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Database: UniProt
Entry: M7BXQ5_CHEMY
LinkDB: M7BXQ5_CHEMY
Original site: M7BXQ5_CHEMY 
ID   M7BXQ5_CHEMY            Unreviewed;       907 AA.
AC   M7BXQ5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=NADH-cytochrome b5 reductase 2 {ECO:0000313|EMBL:EMP36818.1};
GN   ORFNames=UY3_05984 {ECO:0000313|EMBL:EMP36818.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP36818.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
CC   -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC       reductase family. {ECO:0000256|ARBA:ARBA00006105}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   EMBL; KB523694; EMP36818.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7BXQ5; -.
DR   STRING; 8469.M7BXQ5; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd06183; cyt_b5_reduct_like; 1.
DR   CDD; cd00190; Tryp_SPc; 2.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   PANTHER; PTHR24253:SF156; SERINE PROTEASE 48; 1.
DR   PANTHER; PTHR24253; TRANSMEMBRANE PROTEASE SERINE; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF00089; Trypsin; 2.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00020; Tryp_SPc; 2.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 2.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00059}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        638..656
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..224
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DOMAIN          136..285
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          295..407
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          452..748
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DOMAIN          674..786
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DISULFID        295..322
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
SQ   SEQUENCE   907 AA;  101655 MW;  95EBF4CC289B30B6 CRC64;
     MKPWNNFNLL TRIVGGNQVK QGSHPWQVSL KRWQRHFCGG TIVSAQWVVT AAHCVLDRHL
     RDYLNITAGE HDLSLMEEGE QTLPVKAIIK HPNFNPKRPM NYDIALVKLD GAFNFNGILP
     QVLHEVDLPI LDNKECSRAL STLRNPIRGD TLMCAGFPDG GKDACQVGGT DSLADLAVAH
     ISVVCCLIAN KNSSSLCHCR LCVWTLLVPE GMHILLNFSH FDVESDIFCD YDSLSVYSKD
     DRLVGRFCGV DSPLPILLSS NGIKLKFVSD NKASGTGFSM VYRALSPDAL PDSGCGSLAV
     LFEGGVIQSM NYPEPYNNLA DCHWIIHAPE NHVIKLTYEY FEIEENEDCS YDSVTVYEDV
     TREEEIARSC GFAVPAPVLS TSSMMLIIFH SDETETFGGF QATFSFIHVA DLNISDSNNE
     TAPPEGVDTT TEIPDDICGV PSNQPRFLFS RIMGGEEAVP FSWPWQVSIQ ISAEHICGGA
     ALTKEWVVTA AHCFTYKEQY RDLWMVVAGL HDITEQEHSQ RRSVKQYIIH QDFNEITMDS
     DIALLQLTEP LEFNHYVRPV CLPEKDEVVQ PSRVCTTTGW GTHNEDREKS NKLQQLEVPI
     LVSEACQNYY VSHPGKVTQR MLCAGFPLEE GKDSCTDLAL LIAVVVIAVS ALLLVFKARR
     SQRKSDPITL QEPHTKYPLP LIKKEEISHD TRKFRFGLPS PDHVLGLPIG QHVYLSSKIN
     GNLVIRAYTP VSSDEVKGYV DLIIKVYYKN VHPKFPEGGK MSQYLDSMTV GDTIDFRGPN
     GLLVYKGTGI TPMLQLIRHI TKDPNDDTKC YLLFANQTEK DILLRAELEE VAKNHPDQFK
     VRYTLDRPPH DWKYSSGFIT AEMIKAYLPP PGRDTLILMC GPPPMIQFAC QPNLEKLGYL
     KDNTFAY
//
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