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Database: UniProt
Entry: U2UL07_9FUSO
LinkDB: U2UL07_9FUSO
Original site: U2UL07_9FUSO 
ID   U2UL07_9FUSO            Unreviewed;      1090 AA.
AC   U2UL07;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Helicase protein {ECO:0000313|EMBL:ERL25629.1};
GN   ORFNames=HMPREF9108_01810 {ECO:0000313|EMBL:ERL25629.1};
OS   Leptotrichia sp. oral taxon 225 str. F0581.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=1321774 {ECO:0000313|EMBL:ERL25629.1, ECO:0000313|Proteomes:UP000016631};
RN   [1] {ECO:0000313|EMBL:ERL25629.1, ECO:0000313|Proteomes:UP000016631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0581 {ECO:0000313|EMBL:ERL25629.1,
RC   ECO:0000313|Proteomes:UP000016631};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:ERL25629.1}.
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DR   EMBL; AWVS01000133; ERL25629.1; -; Genomic_DNA.
DR   RefSeq; WP_021768584.1; NZ_KI272921.1.
DR   AlphaFoldDB; U2UL07; -.
DR   PATRIC; fig|1321774.3.peg.1727; -.
DR   eggNOG; COG1061; Bacteria.
DR   eggNOG; COG3886; Bacteria.
DR   HOGENOM; CLU_005588_1_1_0; -.
DR   Proteomes; UP000016631; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR   CDD; cd18799; SF2_C_EcoAI-like; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR021835; DUF3427.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR   PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR   Pfam; PF11907; DUF3427; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|EMBL:ERL25629.1};
KW   Helicase {ECO:0000313|EMBL:ERL25629.1};
KW   Hydrolase {ECO:0000313|EMBL:ERL25629.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:ERL25629.1}.
FT   DOMAIN          193..223
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          311..482
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          525..689
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1090 AA;  128448 MW;  1F053F3834180853 CRC64;
     MSILVKKSEP NNLINTEEKN DNFLEITEYK ENLEFEVLET FSEKISDFIG KNDYQKVIEF
     TEKQLYLLNQ AFTDKSEKIK TQNTDFHFEL PLKRKNSDII GNINELIINE KVKFRNFFIY
     LKQELLNCKK FYFIVSFIKY SGIQLLISTL DELEKQGIQG EIITSVYLNI TDSKALRKLL
     SYKNIKVKIY NNSSESFHTK AYLFEKEKYH SVIIGSSNIS QSALYSAEEW NVKLTDSSFF
     NIYKKSLNQF EKLWHSNEAI ELTEDFIDEY EKYKKSINTQ NTFDYRKTKI TQKDEFIPNS
     MQKRVLEKLK ETRENGNKKG LVISATGTGK TYLAAMDIKQ FFEINSNNKN KLFETNEGKS
     KILNIKFLFI AHREELLENA INVFSRILKI DKNEFGRIYG GLKEINKSMI FASIQSLRNC
     YNEFKPDFFN YIIVDEFHHS MSDSYLKTLS YFQSKFLLGL TATPKRMDGK DILSLCDYNV
     VDEIGIKEAL EEDLIVPFHY FGVNDYMINY DNIPYKNGKY NEKVLLENLL LNTRTDYIVE
     KINKFGFDGD KLSAVAFCQN IEHAFFMKEE FTNKSYKSAV ITANTSSNER SEILDKFKNK
     KIEILCVVDI LNEGIDIPTI NLLLFLRPTM SSTIFIQQIG RGLRKAENKD FVTIIDFIGN
     HKKDYLLINY FSNEVDNKDT LFTKKEKIIN EIKNQFSNIP KSCYVELDRV CQNRIIEKIE
     KINFSSKNIL KDLYLDYKEE IGKSENEILK VSDFDTNIEL FQELSLKLGS FYNAQLQFEN
     PEILKMNKIS LNSEEIEFLA YLEKKLMLVE PFTYLIINYL INNEFITSEI TINEYKNYFN
     IKNDFEKEYV INRIFRELVE DKILEQNSKN NNLFKISENY RKIFQNIDKI NNNNKINLKI
     INLDNSQNSN YNFKIRLKEL LYLGLSEFKK SNNLSIFNEN ILIPYKKYKR IELQILLDSK
     VPKGSWRAGY ANTDKDICLF ATIDKTHILQ ENLKYDNSLF ADNIIQWISQ PKTAHNSSVG
     KMFTNHSELG YNVYIFIRKY AFMNNNKTNP FIYLGKANYY KSYGDKPMRI LWKLDEKIPQ
     ELIYELYNLS
//
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