ID A0A433SM31_ELYCH Unreviewed; 2041 AA.
AC A0A433SM31;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=FAT domain-containing protein {ECO:0000259|PROSITE:PS51189};
DE Flags: Fragment;
GN ORFNames=EGW08_022034 {ECO:0000313|EMBL:RUS70208.1};
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:RUS70208.1, ECO:0000313|Proteomes:UP000271974};
RN [1] {ECO:0000313|EMBL:RUS70208.1, ECO:0000313|Proteomes:UP000271974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC2010 {ECO:0000313|EMBL:RUS70208.1};
RC TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS70208.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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:RUS70208.1}.
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DR EMBL; RQTK01001465; RUS70208.1; -; Genomic_DNA.
DR STRING; 188477.A0A433SM31; -.
DR Proteomes; UP000271974; Unassembled WGS sequence.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR024585; mTOR_dom.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE/THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000271974}.
FT REPEAT 777..813
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT REPEAT 1070..1110
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1336..1904
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT NON_TER 2041
FT /evidence="ECO:0000313|EMBL:RUS70208.1"
SQ SEQUENCE 2041 AA; 232779 MW; E428C2529998AA49 CRC64;
MTSKAALQTF VTGLKQRQED VRFKTAVELH HFVVTELREM PQDEVATFMD EFNHHIFEMV
SSSDVNERKG GVLAIEEPPL HPNIGTRVTR FANYLMNLLP SNYYDLGVME MAAKAVGILA
FSSGTYASEY VEFEVRRALE WLVSDRNEGR RQAAVLVLKE LAMNTPTFFY QQVQQFFDAI
FFAVRDPKPS IREGAVAALR AALSVTSQRE TKASQRSVYK QCFEEALSPF DESMARDKKM
SRDDWMHGSL LTINELLRCS NNETEVSKGN QRCNISLHDY FVCTHQDVNN RARGMSSVSA
LQQIQQKSSP LYVFSPGAKD SQQKIPPFES KTCKDLMTGN FDKICNLMLA HRTSRSVHVQ
QTLLNSLPRL AAFNPPVFAR IYLQETINFL LSILKRERER SQAFLALGFL AIAVQGEILT
YMSRIMDIIR TSLPSRDGST KKNRNLVVDP SVFTCISMLA RAMGPQMTHD VKELLESMLA
TGLRNDLCHS RRTWMISGSD LSAMGHCKLN AFKLMNIYNV PQFLFPPQAP PINDPSDVTN
VTLALRTLGS FDFEGHSLTQ FVRHCAEHYL GSEHKEIRME SVITCARLLS PLLKLLLQQQ
GHVSMTAMTT VAEVLNKLLV VGITDSDADI RYCVLTSLDE RFDPHLAQAE NLSALFIALN
DEAFEIREQA ICMIGRLSSK NPAYVMPSLR KVLIQILTEL EHSGMGRNKE QAAKMLGHLI
SNTSRLIKPY MVPIMNALIP KLKEADQSPG VVISVLHAIG EQAQVSGAEI SKWMDQLLPI
ILDMLQDSSS LQKREVALWT LGQLVESTGS VVTPYSKYPN LLEVLLNFLK TEQSISIRRE
VIRVLGVLGA LDPHKHRVNL GLIKDSENGV SKSENKLGGQ DAANGEVNMS ELMSQCSTLE
EFYPAIAIHL LMKIIRDPSL SQHHNMVVQA ITIIFKSLNI KCVPYIQTVI PAYLTVFRTA
DPSFREFLFQ QLGVIIAIVK QHIKNYLEDI FYLIKHYWSP STSMQSAIII LIEQIVNALG
TEFRMYLPQI VPQILRVFMH DTSEDKIVTA KLLKALELFD GNLDDYLHLL LPPVVKLFDN
SENPIHIRRS ALETIDRLTD SLDLSDYASR IIHPLVRTMD STPALHITCM DTLCTLVIQL
SHKFTIFIPM VTKVMHRHGI RHQRFHMLMA RILKGTTIAE EEDDPILMKK ERMDQLKKKG
KDRQDYQPDT TGIKKLSVNF DTIKRALETG RRVSKEDWME WLRKLSIELL KESPSPALRS
CLVLAQTYTG LARDLFNSAF LACWTELTEL QQDEVIASLE KTLVSQEIPE IMQTLLNLAE
FMEHCDKGPL PLECHLLGER AMKCRAYAKA LHYKEDEFHK GPNTQILESL ISINNKLQQR
EAAKGVLTYA INHHQANLKV QESWFEKLHE WDKALAAYKR KQDQNKDDDS LTLARMRCLE
AMGDWHQLHQ IALERWPVVS DEIRTGMARM ASVAAWGLGQ WESVEQYTTF IPRTSHDAAF
FRAVFALHSD NFPLAQQCID KARDILDTEL TAMAGESYNR AYGAMVNVQM LSELEEVIQF
KLVPERREAI KLMWWNRLKG CQRVVEDWQR ILQVRSLVIS PEEDMDAWLK YASLCRKNDR
LALSHKTLVT LLGVDPARQP DHMVPTTHPK VTFAYFKHMW KDNHKEKAYN KLQHFVRQSL
PTKSLQIIGP YESAQRAKLN QLTARCYLRL GQWSEDLHGI SEDSIPQIIE FYNLAKEHDD
TWYKAWHALA LMNYEAVLFY KQKDQAAAAS NIATPEGGLE PVRVDISSSP RLESNSAEIQ
KYCVPAVHGF FKSIALSSLN SLQDTLRLLT LWFDYGQWPG VNDIMSEGIK SIQIDNWLQV
IPQLIARIDT PRLLVQRLVH QLLVDIGKAH PQALIYPLTV ASKSNVALRQ AAANRILKTM
SERGQTLVDQ AMLVSEELIR VAILWHELWH EGLEEASRLY FSDRNVRGMF QTLEPLHAMI
ERGPQTLKET SFIQQAYGRD LMEAQEWCRK YQRSGVVKDL TQAWDLYYHV FRRISKQLPQ
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