ID   A0A1C4GZD8_9BIFI        Unreviewed;      1593 AA.
AC   A0A1C4GZD8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=UvrD/REP helicase N-terminal domain-containing protein {ECO:0000313|EMBL:SCC77977.1};
GN   ORFNames=GA0061077_0044 {ECO:0000313|EMBL:SCC77977.1};
OS   Bifidobacterium commune.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1505727 {ECO:0000313|EMBL:SCC77977.1, ECO:0000313|Proteomes:UP000242610};
RN   [1] {ECO:0000313|Proteomes:UP000242610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-52791 {ECO:0000313|Proteomes:UP000242610};
RA   Varghese N., Submissions Spin;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMBL01000001; SCC77977.1; -; Genomic_DNA.
DR   STRING; 1505727.GA0061077_0044; -.
DR   Proteomes; UP000242610; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF59; DNA HELICASE; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 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}; Reference proteome {ECO:0000313|Proteomes:UP000242610}.
FT   DOMAIN          19..393
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   REGION          651..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1054..1077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1109..1165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1118..1132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1133..1154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1593 AA;  170469 MW;  B3C8CA9060B700D4 CRC64;
     MDENGTLDSV GNAAMDAVKK LLDAQVAAGG DRTHSLLVAG PPCSGKTEFA VAATLEGISR
     FGDAKVLMAV SGRQTADRLS DRVIRAVGSV SSARPVTTLS AIAFRLLSAV RESRREPLPK
     LLNGAEQDAL LRQVVAVHVR HVQAGELCGT CGLMRQYFAN KDWVNTVYDA TGGEKGERPS
     MSATGGRTAA AVSETQPGST SQGIGSSDVL FSRGVSDAFV MQLRDMLARM DELGVGNERE
     DEVLSMLEHS GQTDADYRLQ AERLGVQWRL AFALRREYVQ AVAHGYPSEF RLDSSRLLVE
     GAQVVAWIGE AELPALVVVD DFQDLTLAGL AFLEALAQRG VRLVLVGDPD EAVQTFRGSY
     PEYLFERACE VPIAAEMLEL PVRAVCDGNT ASGGVQHRRE RDVGRTAVED AVGADSGLAS
     GNPSSYLDVL ASRVSLSIAA SDDTFVALPD RPGKLPRFSG ALPIEPLDAN NPLLADSSVK
     AALYHTEREE LDDVVWRIKE EHLSGGREWN EMAVIAHDNS TVRAFGERLR RDGVPVRYSA
     VTKPLKDDLS VQGLFALLEL AGLRRDGIEG NGMTLVHTAK YIRSRVQALL ESPLVSLRGT
     TGVSGASLPA RLAPVESVMK AIASLAHVLD GVAAGSADAS DAAGSVDLVG SDGLTDADGP
     ADSMDSRDSS TSATLSSGKV AGEVSGDSGD IDMTAALPQL QADWQRLRDN MLSQRESSNV
     SVDDSLIDGD AQQQDADMPL GVDALYVMLA LGAGANAGVD STSADLDESR SVADEALGLI
     MAVGNNAYTR AFSHVWKLVG EVERGLSALP GREPEYALDV AWKACRVDKA WQCLALVNND
     EGRAANDRLD VMMRLFAHAS GAGEKQTIED FIASVRSLRI EADSLAKVAP IDQAVTLTTP
     AGAAGVHWSL VFITQIQQDV WPNLAARNTM FGGENLADIV LRGCIGDVRD RNGAPGVDSE
     LAQVLLGEQK SFLVALTRAS GQVVLSAVLS DDAVPSDFLY TYVPEWFDRV RDADPEARNY
     TQLADSGRFV GLDTSSRGLV SAARIELMRQ AGSGLAGADQ GDDIGAGEAD ERDASLAQAA
     DSEAISLART RDAARSLVLL ERNDLHAADP DAWPYTFGGD RGEDDAEGSR EDANPNNDGS
     NGASTGNGSD KGNGGSGNAG HRFNDDTATE APMVVLSPSQ VDRLWSCPVC WMLESQFAGP
     RPSNVATSFG SVIHNVAQKA GDEGLDAPDF MAGSPDDERI AKITDRMMEM YLSLADDLDA
     IDDPEQRYQA ERKDEGARQT LTNIATYFVE SNNKGYPYGN LKNFSVGRLE RSNSELTFTA
     TFNLDDIRDA YNAIDGIDSI GTDELASIMG TLCGGWPEGM RNDLWIRLTG RIDRMEWRDL
     GDGKQHVRLI DWKTGHKHNS EQMLDDLQLV CYQLGLAFPD SVQPDDDSVT VSSMLPNAGL
     RGVEALNAMP DIAQSALFDV DVATAPAQSY GAAETLFQPA LFRSGAINSN AFMPRSHYPD
     PQKVAKLANL PDLPEIAPEG VGERTWEQFL ALRGTQAVWA LTMIARIVYA AAASRSHTLV
     ARPQADHVQF CNMNKVCPAC AGEVDTVYEV RRG
//