ID A0A1Q9E9V0_SYMMI Unreviewed; 2419 AA.
AC A0A1Q9E9V0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cysteine desulfurase, mitochondrial {ECO:0000313|EMBL:OLQ04193.1};
GN Name=NFS1 {ECO:0000313|EMBL:OLQ04193.1};
GN ORFNames=AK812_SmicGene12751 {ECO:0000313|EMBL:OLQ04193.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ04193.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ04193.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ04193.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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:OLQ04193.1}.
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DR EMBL; LSRX01000216; OLQ04193.1; -; Genomic_DNA.
DR OrthoDB; 212394at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 1.10.260.50; -; 1.
DR Gene3D; 3.30.230.80; -; 2.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00331; Cys_desulf_IscS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR010240; Cys_deSase_IscS.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR PANTHER; PTHR11528:SF41; HEAT SHOCK PROTEIN 90-6, MITOCHONDRIAL; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 2.
DR Pfam; PF07690; MFS_1; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 543..566
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 578..597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 671..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 714..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 762..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 798..817
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 823..840
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 872..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 911..931
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1058..1080
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 510..928
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT REGION 313..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2250..2284
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 997..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2419 AA; 268033 MW; 6A402E17FB7FC415 CRC64;
MHDTSSLLYH TGPVRLECTT LIFVVTQVTM EALSDDSTVR QLYMFWEPIL GSRLDVWDVW
ALQFAVMFCL AVQLIASFCM GVFLMSTRSE LRLIRESLRQ ERQTYLHTGV VTSDSPRIFS
MVLREGLQRD HNKVMDQIRL LGKELEEYKE RFLAVQGLLV VIKDHSAPLL RTVPDYLQQI
QNHLDDIKDS FDEGVTKQMD VLETRLISFE QEFAMQRDKI PESINKQNQA VEKICINTTV
SMTQTQTTID NLATAVEELR TYVHDTNSML IEISRHFSAT TIVIQQNQEA MNQKIDKVNG
RLLSLRGILE DKSVIGPAEE EPTQDTSAPT SSDHTEATEP TEAHRSLEGA MDMDIFAVPP
PTAHFVAVLF YNYMRQMRRQ IATSRSEAIL AGLVLGSGSF QLQLLRLAEE RRLVSGYVNF
APDARLAILA VNRQHVDVQV RQTSQRTESP HTLSTMAELT AVAAPPSPAK VDGNDIVDES
TIVDPKSYNT EKATAKSEKP TEEREPRGII LFWLCCVSAL EGLDTQLVPA CQFALQRDLG
LSLGHFAILT TVQMVLTNLA APFWGILADR GTMKRKHILF VGALGEGLAV AIFAFVPNFF
VMVLLRGMSG FFLASLRPVC NGLIADLTSD NRRGKIFGRV QSALLFGMFC SLLIAGNVAN
PYVGNIPGWR FLFAGAGVVA FCVAAGVAGF LVEPPHQLDT AAEKKGCAAV GAELCTVVNF
LCIPTFCVLI MQGVFGTIPW SVMGNNLLYF KLCGLEDWEA SILASEGTVM GMFGNIIGGM
VADALARRFG YHGRPLSAQI TVAIGIPLVF LQFYGIPAGA GSFGTYFALI AAFGILGSWA
QSGTNFPILS DIVPASDRSK VMAWECAMEN SLANAIGPAM VSSLAIGVFG YRFGEEELSG
QSLSSATALG SAMALTICVP WMITLAVYTL LHWSYPLDMR RLLAKQRAAA EVCSWHLPCP
VGEKVTRLCL ARQPHVLPSA PVVLVLEAQL ASPALEARAE SRRRREEGRS PGRGPSQLHH
VVFAAVLWFS ISRQKSGDPN RMAVKAGMAD RRRTSSSLLT AVVFGLLASY LAPTAFSWLA
KPAASGARGF RPRTSLRAVE AATEVSTDAA EGEEFEFQAE VGRVMDIIVN SLYSNKEKDA
LRYIGLQART REVRADPRQR RRRRQCQEPS GGLLAGTPLR GAFDGHEKTA QVLLDAGADI
RTCIKQNLGG LSASAVKQCL RTSAVPAAAL AVAVFGRGCR GLDVPLKTPL MSQTSNRRLR
GMIKFDSATS GARGTYMLVL DVMDVGVLIA CLMADVFLRE LVSNAADACD KKRFLALTES
DAPPEPMKLQ IKTDKDARTL TIEDNGVGMT KAELQENLGR IARSGTANFV KDLGSGEADV
SLIGQFGVGF YSSFLVANKV EVYSKSFKKE GEGKAHRWTS EGHSYKLAEI DDGDFFGEQS
GTKIVLHLRE EAQEYLDTGK LSDLLKKYSE FITFPIELWN EKVQYDQVPD ESAPPPKEGE
KQKMKSVPRS VYEWDVMNKM KPIWLRNPDV VNESEYTEFY KTTFKAFDEP LTTTHFKVEG
QIEFRALIFI PSTMPFELTR DMFSPEGRAM RLYVKRVFIN DKFEEGQAFS PDQIQISAQD
GKGHCEVGVM ALSQLRFALR GRSLAIPVRS AVGARRFKGS LWNEHEERGG PSYLDMQSTT
PVDPRVLDAM LPYYHGRFGN PHSRSHSYGW DAEEATEKAR VQIAKLINAD PKEIFFTSGA
TESNNMAVKG AAEFYEGSGK KHMITTQTEH KCVLASCRRL EVDKGWSVTY LPVDKYGLVN
LQELEDAIRD DTALVSVMHI NNEIGTMQPV EEIGKICEKR KVLFHTDAAQ SVGKVPVDVK
KMNAALLSIS AHKMYGPKGV GALYVRRKPR VRLRAVIDGG GQERGFRSGT LATPTIVGFG
ASAEVCMQEM ENDQKHVEKL YARMHDAITD QLPQITLNGS PSQRYPGNVN LSFACVEGES
LLMSLAKTTA VSSGSACTSA SLEPSYVLRA IGVSEDLAHT SLRFGIGRFT TEAEVDSTVN
DVVREVRRLR DMSPLWELEL EALKTGGQRT RECPLFLSDL LEKVSDLVPR WLTFARGVVD
SEDLPLNVGR EILQKSRTLK IIRKRVVRKV LDTIDDLREK EPTKFETFWT SYGKYFKDLD
YKDELKRFVR FWSSKSGDNQ TSLDEYISRM KEGQDKIYFV TGEGRRAAEI APAMEKMREK
DYEVLYMVDP LDEICSQSIV DYDGKKLVDI NKAGLDLDKS EDEKKDMEDK VKEYEDLATW
LKKQLGERVQ KVQVSDRLVE SMATLVQGEW GMSPMMQRYM KSQTTSSASD SAFAIGSRNQ
AILEINPQHN VIKALKNAME TQPEAAETED MVMMVYETAA LIGGYTIEDP GDFAKRVTRL
MEMQASEGTP GSVDAEVLA
//
