GenomeNet

Database: UniProt
Entry: G1NB28_MELGA
LinkDB: G1NB28_MELGA
Original site: G1NB28_MELGA 
ID   G1NB28_MELGA            Unreviewed;      1145 AA.
AC   G1NB28;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 3.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=RNA binding motif protein 27 {ECO:0008006|Google:ProtNLM};
GN   Name=RBM27 {ECO:0000313|Ensembl:ENSMGAP00000009786.3};
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000009786.3, ECO:0000313|Proteomes:UP000001645};
RN   [1] {ECO:0000313|Ensembl:ENSMGAP00000009786.3, ECO:0000313|Proteomes:UP000001645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA   Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA   Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA   Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA   Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA   Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA   Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA   Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA   Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA   Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA   Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA   Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA   Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA   Zhang Y., Reed K.M.;
RT   "Multi-platform next-generation sequencing of the domestic turkey
RT   (Meleagris gallopavo): genome assembly and analysis.";
RL   PLoS Biol. 8:E1000475-E1000475(2010).
RN   [2] {ECO:0000313|Ensembl:ENSMGAP00000009786.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May be involved in the turnover of nuclear polyadenylated
CC       (pA+) RNA. {ECO:0000256|ARBA:ARBA00043866}.
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DR   Ensembl; ENSMGAT00000010621.3; ENSMGAP00000009786.3; ENSMGAG00000009467.3.
DR   GeneTree; ENSGT00510000046929; -.
DR   HOGENOM; CLU_031853_0_0_1; -.
DR   InParanoid; G1NB28; -.
DR   Proteomes; UP000001645; Chromosome 15.
DR   Bgee; ENSMGAG00000009467; Expressed in bursa of Fabricius and 17 other cell types or tissues.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   CDD; cd12517; RRM_RBM27; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR002483; PWI_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR045137; RBM26/27.
DR   InterPro; IPR034451; RBM27_RRM.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR14398; RNA RECOGNITION RRM/RNP DOMAIN; 1.
DR   PANTHER; PTHR14398:SF1; RNA-BINDING PROTEIN 27; 1.
DR   Pfam; PF01480; PWI; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS50102; RRM; 2.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT   DOMAIN          417..445
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          670..744
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          1031..1100
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   ZN_FING         417..445
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          248..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          995..1019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1100..1145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..326
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..484
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..506
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..773
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1110..1138
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1145 AA;  127522 MW;  C3945D70C49F9FBE CRC64;
     MMAMNAKQPF PMHSALQEPK YSGLHAGAEA MRRVCLPAPQ LQGNIFGSFD ESLLARAEAL
     AAVDIVSHAK SHPFKPDATY HAMSGVPCGP AAXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXARGAS TACANCWGLT GPSHLSYCGA AAVSTKGRNV CDADPSALAN YVVALVKKDK
     PEKELKAFCA DQLDVFLQKE TSGFVDKLFE SLYTKSYLPS HEPTKVEVKP AGQEKEVIKE
     ELSVKQNFQE SVEEERDSRK KKHSSPQRSR ADSSEQRTRE KRRDDGKWRD YDRYYDRSDL
     YREKSSWRRG RSKSRSKSRG LSRSRSRSRG RSKDHDASRS VEHRERSKFK SERNDVEGTY
     NAVSASASNS TEQYSAAQSI PSAVTVIAPA HHLENTTESW SNYYNNHSNP SSFGRNPPPK
     RRCQDYDERG FCVLGDLCQF DHGNDPLVVD EVSLPSMIPF PPPPPGLPPP PGMLLPPMPG
     PARSLRIPVP QAHPQAPPPV VLPVPRPPLT QSSLINSREQ PGTSAVPSLA PVGARLPPPL
     PQNLLYTVSE HTYEPDGYNP EAPSITSAGR SQYRQFFTRA QTQRPNLIGL TSGEMDTNPR
     AANIIIQTEP PIPITNNSSN VTRVVLEPDS RKRSPSSLEC PPLKKPWLGK QANNNQNKPG
     FLKKNQYTNT KLEVRKIPPE LNNITQLNEH FSKFGTIVNI QVAFQNDPEA ALIQYLTNDE
     ARKAISSTEA VLNNRFIRVH WHREGEQQPP LLQQQQQQSP SQALHHQLHL QQQALTPAPA
     VTMHSNLSKA VNKPLASGAY VLNKVPVKRR LGAAGNQPDL SQTGAVVEDC QTFPTPTSHS
     KMVYSSSNLK AAMKPGAGSK PHDVQEALKK KQEAMKLQQD MRKKKQEMLE KQIECQKMLI
     SKLEKNKAMK PEERAEIMKT LKELAGKISQ LKDELKTSST TSTPSKLKSK TEAQKELLDA
     ELDFHKRLSS GEDTTELRKK LNQLQVEAAR LGILPAGRGK TVPAQGRGRG RGRGGRGRGV
     LNHMVVDHRP KALTVGGFIE EEKDELLQHF SKFGDIEDLQ EEDSPLSVVL TFKSRSEAEN
     AANQGSKFKD RRLQISWYKP KVPSVSTEVE EEESKEEETE TSDLFLHEDD DDEDEDEDES
     RSWRR
//
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