ID A0A2Z4I2Y0_9VIRU Unreviewed; 667 AA. AC A0A2Z4I2Y0; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 29-MAY-2024, entry version 25. DE RecName: Full=Non-structural protein 1 {ECO:0000256|ARBA:ARBA00030491}; OS Porcine bocavirus. OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes; OC Piccovirales; Parvoviridae; Parvovirinae; Bocaparvovirus. OX NCBI_TaxID=1165907 {ECO:0000313|EMBL:AWW25132.1}; RN [1] {ECO:0000313|EMBL:AWW25132.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HN13 {ECO:0000313|EMBL:AWW25132.1}; RA Zhou Y., Zhu K.S., Meng F.Q., Xu P., Li P.C., Liu X.; RT "complete genome sequence of porcine Bocavirus."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Multifunctional protein which displays endonuclease and CC helicase activities required for initiating and directing viral DNA CC replication. Also plays a role in viral packaging and transactivation CC of several promoters. Binds site-specifically to 2-3 approximate tandem CC copies within the origins of replication (Ori), unwinds this hairpin CC region and nicks one DNA strand thereby initiating the rolling circle CC replication (RCR). Becomes covalently attached to the 5' end of the CC nick and provides a 3'OH for priming DNA synthesis. The helicase CC activity unwinds DNA in a 3'-5' direction on the longer strand. CC Participates in the transcriptional regulation of several promoters. CC {ECO:0000256|ARBA:ARBA00002892}. CC -!- SUBUNIT: Homooligomer; when bound to DNA. CC {ECO:0000256|ARBA:ARBA00011717}. CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147, CC ECO:0000256|PROSITE-ProRule:PRU01366}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MF590244; AWW25132.1; -; Genomic_DNA. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0019079; P:viral genome replication; IEA:InterPro. DR Gene3D; 3.40.1310.20; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR014015; Helicase_SF3_DNA-vir. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001257; Parvovirus_NS1_helicase. DR InterPro; IPR049901; PV_NS1-NUC. DR Pfam; PF01057; Parvo_NS1; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS52022; PV_NS1_NUC; 1. DR PROSITE; PS51206; SF3_HELICASE_1; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Covalent protein-DNA linkage {ECO:0000256|ARBA:ARBA00023124, KW ECO:0000256|PROSITE-ProRule:PRU01366}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|PROSITE- KW ProRule:PRU01366}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE- KW ProRule:PRU01366}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE- KW ProRule:PRU01366}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|PROSITE- KW ProRule:PRU01366}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01366}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE- KW ProRule:PRU01366}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU01366}. FT DOMAIN 24..287 FT /note="PV NS1-Nuc" FT /evidence="ECO:0000259|PROSITE:PS52022" FT DOMAIN 402..569 FT /note="SF3 helicase" FT /evidence="ECO:0000259|PROSITE:PS51206" FT REGION 638..667 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 133..135 FT /note="RCR-2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01366" FT MOTIF 228..232 FT /note="RCR-3" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01366" FT COMPBIAS 645..659 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 228 FT /note="For nuclease activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01366" SQ SEQUENCE 667 AA; 76254 MW; C49FA6177413F974 CRC64; MASAGVGLSD QEWINYWHGA ITGFKSPCYT YVIHLDLQDW RPHERALMDI YSKDVSVIID DIVDTEKEFL LSDVNYEWKA SLAMKLQNHH GLGQTLCESA DIAVRRLFQL KQQNHNPQYS CFTQAEIGPS KIHVHVVCGG DGLTRFNAKK CTWIIAKFFW NHMLELWEHF ESCYRPTNAQ MAIGVQLRML CERIKSKQDT TVTILTYKDR HNEQHAQRVD GPSYITNYLL PKNRQLVTWL DMDVCTPSVA WFETEKTYMC SHIDRQPITH YLRKGLHDRL VMNSSEETGE PVHKMARWGE LPQVGENSLA RENTRPRPAK ITKKQCVMID TLQRCEDEHI CTKEELTMLH PDLVIMFESS PGGSRTLDEV LEMHRVRVTR SYSALGYILK QYPENKFIKP ENKVVRLLNI QGYNPIQVGH WVATVLSKKA GKQNTLCFYG PASTGKTNLA KAIVSAVKVY GCVNHLNKNF VFNDCQSKLI AWWEECVMHN DWVEPAKCLM GGTTFRVDRK HKDSAEQPHT PLIISTNHDI YTVVGGNTVT TVHEKPIRDR VVQFNFMKTL PQNFGEISVS DVADWLGWCA EDFDCSLDGF KKEWDIDVVP NSFPLAVYCD GHFQDFLFSA QGPCCRCGGY LPHTTTSDGD WTESADPGRT TRMRERETPS GGDGIIS //