ID A0A0Q6PNM4_9MICO Unreviewed; 1163 AA.
AC A0A0Q6PNM4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASC63_03715 {ECO:0000313|EMBL:KQV06546.1};
OS Leifsonia sp. Root112D2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV06546.1, ECO:0000313|Proteomes:UP000051914};
RN [1] {ECO:0000313|EMBL:KQV06546.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV06546.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV06546.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV06546.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQV06546.1}.
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; LMCU01000001; KQV06546.1; -; Genomic_DNA.
DR RefSeq; WP_055810059.1; NZ_LMCU01000001.1.
DR AlphaFoldDB; A0A0Q6PNM4; -.
DR STRING; 1736426.ASC63_03715; -.
DR OrthoDB; 9760715at2; -.
DR Proteomes; UP000051914; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR007527; Znf_SWIM.
DR PANTHER; PTHR10799:SF1020; BTAF (TBP-ASSOCIATED FACTOR) HOMOLOG; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF04434; SWIM; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051914};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT DOMAIN 59..99
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 708..867
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1003..1159
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 107..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 126467 MW; 680F6D42C0616573 CRC64;
MPSSDLPFVD AAHIRKLVGV GAFERARPYA RGGAVLDLNW IADAGRLTAV VQGTANLPYR
CQVTLEPTGR DGYRPVDSAC DCPMREDCKH VAAALLTANA RRVTAEHDAT AAAAARAPAS
DAPGPRNPAP TPGWKSTLSA VTPGRAHGPG GASALRGTGS GTGADSGNGS APLGVQFELR
EKSRRDRGRW QRTSAVTVAA TANTPADRLR VTLRPVTLSA SGRWVAGGLS WSSMQFQLNR
MSLDERQVRW FGQLAALART QASVYTGSDA DRLVLDDYPS PLLWRLFGEA QRLGIQLVGG
GKGAGLTVAT QAAIGLDAAS AEDGTLTLSP TVRFDETAVD AETVRSIADH GLYAVAWEHA
SGAVPQLQLG PTDAPLTAEH RRLLAAGPIE VPAAEVPEFY ADFFPALSRL VPISTTDAQL
QLPELVPPLL VVTTTFLAEH VVKLGWEWEY RSGDRTVRHP LETPGESRGR MTRAAAAGRD
APFEQHTLAA VVAALAGFTT PARAGNTLRD IEAAEFTEHA LPVLESLPGV RVDIVGERPD
YRELHDAPTL RVTTMETEQR DWFDLGVLVE IEGRQVPFAP LFSALSKGLP KLLLIDKTYL
SLKQPVFDRL RELIMEAQSL DEWETGPRIN RYQAALWAEF EDLADESEQA VTWRESVGGL
LKYLQTDATP GENPGAAPGA LPGLTEELPS GLNATLRPYQ HDGYAWLTFL WRHALGGVLA
DDMGLGKTVQ TLALVAHART AAPFLVVAPT SVVANWVSEA ERFTPGLTVA SITQTQAKSG
TPLAETIAGA DIVVTSYTLF RLDFDEYQKQ QWAGLILDEA QFVKNHASRA HRCARDLDAP
FKLAVTGTPM ENNLTELWSM FDIVAPGLFP SLRRFTEDYV RPIAAAASPT QATPAAHGAE
LLARLRRRIR PLMLRRTKEL VAPELPAKQE QVLQIELAPR HRRIYDTVLQ RERQKLLQLL
DDDLDSSRFI VFRSLTLLRM LSLDASLIDE AYASVPSSKL DALLEQLEDV LAEGHRALIF
SQFTTYLRKV ATRLEERGVD YAYLDGSTTT RQKVIDGFKQ GSAPVFLVSL KAGGFGLNLT
EADYVFLLDP WWNPASEAQA IDRTHRIGQT KNVMVYRLVA TGTIEEKVMA LKAQKAQLFD
AVLDADAAFG SALTADDIRG LLE
//
