ID A0A3P9CDL3_9CICH Unreviewed; 1706 AA.
AC A0A3P9CDL3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005020124.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005020124.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005020124.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR006743}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family.
CC {ECO:0000256|PIRNR:PIRNR006743}.
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DR RefSeq; XP_014266417.1; XM_014410931.1.
DR STRING; 106582.ENSMZEP00005020124; -.
DR Ensembl; ENSMZET00005020771.1; ENSMZEP00005020124.1; ENSMZEG00005015099.1.
DR GeneID; 101463778; -.
DR KEGG; mze:101463778; -.
DR CTD; 54464; -.
DR GeneTree; ENSGT00670000098080; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000265160; LG18.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:InterPro.
DR CDD; cd18673; PIN_XRN1-2-like; 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; -; 1.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR016494; 5_3_exoribonuclease_1.
DR InterPro; IPR041385; SH3_12.
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; PF18332; XRN1_D1; 1.
DR Pfam; PF18334; XRN1_D2_D3; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF006743; Exonuclease_Xnr1; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006743};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR006743};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006743};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR006743};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT DOMAIN 1..227
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 274..602
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 656..837
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 849..1074
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1102..1171
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 1199..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1624..1692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1706 AA; 191704 MW; E2E8704F15FDF952 CRC64;
MGVPKFYRWI SERYPCLSEV VKEHQIPEFD NFYLDMNGII HQCSHPNDED VHFRISEEKI
FADIFHYLEV LFRIIKPRKV FFMAVDGVAP RAKMNQQRGR RFRSAKEAEE KIKKALDKGE
VLPTEARFDS NCITPGTEFM VRLQEQLKYF VHNKLSNDKL WENVKVYLSG HETPGEGEHK
IMEFIRSENT KPNHDPNTRH CLYGLDADLI MLGLTSHEPN FALLREEVRF GGKKSQKRIT
APEETTFHLL HLSLMREYID YEFSELKNKM GSDYDLERVI DDWILMGFLV GNDFIPHLPN
LHINHDALPL LYKTYMSVLP SLGGYLNENG HLNLRNFEKY LEKLAEFDRE HFNEVFVDLK
WFESKVGNKY LNEAAGLAAE KEAASKDARK NEDSALCLAS RTTSEKVTGE EKAAAAADDE
EEEDDIFETE FRQYKRTYYM SKIGVDVVSD EFLANQAKCY VEGIQWILHY YYHGVQSWSW
YYPYHYAPYL SDIRNVSGLK LTFEHGQPFM PFQQLLAVLP AASMELLPEC YRHLMTSESS
AIIEYYPLDF KTDLNGKQQE WEAVVLIPFI DERCLLAAME ACNRKLTKEE KARNCHTECA
VYSYDKEMDF AYASPLPQLF PDIVHCHVRT AHIPMDAWQV SLDHVSKPVD RSALYFCGFP
TLQHIKHKFY KKKGGVVVFQ QSSRGENMLL DILPNQEGET TCDDVAAQVL GKSVFVNWPH
LEEARIIAVS DGETKFYLEE PPGVQRVYDR PSTPPPAKVT CLSDKEQKDW IKDVQGITEY
YLKRKGIVIN ETEVVLYGQL LTGRKYVPKA NGVVELEKQW AKQVLPFAYQ AVVKDIKAFC
SSLACFKSLD ELFPPTTTVF MVGNPYYGAM GEVQDSQDVI KDGRIRVVFS VPHEPQLEPL
IQNQHKYSVK YSPGYVLASR LGITGYLVSR FSGSIFIGRG SKKNPCGEQR ANVGLNLKFN
KKNEEVPGYT KRTEKEWLYS AAVEELLAEY LDRFSEVFNN VARNSHDDVF YEDDIWPGED
QNGAEKVAEI TSWLKSHPVS SISRASCDLQ VLDAAIVERI EEAVEKTKVK KSTKKVRVTV
KPHLLFRPLE QQQGVVPDPD AEYRLFDRVI NIRESFTVPL GLRGTIIGIK GAEREAEVLY
EVLFDEEFAG GLNIRCTSSR CYRLPPCALI NLSHGARVDH TGHKLTAIVK PQPATGGNFS
SYRQLAGLNH SPRSPFIPTQ HNNKHGVAKA ASQGNRSSPS KGPIQKHQVR NKEEYSNVWQ
SLQNTGPPNK PPAHWHNNEG HSQQGKNQPA SKSTPPAGIR LLKKNEDVSS FIPSHNIANK
AETQFEDLIA NLKISKGNQQ TPPPPAPPQG GDSQPDGPLS PQSFAMKGTL VLKEMLKIDS
TGTGSQSAQE TSNSTPPAGQ QQNRRRSSKK LAAKINVPHG DAPVLPSPAP AASANALLGS
KVSDLACICG ALGMAPPDFS FMRNRQGLVL CQVKLSNGLM VHGPQCQSEH DAKEKAAFFA
LQRLNSLGSG FPLPPPLYTG VGQIRPPHMG AVFNQQGGVL LPPQGYGPAP LWGMTVPPQH
HQNQPFYGPP GTFPGAARPQ PATTLPIGSH NQFIPLQVTK KRVSANKRNQ ETREFYSAAQ
TVAKNQAQKS QNQPTGQLQG QTEPQSVKIH QQAVNCDLSS GDSTTTALHT PPRQTMPATG
HTPSSASKRR QRKLAVNFEA AQVSES
//
