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Database: UniProt
Entry: A0A0S9R841_9ACTN
LinkDB: A0A0S9R841_9ACTN
Original site: A0A0S9R841_9ACTN 
ID   A0A0S9R841_9ACTN        Unreviewed;      1180 AA.
AC   A0A0S9R841;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Fe-S cluster protein {ECO:0000313|EMBL:KQP78285.1};
GN   ORFNames=ASF37_06850 {ECO:0000313|EMBL:KQP78285.1};
OS   Aeromicrobium sp. Leaf289.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736324 {ECO:0000313|EMBL:KQP78285.1, ECO:0000313|Proteomes:UP000051640};
RN   [1] {ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA   Vorholt J.;
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:KQP78285.1}.
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DR   EMBL; LMNK01000002; KQP78285.1; -; Genomic_DNA.
DR   RefSeq; WP_056579623.1; NZ_LMNK01000002.1.
DR   AlphaFoldDB; A0A0S9R841; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000051640; 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; PF13237; Fer4_10; 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:UP000051640};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          305..335
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          378..410
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          727..1180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..825
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        978..1004
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1026..1040
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1101..1122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1164..1180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1180 AA;  126215 MW;  68E55640FCDDEF15 CRC64;
     MQLVAIIVSL AVTAITIPVT VVAVRRMTAV IRAGGPAPGR TDDPAARTVN MLKETFLHTR
     MLQWSWIGAL HWFVYLAFLV LATAVAQAFF QLFDPEFVWP IIGHFFLYEW ISEAIGLLGA
     LAIIPLAVYR QVKHPKRLQR QSRFFGSRMG QAYFVEFMVF LESAAILFIR GAEYNLLQAR
     GGEDSEYATG FHFPIAQFFG NLYPTGAENI DTLENIIVVI AMIKVTSAMI WLLVISTNLT
     MGIAWHRFTA WPNIWFKRES DGGTALGGLE PIRINGKALD MEAMEDLEEE DFEKLGVGKV
     EDFSWKGLLD FTTCTECGRC QSQCPAWNTE KPLSPKLLVM GLREHAYAKI PALAIPEDER
     TEEQQKEVER PLIGDEEMYG VIDPDVLWSC TNCGACVQQC PVDIEHVDHI DDMRRFQVLV
     ESNFPAELNN IFKGLERKGN PWGMNPKHRM DWAKDLDFEV KQVGVDVESL DEVEWLFWVG
     CAGAFEDRAK KTTQAVAELL NTAGVDFAVL GDGETCTGDP ARRAGNEIVF MQLAMENAEV
     LKETKAKKVV STCAHCFNSL KNEYAEFGVE LEVVHHTQLL NRLVREGRLT PVAGKAGAAA
     AEPEKTITYH DPCFLGRHNQ VYEAPRELLS VIPGAKFAEM PRNSERSFCC GAGGARMWME
     ENLGSRINVN RTQEAVATGA DQIAVGCPFC RVMLSDGLTA QQAAGEAREE VEVLDVAQML
     LAAVKRAPEP TAEESADVVD EAEAATAAAA AAGSSDQATD AEPDATDQAD DASISDTEDA
     APAADAHEEP EATDVPDDEP QDEPATTSRE EDAEVAAKQN MDVDEQGRAA DTSGNAGQAP
     GADEVEADNA KASTESDESG DATPDEAPAA ETSKADETGA DGDEAETEKD EPVQVDAPPQ
     PAKPATDGKA EEGGDEPKAE STTSSDGAPE PDPEPEPGDT TDPEVETVPS NGAGGDDEAS
     PATADEPAPA EDEPVDGGVV EQGAREEEAD AAGDVQAKAD TDGEESETEK DEPVQVDAPP
     QPAKPATDDK AEEGGDEPKA ESTTSSDGAP EPDPEPEPGD TTDPEVETVP SDGAGGDDEA
     SPATADEPAP AEDEPVDGGA REEEADATDV EAKADTDGTG AAKDEAPSEV VAVEDAPNAD
     PESDDVAPLS DANPSGTDVS TAATDAAKDE EPQGEDEPKA
//
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