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Database: UniProt
Entry: A0A498JLG0_MALDO
LinkDB: A0A498JLG0_MALDO
Original site: A0A498JLG0_MALDO 
ID   A0A498JLG0_MALDO        Unreviewed;      2335 AA.
AC   A0A498JLG0;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DVH24_008405 {ECO:0000313|EMBL:RXH95905.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH95905.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH95905.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH95905.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RXH95905.1}.
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DR   EMBL; RDQH01000332; RXH95905.1; -; Genomic_DNA.
DR   STRING; 3750.A0A498JLG0; -.
DR   EnsemblPlants; mRNA:MD06G0103100; mRNA:MD06G0103100; MD06G0103100.
DR   Gramene; mRNA:MD06G0103100; mRNA:MD06G0103100; MD06G0103100.
DR   Proteomes; UP000290289; Chromosome 6.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd00060; FHA; 1.
DR   CDD; cd00333; MIP; 1.
DR   CDD; cd09122; PLDc_Tdp1_1; 1.
DR   CDD; cd09123; PLDc_Tdp1_2; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 3.30.70.2330; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR014905; HIRAN.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   InterPro; IPR010347; Tdp1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF185; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF08797; HIRAN; 1.
DR   Pfam; PF00230; MIP; 1.
DR   Pfam; PF06087; Tyr-DNA_phospho; 2.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF81338; Aquaporin-like; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        73..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        145..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        219..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          358..431
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          1473..1638
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1549..1568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1952..1974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1952..1971
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        775
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-1"
FT   ACT_SITE        1199
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-1"
FT   BINDING         777
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-2"
FT   BINDING         1201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-2"
FT   SITE            1227
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610347-3"
SQ   SEQUENCE   2335 AA;  255326 MW;  0C59459B35A14FDD CRC64;
     MAESEPVTPS ASAPATPGTP LPLFSGPRVD SLSYERKSMP RTKCFPVNAT AWGQSPTCFN
     EFPTPTVSLT RKLGAEFVGT FILMFAASAG PIVNQKYNGA ESLIGNAACA GLGVMIVILS
     TGHISGAHLN PSLTIAFAAL RHFPWVQVPA YIAAQVSASI CASFALKGIF HPYISGGVTV
     PTVSTGQAFG LEFIITFNLL FVVTAVATDT RALGELAGLA VGATVMLNIL IAGPSSGGSM
     NPVRTLGPAV AAGNYTKLWI YLVAPTLGAL AGAATYTAVK LREDEVDAPV REARSFHLSS
     DYGGEVKRCP IHRKRPRPPR SEASTAVSVH VKQLDVPLTC PETGSPVDSI CLQPDRPYTI
     GRSNRGCHFV FADRRVGKKH CQIIYNSFDR KLYVIDGALI SVPQFRNRLE LEECCNVRVS
     LNGVFVNGIR VREGVAVELS DGDRVSLGCS TENCCNPIRI GFVVNKIVCE DQIVQSFDNP
     QGPVKPLCVS CPWGRKRVFA SRAEGSPSSI VGRANFLLSE CRHILLSNDP ISYIRKCCRY
     SFENGFIRSN DIGESPGLDT DRLPLNGEKS LLCQTSHIDC DVKNKMQFTS VMHQCENVVA
     SEPNGVILHK QDNAQVPSET AVADGNLETS SFNFTGREDP PNCDGIVKNK TRCRNVASQP
     GKNFYLNRLS FMGHNSSTSS QDSVISLPEL LYPVQSISQM FIATFTSDIL WFLSSCEIPS
     HLPVTVACHN TERCWSSSPN KRTSSPYPDF PKYPPFPEAI AFGNDRKRHG IACHHPKLLV
     LKRDDSIRVI ITSANLVSTQ WNAVTNTVWW QDFPCRSAPD YTSLFTQFHD GETNQDSKTD
     FASQLAGFMA MLLTDVPSQA QWIVDLTKYD FGGATGHLVA SVPGVHSYKT PFMLDSRHFG
     LADHGASSGA KFLGSVEASV VGLSYLFRNA KDSNGAKLKK LASFLRKSCE HAKALSIVLT
     RNTNVPADAN AVNIVVPDSN EGDSVQLGFL PRNVAKWVSP LWDIGLFSFS GYICPKEALT
     AALGGGNSKK VQLILHVSQG PKFEDISNIM ESQHIFALCS LIGAVQRCTG LWRLQEVLGQ
     YNWPESLDSD FVYGASSIGS INAKFLAAFS VAAGKKSLEF ESEESDPEWG CWSASQESKS
     PSIKIVFPTI KRVKNACNGI FPSKRILCFS EKTWQRLRTI DILHDAIPHP YDRVGHPMHS
     KVARRRFHSK TDGSSFGWVY CGSHNFSAAA WGRPINGPFG LNMNGLGKAN STLGQMLHIC
     NYELGIIFTF PPTDTDGSAN KNSAKLDNIV LPFIVPAPKY RRGDRPATGK AMREALAELT
     EQERQKLLEA ATIEEIMEET PDEDEVVEAD DYVAEEKEEE KAYAKILWSQ VDSSESMSSS
     SSSSVLIPSL QWWTPSLNSS TSNCCCTQFL RYDRSRSRSS GGGRQVFSLY PIRLANPSPP
     FASSFLSPFK ARTFPTGPTG RRKTKLRIVA AVFERFTERA VKSVIFSQRE ARALGRNMVF
     TQHLLLGLIA EEEQHRHLHP NSHGFLGSGI SINQAREAVR AIWHHHSQSQ TSASAEVDPS
     SRAASSSATD VPFSISTKRV LEAALEYSRA RAHNFIAPEH IAIGLFTADD GSAGQVLKRL
     GVDVNQLLAE AASRLQVELV KDGREPSGGF QKSLSKKSIA SGKKKDKSAL DQFCVDLTAR
     ASEGLIDPVI GRDTEVQRII QILCRRSKNN PILLGESGVG KTAIVEGLAI SIAQADVPAF
     LLEKRVMSLD IALLMAGSKE RGEMEARVTT LLSDIRKAVH TLIESGTVGQ RNKGSSLDIA
     NLIKPPLGRG QLQCIAATTA DEYRLHLEKD KAFARRLQPV WINEPSQDDA VRILLGLREK
     YEAHHNCRYE PEAIIAAVYL AARYIPDRYL PDKAIDLIDE AGSRARMDAF KRKREQQICI
     LSKSPDDYWQ EIRTVQAMHE VVLATELKNS DASSVDDIRE PSSSSSTSGD EPAVVGPEDI
     AAVASLWSGV PLQQLTADDR MLLVGLDEKL RKRVVGQEEA VAAISRAVKR SRVGLKDPDR
     PMATLLFCGP TGVGKTELTK ALAASYFGSE EAMLRFDMSE YMERHSVSKL IGSPPGYVGY
     GAGGTLTEAI RRRPFTVVVF DEIEKAHPDI FNILLQIFED GHLTDAQGRR VSFKNALVVM
     TSNVGSTIIA KGRQSSIGFL LADDEVTSYA GLKATVMEEL KTYFRPELLN RIDEVVVFHP
     LQKAQMLEIV NLMLQELKKR LMSLGMGLEV SESVKGLICE QGYDRFYGAR PLRRAITSII
     EDPLSEALLA GGYKPGDTVV IDVDATGNPF IRNGSDQSVR LSNSSVQHPS CNIIR
//
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