ID A0A0V0S809_9BILA Unreviewed; 1844 AA.
AC A0A0V0S809;
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:KRX22844.1};
GN Name=Clec16a {ECO:0000313|EMBL:KRX22844.1};
GN ORFNames=T07_12011 {ECO:0000313|EMBL:KRX22844.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX22844.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX22844.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX22844.1};
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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 -!- 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:KRX22844.1}.
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DR EMBL; JYDL01000028; KRX22844.1; -; Genomic_DNA.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0016020; C: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; 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; IPR045820; CLEC16A/TT9_C.
DR InterPro; IPR019155; CLEC16A/TT9_N.
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; PF19439; CLEC16A_C; 1.
DR Pfam; PF09758; FPL; 1.
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 Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; Transport {ECO:0000256|ARBA:ARBA00023055}.
FT DOMAIN 1078..1256
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 1256..1372
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1400..1517
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 503..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1551
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 1573
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 1599
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 1629
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 1844 AA; 208880 MW; D55ACC5139E0ED0A CRC64;
MPKGKLFSTG GLWKPKNQHS LEYLKYLCDL LTKNAIVTEQ NRALLVEALR LISEILIWGD
QNDSSVFDFF LEKNMLSFFL FIMRQKCGRF VCIQLLQTLN ILFENIRNET SLYYLLSNNH
VNSIITYRFD FSDEEILAYY ISFLKTLSFK LNVNTVHFFF NEICIRKYLH VCVLVNDPQV
IRFIRDNTAV PYFSNLVWFI RQRANEINGS GVDRMRDLIA DHQDHIHYLN DILCLDVEDL
NKVLIDQLMS KLFLPVYLNS IYAIPDINDE RPFSLLVTVF FLTQSGSCSV GNYATPILQL
ILRSHDEDCP VRIATLELCC TYIAQLFHSS KMHSRAFDTF IELFEDEATA FMLLRSWFIL
SKLLTNLRAE SLELEKTMQP VLSVKEGDCM NLGKFFFLLT RCYQTVICWL VQLYTTTIGN
AQLYFVEPDS SKVGWGVVRF VGQLQGCSQS RKYRLVTICD LLHVKVPEPA GPLPSRVFHN
LTTGKANQML PGFVVVHGSS GNPGNETVSP VAPGPSRPFS PKRRSRLAKF TGSKVELSPT
NSSNEEPKKQ DDIDGVVEEM RCIDLGQSPK PAKLLFSQKF NTTIANAAEV TDYCQEQPAS
SSSCTTARTM NTETAGETES TEKAANNENT VSAPLPDHLK PTCMIVLGMA GSGKSTLVQR
ICAYLSATKT SLYPVNLDPA VHYVSYPTAV DIRESVNYKE IMQKYELGPN GGIMTAMNIF
ATTFGKVIDF LENSSINYKY AVFDTPGQIE VFTWSASGAI ISQTLASSFP TVIVYVMDVA
RSSSPITFTS NMLYACSIMY KTQLPMVVAM NKTDIISANF ALDWINDFEC FLEALDSETS
FAGDLTRRLA LGLEEFYKTL KCTGVSAISG EGMKRFFELI DQARLEYETD YKPELEQRKL
QLDKKKIEKQ AERLNRLKLD IASDPPQSHI ASLRENFFGD QFCFGGLQDD DSAEDEENEK
PSSSGVEPIP RPSAPDRASS RWFPFVYGDK TEMRGETSDG SYSSSVGSAL LVLVCWTIGR
SDCSIFWILA LLGLVLLRNH LLRQRSRRIR AHQVTALQEK EVIVTQLKDL PTWVQFPDVE
RVEWINRVIA QTWPGIANFA KDFLKENIEP QIKDNLPSVF RSFCFESIDI GDIPVRVGGI
KVYAENVGRD RIVMDMDVAY AGDCSLSVRV GCFRAGVEQL QFQGKLRCIL RPLISKPPWF
GGFVIFFLNE PAFEFDLTGA GELVEMPGLM KAMRSVISSQ LANICVLPNE IVIPVVPETK
MCDLTMSEPQ GIVRVGVIAA TNLENKDSFL KGKSDPYVRI TVGGQIYQTK TIENNLNPVW
NEEFDAIVDH ADGQYLGVEL YDEDPGSRDE FLGNLDLDMD SVRSKGYVSD WYALNAVKHG
NVNLSVHWMN LSSDASLLDD VQNLPHSVPS SGPRNHALLM IYVDCIKNLP SVRKSFEPSP
FILLTFGNEQ RKTSVKMKTN NPVYQQRFVF LVKNVHHDIL KLEAKDKTSG RSLGEVAIPV
RLLKEENNME LKQQTWHLAL GPHLSPITMT LKLRLVRTAG HLEGNYVCEV GPGPGGITRA
ILEQDPKKLV VVEKDPRFLP TLELIAESTG GIMDIRIGDV LKYEIETEFP ADVKREWSED
PPPVHVIGNL PFNVSTYLII KWLRAMSLHE GPFAYGRTLL TLTFQKEVGE RMLAPIFNRH
RCRLSVMCQY LSDVKRKFTI PGRACVPSPD VDVAVMQFRP KVTPVISHHF DLVEKFCRHV
FHYRNKYCIR GIETLFPDFL KKDFSHEILR FARVSPKLTP PALAIEEIRD MCKIYEEQCL
RVPSLFYYDY RQRKDFEEVQ RNCPVEPPLL KHLSSNVETF SERL
//
