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
//