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Database: UniProt
Entry: E7NS99_TREPH
LinkDB: E7NS99_TREPH
Original site: E7NS99_TREPH 
ID   E7NS99_TREPH            Unreviewed;       768 AA.
AC   E7NS99;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Putative DnaQ family exonuclease/DinG family helicase {ECO:0000313|EMBL:EFW38562.1};
GN   ORFNames=HMPREF9554_00938 {ECO:0000313|EMBL:EFW38562.1};
OS   Treponema phagedenis F0421.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=754027 {ECO:0000313|EMBL:EFW38562.1, ECO:0000313|Proteomes:UP000004157};
RN   [1] {ECO:0000313|EMBL:EFW38562.1, ECO:0000313|Proteomes:UP000004157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0421 {ECO:0000313|EMBL:EFW38562.1,
RC   ECO:0000313|Proteomes:UP000004157};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC       {ECO:0000256|ARBA:ARBA00038058}.
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:EFW38562.1}.
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DR   EMBL; AEFH01000081; EFW38562.1; -; Genomic_DNA.
DR   RefSeq; WP_002696875.1; NZ_GL638025.1.
DR   AlphaFoldDB; E7NS99; -.
DR   STRING; 162.TPHV1_130059; -.
DR   eggNOG; COG1199; Bacteria.
DR   HOGENOM; CLU_012117_2_0_12; -.
DR   Proteomes; UP000004157; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Exonuclease {ECO:0000313|EMBL:EFW38562.1};
KW   Helicase {ECO:0000313|EMBL:EFW38562.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000313|EMBL:EFW38562.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          92..384
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   768 AA;  86989 MW;  75A0BABCFAF94424 CRC64;
     MKNSAKLFGK HFDPSDTEEN SFDDFSDDGY RDADNFGELN DFSDEAYHDS VNDYDVESSE
     IFYDTESDED SEPVIIPLYT AQIVEYLDET GSFASFFERY EVRHAQLDLT EEIANCFNND
     SIGVFEAGTG VGKSLAYLIP AIKWALQNKE RVVISTGTIN LQQQLMEKDL PSAKKIIGKE
     AKDLKVLLLK GRHNYLCIRR LMQALQEPDL FNDDYDEIKK IQAWAATSAD GSKAEMPFVP
     SDKVWAKVCA ESDNCLGRRC PYYADSFVMK LKKEAAKASL LIVNHHLLFA DLAARYEGYG
     YQTTAVLPPF KRLIFDEAHT MEDAAQSFFS KTFSQFELQR QINALYRHKK GKPIGVLPKL
     ITIAHADEIV PEITKTLFEL QTAYAVLDSE ALPLCSSGAI SFQQMLPYQR DALTQKLSAV
     RRNLEIVIHH FTAVIDTVSD DEQSEDTVQD AKLILWRFRE LKETAESFEQ WKKLSEKVFW
     IEKIRSAQKE TVRFHQTPLN LASLLHDAVF FPMRTVICLS ATLKIGESFD YWLNRTGLNL
     PIDAPLITKT FPSPFPYKRN VLLNVPIDAP PPDDKEFQNW INKAIAEMIE LSGGKTLVLF
     TSYESLKTAC AHARAALKDT DLLILQQGED DRSRLLNFFK ENVSSSLFAT TSFWAGIDVP
     GESLTHVILV KLPFSVPTDP VFKAKADAID SAGGSSFMSL SVPEAVIQFR QGFGRLMRSQ
     SDRGIVTLLD KRVIAKRYGQ IFITSLPETR QCFDSFKNIL YNIENFLF
//
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