GenomeNet

Database: UniProt
Entry: A0A1Q9D382_SYMMI
LinkDB: A0A1Q9D382_SYMMI
Original site: A0A1Q9D382_SYMMI 
ID   A0A1Q9D382_SYMMI        Unreviewed;      3620 AA.
AC   A0A1Q9D382;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   05-JUN-2019, entry version 15.
DE   SubName: Full=Ferredoxin--NADP reductase, leaf isozyme, chloroplastic {ECO:0000313|EMBL:OLP89627.1};
GN   ORFNames=AK812_SmicGene28881 {ECO:0000313|EMBL:OLP89627.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP89627.1};
RN   [1] {ECO:0000313|EMBL:OLP89627.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP89627.1};
RA   Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M.,
RA   Piel J., Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T.,
RA   Bayer T., Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT   "Genome analysis of coral dinoflagellate symbionts highlights
RT   evolutionary adaptations to a symbiotic lifestyle.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OLP89627.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; LSRX01000751; OLP89627.1; -; Genomic_DNA.
DR   OrthoDB; 817123at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR013026; TPR-contain_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Heme {ECO:0000256|SAAS:SAAS01057964};
KW   Iron {ECO:0000256|SAAS:SAAS01057964};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01057964};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    369    391       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    398    420       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      528    657       FAD-binding FR-type.
FT                                {ECO:0000259|PROSITE:PS51384}.
FT   DOMAIN     1302   1334       Cyclic nucleotide-binding.
FT                                {ECO:0000259|PROSITE:PS50042}.
FT   DOMAIN     2288   2389       TPR_REGION. {ECO:0000259|PROSITE:
FT                                PS50293}.
FT   REPEAT     2288   2321       TPR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00339}.
FT   REPEAT     2322   2355       TPR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00339}.
FT   REPEAT     2356   2389       TPR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00339}.
FT   DOMAIN     2828   2904       RRM. {ECO:0000259|PROSITE:PS50102}.
FT   DOMAIN     3315   3343       Q_MOTIF. {ECO:0000259|PROSITE:PS51195}.
FT   DOMAIN     3346   3407       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   REGION       88    145       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   REGION      254    290       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   REGION     1097   1147       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   REGION     1983   2142       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   REGION     2646   2713       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   REGION     2732   2825       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   REGION     2899   2932       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   REGION     2961   3000       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   REGION     3177   3199       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   COILED     2369   2389       {ECO:0000256|SAM:Coils}.
FT   COILED     3270   3290       {ECO:0000256|SAM:Coils}.
FT   MOTIF      3315   3343       Q motif. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00552}.
FT   COMPBIAS     89    119       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   COMPBIAS    123    145       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   COMPBIAS    260    276       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   COMPBIAS   1986   2009       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   COMPBIAS   2052   2071       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   COMPBIAS   2108   2122       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   COMPBIAS   2770   2804       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
FT   COMPBIAS   2961   2978       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1Q9D382}.
