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Database: UniProt
Entry: A0A0V1D6S7_TRIBR
LinkDB: A0A0V1D6S7_TRIBR
Original site: A0A0V1D6S7_TRIBR 
ID   A0A0V1D6S7_TRIBR        Unreviewed;      2728 AA.
AC   A0A0V1D6S7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRY57064.1};
GN   Name=PCLO {ECO:0000313|EMBL:KRY57064.1};
GN   ORFNames=T03_3711 {ECO:0000313|EMBL:KRY57064.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY57064.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY57064.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY57064.1};
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:KRY57064.1}.
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DR   EMBL; JYDI01000035; KRY57064.1; -; Genomic_DNA.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IEA:InterPro.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
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; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR039032; Rim-like.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12157:SF21; RAB3 INTERACTING MOLECULE, ISOFORM F; 1.
DR   PANTHER; PTHR12157; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN; 1.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT   DOMAIN          2340..2429
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          2518..2644
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          152..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1070..1091
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1142..1163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1357..1378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1390..1413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2250..2274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1708..1735
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        152..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..202
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1142..1162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2728 AA;  301330 MW;  C1DE4FFC79CD5FD7 CRC64;
     MKCGDSKHFR MFVCVLVRRL RAEVPGIRTG AVNKDAAHWL VRIDRFTNVY RLLEWEFDWL
     PPFPPAGSVE AAVIERFILP RMFGKVFGGI THAVSHTASQ LRTQVLAPQF NATVDPLAGL
     SEVERAHILA VQRRAADEDF KLSQQPMVLP RSTASTVDAT ASLPPPSLAP STLPSRPSSA
     SSTETEGADD TSDDDDDDSG PIPDLDQIGL SEVTPADMRL DGLAEIGQER LLTSQESIEE
     QPTIVVHSPS TNSNGAVDES DANELEREEE EDERQQQHAE EDSLDELEHY SSPESDTQDV
     VEPVVQIPGD QENLQLAATG AGDESPSSSG DEWNCEYAGE SFTAPIRKSI EIDEPTTTPQ
     SNERPIYQTE PAASSPPPAA DTTASSLFNY DQTDPTEWTN VEPLLQTQEI ELSSNETDQS
     VMNKAPGVEM DEEASSQTFY GDESSNPFLD GASFADDQAI SELVPVEEPD EEVDEEKFNN
     DNEQQLVIDA SADEQLSAAL AEPIPSSDDD TFGVDEKIIS QAEKTFATVA DHADSFGISN
