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Database: UniProt
Entry: A0A1H1N1P4_9CELL
LinkDB: A0A1H1N1P4_9CELL
Original site: A0A1H1N1P4_9CELL 
ID   A0A1H1N1P4_9CELL        Unreviewed;      1212 AA.
AC   A0A1H1N1P4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Replicative DNA helicase {ECO:0000256|ARBA:ARBA00021957, ECO:0000256|RuleBase:RU362085};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU362085};
GN   ORFNames=SAMN04489860_0407 {ECO:0000313|EMBL:SDR92916.1};
OS   Paraoerskovia marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Paraoerskovia.
OX   NCBI_TaxID=545619 {ECO:0000313|EMBL:SDR92916.1, ECO:0000313|Proteomes:UP000185663};
RN   [1] {ECO:0000313|EMBL:SDR92916.1, ECO:0000313|Proteomes:UP000185663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22126 {ECO:0000313|EMBL:SDR92916.1,
RC   ECO:0000313|Proteomes:UP000185663};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in initiation and elongation during chromosome
CC       replication; it exhibits DNA-dependent ATPase activity.
CC       {ECO:0000256|ARBA:ARBA00002835, ECO:0000256|RuleBase:RU362085}.
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=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665,
CC         ECO:0000256|RuleBase:RU362085};
CC   -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008428, ECO:0000256|RuleBase:RU362085}.
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DR   EMBL; LT629776; SDR92916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1N1P4; -.
DR   STRING; 545619.SAMN04489860_0407; -.
DR   eggNOG; COG0305; Bacteria.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000185663; Chromosome i.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   CDD; cd00081; Hint; 1.
DR   Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR   Gene3D; 3.10.28.10; Homing endonucleases; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR   InterPro; IPR007692; DNA_helicase_DnaB.
DR   InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR   InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004860; LAGLIDADG_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00665; DnaB; 1.
DR   NCBIfam; TIGR01443; intein_Cterm; 1.
DR   NCBIfam; TIGR01445; intein_Nterm; 1.
DR   PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1.
DR   PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1.
DR   Pfam; PF00772; DnaB; 1.
DR   Pfam; PF03796; DnaB_C; 3.
DR   Pfam; PF14890; Intein_splicing; 1.
DR   Pfam; PF14528; LAGLIDADG_3; 1.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 2.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 2.
DR   SUPFAM; SSF55608; Homing endonucleases; 1.
DR   SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
DR   PROSITE; PS51199; SF4_HELICASE; 3.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362085};
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU362085};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362085};
KW   Helicase {ECO:0000256|RuleBase:RU362085, ECO:0000313|EMBL:SDR92916.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362085}; Primosome {ECO:0000256|RuleBase:RU362085};
KW   Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185663};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          195..232
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   DOMAIN          358..548
FT                   /note="DOD-type homing endonuclease"
FT                   /evidence="ECO:0000259|PROSITE:PS50819"
FT   DOMAIN          639..805
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   DOMAIN          1132..1154
FT                   /note="Intein C-terminal splicing"
FT                   /evidence="ECO:0000259|PROSITE:PS50818"
FT   DOMAIN          1154..1212
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1212 AA;  132236 MW;  D16CF3F72522B40E CRC64;
     MSIEELEAGF GGEGPSGGAA FDRTPPQDVA AEQSVLGGML ISKDAIADVI EQVRGTDFYR
     PAHEAVYDAV VDLYGRGEPA DAITVVAELQ KRGELGRIGG APYIHDLISM VPTAANAGYY
     ARIVRERAVL RRLVEAGTRI VQLGYAADGG DVDTIVNNAQ AEVYSVTERR AAEDYVPLGD
     IIGGTVDEIE AAGHRGEGMV GVPTGFADLD RLTNGLHPGQ MIVLAARPAI GKALALDTPL
     PTPSGWTTMG EVQVGDELIA ADGTPTQVIR ATEVLEDRPC YEVVFDDGTT IVADALHEWA
     TTTRAERRHR GSRGGIRTTD EIAATVRCDT ADRRANHAIR TSAALELAEA ELPLHPYALG
     VWLGDGHAAG ARFTSADPEI PMRIEGLGLV ATQQGNSDGA AQLYSLRLPP APAIEERPCV
     VCGAVFLPRT SQVRTCGRSC GGRAKAVSSP VPEPTCPDCG RESTGLRRCQ SCHNAHGTVQ
     AILRSLDVMS NKHIPEQYLR ASESQRRELL AGLLDTDGTV NPTGSPQFCV TSRRLALDVR
     ELVHSLGYRS GWSERAVRGR TVGTSTAYTI TFTTDDDVFA LERKRLLHKE RRRPSTPRLT
     SRFVVDVREV PSVPVRCVEI AHPEHLYLAS RSMIPTHNST LGIDIARSAS IKHDMTSVVF
     SLEMSRNEIT MRLLSAEARI HLQKMRNGSM GEDDWQKLAS TMGKITEAPL FIDDSPNMSL
     MEIRAKCRRL KQKHDLRLVV IDYLQLMTSG KRVESRQQEV SEFSRALKLL AKELEVPLIA
     ISQLNRGAEQ RTDKKPAMSD LRESGCLTED TRVLRADTGA ETTMGELFAL GAKDVPVWAL
     NERLQYVRRH LTHVFPTGVK QVYRLRLSSG KEISATANHP FLTYDGWRPL GELEVGSRLG
     VPRHVPAPEQ EAEWDDRKVA ALANLVSGPM KGSTTPETLG DDVWLDREVG VPAAVFQLPK
     RQIALFLHRI ASLCGRVVLH ESGTGVVQIV GTVRSLDGIA RLLLRFGISA QSRDVARGSA
     LEIRGTDDLR RFLQEIGIER DERSADELLL RVREAAGDLN SGPLTVWDEV RHILEADEPT
     TRAGVQVVPR GESRTTLGAV AGVLERADLE IEAVNDLAWE EIVAVEPLGE QAVFDATVLD
     SHNFIANGIA VHNSIEQDAD MVILLHREDA YEKESPRAGE ADLIVAKHRN GPTDTITVAF
     QGHYSRFVDM QA
//
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