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Database: UniProt
Entry: C5LJM6_PERM5
LinkDB: C5LJM6_PERM5
Original site: C5LJM6_PERM5 
ID   C5LJM6_PERM5            Unreviewed;      1357 AA.
AC   C5LJM6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Succinate dehydrogenase, putative {ECO:0000313|EMBL:EER03043.1};
GN   ORFNames=Pmar_PMAR001788 {ECO:0000313|EMBL:EER03043.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EER03043.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC       {ECO:0000256|ARBA:ARBA00038168}.
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DR   EMBL; GG682469; EER03043.1; -; Genomic_DNA.
DR   RefSeq; XP_002771227.1; XM_002771181.1.
DR   EnsemblProtists; EER03043; EER03043; Pmar_PMAR001788.
DR   GeneID; 9051709; -.
DR   InParanoid; C5LJM6; -.
DR   Proteomes; UP000007800; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 6.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 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; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR010960; Flavocytochrome_c.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR   PANTHER; PTHR19359; CYTOCHROME B5; 1.
DR   Pfam; PF00173; Cyt-b5; 6.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   SMART; SM01117; Cyt-b5; 6.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 6.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 6.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 6.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1093..1112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1133..1154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1174..1198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1210..1233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1276..1297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1317..1339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          427..503
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          532..608
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          629..705
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          736..812
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          837..913
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          968..1044
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          716..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          921..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..737
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        926..940
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1357 AA;  145586 MW;  3CD1C6460037F1D5 CRC64;
     MVEHSGPSVN WLMDVFGLDL SLLSRLGGHS VERTHRGKER FPGMTITYAE MQMAEAIAKA
     HPDKCQIINK ARATELETDN EGNVIGVKYE KDGKSYVVDG PVILATGGYG ADFTKDGLLA
     KYRPDLLKLS TTNGEHCTGD GIKMGVAADA DVVDLEWVQV HPTGLVNPKD PDSKVKFLAA
     EALRGVGGIL LDADGHRFSN ELGRRDYVSD RMFHNKGPFR LVLNTASANE IRWHVEHYKG
     RGVMKDFDSA YDLAKEMGIP ASTLEQTFKD YKEVASKQEA NPDGGEYDAY PTGKTFDKFG
     KKFFTNYDFK MDDHYSVAIV TPLVHYCMGG LKIDTAGRVI SKETKKPIRG LYAAGEVMGG
     VHGNNRLGGN SLLDCVVFGR LTADDACEGL LGLKKSVSLP ALAKAPASVP KKVAQAKVAA
     APAAPVVHGY TKEEVAKHTT ESDCWVIING QVLNVTNFLP EHPGGKLAIM TFAGKDASKE
     FNMIHPSDVI EKYAPDCVLG PVVDKATAAA APVAPAAPAA VTVTPTNSAA AGKSYTMEEI
     SKHNSRESCW VVIDGEVLDV TGFLPDHPGG DISILNYGGK DATEPFHDIH PAGIIQKYCP
     DAVIGVVGTG SAAPSTVSTA PASAPAPAVS GYTKEEVAKH ITESDCWVII NGQVLNVTNF
     LPEHPGGKLA IMTFAGKDAT KEFNMIHPAD VIEKYASECV LGPVVEANSA PAVAATSAPA
     APTAVTTTPT TSGAAGKSYT MDEISKHNSR ESCWVVIDGE VLDVTDFLPD HPGGDISILN
     FGGRDATGPF HDIHPAGIIQ KYCPDAVIGV VGTGSAAPST ASTAPASAAA SAPAPAVSGY
     TMDEVAKHTT EDDCWVAING QVLNVTDFLP EHPGGKLAIM TFAGKDATKE FNMIHPPDVI
     EKYASECVLG PVIEGKSAPA PVASTPAPVA STPAPAPVAS KPAPATSTAA STPAPTPVAP
     VVATSAAASG ITMDEVAKHT TEDDCWVVIN GEVLDVTDFL PKHPGGKMAI LTFAGKDASK
     EFNMIHPAGV IAKYAPDATL GPLVEKTAGP AAAGGDLSQP LLADQFESKA LTEQWWGEDR
     NKSDMFGPLG PSISSYAISL CYLIWMFVID TLKTIFSVKN YKVLSDKSGL QRSAIFMMVF
     VTIHALGNIN LLVGDRNFEG YAYLLNHPCP WSTLFLPVEI YLLLAGILHV VVATVRTFKF
     KSMNSSFRDL EMFITGCILL IFLIVHLIQF RFVSEASAPK YWMRDNWFPC ADDDTSCPII
     HFKDLYKMAF QIFESFGWVC FYIVGVIAFF IHMKSGLSRV IMTNGNIPRK YKSTTQFWGS
     VMSWVLFLLY LTYPLFAYFN PVKDWAAYDA KQIRPKF
//
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