ID A0A0V1BWH3_TRISP Unreviewed; 2816 AA.
AC A0A0V1BWH3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Large ribosomal subunit protein uL11 {ECO:0000256|ARBA:ARBA00035203};
DE AltName: Full=60S ribosomal protein L12 {ECO:0000256|ARBA:ARBA00035320};
GN Name=XRN1 {ECO:0000313|EMBL:KRY41249.1};
GN ORFNames=T01_10661 {ECO:0000313|EMBL:KRY41249.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY41249.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY41249.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY41249.1};
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 -!- FUNCTION: Binds directly to 26S ribosomal RNA.
CC {ECO:0000256|ARBA:ARBA00002805}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000256|ARBA:ARBA00010537, ECO:0000256|RuleBase:RU003978}.
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:KRY41249.1}.
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DR EMBL; JYDH01000009; KRY41249.1; -; Genomic_DNA.
DR Proteomes; UP000054776; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd18673; PIN_XRN1-2-like; 1.
DR CDD; cd00349; Ribosomal_L11; 1.
DR CDD; cd08048; TAF11; 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; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 1.10.10.250; Ribosomal protein L11, C-terminal domain; 1.
DR Gene3D; 3.30.1550.10; Ribosomal protein L11/L12, N-terminal domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR000911; Ribosomal_uL11.
DR InterPro; IPR020783; Ribosomal_uL11_C.
DR InterPro; IPR036769; Ribosomal_uL11_C_sf.
DR InterPro; IPR020785; Ribosomal_uL11_CS.
DR InterPro; IPR020784; Ribosomal_uL11_N.
DR InterPro; IPR036796; Ribosomal_uL11_N_sf.
DR InterPro; IPR041385; SH3_12.
DR InterPro; IPR006809; TAFII28_dom.
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; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR Pfam; PF18129; SH3_12; 1.
DR Pfam; PF04719; TAFII28; 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; SM00649; RL11; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF54747; Ribosomal L11/L12e N-terminal domain; 1.
DR SUPFAM; SSF46906; Ribosomal protein L11, C-terminal domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU003978};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU003978};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT DOMAIN 2311..2370
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT REPEAT 2464..2505
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 2722..2754
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 258..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1806..1967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2162..2192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1730..1753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1754..1771
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1848..1864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1879..1904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1905..1924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1927..1941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1942..1967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2816 AA; 318435 MW; F602F5393428B8A8 CRC64;
