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Database: UniProt
Entry: A0A0V1PIZ8_9BILA
LinkDB: A0A0V1PIZ8_9BILA
Original site: A0A0V1PIZ8_9BILA 
ID   A0A0V1PIZ8_9BILA        Unreviewed;      2974 AA.
AC   A0A0V1PIZ8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Protein argonaute-2 {ECO:0000313|EMBL:KRZ95995.1};
GN   Name=ago2 {ECO:0000313|EMBL:KRZ95995.1};
GN   ORFNames=T08_2074 {ECO:0000313|EMBL:KRZ95995.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ95995.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ95995.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ95995.1};
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 organo anion transporter (TC 2.A.60) family.
CC       {ECO:0000256|ARBA:ARBA00009657}.
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:KRZ95995.1}.
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DR   EMBL; JYDM01000009; KRZ95995.1; -; Genomic_DNA.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd17404; MFS_SLCO5_OATP5; 1.
DR   CDD; cd02846; PAZ_argonaute_like; 1.
DR   CDD; cd04657; Piwi_ago-like; 1.
DR   Gene3D; 3.40.50.12610; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   Gene3D; 2.170.260.10; paz domain; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR014811; ArgoL1.
DR   InterPro; IPR032472; ArgoL2.
DR   InterPro; IPR032473; Argonaute_Mid_dom.
DR   InterPro; IPR032474; Argonaute_N.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004156; OATP.
DR   InterPro; IPR003100; PAZ_dom.
DR   InterPro; IPR036085; PAZ_dom_sf.
DR   InterPro; IPR003165; Piwi.
DR   InterPro; IPR045246; Piwi_ago-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR048999; STT3-PglB_core.
DR   InterPro; IPR048307; STT3_N.
DR   InterPro; IPR031420; UPF0669.
DR   NCBIfam; TIGR00805; oat; 1.
DR   PANTHER; PTHR22891:SF174; ARGONAUTE-1, ISOFORM A; 1.
DR   PANTHER; PTHR22891; EUKARYOTIC TRANSLATION INITIATION FACTOR 2C; 1.
DR   Pfam; PF08699; ArgoL1; 1.
DR   Pfam; PF16488; ArgoL2; 1.
DR   Pfam; PF16487; ArgoMid; 1.
DR   Pfam; PF16486; ArgoN; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF03137; OATP; 1.
DR   Pfam; PF02170; PAZ; 1.
DR   Pfam; PF02171; Piwi; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF02516; STT3; 1.
DR   Pfam; PF21436; STT3-PglB_core; 1.
DR   Pfam; PF17065; UPF0669; 1.
DR   SMART; SM01163; DUF1785; 1.
DR   SMART; SM00949; PAZ; 1.
DR   SMART; SM00950; Piwi; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   SUPFAM; SSF101690; PAZ domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS50821; PAZ; 1.
DR   PROSITE; PS50822; PIWI; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1017..1037
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1049..1068
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1074..1092
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1104..1137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1143..1163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1170..1192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1256..1280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1308..1329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2079..2100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2266..2287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2307..2328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2335..2357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2426..2451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2463..2484
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2504..2524
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2566..2588
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2603..2626
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2638..2658
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2784..2800
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2821..2845
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2876..2898
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          277..397
FT                   /note="PAZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50821"
FT   DOMAIN          566..881
