ID A0A1H6E5A8_9ACTN Unreviewed; 1135 AA.
AC A0A1H6E5A8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=ATP-dependent exoDNAse (Exonuclease V), alpha subunit, helicase superfamily I {ECO:0000313|EMBL:SEG92471.1};
GN ORFNames=SAMN04489712_1346 {ECO:0000313|EMBL:SEG92471.1};
OS Thermomonospora echinospora.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=1992 {ECO:0000313|EMBL:SEG92471.1, ECO:0000313|Proteomes:UP000236723};
RN [1] {ECO:0000313|Proteomes:UP000236723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43163 {ECO:0000313|Proteomes:UP000236723};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNVO01000034; SEG92471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6E5A8; -.
DR OrthoDB; 4524286at2; -.
DR Proteomes; UP000236723; Unassembled WGS sequence.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.940; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014862; TrwC.
DR Pfam; PF13604; AAA_30; 1.
DR Pfam; PF08751; TrwC; 1.
DR SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:SEG92471.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Exonuclease {ECO:0000313|EMBL:SEG92471.1};
KW Helicase {ECO:0000313|EMBL:SEG92471.1};
KW Hydrolase {ECO:0000313|EMBL:SEG92471.1};
KW Nuclease {ECO:0000313|EMBL:SEG92471.1};
KW Nucleotide-binding {ECO:0000313|EMBL:SEG92471.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236723}.
FT DOMAIN 10..98
FT /note="TrwC relaxase"
FT /evidence="ECO:0000259|Pfam:PF08751"
FT REGION 126..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 878..912
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 160..181
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 121817 MW; 53DD407704FDEAA6 CRC64;
MEHAGNGGWE FYRHVEVVGA LAQARFRAKT TALGFRWERV PGSRVWELAG VPARLREVFS
KRSGQTSGML VRLGIDPDRA TTAQIKAASA MCREGKDTAP LAPASLVHAP VATGTLEADL
RESWRRQTVE SGADPDTVVA AARRGGGPDG GTGIGGPDGP VGPDLPPRPP RTVPPSPPSR
RNAEQPAERT TERAERTTER AERSAERVER SAEWAGRPAG EVAERIAAAV FDPEHGLTAH
AKVVTRPKLL AAVLDELPAG ITSAAAAEEL ADAVVAGEGP AVRLERQGPA YRTHPERYTT
RDIIAAEQQI LAAARDGYQR PGREDEGLAV VDAQAAELAI ETFEAAAGFE LSREQREVIQ
RLTGAGHGVD AVVGVTGAGK TTLMAAARAA WEAAGMVVRG AAAAAVAAQA LQAETGIPSS
TIASVQRALE DPDAPGLDGV DVLVIDEAAM ADDRQLADVL SAAQRTGTKA VLIGDPLQMK
AIGVRGTLAE IHRQVAGPLL TENRRQREPL ERRALQLWRA GDRHGALRTW AVAGRVHAGG
RREDTLARML TDWESARDHL ARTSGERDVH EELDRLLMLT GTNADVDLLN QGARLTRRKR
GEITGPDHSY QLATGGTLAL AVGDYVRVRR NDYRTRHKDA PADAVDVLNG YRGIVTGFNG
RDPVVQRRSQ TEDGPGVETA TIPAARIAAG DLSYGTAMTV ASAQGLTSDI TFVYGPGLGP
HTVYPAMSRN RKQAHLYLPR DLLETDTDRA RHGAPHSPVD ELARAIGAYA RTLTGDRADR
LALTELGTVP APPTGTPATE AAPAAQAAGA GRESIQPSAV PHWRKRPYGT YTDKYLDRLA
TAYRAQLDRF QRIEARTAAE TAAARRGKGP AATVLAERRQ ALAQAADIEA QLTQAREEAD
QAGADIADAT RQVTAARELT QHGRLALRMA SISRAQAQQQ LQDAHDAWQA ACDRQTTAQQ
RTDRLARQAA DAYRQAPALH LPGAGQESGA DQESGRWHHG AATADLAALT RRWDEYLALA
IRADLRTAPK RAAQTTLGRA YAAHLAGIDT PHQAVDADEA HRQLAAITTE QNLRRQMPTD
HADQERTQRT QHHRRQTTGR TAHQAGRAAA HEQDRQYEAS RPPGPRYDHG RGSSR
//