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Database: UniProt
Entry: A0A1Q9C612_SYMMI
LinkDB: A0A1Q9C612_SYMMI
Original site: A0A1Q9C612_SYMMI 
ID   A0A1Q9C612_SYMMI        Unreviewed;      2994 AA.
AC   A0A1Q9C612;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   SubName: Full=Carnosine synthase 1 {ECO:0000313|EMBL:OLP78335.1};
GN   Name=CARNS1 {ECO:0000313|EMBL:OLP78335.1};
GN   ORFNames=AK812_SmicGene41502 {ECO:0000313|EMBL:OLP78335.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP78335.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLP78335.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP78335.1,
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:OLP78335.1}.
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DR   EMBL; LSRX01001625; OLP78335.1; -; Genomic_DNA.
DR   OrthoDB; 2149754at2759; -.
DR   Proteomes; UP000186817; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0047730; F:carnosine synthase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0035499; P:carnosine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.11980; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.10.10; DNA Methylphosphotriester Repair Domain; 1.
DR   InterPro; IPR035451; Ada-like_dom_sf.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR031046; CARNS1.
DR   PANTHER; PTHR48066; CARNOSINE SYNTHASE 1; 1.
DR   PANTHER; PTHR48066:SF1; CARNOSINE SYNTHASE 1; 1.
DR   Pfam; PF13535; ATP-grasp_4; 1.
DR   SUPFAM; SSF57884; Ada DNA repair protein, N-terminal domain (N-Ada 10); 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186817}.
FT   DOMAIN          2691..2895
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          1..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1092..1134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1319..1349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1438..1464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1897..1982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2024..2122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2409..2485
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..778
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..868
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        942..967
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        974..998
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1319..1344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1897..1911
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2060..2074
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2075..2105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2106..2121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2994 AA;  339846 MW;  C3F77F61895002ED CRC64;
     MENGPERDER MEEVPAPEAE RNSEEPTTGL VPSAGTLELQ QGGEAEAPTG RRHTEVLELP
     KVDRGSAPAT PAIRPGESST PATGTKSRAE RKQEKKTARK EEKRNKRAEK SARKAEKAEE
     EKPEGTSPKT PVRRKLDAAM ESAGSIESVL LLEREYKALQ RDPSHRPNFY FLIDRLISNL
     RHIPRTVSAG EEERIKLTKL REEEEEAEDA EAAKRAAARV EEADEGSASR KRKLEELEEK
     KRALEEENDR KRKELEEESR RLRAVEEAER RAREQRSRNP KVQVPVASEK EKGETWFERK
     ATELVENYIQ SYGPQQKKSK EAAAEYTTAC KNSEQAQEDF ISALRKTQEK AEVLQKCLGR
