ID Q21KE8_SACD2 Unreviewed; 1113 AA.
AC Q21KE8;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABD80831.1};
GN OrderedLocusNames=Sde_1569 {ECO:0000313|EMBL:ABD80831.1};
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD80831.1, ECO:0000313|Proteomes:UP000001947};
RN [1] {ECO:0000313|EMBL:ABD80831.1, ECO:0000313|Proteomes:UP000001947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024
RC {ECO:0000313|Proteomes:UP000001947};
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(2008).
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DR EMBL; CP000282; ABD80831.1; -; Genomic_DNA.
DR AlphaFoldDB; Q21KE8; -.
DR STRING; 203122.Sde_1569; -.
DR KEGG; sde:Sde_1569; -.
DR eggNOG; COG2010; Bacteria.
DR eggNOG; COG3258; Bacteria.
DR HOGENOM; CLU_281431_0_0_6; -.
DR Proteomes; UP000001947; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR013039; DUF1588.
DR InterPro; IPR013042; DUF1592.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF13442; Cytochrome_CBB3; 2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07627; PSCyt3; 1.
DR Pfam; PF07631; PSD4; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51007; CYTC; 2.
DR PROSITE; PS50853; FN3; 2.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Reference proteome {ECO:0000313|Proteomes:UP000001947}.
FT DOMAIN 107..176
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 349..444
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 445..537
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 534..620
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 66..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 120882 MW; 70782454813A6A82 CRC64;
MPRPNPFYGH MANIDCTANY LPYAKNILLD LDMTHAIRPI SLLSILLCLP LWLTACGGEP
VGGVDNAPLV TTETPENNQP STGESTGEPA TETNTQEEVD PPQRPPGDII LGKTTYTGQC
AMCHGEAGNG AFPLFINAVE FEAIEDVTHR TMPFGDASAC EGECATNVAA YLVSLISISL
PETPAVEPPD NSTETETETE TETETETETE TETETETETE TENENNSGDP SQPVTPALPA
QCANPQWVSG TEYAVNTLVV NREAAFRCVI AGWCASTASW AYEPNSGLYW EEAWEKVALC
SESTSNGNTS GEPTTPNTDG EEQTENNGAE TGTENETETE TEPNENASAP KAVSTVIAVA
SANQDRIGLS WTDNANNETG FAIRRRTNNG AVVQIHNAPA NSTSYTDANV KLDNQYQYDI
IAFNAVGSSA AVESNQVSLV TPVTAPNAIT NLNATLNNNQ IFLSWSQADA TADTIAIYRT
LDDIQWQQLT TVAANTTQYN DTNITTNTTY GYRLVAINTA GESQASNTVH VSVTPIAAGQ
TLFNQHCAAC HSASGIGGDL FSSQTQTAWL NKTLSQLETK ISTMPAQQCD ANCQKVVADF
IWQDKWNRVV DIIEEKITSS GVRGVRLLTP YEYANTIKAT LNVTVNSEDL PSARFDSHFK
YPSQSSQGLV LTDEAAAYQQ LAQDIASKTT ITKHTCSTAS CRQNAVNKLG LTLFRKPLTA
AQTASYSTLF ETNGFESVIT SMLMSPYFLY LTELGKWDAQ TESYRLSNYE IATHLSFSLW
GMPPNSTLLN LAATGTFSSD EGVKNQAQTM VNDARFAAHV SEFIRYYANT YSVVDEKPGL
STDVIAAMQQ EQTEAIHYLI NAGSASFYEL LNPSYTYLNS TLANHYGLTS TAQNAGSSMQ
KYNVNSLRGG LMHQGIFQVS NSDFSATSLV KRGKFIRENM LCHMMGTPSG VDPDTITLPE
HPITTRERWD VITGPNASDG QCWQCHQLMN EPGSALENYD HAGRYRTEES AANDSRVALT
IDASGILRDN SGFNTLTQYA DARALSEYLA VSEQALSCFV DNAYRFTTGQ QTDAQSENAI
NALQQDFIID GDIKTLFIEL ASSPAALYRS DRD
//