SQ   SEQUENCE   3620 AA;  394738 MW;  8B9D35C6FE1D4590 CRC64;
     MAQRLDTSIF NGYACMAPFC RKLFWKWEEA KRHMHHECKA LPRSTNRPKQ VESIRKALDI
     GRKHREDHPE LQDDRFVFLN ADGAVLPRPQ EVGRKKKDDK LKLNNDGTVD GDVRRDGKSQ
     GAPTIKPVTT DVTAPTAPMT EKPSEQPNIS IFKGYACLAC SCQAVFWEWE EAKHHMLLAC
     ASFPRSIKRP QEVASMRKAL DLARRKHHPE QRGHPPERND EAIFLSADGA LPQEGAFQEA
     RTIELLTVTA PRTAPLLPKP STVANGSQSQ GVRPQSKKRP RTSKISVVPP LPKSATADIS
     NLQIVLWDEA ASQPVNTKDP DVLGVVVEQE CSLLYVDMPR VEQVLGCDDW RSCGGGAGGK
     VAGRVAQEWA VPMAVAALEV EIIVIITIVI ITITTIIIIM IFILIILILI FILIFILIII
     THHPSSIINI ANSNKSHDNR DRNDHSLLHE RLCSALLRWV DVHSWHQAAS NSRSTSPEAR
     APRTLRGASQ AAVTACRAAA VKKKGVKAHG NDLTICRAEP EAPSDIDRGY RRCQLGDDTC
     DSVLDMFLVE VTFDHDGKVP YIEGQSIGVI APGPDKKGET PARIRLYSIA SSAVGDDETS
     KTVSLCVKRV VEDTPDKAGT AFPDNKVYRG VCSNHICDLS VGDDVMITGP TGAEMLLPED
     PEANIVMLAT GTGIAPMRAY CRYLFNDKVA AEGDGRKFKG LAWLFMGVPY SKSLLYDDEH
     QEYISKYPDQ FRYDYAISRE QTNAAGQKMY IQTKMAEYAE ELWELMQDEK THIYMCGLKG
     MESGMAECFT PIAEKYGKDW AEFAKAMKKA DRYHVEELIN QLVASIRDLP FFEDFALPQL
     RGLARGLRFQ SAKNGPGAPG EALPRPLHLP ASRSCQRWPA APEVLLLKGA SEMFVWGLGR
     RSLPKMWVAA LSLQVGKHIL VEVVVAGKYR RVTAGGDELI AAQRRGGKLI DLLAVEQGAY
     REEGKPRGVT KKRLVSPSPG EKTEKKVLLF DGVFRQEIFG SALAVSSQAK AGAGGILPGR
     EVTSSMQDSE KPVSLDMPML AEEVDAATQL ESVGGSGVAD LLCVPLSSPE PAGATQMDTP
     SPVPEASVSV ALINPEPSAH PALETPPRNK RSLTDAEDQL FTPPATARFR RTEGSASASP
     EIPTPPSSEI REVFQARGDR TDILGFDPIL EQPCVMVTAS TQVIHLWAHV YEPDHCISTE
     TYKSQELKKQ LFHRARHTLA QSQKKPDNED GKIYLKRYGD LQKGFVLGQR DIVDPGGREA
     SNRACAAQYP SVQEQLSLLA KLVRNTPELK NFERPTLMQV LGRVLCKQGE IGDQFYAIIE
     SRTDTSPRYD GEEKGTMSRN LHRHSPSHPA CVVDMWGVEA STSAAICNNL EVVMRASPTS
     RRFQKVKLSL QPCWLLFVLS AFSRTSKLSR MARPFHAFLA ALLRQSAQEA VPGDLLGDDE
     CLESSTCALN ALQMRGKAME AVEERQMPWM MMPPPSRWGM PAYHPSPVMP PWRRPEPMGP
     MPYYSPESYM HPQPASYMHP QPVEPADMPQ PEEEHPKMVT RHVKYLPLSP IGWGMIADDE
     GVQVRQLTSD LKGCEGECTK DEKIGRPKVA MLEASKSIAE LRWLLLHLLD PCRGHLAAIG
     EVQHVEVKQC GKDEVPEPSG SCVASTKPEL MTFYQYSAQK KQNVDDRVWE NVNFAKWPHS
     ARANIGGVMF YLHNEVVDKA GEMRNAEGDR TPKFNIDRIL RFKVTMKNPE ALWKKYRQFI
     QFDYGQATFG MPNHVEKCNE IWETVGYEVD ACKIEDAVEG QDKAPQGGYA KTAECMERQG
