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Database: UniProt
Entry: A0A0Q6VLC7_9ACTN
LinkDB: A0A0Q6VLC7_9ACTN
Original site: A0A0Q6VLC7_9ACTN 
ID   A0A0Q6VLC7_9ACTN        Unreviewed;      1250 AA.
AC   A0A0Q6VLC7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Fe-S cluster protein {ECO:0000313|EMBL:KQV77503.1};
GN   ORFNames=ASC64_01255 {ECO:0000313|EMBL:KQV77503.1};
OS   Nocardioides sp. Root122.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736431 {ECO:0000313|EMBL:KQV77503.1, ECO:0000313|Proteomes:UP000051395};
RN   [1] {ECO:0000313|EMBL:KQV77503.1, ECO:0000313|Proteomes:UP000051395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root122 {ECO:0000313|EMBL:KQV77503.1,
RC   ECO:0000313|Proteomes:UP000051395};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV77503.1, ECO:0000313|Proteomes:UP000051395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root122 {ECO:0000313|EMBL:KQV77503.1,
RC   ECO:0000313|Proteomes:UP000051395};
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:KQV77503.1}.
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DR   EMBL; LMDE01000001; KQV77503.1; -; Genomic_DNA.
DR   RefSeq; WP_056905703.1; NZ_LMDE01000001.1.
DR   AlphaFoldDB; A0A0Q6VLC7; -.
DR   STRING; 1736431.ASC64_01255; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000051395; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   PANTHER; PTHR43255:SF6; IRON-SULFUR-BINDING OXIDOREDUCTASE FADF-RELATED; 1.
DR   PANTHER; PTHR43255; IRON-SULFUR-BINDING OXIDOREDUCTASE FADF-RELATED-RELATED; 1.
DR   Pfam; PF02754; CCG; 2.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051395};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        68..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          291..321
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          373..405
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          722..1088
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1104..1250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..801
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        943..962
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        975..994
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1056
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1073..1088
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1250 AA;  129913 MW;  6A523FFBB5F17F5B CRC64;
     MQMFAIVVSL AATAVAVVLT TRAVRHMVGV IRSGQPVSRS NDPAARLLHM LKESVLHTRM
     LQWHWIGILH WFVYAAFIFL SSAVMAGYVQ LFDPMFEIPV VGKWYIYGWA AEVLGLLGTL
     GIIALAIYRQ VKHPRSLGRR SRFFGSNFWQ AYFVEAMVLL ESAAILFIRG AEYKLHDGTK
     LHFPLSHLVG DWFYPDSEQA LKNIVFFVAM VKITSAMIWL IVIASNLTMG VAWHRFTAWF
     NIFFKRESDG STALGAMKPL TSDGKAVTLD DIDDLDEDSV LGAGKVEDFS WKGILDFTTC
     TECGRCQSQC PAWNTEKPLS PKLLITSLRD HAYAKHDGVE GHADRALVGV GSKGESAGSG
     TDVLDYFYNP SDGDFVIDED VLWSCTSCGA CVQQCPVDIE HVDHIMDMRR YQLLVESNFP
     AELNQLFKGL ENKGNPWNMS PSGRLDWAKG LEFDVPVVGD DLESLESVDW LFWVGCAGAY
     EDRAKKTTRA VAELLNIAGI SFGVLGNGET CTGDPARRAG NEFVFQGLAQ QNVETFKEYK
     VKNVVSTCAH CFNTLKNEYK DFGIELEVVH HTQLLNRLVR DGRLTPVKDG AGAAKRSITY
     HDPCYLGRHN EVYSPPRELL QVLPGAEVVE MERNSERSFC CGAGGARMWM EENLGERINV
     NRTKEAVGTG ADQIAVGCPF CRVMLSDGLT AQQAKGEARE EVEVLDVAQM LLASVKGEQA
     TKAAPGSSPA AAPAAASAAT APASTDVATK DEPETGDVTI TEDTVTETAD AGPAAKASGG
     SSLFDTPADS AGSTGSTGGA GGSLFDTPAP NAKATPAESG GSLFDTPAPE PAAAEAKPAE
     TEAAAPKPAE KPAADLGTGG SLFDLGTPAE PEAAPAAPAE AAAPAAAPAK EAEPAAAPAA
     APAADLGGGG SLFDIAAPEP DAAPAAAAQP EPSAPSAAEP ETVSEPETEQ AQAATETPAA
     QSEAPAATPA ATPAATPAAS GTTSTPTTDA DLSSLGSLFD LEAPAAQPAP AAPAAADAGE
     PEAAAGTETV TETASVATDD DPETILDSED APEPEPDGQP ETVAEVATEA APAPASGTTS
     TPSTDVDLSS VGSLFDIEAP ATVAAPAAAA APAAAPQAAE PAPDAAPEGT AEPGAAAEPD
     APEPDAAPDA ATEPAQAPSA PPSGADLSQA ATFRDPEDVP AQDEVEAPAE IPAEGPVPAA
     AEEPEPAADE DEDDVPAEEQ PAAKPGAPDG PAHTPRTDVD ISGSGSLFDL
//
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