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Database: UniProt
Entry: A0A1G5SA32_9CAUD
LinkDB: A0A1G5SA32_9CAUD
Original site: A0A1G5SA32_9CAUD 
ID   A0A1G5SA32_9CAUD        Unreviewed;       661 AA.
AC   A0A1G5SA32;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=DNA gyrase subunit A {ECO:0000313|EMBL:SCZ84033.1};
DE            EC=5.99.1.3 {ECO:0000313|EMBL:SCZ84033.1};
OS   Enterococcus phage VFW.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Andrewesvirinae; Vipetofemvirus.
OX   NCBI_TaxID=1813888 {ECO:0000313|EMBL:SCZ84033.1, ECO:0000313|Proteomes:UP000278763};
RN   [1] {ECO:0000313|Proteomes:UP000278763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Duerkop B.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|ARBA:ARBA00008263}.
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DR   EMBL; LT546029; SCZ84033.1; -; Genomic_DNA.
DR   Proteomes; UP000278763; Chromosome vfw.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SCZ84033.1};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          5..442
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   COILED          414..441
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   661 AA;  75695 MW;  A19967D46756EAC2 CRC64;
     MINKVGLGEQ LNDAMMGMSA YTILQRAIPD FRDGFKPVNR RIITSMLLNK TFNFTKSATV
     EGRVMQLHPH GGSYGSIVGL VQKDRNSLPF LTGKGSWGQY TSSDQQPAAA RYTEVKLGKN
     ALEVTKELKE KSVDYVPNYD GTISVPEVLP VTYPSILTQS QSGIANGFAT SILSYNIHEL
     YDMIDDILML RGRTKPIYPD FPTGATIIKD DEEALNVIRT GRGSFTMRAK IEIDNNKLIV
     TEIPYGVKRE QIIKKIIELN KRGTLKEVTD VRDGTSFKGM KIVITAKKNT DMKELIVKLY
     KLTPLQSKVS ANMNVLIDGR LEVLGVEELL LNWIKWRVSV IKRGLNNKLT SMKKELHILE
     GLRKIASVDE VIRIVRFEDD DKVDQLLMEA FNLTKEQAEY IGKMTLRSLN EKRIQNRLKD
     IEDLENKIKD LEETIDNDGL LKVILQRRMM ETMKEIDAPK RKTEIITIDE EKEKEVHKIV
     KVKEVDNTKH FVCFTKNGWL LKGKNKNDME SQLILGDEIV QYWEAQNDKN IVLFMKDKSV
     RNIKVKQIKE KEFIGNDALF AECNVDEKAL MLLVFDEGHI VKIPIDAFVK NRQVMEKGYF
     DGEKLIYVKQ LSDEKMINIY IGDKKPKTIE IENINIKKNR LARGQKLFNN KKLEKVNVTL
     G
//
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