     RAGYAGEDPF MSTGRFILLD DLVGQNLKEL YKKGGTQYDK KLDCKNCVTT DAGQGTSFWN
     GKKDTAKCKE RWHVHAAHGF GHVMLTSKPH DHMVTSRFAI SRQQKRNLFA EKYRDQPAAL
     TVRPPKIGLE AQFWAGEWQE RFCEGDAAGG LSRLESALTA DRAARPQCCY AYGLDLVAKC
     PGAKTRNKRS QLSDTSKNLS PSSSPIPGVV APVSSGGSGL APVPVAPKGA HRGRRHGVRL
     TFHEDSDEAK RSSLQLQVPL KRSSRTPSVA EELSTSDREE SSLPTPPLSP PALASPEPEV
     AEEEEASSEN SLGASPSISP MPSEKDTDEG PQQSEVPGSE VTQDLGKMVN RLGAGAAFGA
     KTLLKKARTA SVMTVEPTKL LVLALVVTRE DYVALLGSME EARQMSFPKL PPAPIFGALP
     WEPRSVGPRG PVIKPSAAMV VRAANGRKKP KARKAAGLLK RKAAEPSVPF WNRETPYSRL
     AMEQCSSADT VFRQATALAE DGHFGRAAEL FQKASQLDPS SAKHYEARAQ CLMELGQFQG
     AVASAEQAVK LSADWLPGKA TLGRALFNAG QLEDAVGQFE EALKLAESDP EWAAELGGEL
     AEFTSLLHRH WAEHHDILLP VRAGLQLRIR QALNCRYCRL SNAELGPGGA VWGAGCILAT
     QAPSILAGLE KPRPRILELG SGTGAAGLAA AAVGAEVVLT DHSNLLNLIQ LNTQMNAHFI
     QSAGGSASSC AFDWEEKPAD ELLQRHFDLV IGADLVYSFA AVEPFTVALQ AVLLPQAAEG
     RTQALAPAML YAHYPRFPDL DTAMTTALAA RGLVLQERAL PPWKGDVGSI PEDVLCHVKL
     LEIRPGTPST SGAVSEGQQD QHGGGHGWDY HPMDCDCGQE HGQQDAQPGH GEPGHGYGGD
     GHGQPTVGPS EGEQPLAAEV SAFVESLGGL GGVADATWKR PKIPTEEEDL PPELQDAEIL
     GGSSDADASI SSEDEGKVPM NRKERKEAEK QARKQAEAEK KVQQAKAPAK TPAKPAAQSQ
     SAGGKRDGQI FLAALPPSVD GDTLRKDFAK FGEISRFYFH KDSDGSPRGT ACIFYKDPDD
     ADKVILLDGI DYKGNAIKVK RRPPRKPGGK QVKKQQERAV NEAAPTKEPA ATQTSVPFAC
     KAPGSGILKR TQKHVAKHTA AKEAEVTADE AMPEGAPKAK KAKRKRVGPF APRPPPANGQ
     LLTDRSSHFE GNVGASDLSV PYEAEWGKNE MKSCTLDRGS AVALTVLLRH GEPECKEVTI
     LRQAQGAVAF CYPPGHEGKE ARSARTPRYA AAAMGASQIV TTPGELIGVY SAIFKATVRV
     ESATCDIYRV PWAGYASNVQ QAEPPIINSQ ESKSINWLGA VVMALVTEAF SLGAPPTLPV
     TRPAPPHGRT RGAPERGVSS TLTPAATALA AGVLANRRSG GARGAPARGV RIQAVSSRTN
     GLVEPHVEGP TDLEQELGSL GAKAADVQAM ELSKLEAEEA EDEEAEEEGS ALEPAKRIVN
     TREVELWPGI PDPMVDFGGL PIPQRLADAF TERGILQPSS IQELVMPKLA KGEHIILHAP
     TGSGKTLAYL LPILARLQPT MHVGAQAIIF VPTPELALQV TRELKWLIYV LAGGSDGTCW
     FNPQVPQGFS CDPASDAFDP RFRCLETCLG YGSSSQNFLR TQYFRLGDPC IMAPMSHPMD
     QQITAEGPTI AIFNVAMIGH VNPTFALVQE LCKRGCKVSY FLPPVAPIRA AAMESGAVVE
     GYLPEDPSDF VMEKCGIDEP LCHVVPEILE DDRALYERAV WPLAQALLCG EYVIERCRQL
     GVSVVLYDPS CPLGSWQPRS
//
DBGET integrated database retrieval system