FT                   /note="Piwi"
FT                   /evidence="ECO:0000259|PROSITE:PS50822"
FT   DOMAIN          1560..1841
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          2270..2902
FT                   /note="Major facilitator superfamily (MFS) profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50850"
FT   DOMAIN          2683..2732
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          889..911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2974 AA;  334706 MW;  3C95D38E8A57DED6 CRC64;
     MYHHTRQVKP GPSKSSAKPG PSKSSTKPST SRDYVNSNIS GTQNLQSQQQ SEVPSTSSAN
     ANDQNDNGDE QGEFTFVAPR RPSFGKLGDQ ICLRANHFQV RIPTGSLYHY ELVIEPERYH
     RDIIETMIQA YQKVFSNGRP VYDGKRSLFC KEMLPIGRDW VVQLDVTMPT EREDRRYQVG
     IKLNSQVSLS RLQEALDGQI RFLPQDTVDA LDVILRHLPS LKYTPVGRSF FSPPERFFHP
     LGGGREVWFG FHQSICPSQW KMMLNIDVSA TAFYKSMPVV DFLSEVLDAP HIPENRRPLS
     DAQRIKFTKE VKGLKVEITH CGQMRRRYRV CNVTRRPAQT QTFPLQIENG QTVECTVAKY
     FYDRYCIRLK YPQLPCLQVG LEQKHTYLPL EVCNLVPGQR CIKKLTDTQT SSMIKATARS
     APDREQEINE LVKRADFNND PFAREFGISI SPFMAEVYGR VLVPPKLLYG GRTRATAFPE
     KGVWDMRGKQ FHTAVDIRNW AIACFTPPHM CREDNLRTFI QQLQKISHDA GMSIVGQPCF
     CKYATGADQV EPMFRYLKSQ YPQLQLVIVV LPGKTPVYAE VKRVGDTLVG VASQCVQAKN
     VNKTSTQTLS NLCLKINVKL GGINNILLPS IRPKVFNEPV IFMGADITHP PAGDGGKPSI
     AAVVGSMDAH PSRYSASVRM QYPRRVPDER TGRMKDERLE RIEDLALMVK ELLIQFYQST
     RFKPTRIILY RDGISEGQFY QVLQHELGAM REACIMLERG YQPGITYVAV QKRHHTRLFC
     AERRDMQGKS GNIPAGTAVD SGITHPQEFD FYLCSHAGIQ GTSRPSYYHV LWDDNNFSAD
     EMQQLTYQLC HTYVRCTRSV SIPAPAYYAH LVAFRARYHL VDSDRDSAEG SVNSAATENG
     ENAEEETPSS SSSSLSRAVI IHPNTNRAIC KFAFLFNHAE GVFKACIAAS GDVAEDGGFG
     FGSPFSTRLF SVLRFESVIH EFDPYFNYRT TRYLTEEGFY KFHNWFDDQA WYPLGRIIGG
     TIYPGLMVTS TFIYRILHFF NITLHIREIC VFLAPLFSSF TTLITYLLTS EFKGDGAGLI
     AAGMIAIIPG YISRSVAGSY DNEGIAIFCM LLTYYFWIKA VKTGSIFWST LCALAYFYMV
     SSWGGYVFLI NLIPLHVLTL LCCSRFSHRI YIAYSVVYTL GTILSMQIPF VGFQPVSTSE
     HMAVGFAFEI APWTGRFYSL LDPSYAKNHI PIIASVSEHQ PTTWSSFYLD THISGVMVRL
     MLVLAPVMCV ISGIAASSIF ESFLRNFSHS ASTGLEKKSK KHENDYSWKN EVAATVVFIL
     TLFFINYTFH CTTITETAYS SPSIVLSARS GHGNAIIFDD FREAYYWLRM NTPPDSKIMS
     WWDYGYQITA MANRTVLVDN NTWNNTHISR VGQAMSSPED KAYEIMQELD VDYVLVIFGG
     LIGYASDDIN KFLWMIRIGG STEKGKHIKE EDYYSATGEY RVDKEGSKTM LNSMMYKFSY
     YRFGETNRLV TIAFEEVKLE TRKSNSNISK KRSQRNIGFM SKQGKEPSLV HVNEVIDSRY
     KVKKLLGKGG FGAVYQVLDQ TTNKMGAMKI EVSSQDFRSL KMEVSVLKEL VANESRNCCD
     LFSVGNKPNY SYIVMTLVGP SLHSLAQSIG SKRLSLRSAV HLGIRCLRAL EDLHFCGYIH
     RDVKPMNYAI GREPEYRRVF ILDFGMCRKY VRDDGSHKRP RSECGFRGTL WYASPMSLSG
     QEQSRRDDLW SWFFTIIELL TGTVPWQNVQ IKRNASFAEK KQAFMEKKME FVQSPGEALR
     GLPREFNNIV EYLSTLQYYE CPNYGYIYQL IMTTFRRHSY SLEQALDWEP TGQFHEETIM
     APDHNMLPGQ EENDPAEVNS FGSFCTNDLN LFAQRKARTS VLRHVQASLW KGFRNDVYME
     FVFVVIVILC YQHFRVIGES SSPVVQQVFS GELQAGKSAY FKLTKTGAIG ILLKSFSGDA
     DLYVSTVTSE PSFKIGENEF QSVTCGVDLV RVPEQTSRPL YVAVYAHPSH LVSQYALVIN
     VFEGNGSDQR MHRWVEQKSG SELTSLQEVE ALFNDERQYL ISSKLIYITE LISTLILLLV
     DASSAKQRSN SSVGVLGPAA STSTKDTLHL IEDETAAKPS VAVGILPSIH HHGTTSFTGS
     LRAKMNASSS FLPNYAKSAS QMLLNSDDTT VWGDVALEST NHASSAAVPC DHESTMIKRH
     FCDEPQQQQQ QQQHYRKYLS MSPTSAAYWS LESLRKKVRR FPWTNVKTFV GFICFLITVH
     GALSTGYTMS VITTIEKRFQ IPSTTSGLIV SSYEIGSLLS VVFVSYFGSN GHVPYWIGFG
     GLVLSLGSFL FSLPHFVATP YSYLENKSIE ALLLLSPNAA NNLGKDHSLF DQSASAPLCQ
     LSNQSSSSLY NTTCLSQETE SSNNHILVMM LAQILLGVGG SPLFTLGTTY IDNHVDKESS
     SIYLAFMYVM LAFGPVCGFL LGGLLLSEYV NPNSAPPDLT IQSIGWIGLW WGGFIICGFF
     YLLASLPFFC FPRRLTDDQD NSPRSDYGKD IRKIPVSIFR LITNKVYMVT SFNACLDLAI
     VSGFTVFLPK FLETQFLVSK SDASLFTGSV AVPGACIGTL FGGWVLKRLK MVMSHVANYV
     VLVNIAAVLL LSLLFFIGCE NFKIAGVSQT YPSSAIFDDR MFISAWDQCN VNCSCSLQGI
     QPICGIDGIT YLSPCFAGCK ASAITTGGKR PSIVGTVDRL YRTYSNCSCI LSNLNITVNV
     HNTSNAVASS IQAWYGLCPS NCRMLVPFLV LLFIVTLTAA NNQMPLVMIT LRAVSEEEKA
     FALGLQVVML RLLSYLPAPI VYGAIIDTAC RLMDDSCGTT GASCLFYDIE TFRFRFAFLC
     LMLKLFGLLV SVVMLFCIRR RYVPFSSPVT MSEIVHRLGD IENLHLQRCN AKGSLRHWVS
     DDSLYSRPRS PRHRKTLSSY WFHTCAYIHT YMYM
//
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