ID A0A0V1NQA0_9BILA Unreviewed; 2374 AA.
AC A0A0V1NQA0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=5'-3' exoribonuclease 1 {ECO:0000313|EMBL:KRZ86152.1};
GN Name=rpl-12 {ECO:0000313|EMBL:KRZ86152.1};
GN ORFNames=T08_16010 {ECO:0000313|EMBL:KRZ86152.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ86152.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ86152.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ86152.1};
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:KRZ86152.1}.
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DR EMBL; JYDM01000125; KRZ86152.1; -; Genomic_DNA.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd18673; PIN_XRN1-2-like; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.25.40.1050; -; 1.
DR Gene3D; 2.170.260.40; -; 1.
DR Gene3D; 2.30.30.750; -; 1.
DR Gene3D; 3.40.50.12390; -; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR041385; SH3_12.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR040992; XRN1_D1.
DR InterPro; IPR047007; XRN1_D1_sf.
DR InterPro; IPR041106; XRN1_D2_D3.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR004859; Xrn1_N.
DR InterPro; IPR047008; XRN1_SH3_sf.
DR PANTHER; PTHR12341:SF41; 5'-3' EXORIBONUCLEASE 1; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR Pfam; PF18129; SH3_12; 1.
DR Pfam; PF00400; WD40; 3.
DR Pfam; PF18332; XRN1_D1; 1.
DR Pfam; PF18334; XRN1_D2_D3; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 4: Predicted;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT TRANSMEM 1593..1614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1621..1639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1848..1907
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT REPEAT 2029..2070
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 2287..2319
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1220..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1261
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2374 AA; 268727 MW; 1919385E022BA29D CRC64;
MGVPRFFRWL SERYPGLSQL VVESQIPSYD NLYLDFNGII HSCSHPNFPD PTFRCTEVDI
FTNIFSYIEG IFQLIKPRKL LFIAVDGVAP RAKMNQQRSR RFMSAKEAED SRLKAIRNGE
VIPDSDPFDS NCITPGTEFM ERLHIHLKYF INLKLSSDPL WQNVDVYYSG HDCPGEGEHK
ILAFIRFMRS QADYDSNTTH CIYGLDADLI FLGMAMHEPY FSILREEVVH YSRSKKGLRM
VEDQKFYLLH LILLREYICL EFEHLKQVKP DVYDEEKIID DWIFMSFFIG NDFIPNVPML
ITNENALPNV WLAYQNAFPN MDGYLNNGGH LNIPNLKIFF NELKKFEYQK YENHLKARGW
LESKRAQRDA QQQSRRKDFS ATSTSLEITS FSSQSETANG SSDSCVLQSV VVFSEKLPDT
CSCALENDDG SLFDDDDDDS EDAVDMRSET CDGLYGVSVL TEEESDMSLH SLFRKYRASS
ALQNVITNYV EALQWILYYY FHGVPSWKWF YGFHYAPFAS DLCDFNVEEI TFELGEPFLP
FQQMLAVLPP SSRKLLPEPY QDLMVNPDSP LSYAYPEDVE RDMNGKRYEW ECILKLPFID
EEILFVAVYP FNDALKDDEK RRNRFGKCYL YRYSGSHGER RTTTYRSSLP DIFPDIENCT
CECTELPIDH FELNETLIKY GRLQRNEEIK LNKAEVDGPL SLKVCSSFNM TFSDAAALYL
GKRILFSWPY SIIGLCVKVS TLDSNCAVLD EDGNCNITYV EHDGNAKIMW KRMAKICEEQ
YLDKFGIKMK VKILLHYKLI SGWKHVLNNN GNFELIPFWS DKEAETPVQL VLPEFVIDDK
YFTERPIEKF APFASYAFSL HRKCYGAMCQ ILEYGTNMRL SVSLRRFPAV RFNITLDMME
ETLANWYSTK ELIEMFQLLP STLGRLTGSL LIAKNKDLER KVNIGLNLKS NQKSAEKLGY
AMRIDGKRWI YSEDAVKLIE GYIQEFPDII AYLEMNNCDA LKYLIATDIW ENEDCRTHTK
MPLLCCGPIA ADPDTDFQLF DRVINVRAGC CVPYGMAGTV INLPGGASHP KGNLEVLFDR
PFVGGMSIRG SKPSAFRLPS YALVNFTYSQ RKKKQRCLAN KTKTGESSAN ELFPTGGISF
FRSTAHPAVR HLDKKPTTST NSSAFLNSKE AHTLMHCGRG SYGVDVFNSR AGSTSFISPT
HATEQIKQCL GLNQVEDTNC KQQDRPVASS SSTASNHGNR IKKTVSQPHY RHQHWQRHHH
QQRQQQQQQQ QQRDDDFSNS GLLIDSSVLS SMLMEGGKKS IAQTTTTTTT TTATKELHKS
PVNLPTTHSA KETTIPTKST PKPYYFRPTD RYASLQWNNE ASARSSSQRY HTSSHRNSQP
NRRKVRKVDE IAALLKRLLE GPEDTTSQRQ PSVGKSDSSV GSAQLSGAKQ DRIPRDGDME
RGRQQAASLH EHGDEFIYAL NQSPRSGGQL ERQQQQQQKQ PQHQTDIAVQ LAQMGIEICQ
AEKQNEQNVV VRSISEMNQC EILAECSDDE SYSGAKVSDS RAWIPDQETA KELLEKIKQG
GYGELPKLES TLPSSTVNLP PNPPGRSNFL RTLIHVCRLA KFTFLSIIVF SVWIGFGQDQ
IIITVVCIYT VFLTFSSLVK CNRRILLHYC IVYEQGVVSR GCCLSLDASG DLDTCCCVES
EESVCSTVDL DPTRAVEGTS AASEARAVPS AGPSTGHCPS SPPPVKRPRM QDHLQVDVSA
STACSTTAGV IPSPSSCHAA SPNSASMTNT ITCRLKKLVH ACNGTSPQNR ENRPAAWSSQ
HGLLKSAGHS RLPDADQELI RIVAQYLRNM GFSETVKVLS LESGCSMENP LATKLREYVF
RGHWNRALRT LYDLKVFIEK EEDFVEMQFM LLQQKFLSLV EKGRVLHALK LLRDKMSILK
VDRAKLNALS YFVMANSADV VKHPDYTGGS VSARENLMNE LQNFLPTTLM LPPQRLQALI
KQSLELQRLR CRFHNRRDTS PCLDISNNSL LSDHTCKKTD FPCQTVQVLL DHCDEVWYCQ
FSHAGKLLAT GSKEGVIYIW DVNLSSRSVT KKFTLDGHSF GAAYFVFSPN DKYLACVGPE
DSPDLWIWDT ETGILRIKIT HSPDDSISCV SWHPDGTKVV CGGTKGQFYQ CDLEGTVVDS
WEGVRVRSIQ YRKDGRTVLA ADTHHRIRSY CFDDLTDKTV IKEDHSLMHF SIDKSEHFAL
CSVANQGVHL WDLESGSLVR RYRGVVQGYF NIFSCFGGVD EKYVASGSEV GKVYIWHRDE
EAPVVVLSGH SSVVNAVSWN PAEPSLLASC SDDGSVRIWG PHECCSNPES CSLCRVGIAE
DDNEVLVGGE EMEKRSNLKF LSLGMAFQII FSIK
//