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Database: UniProt
Entry: A0A0V1ADH4_9BILA
LinkDB: A0A0V1ADH4_9BILA
Original site: A0A0V1ADH4_9BILA 
ID   A0A0V1ADH4_9BILA        Unreviewed;       817 AA.
AC   A0A0V1ADH4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Double C2-like domain-containing protein beta {ECO:0000313|EMBL:KRY22848.1};
GN   Name=Doc2b {ECO:0000313|EMBL:KRY22848.1};
GN   ORFNames=T12_6599 {ECO:0000313|EMBL:KRY22848.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY22848.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY22848.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY22848.1};
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   -!- 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:KRY22848.1}.
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DR   EMBL; JYDQ01000006; KRY22848.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1ADH4; -.
DR   STRING; 990121.A0A0V1ADH4; -.
DR   Proteomes; UP000054783; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd04035; C2A_Rabphilin_Doc2; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR041282; FYVE_2.
DR   InterPro; IPR010911; Rab_BD.
DR   InterPro; IPR043566; Rabphilin/DOC2/Noc2.
DR   InterPro; IPR047022; Rabphilin_Doc2_C2A.
DR   InterPro; IPR001565; Synaptotagmin.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45729; RABPHILIN, ISOFORM A; 1.
DR   PANTHER; PTHR45729:SF6; RABPHILIN, ISOFORM A; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF02318; FYVE_2; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50916; RABBD; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          115..235
FT                   /note="RabBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50916"
FT   DOMAIN          163..223
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          540..662
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          678..811
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          275..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..346
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   817 AA;  92740 MW;  757371A8C9FF02B7 CRC64;
     MTSCLVFIIA YSYNQCLTSD QCTFCKHYLA FTISNQIQHQ QYCNVKTECF EVVLSVNNVI
     FSVQTIITMR KKDYHISEST KMPGKQSSWI CPSDRFLILR SQLSAGWSVW SDTQRADKST
     ISDNEMQQIK DVIARAEHIE ENEQRRIGKL VERLDRMKKM AAGNGINQCM LCGAKFGMIG
     TRSFASFCHD CNKYVCQKNC GLETLDSNGQ TIYLCKLCSE TREMWKKSGA WFYKGIPNFI
     KDTGLRSKSN DVSVSNSDDR SGFDTVSLTS MDSRCSKESL PSWSGKAKHA KRLLPTPPSE
     SHIRPSQPRW AIISQSIQSF DKCVDSSSEE EEEDSKDEQE TEEDIDQNNE NLNRSLFLDD
     SDTPYSRQSS CLSELDNSKP LSELESPELK RLSEEEKRTT DDVKGETEIY DSKSSISEVA
     VHSDSPVQSC TNSSSRYTME IAEDSDASIA LSTSVHDQAT SEVNKIADQL ADCSMNKPYA
     TTTLQHSDSA KSFDSSLYDS SPDNDIKRNM SLDKNALDKP VHEEYSTEQC SNGFSSPTAS
     FGSLEYSLLY DETEEMLVVT IFQASNLPAM DSNGFSDPYV KLHLLPLANK STKLRTSTKW
     KTLNPRWNER LIYYGMSKDD LRKKTLRLMV LDQDRIGSDF LGETRAPLKR LQSGKEKYFN
     VYLEKQMPVE KCDEFTEERG KILLALCYDL QNKLLAVEVV RCAELVGMDS TGYSDPYVKL
     TLKPGALKSY HVKTEVKKKT LNPEYNRVFQ FPVSYDELAK KSLDVEVWDK DVGKLDDFIG
     SVTLSANAKS DRLKHWIECI QNPNKRIKKW HKLTGKV
//
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