MPPKFDPNEI KIVFLRCVGG EVGATTSLAP KVGPLGLSPK KIGDDIAKAT GDWKGLKITV
KLTIQNRQAK IEVVPSAASL IIRELKEPPR DRKKTKNSSI LSAFFYLVRH GGNLSLEQII
QIAKMMRPRS MAKKLEGTVK EILGTCQSVG CTVDGQHPHD IIDKIRAGER KEKGLYSFEF
LVFALLADFQ RQHLKNRQSW FGIGECRLSL WRNYFPTAMR ISISVVQRMD TTDAAAESSG
ISDFHQALLL ISNEPIVSSE SLEEQEEEET KDVGKTDEEE QLESEQYVGS TEETSKSESS
KVESESEQQT ATEVDVDRLK MQLLVSNFSK EQLSRYEMFR RSVFPKPFIR KIIQQTTGYA
ASANVVIAMA GIAKVFVGEL IEEALDVRDL WKDSKEPLKP RHIREAFRRL NAKGKVFPLS
PKKRNLTFEL LYVHAVLLFN SRRSQLFVVI RSIMGVPRFF RWLSERYPGL SQLVVESQIP
SYDNLYLDFN GIIHNCSHPN SPDATFRCTE VDIFTNIFSY IEGLFQLIKP RKVLFIAVDG
VAPRAKMNQQ RSRRFMSAKE AEDSRLKAIR NGEVIPDSDP FDSNCITPGT EFMERLHIHL
KYFINLKLSS DPLWQNVDVY YSGHDCPGEG EHKILAFIRF MRSQADYDSN TTHCIYGLDA
DLIFLGMAMH EPYFSILREE VVYDSRSKKS LRMVEDQKFY LLHLILLREY ICLEFEHLKQ
VKPDVYDEEK IIDDWIFMSF FIGNDFIPNV PMLITNENAL PNVWLAYQNA FPNMDGYLNN
GGHLNIPNLK IFFNELKKFE YKKYENHLKA CGWLESKRAQ RDARQQSRRK DLSATSTSLE
ITSFSSQSET ANGSSDSCVL QSLVVFSEKL PDTCSCALEN DDGTLFDDDD DDDEDSEDAV
DMRSETCDGL YEVSVLTEEE SDMSLHSLFR KFRASSALQN VIRNYVEALQ WILYYYFHGV
RSWKWFYGFH YAPFVSDLCD FNVGEITFEL GEPFLPFQQL LAVLPPSSRK LLPEPYQDLM
VNPDSPLSYA YPEDVERDMN GKKYEWECIL KLPFIDEEIL FDAVYPFNDA LKDDEKRRNR
FGKCYLYRYS GSHGERRTTT FRSSLPDIFP DIENCTCECT ELTIDHFELN ETLIKYGRLQ
RNEEVGSKQI CFPTFSFHDL KIKLNKAEVD SPLSLKVCSS FNMTFSDAAA LYLGKRILLS
WPYSIIGLCV KVSTLDSNCA ILGEDGNCNI TYVAHDGNAK IMWKRLANIC EEQYLDKFGI
KMKVKILLHY KLISGWKHVL NNNGNFELIP FWSDKEAETP VQLVLPKFVI DDKYFTERPI
EKFAPLASYA FSLHRKCYAA MCQILEYKTN MRLLVSLRRF PALRFNITLD MMEETLANWY
STRELIEMFQ LLPSTLGRLT GSLLIAKNKD LERKVNIGLN LKSNHKSAEK LGYAMRIDSR
RWIYSEDAVK LIEGYILEFP DIIDYLEMNN CDALRRMLVW LRNLPSASAT FVPFGTKFVN
SDDIKFIESE VEKLTDTYED GWNMDSNSLF FPLLCCGPIA ADPETDFQLF DRVINVRAGC
CVPYGMAGTV ISLPGGASHP KGNLEVLFDR PFVGGMSIRG SKPSAFRLPS YALINFTYSQ
RKKKQRCLAN KAKTDKPSEN ELFPTGGISF FRSTAHPAVR HLNKKPTTST NSSAFLNSKE
AHTLMHCGRG SYGVDVFNSR AGSTSFISPT HATEQIKQCL GLSQVEDTNC KQQDRPVASS
SSTASNHGNR IKKTVSQPHY RHQHWQRRHH QQHQQQQQDD DFSNSGLLID SSVLSSMLIE
GGKKTTTTAT KELHKSPVNL PTTHSAKETT IPTKSTPKPY YFRPTDEYAS LQWNSEPSAS
SSSQRHHRSS HRSNQPNRRK VRKVDEIAAV LKKLLEDPED TTSQRQPSKS DSPVGSTQLS
GAQQDRIPRD GDMERRQRRN SNQSPRSGGQ LERQQQQHQQ QQQHQTDIAV QLAQMGIQIC
QAEKQNEQNM NQCEILAECS DDESYSGAKV SDSRAWIPDQ ETAKELLEKI KQGGYGELPK
LESTLPSSTV NLPPNPPGRS NFLRTLIHVL RLAKFTFLSI IVFSVWIGFG QDQIIITVFP
GEVQQANLAV HYCIVYEQGV VSRGCCLSLD ASGDLDTCCC VESEESVCST VDLDPTRAVE
GTSAASEARA VPSAGPSTGH CPSSPPPVKR PRMQDHLQVD VSASTACSTT AGVIPSPSSC
HAASPNSASM TNTITCRLKK LVHACNGTSP QNRENRPAAW SSQHGLLKSA GHSRLPDADQ
ELVRIVAQYL RNMGFSETVK VLSLESGCSM ENPLATKLRE YVFRGHWNRA LRTLYDLKVF
IEKEEDFVEM QFMLLQQKFL SLVEKGRVLH ALKLLRDKMS ILKVDRAKLN ALSYFVMANS
ADVVKHPDYT GGSVSARENL MNELQNFLPT TLMLPPQRLQ SLIKQSLELQ RLRTDFPCQT
VQVLLDHCDE VWYCQFSHAG KLLATGSKEG VIYIWDVNLS SRSVTKKFTL DGHSFGAAYF
VFSPNDKYLA CVGPEDSPDL WIWDTETGIL RIKITHSPDD SISCVSWHPD GTKVVCGGTK
GQFYQCDLEG TVVDSWEGVR VRSIQYRKDG RTVLAADTHH RIRSYCFDDL TDKTVIKEDH
SLMHFSIDKS EHFALCSVAN QGVHLWDLES GSLVRRYRGV VQGYFNIFSC FGGVDEKYVA
SGSEVGKVYI WHRDEEAPVV VLSGHSSVVN AVSWNPAEPS LLASCSDDGS VRIWGPHECC
SNPESCSLCR VGIAEDDNEV LVGGEEMEKR SNLKFLSLGM NCHPGAAATA TITTTA
//
