ID A0A0V0V523_9BILA Unreviewed; 1283 AA.
AC A0A0V0V523;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Extended synaptotagmin-2 {ECO:0000313|EMBL:KRX58571.1};
DE Flags: Fragment;
GN ORFNames=T09_4768 {ECO:0000313|EMBL:KRX58571.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX58571.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX58571.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX58571.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC {ECO:0000256|ARBA:ARBA00005290}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01026}.
CC -!- SIMILARITY: Belongs to the extended synaptotagmin family.
CC {ECO:0000256|ARBA:ARBA00005867}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01026}.
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:KRX58571.1}.
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DR EMBL; JYDN01000084; KRX58571.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd08391; C2A_C2C_Synaptotagmin_like; 1.
DR CDD; cd04050; C2B_Synaptotagmin-like; 1.
DR CDD; cd17870; GPN1; 1.
DR CDD; cd21670; SMP_ESyt; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037733; Ext_Synaptotagmin_C2A.
DR InterPro; IPR037749; Ext_Synaptotagmin_C2B.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030230; Gpn1/Npa3/XAB1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR039010; Synaptotagmin_SMP.
DR PANTHER; PTHR45761; EXTENDED SYNAPTOTAGMIN-LIKE PROTEIN 2, ISOFORM C; 1.
DR PANTHER; PTHR45761:SF1; EXTENDED SYNAPTOTAGMIN-LIKE PROTEIN 2, ISOFORM C; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00398; RrnaAD; 1.
DR Pfam; PF17047; SMP_LBD; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01026};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01026}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00023055}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1283
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006870568"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 510..688
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 688..804
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 832..949
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 384..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 983
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 1005
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 1031
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 1061
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX58571.1"
SQ SEQUENCE 1283 AA; 145309 MW; 45381B594D92BA11 CRC64;
LLLMLYLFIY LFLIILLLST MDTETAGETE STEKAANNEN TVAAPLPDHL KPTCMIVLGM
AGSGKSTLVQ RICAYLSATK TSLYPVNLDP AVHYVSYPTA VDIRESVNYK EIMQKYELGP
NGGIMTAMNI FATTFSKVSH LFLYSLNLTT VLIFTLFKVI DFLENSSINY KYAVFDTPGQ
IEVFTWSASG AIISQALASS FPTVIVYVMD VARSSSPITF TSNMLYACSI MYKTQLPMVV
AMNKTDIISA NFALDWINDF ECFLEALDSE TSFAGDLTRR LALGLEEFYK TLKCTGVSAI
SGEGMKRFFE LIDQARLEYE TDYKPELEQR KLQLDKKKIE KQAERLNRLK LDIASDPPQS
HIASLRENFF GDQFCFGGLH DDDSAEDEEY EKPSSSGVEP IPRPSAPDRA SSRWFPFVYG
DKTEMRGETS DDSYSSSVGS ALLVLVCWTI GRSDCSIFWM LALLGLVLLR NHLLRQRSRR
IRAHQVTALQ EKEVIVTQLK DLPTWVQFPD VERVEWINRV IAQTWPGIAN FAKDFLKENI
EPQIKDNLPS VFRSFCFESI DIGDIPVRVG GIKVYAENVG RDRIVMDMDV AYAGDCSLSV
RVGCFRAGVE QLQFQGKLRC ILRPLISKPP WFGGFVIFFL NEPAFEFDLT GAGELVEMPG
LMRAMRSVIS SQLANICVLP NEIVIPVVPE TKMCDLTMSE PQGVVRVGVI AATNLENKDS
FLKGKSDPYV RITVGGQIYQ TKTIENNLNP VWNEEFDAIV DHADGQYLGV ELYDEDPGSR
DEFLGNLDLD MDSVRNKGYI SDWYALNAVK HGNVNLSVHW MNLSSDASLL DDVQNLPHSV
PSSGPRNHAL LMIYVDCIKN LPSVRKSFEP SPFILLTFGN EQRKTSVKMK TNNPVYQQRF
VFLVKNVHHD ILKLEAKDKT SGRSLGEVAI PVRLLKEENN MELKQQTWHM ALGPHLSPIT
MTLKLRLVRT AGNLEGNYVC EVGPGPGGIT RAILEQNPKK LVVVEKDPRF LPTLELIAES
TGGIMDIRIG DVMKYEIETE FPADVKREWI EEPPPVHVIG NLPFNVSTYL IIKWLRAMSL
HEGPFAYGRT LLTLTFQKEV GERMLAPIFN RHRCRLSVMC QYLSDVKRKF TIPASWVFIE
GRACVPSPDV DVAVMQFRPK VTPVISHHFD LVEKFCRHVF HYRNKYCIRG IETLFPDFLK
KDFSHEILRF ARVSPKLAPP ALAIEEIRDM CKIYEEQCLR VPSLFYYDYR QRKDFEEVQR
NCPAEPPLLK HLSSNVETFS ERL
//
