ID A0A1H6CX35_9ACTN Unreviewed; 723 AA.
AC A0A1H6CX35;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=MinD-like ATPase involved in chromosome partitioning or flagellar assembly {ECO:0000313|EMBL:SEG77065.1};
GN ORFNames=SAMN05444920_104444 {ECO:0000313|EMBL:SEG77065.1};
OS Nonomuraea solani.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1144553 {ECO:0000313|EMBL:SEG77065.1, ECO:0000313|Proteomes:UP000236732};
RN [1] {ECO:0000313|EMBL:SEG77065.1, ECO:0000313|Proteomes:UP000236732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7037 {ECO:0000313|EMBL:SEG77065.1,
RC ECO:0000313|Proteomes:UP000236732};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNVT01000004; SEG77065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6CX35; -.
DR Proteomes; UP000236732; Unassembled WGS sequence.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43384:SF14; ESX-1 SECRETION-ASSOCIATED PROTEIN ESPI; 1.
DR PANTHER; PTHR43384; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF01656; CbiA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Cell projection {ECO:0000313|EMBL:SEG77065.1};
KW Cilium {ECO:0000313|EMBL:SEG77065.1};
KW Flagellum {ECO:0000313|EMBL:SEG77065.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236732}.
FT DOMAIN 477..690
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT REGION 26..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 79900 MW; 1F86CC0709492D54 CRC64;
MARHDREESL EEQLAWLDAI KETDDAPVPV SASAAAADEP VASPYPKDPW SLVPQQHETP
TPPLFRAAVD SVYGAEAAED LPGGESEAAE WLGETGVKEE SPAPAPRPDD PFLAPLKPLP
RPDDTDTYAL SFTPPGRNDK PEETDDKPWL SADWSRTIEP ASEPATESDD EPAEDAPAAS
RQDEEPAEEA PKRGERSAWA DTQPRNERPS WAEQSPEKSP EKSPEKSPEK SPPKDEIPPW
AESSETMPRG ERPQWSEPSD SSPKNPSESA LRNQPSESSS RNQSESSPRN ERPAWADSSP
RNERPQWADS SSQDERPMWA DSSPRNERPQ WNEPESSAHE PDQQQERSPW ADRSERREQP
ERSEWAEQPE RPQWTEQHEW RPAEREIPPV RPRRRPAPIP VFTAPPRPPA TGRPTADSLD
PESLLRGRRN APSKGWRRLV YKASGGWIKP GEPPEVRRRR ELMARARTPV TAGHHRVAVL
SLKGGVGKTT TTVGLGATLA AMRGDRVIAV DANPDRGTLS DKLVLETSAT VRDLLNERDQ
VKRYVDIRAF TSQAPSRLEI LASDRDPSVS EAFSAADYQA VSQVLENFYS ICITDCGTGL
LHSAMGGVLG LADQIVLVSS PSVDGARAAS ATLDWLEAHH YADLVKNATV VLCSVRPRSK
SAVDIKKLEA HFAARCRAVI QVPYDPHLEE GAEIDLDRLQ EHTRDAYLQL AACVGEGFAG
IRE
//