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
//