ID A0A2I0J1Z4_PUNGR Unreviewed; 744 AA.
AC A0A2I0J1Z4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=CRG98_029327 {ECO:0000313|EMBL:PKI50254.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:PKI50254.1, ECO:0000313|Proteomes:UP000233551};
RN [1] {ECO:0000313|EMBL:PKI50254.1, ECO:0000313|Proteomes:UP000233551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AG2017 {ECO:0000313|Proteomes:UP000233551};
RC TISSUE=Leaf {ECO:0000313|EMBL:PKI50254.1};
RA Akparov Z., Amiraslanov A., Hajiyeva S., Abbasov M., Kaur K., Hamwieh A.,
RA Solovyev V., Salamov A., Braich B., Kosarev P., Mahmoud A., Hajiyev E.,
RA Babayeva S., Izzatullayeva V., Mammadov A., Mammadov A., Sharifova S.,
RA Ojaghi J., Eynullazada K., Bayramov B., Abdulazimova A., Shahmuradov I.;
RT "De-novo sequencing of pomegranate (Punica granatum L.) genome.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PKI50254.1}.
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DR EMBL; PGOL01002138; PKI50254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0J1Z4; -.
DR STRING; 22663.A0A2I0J1Z4; -.
DR Proteomes; UP000233551; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; 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; 2.
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 PANTHER; PTHR11972:SF69; METALLOREDUCTASE AIM14-RELATED; 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 SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000233551};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 579..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 617..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 343..458
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 744 AA; 82789 MW; BB115502029A7E7B CRC64;
MEELSGSAEH QYLLSSKDPA PPCSESIAAG RILVKWFLEM AMGLIFAAWV TFIFLFPAPL
VTELYYEWRA LTSDTIFGGN GSAFLIFSGP VLAITILAIA RRIVMCSREE QFVLWKLKPA
KYPRFRLSTF PVVADGPFGV VSAAELIGIC LVVAYVVWAI SAYTLEDLSE YSKSPLPPIL
KSATMLEFLA SRIGIVGEFC LAFLFLPVAR GSALLRLVDI PFDRAARYHV WLGHLTMLLF
TLHGLLYVIA WAMQGTLLEE ITSWQVSDTS NFAGVIGLSV GLLMWVTSLP PVRKMQFEVF
FYTHQLYIVF VIFFAMHVGD YFFTFACGAI FLFLLDRFLR FCQSRRTVNV ISATRLSCGI
IKLVLSKPAS LRYNALSSIF LQIRELSWLQ WHPFSVASSP LDGKNHLSVL IKVSGEWTAK
LDRNMLDNQE TCDQNETTFL PPKITASVEG PYGHEFPYHL SYENLVLVAG GIGISPFFAI
LSDILHRVGE GKPCLTSNVL LVWAIKKSNE LPLLSTLDME SICAFSPDKL NLDIVIYITQ
ESAPSLEEGI IIESAESSHV FPVSNGCGIS VLAGTGNNIW LGLYVMSSIA GFIVLMTLLE
IFNLLSYTET KSRYRGLLFV VCMLASVIIF GGPAVFLWSC WEKRTSAVEK SEHCEQNVQT
APLMPSNLPQ RESISSRRVL YCSRPNFQEI FGSVSDQWGH VDIGVIVCGP ATLETSVAGE
CRSRNLKRGS DSPIFHFHSH SFVL
//
