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Database: UniProt
Entry: A0A444Y8T0_ARAHY
LinkDB: A0A444Y8T0_ARAHY
Original site: A0A444Y8T0_ARAHY 
ID   A0A444Y8T0_ARAHY        Unreviewed;      1541 AA.
AC   A0A444Y8T0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=RecA family profile 1 domain-containing protein {ECO:0000259|PROSITE:PS50162};
GN   ORFNames=Ahy_B08g094418 {ECO:0000313|EMBL:RYQ98372.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ98372.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYQ98372.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYQ98372.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000256|ARBA:ARBA00008668}.
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:RYQ98372.1}.
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DR   EMBL; SDMP01000018; RYQ98372.1; -; Genomic_DNA.
DR   STRING; 3818.A0A444Y8T0; -.
DR   Proteomes; UP000289738; Chromosome b08.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd01121; RadA_SMS_N; 1.
DR   CDD; cd01837; SGNH_plant_lipase_like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR004504; DNA_repair_RadA.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR041166; Rubredoxin_2.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR035669; SGNH_plant_lipase-like.
DR   NCBIfam; TIGR00416; sms; 1.
DR   PANTHER; PTHR32472; DNA REPAIR PROTEIN RADA; 1.
DR   PANTHER; PTHR32472:SF19; DNA REPAIR-LIKE PROTEINRADA; 1.
DR   Pfam; PF13481; AAA_25; 1.
DR   Pfam; PF13541; ChlI; 1.
DR   Pfam; PF00657; Lipase_GDSL; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   Pfam; PF18073; Rubredoxin_2; 1.
DR   PRINTS; PR01874; DNAREPAIRADA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
DR   PROSITE; PS00143; INSULINASE; 1.
DR   PROSITE; PS50162; RECA_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016};
KW   Zinc {ECO:0000256|ARBA:ARBA00022771};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          657..810
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   REGION          399..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..529
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..549
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1541 AA;  167526 MW;  4F8E75469B6B9EBC CRC64;
     MIIENKMKIN RKEVEVVFVI FAFVLLVVWG NAQDTLVPAM ITFGDSAVDV GNNDYLPTIF
     KANYPPYGRD FLNHQPTGRF CNGKLATDIT ADTLGFKSYA PAYLSPQASG KNLLIGANFA
     SAASGYDEKA AILNHAIPLS VQLNYFKEYQ GKLAKVAGSK KAASIIKDAL YLLSAGSSDF
     VQNYYTNPLI NKLVTPDQYS SYLVRSFSSF VKDLHKLGAR KIGVTSLPPL GCLPAARTLF
     GFHENGCVSR INNDAQGFNK KINSAAKNLQ KQLPGLKIVV FDIYKPLYDL VQSPSKFGFA
     EARKGCCGTG IVETTSLLCN PKSLGTCSNA TQYVFWDSVH PSQAANQVLA DALIKSITMT
     LFPRLIFIEH QRHRLFNLTC IFSASSSSSS SSQYRYLRSS PFSSATTPSP QTQTDDPAHR
     GTSPRTRWST YGDIFDSHTK RAPAISDHEL EEHEEEKQLK EEERKVEEEE DSIEKLRRAL
     EKRERSRVKT VSTVNNELEE HEEDKQLKEE EQEVVVEEEE DEEEGEEEVE EPRRAITKQR
     ERSRVKTESS IHGGDVLPER IISTKRSGGA KAKKQWLCSN CGYTAGKWWG ICPSCELSGT
     MREFHEAKVT DADKSRAKSG LAVCEDTIRL WLPQNAAELR PIKLEEVNKG FSHKQWRIPL
     PGTFGTEVST VLGGGLVPGS LTLVSGDPGI GKSTLLLQMA AMIAKGCSEG KASRVLYVSG
     EESLEQIGNR AERLGIKSDI YLYSSTDIED ILKKAQLLSP RAMVVDSIQT VYLKGLLSSA
     GGILQVKECT AALMRFAKTT NIPILLVGHV NKSGDVAGPR VLEHIVDVVL YLEGEKCSSY
     RMLRAVKNRF GSTDELGVFE MVQLGLKAVP NASEIFITEQ PTHSEVLTGI AVTVLMDGSR
     TFLIEIQALC LCPSPIPTSS VDLQVNGIST KRATMIKCVL IKQAGLKLQD NAVFLNVVGG
     WTLAETAGDL AIAAAICSSF MEFPIPKGVA FIGEVGLGGE LRMVPRIEKR VNTVAKLGYR
     TCVIPKQAEK VLETEGLGNM RVIGCNNLKE GHGRTLGATR LAASSAAATK PASGGLFSWL
     GGSFSSLPPL DTPLAGVALP DPLPDRVEPS KTKITTLPNG LKIASETSSN PAASIGLYLD
     CGSLYETPMS SGASHLLERM AFKSTANRSH FRNVREVEAI GGNVGASASR EQMGYTFDAL
     KTYVPQMIEL LVDCVRNPAF LDWEVNEELR KVKAELGELS NNPQGLLLEA IHSAGYSGAL
     ANPLLAPESA INRLDGSILE EFVSENYTAS RMVLAASGVE HEELLSVAEP LLSDLPSVAH
     PGEPKSVYVG GDFRRQGESG GAHVAIAFEV PGGWQQEKDA IVLTVLQMLM GGGGSFSAGG
     PGKGMHSRLY LRVLNEYQQI QSFSAFNSIF NNTGLFGICA STSSDFVAKA VDIAAKELIA
     IASPGQVSQV QLNRAKESTK SAVLMNLESR MIASEDIGRQ ILTYGERKPV EQFLKAVDGI
     TLNDITRISQ KIISSPLTMA SYGDVINVPS YESVNRKFHA K
//
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