ID A0A0V1L9A7_9BILA Unreviewed; 637 AA.
AC A0A0V1L9A7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE SubName: Full=Synapse-associated protein of 47 kDa {ECO:0000313|EMBL:KRZ56083.1};
GN Name=Sap47 {ECO:0000313|EMBL:KRZ56083.1};
GN ORFNames=T02_6598 {ECO:0000313|EMBL:KRZ56083.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ56083.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ56083.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ56083.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) 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:KRZ56083.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDW01000101; KRZ56083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1L9A7; -.
DR STRING; 6335.A0A0V1L9A7; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd09339; LIM4_Paxillin_like; 1.
DR Gene3D; 1.10.3970.10; BSD domain; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR InterPro; IPR005607; BSD_dom.
DR InterPro; IPR035925; BSD_dom_sf.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR16019; SYNAPSE-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR16019:SF6; SYNAPSE-ASSOCIATED PROTEIN 1; 1.
DR Pfam; PF03909; BSD; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00751; BSD; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF140383; BSD domain-like; 1.
DR PROSITE; PS50858; BSD; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 4: Predicted;
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT TRANSMEM 305..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 167..219
FT /note="BSD"
FT /evidence="ECO:0000259|PROSITE:PS50858"
FT DOMAIN 562..628
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 231..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 71993 MW; B556C695F60AB1DD CRC64;
MDTGAIKNFC VIKYSTIRCT LPTRSVHHQF SKAEIGSSRS GGADISCLSM LNRWLSAKWN
KAEVSEASGI ESSEFVENET NSTKETKKFD VWNVLNEAKK FLVSSGSEVE NILKRKAESF
VMRSQENTNS VAVSFWDGLE NEFLVKKQIM SLSLDEEAFL RAPPIGTEFS FDFDSYVSQA
EAALKADPNL ENIRFRLVPR KIKEEDFWRN YFYRVHLVRS NAAAAAELAT PVEAAEDGKT
KEKKSDETED IEQELEDEDL SVDEKGRPVL DSCDFDLLGD SWEEEIQRIC QFSNMTMRLN
RFSHVVMKVV VVVVVVVVVV VVVVAVAVAV SNTNTGKVEQ PSSPSNKQAA VLLVVICDVF
TQLKSIRIVL TLAMTTVKTT NSYYYEETSQ SSPVRPPRRS KNVTHKQMNQ ILDEVKSEQE
KNVVIDTLAA LVTDVNATAQ VLRRSVSRTR LEEYDRETPL LDVSRSDSTF ERPPSTVWDR
RGPEVEYHLL IHSPAHMDYT DSRYSPAGSR KHAWDQDSQK SGAPFTSMES LSRARSETPS
RKIIVLENDE QYLREPVKSA SPVCAACKQP ISGPCITALA PNSTKAQKYH PSHFVCSYCM
KPLNLKGTYR EHERKPYCHE CFYRLYSGHI YETTSKI
//