     IAAAASSVVI ERQTSRFLTE MTSRSVKQPF DMPAASQAKL QSANKIASAA LDGFGGKSLK
     NFGGLFSRPK VDFSSFATSV KKSTEAALKK ATDSVASSFS SSSVVSMSQD SFNSNNQTCT
     VPPKSPSSSA INADNASVNS NKSSDQWSAL EVDKADNNNN NNSSAVMKST AAAVVGKKGI
     QPSPVVSNTF RVSCNSDSTE DTGYSSRCSP EDEFYRVGSD GAQFLITYDS SRKLGVDTVK
     APLSPRRRIN PFIEDGIFSQ RLITSVIVEQ ADDQLTKSFH VSGQKRQLDI VEKVEPGEQE
     KFHLIAEQSF WSSEPLQSQQ LFGEIDGPQE ISQAGKDSTP KIEEVETLPL PDESTPLKYP
     PQQSIANSGA DEIAKLFAVE DSAPDSSACT QMYDSSEVSS EQFDEDAQKR ITEIESEFLL
     QNNQSADSAE DWQMCPLCQM AEVHVRPDGV SINGQPCGNC GLTVCSKCGH VVEQNGYGYV
     AYAIQILPKL MVAGIVMVMP DRDAYAFCVY WFRTKSQAIS EDDNSKLTFE KSQEVDSDIS
     DQASDSSDSY PDVVIEVPSS PVKQLDFDQE FSTSNSKQCY KVFRDIEKHF MNNFDQCDDT
     KHEGKVDHHD QQTGHSDKGN FETDPFKTVP ISVGQSPTFE KLTEQASPSD AQLSIGEEIF
     GKIVPPEQSC PSTNSNNAQE DSIDYAQAMR YYNTQPFYIH RPGPVYTILE DDEEVMELNQ
     DGKNKTAYMA AISASRPSTL SSSSSKSQLT SFSSPLANSY VGLDRPAQQM QTSSNASTEQ
     LTSTVSSDVL VQHFFATSTT STTTTSITAS KSHALQSNST FTPKPVRIAP PPPPPSQYSI
     SRDAKIEKSI HQETSNKPTG GRRHSADVPL STDVNDSVVS GSLNGTAFKP VHSSSSTWTI
     LAGQKKSDTP SSSTVAVSFA LPVVRTIDMD ASDPSSCLPL YSAASTLCTT ATTAPATTPI
     TTNEADDDEA VVECSGTGPF VSRLKRSPAM LLNCIKNETD LRAGSLQTAL QSTPTSALTA
     CSSTSYPSSR LIDSAIPTPT KVVSSTSCGD TLQSGKTFLN ERLFFAQASP GEMGRRKLPN
     IPKIASNRHQ QDVDEQLCNI SWSAGPVCSS TTTVNGSGIT GITGGSSYNN VISMPSSWKN
     IGQTLRPQHS TPLATNCRRL LPPTLARVLL KQELREALTK RLDKLEAAEI EANQREFVVG
     RYMATGVYPQ SAGVDSAPSV VRCGLSPEMV RGCVVHFDRS RYLSSIRQRE SSKAEFSNSY
     GQSSRYGSYG GEEQWNSSRL VRKKESFVKK DDSVVLLFVK FCGSSSVQTK RNDFTVQTSD
     VLERYKDAST QTVQQSSETT NSGNFVRFKP KDDLLLSKHK NVGVSTSEGP TCRTISTSTD
     EIDEDRLMAR RRSEGNKKWR NLNSKSFTYF SADDDFASRE SRRSKIRREI ARRREKFSSY
     EDLFNLPPHR ADSTYRYMDD GMELNNYLTP SLYSSSRFSG HYGSLPRIDR LYDYSPMSRN
     ALYDDEPSSF SASYPLRPYQ KYDRLYRSDT APFVDGQDSA FHRGNYGTLT WRDQKPWFID
     GQRSLSSSLP YLNNLYESLD SQPECSFRGY SRGRRFGEAG TEQVNTPRSS SMLSHYANYL
     HNDFLRRSSA LDDGYGNLCE DRSTAKCMPY ADSSTEFNCR PSSVMEPIAS RLPYDKYDEP
     LNDCLSLHRC RTDAPMETYP STRDYCSMTA QQPTFNSRRR RSRRQQDQEP LYSGVKSAQY
     DADLKTQSYN PYLIDSSLQN ASVENHHRQR ASSQILLEEG KSTFRQASSP SSANIKRLLL
     VRDVRDRSGH GIGMRVIGGK ILPGSDGELV AYVAAVYKGG LVDLMEEVKE GDQILEWNGI
     KLTGKTYEEV QSIIDNTEGE FEIVLRSDAN LNQVYRLEEG PSSSLDKGYE SDCYLSNLAH
     PRLAKLALQR KTGLDQTNDR HCQGLDFGKA SPCFSTTPRS RSPFTANQQQ NSLLAQDLAN
     EGLLKLRVCF DHTSDTLFVT VLCAARLPNV DAKKRRPPNP FVKIYILPER IVQNKRRTKF
     IARSNNPVWN QTVVYKDLNL EQALSKMLEF TVWSYDRFKQ NTFLGKVIIN LSAANRWKKH
     DYTVIPFEVC ISMVKMQLFI HLIAALLFLF ARGEDDAVVE PTFADLKNLI DLYAREMEAM
     NALGTSRRLK TIPLRDPRFI TRKLFKND
//
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