSDDGAGFSS
PNTNDEVMES MSRTLLDMGS PETLSEVPSI VMLNGKALPS QISNEKVCGD DQKLNQKFVV
EDGSGVSVHT PFSQYTKRDC ATESNHSIMG KTVLLPSQDS KITSCRPNLM SAGLIVKNTQ
LGPLIPRAFP GRSSFLLTNS NKTGSSARIA KPRTWHRTGP APPLPVNKPF TNNIPPKRQL
VENNVKSHSM SYIRKGNSLV RKPAPAAAQH HSSHGLSSSV YRASSSVVDE SKKITGFDSR
ADVTDPHNLL RVGMHTPLER PRTPPLPSGT KISTRTAISS GDNTSSPLAE SPFSGCCETT
SDPMKFTETN NVPESAEDLL KISESPTGTS SNNLEIQSEL SDGNLTSFNM KRIVYVKRKS
NQLVAASNPC DLSVHNGNNI QATSDGYYKR RKNQLIRASL ENQIKKSVSM TDDLLNSGGQ
RVPKVVSSRK FSKRRLHKVV AKTCKPVKSS LVWTLCGMQS LKNDSDSSDH QKSLPYRFPW
KRATYGRSFV HNQVSSSNNS SLSMISRKLL LLRKRDTVYT RSINGFSLRK FKVLSVGGSS
LKWSKSIEKN SKKANEEATL AVAAVEKKKR EQNGAAGTSS QTKNRNHSSR ERIFRIGSVR
YKMDSTKRTL QRISDDRSTC STSPQPEKDA KKSYIPKRLV IGNDEYVRIG NGNQLVRDPK
KRTRILASEK VRWSLHTARL RLAKKRTYCQ FFTRFGKCNK DDGKCPYIHD PSKIAVCTKF
LNGLCSNPDC KLTHKVIPER MQDCSYFLQG LCTNRNCPYR HVSVNPKAST CEGFLRGYCA
NGNECRKKHS YVCPNFEAAG TCPQGSKCKL HHPKSRSKGK KRKRLGEQKN TRGRYFGSRH
VNVSEPRTAV HEKHSTQNND DNFLEGKFAD YINLDVSDEQ VGESNDHTSE QTFCDSDPLD
EQLDDLDELI KPVRIMINLT T
//
