(data stored in ACNUC7421 zone)

HOGENOM: STRS4_1_PE13

ID   STRS4_1_PE13                         STANDARD;      PRT;   1227 AA.
AC   STRS4_1_PE13; C6GYT2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP-dependent helicase/nuclease subunit A; EC=3.1.-.-;
DE   EC=3.6.4 12;AltName: Full=ATP-dependent helicase/nuclease AddA;
DE   (STRS4_1.PE13).
GN   Name=rexA; Synonyms=addA; OrderedLocusNames=SSUBM407_p015;
OS   STREPTOCOCCUS SUIS BM407.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Streptococcus.
OX   NCBI_TaxID=568814;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STRS4_1.PE13.
CC       Streptococcus suis BM407 plasmid pBM407, complete sequence.
CC       1..88329 annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:C6GYT2_STRS4
CC   -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA
CC       helicase and an ATP-dependent, dual-direction single-stranded
CC       exonuclease. Recognizes the chi site generating a DNA molecule
CC       suitable for the initiation of homologous recombination. The AddA
CC       nuclease domain is required for chi fragment generation; this
CC       subunit has the helicase and 3' -> 5' nuclease activities (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Heterodimer of AddA and AddB/RexB (By similarity).
CC   -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC   -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain.
CC   -!- GENE_FAMILY: HOG000285114 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C6GYT2; -.
DR   EMBL; FM252033; CAZ55679.1; -; Genomic_DNA.
DR   RefSeq; YP_003024062.1; NC_012923.1.
DR   STRING; C6GYT2; -.
DR   EnsemblBacteria; EBSTRT00000087171; EBSTRP00000081228; EBSTRG00000087693.
DR   GeneID; 8149063; -.
DR   GenomeReviews; FM252033_GR; SSUBM407_p015.
DR   KEGG; ssb:SSUBM407_p015; -.
DR   GeneTree; EBGT00050000027178; -.
DR   OMA; NSVKVSM; -.
DR   ProtClustDB; CLSK855033; -.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:HAMAP.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:HAMAP.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:HAMAP.
DR   HAMAP; MF_01451; AddA; 1; -.
DR   InterPro; IPR014152; DNA_helicase_suAddA.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR011604; Exonuc_phg/RecB_C.
DR   InterPro; IPR014016; Helicase_SF1_UvrD-rel.
DR   InterPro; IPR011335; Restrct_endonuc_II-like.
DR   Gene3D; G3DSA:3.90.320.10; Exonuc_phg/RecB_C; 1.
DR   PANTHER; PTHR11070; UvrD_helicase; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   SUPFAM; SSF52980; Restrict_endonuc_II-like_core; 1.
DR   TIGRFAMs; TIGR02785; AddA_Gpos; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
DR   HOGENOMDNA; STRS4_1.PE13; -.
KW   exonuclease RexA;
KW   ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Exonuclease; Helicase; Hydrolase; Nuclease; Nucleotide-binding;
KW   Plasmid.
SQ   SEQUENCE   1227 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDGTNERRSG LMAFEQFLSA EEIKAVQLAE AHSDKQQKRT AEQIEAIYTH GQNVLVSASA
     GSGKTFVMVQ RILDKLKRGI GIDQLFISTF TVKAAGELKE RIEKKLNETI AETTDMELRR
     HLSAQLADLT KADIGTMDSF TQKLVTTYGY SLGISPQFRI LQDETEKASL KKEVFDQLFA
     DYLEEDENGA FRKLVRNFSG NRKDNSGFRQ VVYQVHDFSQ STSSPTKWLK EQAVQADLYS
     QERIEQMLEQ GFKEKVLDKL YQAADFFRYH VEWGRNDFGS AKYFANVEEV LDLLTGLDSL
     DQKDLMERVE RILLINNQSR GKGLTNANRP KDEHLIAFKE EYNAGKSQII SELRDLGQEV
     YELTLLKDYQ VQALPLLILL RDFVLDFSQA YLDVKIKEAA FEFGDIGHFA IRILEENADI
     RQFFQEKYHE VMVDEYQDNN HSQERMLDLL SNGHNRFMVG DIKQSIYRFR QADPMIFQEK
     FELYQANPQS GKLILLKENF RSQIEVLEAT NAIFTRLMDR QVGEIKYDDT HSLVAGSPGQ
     KIAQPKNEME YLIYDQQDSA NSSTDAEEET PLTAGEIEVV AKEIIRLHNE EGADFKDITL
     LVQKRTHNDL IMSIFEKHGI PIVADGGAAS YLQSLEVMIM LDTLRVINNP LNDYALVALL
     KSPMFRFDED ELTRISLQAG TGFFYQKMEI AQQASGQHPE LMSEKLKKKI TDFLSILENW
     RAYAKLHSIY DMIWKMFNEK FYYDYVGALP NGSKRQANLY ALGLRANQFE KTGYKGLSRF
     IAMIDRALAN DKDLADVQEF LPQNAVQLMT IHKSKGLEFK YVFLMNIDKR FNLEDHYQSV
     IISRKNGLGI QYLADMKDKV NSPLPQVRVL MNTLPYQNNL QELKIANLSE QMRLLYVALT
     RAEKKLYLVG KGNADKLAEK YDGKKENGVL AQSTRESMAT FQDWILAIDE AFSGEDLHFK
     KVFVTDEDLT EEKIGKLTLK SKLEDASLKD IRQSEDIAQA LDQLSSVQEL NERYKAAIEL
     PSLRTPSQIK KLYEPILEQE GMEVMEKYQP KRTFNLPDFS KKPKITGAQV GSAVHELMQR
     LDLSWLVTED TVRAALEAVH AEQAIKDKIN VQMILDFFDT DLGREILANT DKLHREAPFA
     SLQTDSVSQE NFVLRGIIDG YLLYDDHIVL FDYKTDKYDQ PIQLSQRYQA QMQLYAEALK
     KAYKIDRVDC HLILLGGERI EVVEVNI
//

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