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Database: UniProt
Entry: A0A3S1BT91_ELYCH
LinkDB: A0A3S1BT91_ELYCH
Original site: A0A3S1BT91_ELYCH 
ID   A0A3S1BT91_ELYCH        Unreviewed;      2071 AA.
AC   A0A3S1BT91;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
DE   Flags: Fragment;
GN   ORFNames=EGW08_001475 {ECO:0000313|EMBL:RUS90764.1};
OS   Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC   Plakobranchidae; Elysia.
OX   NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS90764.1, ECO:0000313|Proteomes:UP000271974};
RN   [1] {ECO:0000313|EMBL:RUS90764.1, ECO:0000313|Proteomes:UP000271974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC2010 {ECO:0000313|EMBL:RUS90764.1};
RC   TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS90764.1};
RA   Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA   Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA   Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT   "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL   Submitted (JAN-2019) 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:RUS90764.1}.
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DR   EMBL; RQTK01000025; RUS90764.1; -; Genomic_DNA.
DR   STRING; 188477.A0A3S1BT91; -.
DR   Proteomes; UP000271974; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019205; F:nucleobase-containing compound kinase activity; IEA:InterPro.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359:SF255; NUCLEOSIDE-DIPHOSPHATE KINASE; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF00406; ADK; 2.
DR   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271974};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          64..204
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          424..1029
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          1632..1767
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          193..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1053..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1197..1309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1385..1455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1462..1481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          492..534
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          783..835
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        223..250
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..575
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..599
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1053..1076
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1202..1224
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1283..1297
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1400..1436
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1437..1455
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         2071
FT                   /evidence="ECO:0000313|EMBL:RUS90764.1"
SQ   SEQUENCE   2071 AA;  237033 MW;  FD844CCFC9CCADB9 CRC64;
     MEEVADLRAP NDPLLEPINV ELTAVSVDED KCEASVQHVA DLAKHLDIDP YSEDETELRY
     LYSKPTCFLV LGKPGVGKTS LARRFAAEWK CELINSTDVI LQNMEMQTEA GLKCGEILSR
     GEAIPDEMVL KMMEEKVNSP EVAHHGYIMD DFPCLSEELM SIKDQLELIK NWKLAPDFVI
     NLRMPEKDIE RRRLGQKLDP ETGDVYTRDV YAPDKPVPPP SPEKEEEDEE EEEEAEEEEE
     TPEDEEPNIE LPLEVLGRLI KRPEDLPQQV EENLGKFKNN MLRILEDYMG DHSQQYLVEL
     DGNQTLLTLF KQLIQKLQTF VLRPAAVVTR LNDPEEEEMP EEMETEELLR ALGPKQMVAP
     RYRWRRSRWQ RLCPVALYEG NIVQGKPEFS VSFLDKMYCL SSAEALEKFV KNPRPYLLPA
     QPRPPCKISV LGAPFSGKTT LSNLLAYKYG GKVLDMETLM KGRIDEERKK NMEQVRKDTE
     EQSILKIKAR IKEKLEADAA AKEEAIQAAA ALKAQREQEE RERQEAMREA TLQAELKMKK
     DFEAMFGTGE GEDDVKEGEE TGDGEAVEGE GETDTVAEET TQKESKSKEA NENENTTKDA
     DAENTLGNDG EEAEVDQSDN KSRKSHHKTA SATTNVAHHV LSETGESTED LDIEVDENHP
     EVIRLVKAAV REAELAPIIL SPEVQVEVLE GAIRDWEKEM RNKKKDGPMN GCWILDNFPS
     TREQWNACVE KNLLPDDVIV LGTDGGADKV VDDSMVKLML ARYCLKHRDK IIEAMETRAQ
     EVLFREEQKR QEQERKAAID EEERIRQAEA EETKVQALLE QAAAIEALKQ QELEEKQASV
     RIMQILWDTL SGELQTSTQF HDLGIEQPRG PSFINDLALE YQDYADLHQA LKNLAHRRRL
     RDEGRPIPST EIWDGADDIS ADESPPAEMK ETIDEEMVEE EHIDGAIEEE REEREEEEEH
     EEIPEAPPKS ELEILMEQPE AQIFLDMMKD FDKEQANLLA TITGTSAIEP FILEIAGRSP
     EQILEDVIKH LERMFKYVSW EMGTVDIDEE EEDLEAEALE AEEEATEEEG GEEEQEEDPN
     RSIKRKFLGD SNYFDPVVLR ETGVLYPGNP EIAAVYREKV YYFSTNESRD KFLEEPPLFL
     NEDEPLQAPP IRLLILGARG AGKSLHGRHL AEKMGIFHIS FKERLQELII AKTKKKIGPE
     YEEEEETEEE EEEEEEDSEV EDGGDQATPE LPLGNGPSEN PIAGVASMVS AESTASNTNE
     GKEIKQEKSQ QLFTQSIDKG EPTIVEEEEE EPELTEEEEA IKANLESQDP LPTELLDSIL
     TSWWTKEPFK STGFVLEGFP RTSEEVRYLQ DAGLFPDAAI ILQASDEDVI GRLLPPKLDK
     WREKRDKRLA KKNRKKEKAQ KKREAAIAKR REELVKEREE RKQNRLAEKA AAGGEDSENE
     DDVEEEEEDD DEEDDIEAIL AEEFEEEEEE EEEEEELEED AVERMKNDFN EVYDDDTNRL
     SAVEEALEEA LIPRLDVTAG RKPHIVRYIL HKKLRPYVEF RHSIFERVYP LNERQARRML
     QVGYKHPSRF GRWDPVMIKD GDCIQPMSGP GYPSFPCFYR SHIYFLSSAQ NRQTFMQDPM
     TFLKQETPKP VVPLKICIIG PPKSGKTTLA KRFADDYGVV RLSIGEAMRQ VLTTQPKSEL
     ARQMNWHLFR GRVVPDDLQV QALETVLLDM RCQTRGYVLD AYPMTQSQIT LMKERSIIPV
     RVIELQLDSK AVMIRGARDR IAPTRTRPVH DSAQILAIKL SCYLKTAPEV RNYYNKEHQN
     HVTIKADQSK WWVWDSVHDV ATKSIKRIQD YLQRTGDAKA AGIADLCITP NEFTQRIGDF
     GQYCPVSLCD RGELVDCSIN NTLQYAAEFR GHYYKMAGQD ELEQFLKEPE KYVPPMAPRA
     LPQVELLPRR IFPVEVKGRK YENLGYCPVT YLDGKLRYEA LIPGNPDYIA EYKELLYIME
     SEEKLFKFMK LPEKYASLKL PHKLPPKPEE LPFANLPMLG FMEQTCAVAM VKALTAAGNV
     KPKYPFVSST RSALIYIAYH LKAYNPKSSP Y
//
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