ID A0A166ALE7_DAUCS Unreviewed; 1130 AA.
AC A0A166ALE7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Steroid 5-alpha reductase C-terminal domain-containing protein {ECO:0000259|PROSITE:PS50244};
GN ORFNames=DCAR_010202 {ECO:0000313|EMBL:KZN01448.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZN01448.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZN01448.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZN01448.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the disease resistance NB-LRR family.
CC {ECO:0000256|ARBA:ARBA00008894}.
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:KZN01448.1}.
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DR EMBL; LNRQ01000003; KZN01448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166ALE7; -.
DR EnsemblPlants; KZN01448; KZN01448; DCAR_010202.
DR Gramene; KZN01448; KZN01448; DCAR_010202.
DR OMA; ENDHENK; -.
DR Proteomes; UP000077755; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.120.1630; -; 1.
DR Gene3D; 1.10.8.430; Helical domain of apoptotic protease-activating factors; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010721; UstE-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR33463; NB-ARC DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR33463:SF205; RPP4C3; 1.
DR Pfam; PF06966; DUF1295; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR PRINTS; PR00364; DISEASERSIST.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Plant defense {ECO:0000256|ARBA:ARBA00022821};
KW Reference proteome {ECO:0000313|Proteomes:UP000077755};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 887..906
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 927..947
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 959..978
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1009..1027
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1033..1054
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 964..1032
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 1130 AA; 128637 MW; E57FC0AE9965831B CRC64;
MCSLSDIPVV GKAVDKISVV IVEAGTRGLV HLFCYKGVVK DLKATKINEL QIQEESVARK
AAAAKNNGQI LLKHVVDWQE KVVEIKDQVK VFVEEYENRP SWLCCFEALR IPDPVTRFRL
GRSGAKMSKR VEELIESGKE LVHEDIAQYP PFENVPISGG DRYYNFESRR TAYGKIWEAL
VKEDGFSVLG IYGMPGVGKT RMMEQTWKEI KEKGVFDKVA RANFGNGKLD VINIQEQLSF
HLECHLESKD NEEYRAFQLR NSIMNGGKIL FILDDVWRYI PLNRIGISFD EGTPGGCKIL
FTSRAQDVCL KNNCKDPVRI DTLTAEEAWE MFSNVVGSSK IYSLLDKTLA MRVCNKCARL
PLLIVAVGNS VAIMGECQWK DALDLLENHK IEKIHGIEGD IFACVELSFN QLHEDEKIFL
LLCSLYREDA EIDKSLLFKL ATDCELLEGK RDRVHSIVQN LKSSSLLLPG RNDKYIRLHD
IIRDVARSIA SRQEYAFLSI TCNSWLPNQS AYSTRKVMYL NLEVDNVSSP DDLVCPDLHT
LWLQSNFHSQ QLSDSFFKMF PNLRFLRYPD MAPIQPRDSD SSTKYFVCCD TIVGGGKTLA
ERAENLFLTN VGTTNPFIDN NKGAFKDLRV LYMENCHYVE NLAKIPGEES KHIQQLTAFS
NLSVLNIVDC RGMTYLFSAS VAQGLVQLQV LLVRNCPAME VIIGSEGTDN KKVIKFAQLK
SIVLKAMPKL KSFYGHRRYI NSTTTESTDV SSVHPASLFD KMVVFPSLVE LKIIMLKVAS
DVWGENDHEN KLKNLEKLDI KFCSKLRNVM SPWIARDLVH LKVMRVRGCA MIKEIIAASG
RSKQETDDEI VFPVLLSLEL IHLPSLINFW CYESWEPKNE QRQPHKVILS LLVIVWGIRL
AIFLLMRILQ WGEDRRFDEM RDNLGKLAFF WMFQAVWVWA VSLPLTVVNA SDKDPSLKAA
DIIGWIMWSI GIISEATADQ QKLTFKNSPE NRGKWCNIGL WKYSRHPNYF GELFLWWGIF
IASTPILNGA EWLVILGPIF LTLLLLFVSG IPLLEVSADK KFGNVDAYRM YKETTSPLIP
LPPVVYGKLP SWIKKVFLFE FPLYSKTLPQ GELSWYRSNS GGSREGMKLG
//
