ID A0A1Q9DFU7_SYMMI Unreviewed; 2197 AA.
AC A0A1Q9DFU7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 1 {ECO:0000313|EMBL:OLP94042.1};
GN Name=PFP-BETA1 {ECO:0000313|EMBL:OLP94042.1};
GN ORFNames=AK812_SmicGene23994 {ECO:0000313|EMBL:OLP94042.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP94042.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP94042.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP94042.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT 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 EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLP94042.1}.
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DR EMBL; LSRX01000561; OLP94042.1; -; Genomic_DNA.
DR OrthoDB; 5475862at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR Gene3D; 2.60.40.2030; -; 1.
DR Gene3D; 3.40.50.450; -; 2.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 1.20.5.1230; Apolipoprotein A-I; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR035966; PKF_sf.
DR PANTHER; PTHR43650; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR43650:SF1; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT BETA 1; 1.
DR Pfam; PF03160; Calx-beta; 1.
DR SMART; SM00237; Calx_beta; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF58113; Apolipoprotein A-I; 1.
DR SUPFAM; SSF141072; CalX-like; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:OLP94042.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1490..1508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1685..1702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1264..1360
FT /note="Calx-beta"
FT /evidence="ECO:0000259|SMART:SM00237"
FT REGION 463..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1926..1960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1982..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2087..2197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 157..184
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 466..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..719
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1982..2012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2087..2130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2154..2175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2197 AA; 242177 MW; 147B69942F7F7285 CRC64;
MDAGMTVMDA AMGPAHMQML TPQTFLAGVG AVCFVLLVSC LCRSTTPGGD YFLKAQVGQI
LAQQLQEQLP EILQTSLQPV MDSLTSQVAE DKFTEVLQST LQPLREAVEK QAADASPYTA
DEAKTQLQKL LETYQVDMET QLKSLRDDME GIHGQQIRAV GKEVEALQTQ LAQAMQKANT
AEQGRFGTLD GALKTRFDAL EAGVKSRIDL LNNDFNQKLD GVDKALKQTV QDLGKAPQDI
KAALDKVDAT VVAWDKACTK LMAHCDRTEN MLREKFGSLQ GDTNKIIGET AQLGRDWQSS
LRSNTKALDS LQQAVATMGA ALSNRPLDST GVTEAVEIGR NMQNQISELV NQATETTGHL
REVRDQLRQP RVAEVRSSHQ ETAPAAAAAP SIINLASRIP PTTTGGLVRV ILSNGREVLT
SEDEVLGPPA FPYGSRAVGH VAVSHDDATL AFAVEAGDRL IRKHGSSSSG DSVKSSKSRS
SSSGCVMEEP AHQPAQPASD NPVNPDIDRA KKEALEQLLK LKSVESREQR MKEWRELLRH
WHPDKNPHRT EVATAVFQFL QKGKPMLDLL CQFGDPSTLA FKDHLQAAIE TISRHKLDGL
VMVGNEANQV DSAFLAEACA ASRLSTRVIG VPEGRKEGRK EGEKADGGAG DELVKIVAKW
NPAVEEESKS TKKPWLSSGM GEHKTPRLPS CATAKKTKAK KAKEKKKQKE KKEKKQKKTA
KTGKHDTADA GDPTKTDDVQ CNNAAANPSH EEVDWGTDDD EAELDSTPNA ATNLGECDSD
NEDAPTTAPE GYGSVCEVAA LPLRSNSLYP KVVRAPPTAR SGVQVARAGG HSATWSYVAS
GTASAEAHAG RQTTTVKETR NSERPEHAAC GGNMGQPEWQ PEGVPAIVVG RLLEADLSWK
KREAPHCSIV CVYRHGELKQ SGVRGNLHLS ARSDGNPDRA KTVSLDCNFP FVQQTIGFDT
VTRTLSAFIG TIGNLVKTSR NMWIFVRTMG DAWSHVAVQI ALQTHVHMVL LSGSQLLGQY
LVNIVSCLCD LIVKRHDAGE DYGIIMLPVG FVNDILELRI LFSELMEVMS KDHYEQSWES
IPKIAARLKP ATAALFDVIP RDVQFEICFG GRERYMNKID FSTISTDRLL LRFVEMELLR
RRQLGHISKS AMPEEDKWSA VPLLAPTRTC CECSKVSIDI DECTSQDPRG SASEAFALSW
LKDEASDDDI ARVLTQLLLA RPEAEPTLLA VLNCVAAIPG EFGRKTRGGL VDPPEIVDLP
EVSLDVPVAD RPRLRFATCN YFVGEEELKV EVQVLRSGNL NCESRVQMHT RDLSAKAGIN
YVHASKMLVF KPQAESVLFS VDLIASDEWS PTLEFEVVLD PTTVTNADLD AYGARSRVKI
DDKDAFPSNV VDVRQLAKSL SWEHLRQALE NAPMLVLMAE YLKLNFRNDV VRRGTFKMCL
QGQCHHLYGI LRLFLSVLLV DRVLKGSEED WMAGTTDSLS EWLFHTRPGM LVLVMSGMLI
PFVGLHYLDF ISMTWRVGGT SRAQLLSALV RRLLHYDVTS RIDIKQGAEI MAMTKDVDDI
VQNGYMGVLE IISHLQNLAT VLAYQVISRL ILQEPISPWS IAPLLIHPIL LAMFAICRRS
ATVDVQQVEN AERSALVSQM QNVTLNNTII RNLGGVWKAI DQFESRVAGY NTAVNSTLQV
MKNNIYFTNW VGLAMLAAYT LVGGLEVVDG KMRMGLFLAD ITLFTQINVT WSMICSRGVE
INSIFPGLER VVILMNLPTD LPERRRLLRE NLYRTIVSYL QTDDLANHAG EQRDKQWKAS
RITSTAFLMH TGAEASDSIA LMSWKVAVSG HRKSGPQAGN AIFSYTLVAE SKSFRSWVAA
SDYALKKHLE DPPYYDVFFN VDGSPKEQEE PTSRPNIAVV APGDKQIEAM KAMKTKKATK
TKKAMKAMKL PSKAMQAMKK PAAATKTTKA MKAMKRPSRA MHAIKKPATA MKAMKAMKVV
KTMKDGNKKK DDDKMAKKKD DDRKKDDDMP GWLVDPFRYT DDDGVIRVEV SQLEVGDNGT
DFICTDGMDV NQSIQAMISS MEFAGCSADK ISYQAVGIAV CVKKIDKKKD DDDDDKKKDD
DTGKDDDKKK DDDQGQDDDQ KKDDDTIDMR SMPSSSDGPH KLRGPPGDGL SDLEMDDGSP
KDDDKKKDDD QSEPHTPPEW IPGHVYNSVT RRHEPLE
//