     ALEAAMAFGR EEERAQQYAQ AKDKCSRPEV PRVKARPQIP AGLQERIRKE RAQKEESSKP
     GKKEGSEVPT TTKPGPFWGV RARKQPAEEE PGKEWREKIS EDVWKVGRLL KEDEKYLECT
     YYPFSPEWQE KLREELLNLA HRGFAKKEDG ELYPTRRFGW QLQSTREFES INQSLERDYG
     VRLVWKSQEV KGKSKSVDDF HCYPIGRGKM EKVTKFGVQY TVLGTLPPNK SMCSICWSEG
     HWKSGCQLKD MVFELWEPAL AVLVPAERLR KYPCRNIVCE RYQHDKDNDF QYFYPAIAFA
     DYGAVSSQIS EINSKRYKDA KLRSPEEYPE IEPPEDEREE CPALSTEQAM EYAASKKAAK
     PSDPEQRMAS HSETLLDMQD QAKKRRAKLL EKESKQKAID VDDESTSKKE ESASKKARGK
     GQGSESGIWT KEPLPAGHWQ DRPRRESLPS ESQEAKDALR QKLEAHKKEQ LEKEQLEEQQ
     KKKLRETFET HFKKETSSKE EEPAARKGPG PDEAGSDPSS EESSESSNST DDPEGATCSE
     LYLYAKESES YAQYPMETKS ETEAMEAAGS PGSIGADMPP AKDGKESTKA KEKERKDLAK
     RLEPLVLCKQ AKDSGLAEVE EKAKEEEKDE EKEKERKVAK VRKVKVKAKA KAAKERKEKE
     SVWEEQHAVS AIKKDIGEMS APTDIQYETL KQKNMYQEFP EVFPLASEEE GEEGDDIPIL
     YTRMVRETEH KEEKKVEESL EDLEPITNPF YGKLPSPGFT DSEGEGEEVE DSGLCKGCGT
     RLELTCTRPP RSVSSQYPSM PELYPGEDRY LRLQRKLRSE GKPYDKQALE DSARREHEWI
     EFHLDLEREK KKESEADQVR MVRTDEFYDV AEWFVMDDTD GDDDWYVIGE TNTPDVVRAV
     QTEEAPVGRA AHLDKVPDEF TELLDSTPNG KWTIMDEPER GVPEELRTPV VPVKVAPGKE
     KVRVEAQPGE PTEQDHEKKN PEAGKDSVGV PYPIVQLDFM FLQGKQTERK TVEKVLKWVH
     SIGHLDEVGF VGDSEEAMDQ YEGLVPDGER QGKFKNLKQI RWNERTGEDI EYEDLVEEEM
     EDAPKNDQGE SPPEVSPEEL DSMDQEAAVE ELNRLSKIGV IEEFAESGAS GSEKRMDLRE
     VYDWRYRDGK WRRRCRIVAR EYRAGATSTA ETFSPTASNA AARLVLILHL LNPTWVILVL
     DIKDAYLQVP QQEEVLVTIS DWMKKACNIG EGIVWRLKRC LPGENVRLKH VDVRLCQLQD
     WVRENTISIG TVKTVLNVAD LNTKKLTYAR RAFLMYFLSQ VEYSEGEEII HTGVDEYERY
     EQEKKLKEYV SSGQVKDLIR LIQVFSVIKP VTAAVWTNDE DLDSQYSGST DAMEEVKYSR
     SEVMMLMTLL VLVIPYIWMA VRKVYSEWTR ISMIGMVRIN SSSKNYIFHR TTCRYVQGKA
     RNGYFIHLEY DTTVAQGYRP CYVCFPEAKK AQKHDEDDEW ELTSESTDTT ENEGCGKKCT
     WCKVRKCTRK KPAHVYCSCT ECIQKYTEDL WRGQYDQVPE ASSSTQGPIG KKGSGTLEYM
     PPHVNKKGNR PAGQGSKGGR RGRAAMEPVA EEQNGPMLPE GFTQETPEVE EQPPTYEDSY
     DMIVDPGTPD STEERTMGPP DLCPQRPIYF AVQHKYLEVA SNRNKAATSK KRKGHEVIPD
     PPSFRNPKQA ACARTAKAAK TSHPEVEKTH FQRSGTHATR PWANSQQARH QRQGVQVAHQ
     EASQAKKGKN GTRHDWGPES KHAGSEQLLD CFGRAWNMNK VVVNFLNIGH YYGSKVMKLE
     QQMFQWEGVR RCVRYLKTEM NLQVTGVIPE NYRGMDNGRK QLPLPADIKN MCETVEETPR
     FGDQRNHRSA DDEMTIKCAY RRACRFLDND NYKEWVVQLQ DAKARTWLQK HKDMAHMRFY
     FDIGTGTFDI LGGNYPTTSL AQNDVVDKHD LCNMGRFMSC ISWQPQHFLN PPQGEIEDIC
     VRSKDPVAGW QLDAGALDFI ESEGGAFDGR SGIGFGEADF PLERGAAQAP PDRPDRSDRD
     LSRRFEKVLS ADREICQQID EEMAGLEQEL ARIEDATLKV EQQCMQDSKA KDYMVEEAQQ
     LEHKVAEAQR RLVELRDDGR ALNLESLSLR KDRNHLVEEL GFLQRSLDDE MHTLQSLQQM
     NASFQAFHAD MEANTELLLH QRKELIGQVS KERELSRHDA RQNNELRNLL ERRRHAERCL
     NGHIEDDEMQ CGGSGSLTGT RANEDAQLVL VKRGGSGSLT GTRANEDAQL VLVKRGCGQF
     LRISSPSFAE ISAREEQQAH SLLLQLPDAV VLASEIIHEL WMGQAVLDVL SQFLEPGGFA
     IILNAASYHR FGAEEFQLLA KEQNVPDKTS TLRGGFSSKR FQVSSEAVGD VDTEDDGQQG
     AAVGASAVIG ARFVLESYLD GEEVDVDVVM SDGEWQYAAV SDNGPTLEPY FNETWAVSPS
     LLPREKQLAL RELAVSSVKA LGFQDGIFHV ELKYTSQHGA QLIEVNARMG GGPVYSTNLK
     TWGVDLVEET LFCAAGIPSR PVATRKPVEC IANADVNALR SGRLVDLSFM KPLLQREGVV
     SHNCHVREGE EVVGPQDGLP TWLVEVVVSR PTPREALDFL MKLEAEIQAL VKLA
//
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