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Database: UniProt
Entry: F4CER0_SPHS2
LinkDB: F4CER0_SPHS2
Original site: F4CER0_SPHS2 
ID   F4CER0_SPHS2            Unreviewed;      1114 AA.
AC   F4CER0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   OrderedLocusNames=Sph21_1311 {ECO:0000313|EMBL:ADZ77874.1};
OS   Sphingobacterium sp. (strain 21).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ77874.1};
RN   [1] {ECO:0000313|EMBL:ADZ77874.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=21 {ECO:0000313|EMBL:ADZ77874.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA   Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT   "Complete sequence of Sphingobacterium sp. 21.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
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DR   EMBL; CP002584; ADZ77874.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4CER0; -.
DR   STRING; 743722.Sph21_1311; -.
DR   KEGG; shg:Sph21_1311; -.
DR   PATRIC; fig|743722.3.peg.1406; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_010638_0_0_10; -.
DR   OrthoDB; 9810135at2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   Gene3D; 1.10.3170.10; Recbcd, chain B, domain 2; 1.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF64; ATP-DEPENDENT DNA HELICASE REP; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          1..473
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          519..784
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1114 AA;  128223 MW;  BE91B073902050E2 CRC64;
     MANLPPVKIL KASAGSGKTF SLAAHYISLL FTSKVHFSEI LAVTFTNKAT AEMKHRILTV
     IEGLALGSEA VESYRNIILE AHPQLSRQDI QQKAMEVYRQ ILHNYSRFAI STIDGFYQKI
     IRSFSFELGL NAAYRLEMNS DKVKQDLVVR LNKLLNDRDD LLQWIINYAR KQIENDRNWN
     YTTVLKKLAD ELFKERFHPF DEAISQLSEA DRQVVFTTIS DLSDELITRF EKEIERLLKI
     ATEIVNSSGV SSDLFLRKSQ NLIPKIPSLA PDNLEAIDKF ADYIDNPEKW QKNGVSGAVS
     DLYNKLNPLL RQILNYKEEH SRTYFLAKAV QANFYYLRLL KEMSVLLADY RAEHDVSLIS
     DAQNLLKEIN RHQDQNISFI YEKVGNRYKY FLFDEFQDTS SNQWYNFQPL LVNALASTEG
     NRSIPHHLIV GDVKQSIYRW RNGDWRILQY QSTRDLGDHH IRFQTLQENY RSLPNIIKFN
     NFLFTQAPKL LQQIINDKIY TEIGDSLYNS WWQASGYTQI LTDAYAETVQ KIPSDKGEEG
     GRVTVSFFPV TSSFAKTRGK EIKPAALKAL SDTIINWLTE GRYQARQIGI LVRNNTEARE
     IIEYLLHIQK ELDESHKFEV ISGDALLLVN NPGIRLLINT LKAMITPVEE ASLYRANCLL
     LYQQVYGLNQ EDEASIWLNA TQYDIKVWGK ILPPIVINNW YVWQQHPLTE LVESLINGYG
     ITHDEATIPY LIAFRDIIAE FSSQGERGIA SFLGYWDEEG KTKALPANEG SNAVEIMTIH
     KSKGLAFDVV MIPFCSWELD GMVNSNFWVD TSGTSYEILR SVPVKYNSML VKSSLFKAYL
     EEMLFNYMDA LNLLYVATTR ARKELYISAP DIKEGKESDS LIADVLRSVL ALHSDELGIE
     YSHGIVYPST TPFKDIKKSP TLPVKYQEGC IDFWESPPNY NWSFNKYPIS ELLKEALDNR
     KIKKELLSLG EQNAATRQGL LLHELLSLTT EIAEFPNYLH AMQSEGLITK DELMTLLDEA
     IRLRNNEQLA ALLDKPYQSL NEQRIITKDG SVLRPDKVLI GEHETIILDF KFTGMERPQH
     IAQVKEYQQN LQEMGYPNIR TFLFYAFNNR LVEV
//
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