ID A0A151NTV9_ALLMI Unreviewed; 789 AA.
AC A0A151NTV9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=XK-related protein {ECO:0000256|RuleBase:RU910716};
GN Name=NOX3 {ECO:0000313|EMBL:KYO40183.1};
GN ORFNames=Y1Q_0000031 {ECO:0000313|EMBL:KYO40183.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO40183.1};
RN [1] {ECO:0000313|EMBL:KYO40183.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO40183.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU910716}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU910716}.
CC -!- SIMILARITY: Belongs to the XK family. {ECO:0000256|ARBA:ARBA00008789,
CC ECO:0000256|RuleBase:RU910716}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO40183.1}.
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DR EMBL; AKHW03002066; KYO40183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151NTV9; -.
DR STRING; 8496.A0A151NTV9; -.
DR eggNOG; KOG0039; Eukaryota.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR018629; XK-rel.
DR PANTHER; PTHR11972:SF60; CYTOCHROME B-245 HEAVY CHAIN; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR Pfam; PF09815; XK-related; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00022882};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU910716};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU910716};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU910716}; Transport {ECO:0000256|ARBA:ARBA00022882};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..789
FT /note="XK-related protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007586360"
FT TRANSMEM 35..58
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU910716"
FT TRANSMEM 241..263
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU910716"
FT TRANSMEM 275..300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU910716"
FT TRANSMEM 334..352
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU910716"
FT TRANSMEM 398..423
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU910716"
FT TRANSMEM 435..456
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU910716"
FT DOMAIN 516..626
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 789 AA; 90249 MW; 2559E3179680F5DA CRC64;
MKFPGSVLVS LFLFVAETAA ALALGSTYRA AGDRMWLALT LLFALLPCAL VQFSLVFVHR
DLSRDRPLVL LLHLLQLGPL VRCVEVFYIY FHAGRVEEPY VSITKKRQMP KDGHSEEVEK
EVGQAEGKLF THRSAFSRAS VIQAFLGSAP QLTLQLYISV LQQEITAARK ARSFGVLQFT
LAETAQNSYR YLFHIWLTSP VSTQLESSTD VIFSRTMKDI VDNQTAKSKA TMGNWVENEG
LSIFVIVVWL GLNIFLFWWY YLVYDVGKEY IYTRVLLGHA LALARAPAAC LNFNCMLILL
PVCRNLLSFL RGSSACCSTR IRRQLDRNLT FHKMVAWMIA LHTAIHTIAH LFNVEWLVEA
RLNEEGNLSY ALSQLGDKPD QTYLNFVRER YKNPVGGLYV AFTYLAGLTG VIITLCLILI
ITSSTKTIRR SYFEVFWYTH HLFVIFFIGL VIHGVGRIVR RQTKESLEVH SPQDCANYNE
WGSQKCPVPQ FAGNPPMTWK WVVAPMFLYL CERLVRFWRS QQKVVITKVV VHPFKTIELQ
MMKKGFKMEV GQYIFVKCPA ISRLEWHPFT LTSAPEEDYF SIHVRIVGDW TEGLFNVCGC
DKQEFQEAWK LPKIAVDGPF GTASEDVFSY ETVMLVGAGI GVTPFASVLK SVWYKYCHDA
TNLRLKKIYF YWLCRDTHAF EWFADLLQSL ETQMQERDNA EFLSYNIYLT GWDESQATHF
AVHHDEKKDV ITGLTQKTLY GRPNWENEFK TIAQKHTGSR IGVFLCGPEA LADSLNKQSI
NNSEADPRG
//
