ID I3J5D1_ORENI Unreviewed; 997 AA.
AC I3J5D1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=RNA binding motif protein 26 {ECO:0000313|Ensembl:ENSONIP00000004071.2};
GN Name=RBM26 {ECO:0000313|Ensembl:ENSONIP00000004071.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000004071.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000004071.2}
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 AlphaFoldDB; I3J5D1; -.
DR Ensembl; ENSONIT00000004072.2; ENSONIP00000004071.2; ENSONIG00000003242.2.
DR GeneTree; ENSGT00510000046929; -.
DR Proteomes; UP000005207; Linkage group LG1.
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; cd12258; RRM2_RBM26_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 1.20.1390.10; PWI domain; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR039511; RBM26-like_RRM2.
DR InterPro; IPR045137; RBM26/27.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14398; RNA RECOGNITION RRM/RNP DOMAIN; 1.
DR PANTHER; PTHR14398:SF2; RNA-BINDING PROTEIN 26; 1.
DR Pfam; PF14605; Nup35_RRM_2; 1.
DR Pfam; PF01480; PWI; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
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 311..339
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 562..636
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 885..954
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 311..339
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 165..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 706..736
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 770..818
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 165..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..416
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..870
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..989
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 112774 MW; 1DACA9E755ADF6C4 CRC64;
MIIENLDALK TWLSETLEPI CDADPSALAK YVVALVKKDK SEKELKALCI DQLDVFLQKE
TQPFVDKLFE AVNNKSYLPQ LEQAPSVVKV EKEEQKKDEV IQEIFATRES QPPAIKFSLQ
QRQQVCAFAC SHLEKQNKNH FNMCFSFTHF CVFVKYIFRR GDDRKRDDRS RKRDYDRNLP
RRDSYRERYN RRRGRSRSYS RSRSRSRSWS KDRIRDRDRD RDRDRDRDRD HSGKLKYDHE
RGDRSESGDG YTPAVLVSTA TTSHFPVPTL SSTITVIAPT HHHSNNTTES WSDFHPEHPM
DRVPFNRGPP PQQRNRCRDY DEKGFCMQGD MCPFDHGSDP VVVEDVNLPS MLPFQPPPIP
GVEPPPPPGL PPPPPLMNPP PVNLRPPVPP PGALPPSLPP VAGPPPPLPP LQPAGMDGPP
NSITSSVPTI VTSGMRSSLP PPSGPLFNSG NVSNLLCNHY DTDVYNPEAP SITNTSRQIY
RHRVNAQRPN LIGLTMGEVD QPHRDKIPNN SMRIVMESDS RKRPAPSHDG GLPTKKPWFE
KLNFNKPNHQ GIHKRAQFPP NAKLLVRQIP PELNNISKLN EHFSKFGTIV NLQVAYQSDP
EGALIQFSSP DEAKRAMQST EAVLNNRFIR VHWFREDGND AQGQSQLQQQ SQPQVATVKV
ISTLCSEVFV CLLKYPTLAN VIVFSQFQVC STSMGLTKTV YNPAVLKTAQ RTSEEALKKK
QEALKLQQDV RKKKQEILEK HIETQKLLIS KLEKNKSMKA EDKGKIMETL DMLTKSITKL
QEEIKLISSN SNPLRIAKSK AQAQKELLDT ELDLYKKTQA GEDTALLKIK YTQLQIEAAK
RGLLSPGRGR GVHPRGRGAV RARGRGSRGR GRGVPLHAVV DHRPRALKIS GFNDTDRIDL
LPHFAQFGEI EDCQIDEGNL SAVITYKTRA EAEQAALHGV KFNNHTLRLA WHKPVTTLTT
ADADEAEPEE DESLSDDALL ADDDEEEDDN EPRPWRR
//
