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Database: UniProt
Entry: A5D604_PELTS
LinkDB: A5D604_PELTS
Original site: A5D604_PELTS 
ID   A5D604_PELTS            Unreviewed;      1008 AA.
AC   A5D604;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Restriction endonuclease {ECO:0000313|EMBL:BAF58333.1};
GN   OrderedLocusNames=PTH_0152 {ECO:0000313|EMBL:BAF58333.1};
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF58333.1, ECO:0000313|Proteomes:UP000006556};
RN   [1] {ECO:0000313|Proteomes:UP000006556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT   evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
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DR   EMBL; AP009389; BAF58333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5D604; -.
DR   STRING; 370438.PTH_0152; -.
DR   REBASE; 15345; PthSORF151P.
DR   KEGG; pth:PTH_0152; -.
DR   eggNOG; COG3587; Bacteria.
DR   HOGENOM; CLU_011799_0_0_9; -.
DR   Proteomes; UP000006556; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0015668; F:type III site-specific deoxyribonuclease activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR045572; RE_endonuc_C.
DR   PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR   PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR   Pfam; PF19778; RE_endonuc; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   4: Predicted;
KW   Endonuclease {ECO:0000313|EMBL:BAF58333.1};
KW   Hydrolase {ECO:0000313|EMBL:BAF58333.1};
KW   Nuclease {ECO:0000313|EMBL:BAF58333.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006556}.
FT   DOMAIN          64..249
FT                   /note="Helicase/UvrB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04851"
FT   DOMAIN          893..999
FT                   /note="Type III restriction enzyme C-terminal endonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF19778"
SQ   SEQUENCE   1008 AA;  116366 MW;  22B2C9D8753D9AA6 CRC64;
     MKLKFKIQQF QTEAVNAVAD CFAGQPNGQS LFTLDIGQLN SGPQLGISYE VTGFRNRPIE
     LTPEEVFENI KKVQVRGGLK ISPKLEGKYN LTVEMETGTG KTYVYIKTMF ELFKRYGWGK
     YIVVVPSIAI REGVKKSFEI TEEHFMEQYG RKARYFIYNS RQLHKIDQFA SDPGINVMII
     NTQAFNARGK DARRIYMELD EFQSRMPIDV IAQTNPIMII DEPQSVEGTK TVEALKLFKP
     LFTVRYSATH RYEYNKVYRL DALDAYNKKL VKKINVKGIN VKGTTGTDGY LYLEGVDISQ
     KHYPLARLEF EKKTRSGIKR ELRRVSVNDN LYELSGHLEQ YKGYVVSEIN GGKNTIEFAN
     GISLSAGDVL GDVNELTLRR IQIRETIKSH LEKERDLFYR GIKVLSLFFI DEVAKYRQYD
     KNGNKLNGEY AQIFEEEYRI LVEEYLRNAG EKDRYADYLR QIDAEKTHNG YFAIDKQGRM
     TDPKVKARET DSEDEDAYNL IMKDKERLLS FSEPTRFIFS HSALKEGWDN PNVFQICTLK
     HSDSTIKKRQ EVGRGLRLCV NQDGERIDDS VPGIDVHQVN VLSIVASESY DAFARELQRE
     IAETLSDRPR KADVQFFLDN VLTNEREEKI RIDERLARKL YQTFVKNNYI DEEDNLTEDY
     YQAIEKGAVV LPEELKEHKH AVIKLVSTIY SESASPLVHN ERNKNVELKL NDNFYKEEFQ
     KLWKKINVKT AYTVKFDTEE LVDKCINALD TRLRIADISY QIKDGVLEVI DSKEQLERGE
     GFVLKEAETG KVDGKVTSGV RYDLAGKLMV ETGLTRKTIV KILTGIKRET FDLFKKNPEG
     FILKVARIIN EEKATTIIER ITYDPLKETY DTDIFTQNTL KGMLGENALP VSKHIYNYVI
     TDSHTESKFA RDLDASREVC VYAKLPRGFF IPTPVGNYNP DWAIVFEENK VKHVYFIAET
     KGSMNSLELR KIEEAKIHCA KKHFEKISNN SVKYGVVENY EKLLEMVS
//
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