ID A0A0G4G395_VITBC Unreviewed; 1752 AA.
AC A0A0G4G395;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Vbra_16885 {ECO:0000313|EMBL:CEM22724.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM22724.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEM22724.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CDMY01000556; CEM22724.1; -; Genomic_DNA.
DR STRING; 1169540.A0A0G4G395; -.
DR VEuPathDB; CryptoDB:Vbra_16885; -.
DR InParanoid; A0A0G4G395; -.
DR OMA; CAMASIM; -.
DR OrthoDB; 4560at2759; -.
DR PhylomeDB; A0A0G4G395; -.
DR Proteomes; UP000041254; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd08760; Cyt_b561_FRRS1_like; 1.
DR CDD; cd09631; DOMON_DOH; 1.
DR Gene3D; 1.20.120.1770; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR045266; DOH_DOMON.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11475:SF144; NAD(P)H OXIDASE (H(2)O(2)-FORMING); 1.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF03351; DOMON; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM01117; Cyt-b5; 1.
DR SMART; SM00664; DoH; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS50836; DOMON; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR619791-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR619791-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1752
FT /note="Cytochrome b5 heme-binding domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005190141"
FT TRANSMEM 782..807
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 819..843
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 849..866
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 886..909
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 921..940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 614..746
FT /note="DOMON"
FT /evidence="ECO:0000259|PROSITE:PS50836"
FT DOMAIN 1003..1080
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1313..1425
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 29..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1630..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 332
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 1752 AA; 191824 MW; DF99CF44660F9136 CRC64;
MKIWPLLSGF VYISGSFVLA QRTNYEEGIQ ASPEDDNGGW DYYRPDGLGN SRDSGAARRP
YRRHGNSHSY DDLPGQVQPD LPSAAEVSRR IFAFSPHHPH PSVSVLYTGW GQMIMHDIVA
TQEGTEPMPI PLPTQWQCNV PPLPIVAGTF SCPSPEAETP ESIPFNRSHY EVGDDNVRVP
VNTRTAWLDG SSLYGVEREA VMALREGRGG RLKMDDEGFP PRVPGGDKGC ELFAFAQGAV
NLHPVLTSIG IVMVREHNRY AKLLESRHPD WDDEAIFREA KAWVVALIQK ITFYWYLPIL
LGSPLPSWQA HNATIDPQVD VFNAATAFRY GHFAISDTVF LLSAHFTTHP LGHQPLLATI
RRPCAIREAG VEPVLRGAMV QPEEKMEAVM GQSVRLASPA DLPALNIQRN RDWGVALYND
MREAYGLHRV SSLEELVGRD RSDLLEALED MYDGIDAVEA YVGAMLEPLE LAKSSGYDAT
TPVVPPLIAV SIRDAFTRLR SSDRFWHEQY LPYLRDSIPY ETAKKELPWF PFRDVELARD
LATYGLTELL LNNTRLCWAP PNPFRIESFA NAREGLQKTM KMDTTLPKWT QCDEGAMPEP
FTSTRRQSLT FLSGQYQLEW EVRPPNMGDG SAPNRMDITI SGRTSGWVGL GVSPDGRMIG
ADLLIGWIDA DTAAPVLHRY TGGPDRYPVA VREEMDIDTQ TVSGREMVVN GESWTTLSFS
RPLRWPSGDG KAIKLGETTT ILVAFGPEGA KELRFHGSRR QVAMVDFASG RSTVMESSKS
VLYVHGLIMW FLASILIPGS FCSVRYFKHR EGWLNMHERL ALMSMSNMIG MAFSALASTN
AILATPHSIL GLLLVGCIAL QTILGISNKY WHYSASKRIL PRHARVVLRF LHALLGTTIL
LASLANSVFG AKALFPNHPI WVVQLLIVLA ITCMIGLLEF RRRLPTHFFA FVDSLPPYLR
VGVLSPVEAQ PLVQQPTKQP KWHPLRILQR LGGGGLNVIG SGEQSFTPDC VCEAVENGSQ
WVVVLDGVYD IRNFVGSHPG GTALLERHVG CDITALFLGL VVPGSATSDL RSTPRASPIT
MPRRPRFATI GVTVQAATSA ENAPVASPSA PPHDNGTANT GGSGCAAGGG QQVAPCAMAS
IMEIGRRFSN SGRVIRLGSP TRAESFEPTV VGRPHSVFAA CTLRKYRVGT LSLQDGRGER
EGSFNPPPSY FPQKVMGPNN AQPALMALLK PLLQASPTPE AIRGRTSTRS DMRQRTLLMY
GMLFKHVSNT PVAKAVGGAG SGSSITHSSL VSVPSEKSSR EATPGKGGNV AAGLYQPFIV
VENTQLNARR PGERQLAIHR ITLESATTLS IEHYRPGLHV CILEDIAGRR FKRSYSVAAT
PSSHLLTFLV KSYPSNGRGM AEFLSSRRQG DTLRLRGFQG TNLLHDAPSV PGMSTDTEED
TDDDAILAFS PARDPHFGVY WPFCAVISAG TGMTPFLNLI RHQGQVMGRL ARDPTTRQAA
LLSQLSVLHV SRHRDEALAL GWDEIRSIKA TVNGALADAP APRVTANVVI SGESRGQSAI
EAIFKHAARP GRAAQLHRGG LDGDNDVHET ATVDRQLLEA CVPWLGRLSS RPSTPHTPPL
QELPEESVLV AQEESPRDPP AMQTRQSPKH DKWLQSTPVT VLKSLVHRAK GGASPTQPTQ
TVNGTPEQSA FLSAWSMAAP AQQEPSLSAI LARGPSPSTA RIFICGPASW VHSMRRVLES
EMRVPREYVK TL
//
