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Database: UniProt
Entry: A0A1H6CX35_9ACTN
LinkDB: A0A1H6CX35_9ACTN
Original site: A0A1H6CX35_9ACTN 
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
//
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