ID W5MWN3_LEPOC Unreviewed; 970 AA.
AC W5MWN3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=RNA binding motif protein 27 {ECO:0000313|Ensembl:ENSLOCP00000012792.1};
GN Name=RBM27 {ECO:0000313|Ensembl:ENSLOCP00000012792.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012792.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000012792.1}
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 EMBL; AHAT01021397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MWN3; -.
DR Ensembl; ENSLOCT00000012817.1; ENSLOCP00000012792.1; ENSLOCG00000010426.1.
DR GeneTree; ENSGT00510000046929; -.
DR HOGENOM; CLU_006190_0_0_1; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000010426; Expressed in ovary and 13 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 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; 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 Pfam; PF00642; zf-CCCH; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
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 286..314
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 523..597
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 855..923
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 286..314
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 83..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 690..757
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 89..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..963
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 109343 MW; 4A72BE32F9F2FF62 CRC64;
HFMKMIIENV EALKSWLAKL LEPICDADPS ALANYVVALV KKDKPEKDLK ALCADQLDVF
LQKETTGFVD KLFECLTTKN YLGNQEPPAK EVSKEEAKPA AQKVEESKEE TGNGDEEREG
RRRRSPLRNR SDLNESRVRD DKRRDDRKRR DGDRHGKASD PYRERYDRRA GTNRARSFSR
SRSKSRSRSG SRGKMGDKDH SRGKDHRLKF EMERKEPEGY LPPSVPMCSS LLPLPPPPPQ
QYSSGGQAVP SSVTVVAPAH LPDSTTESWS NYYSNHTDSK PFNRSTALKR RCRDYDEKGF
CVRGDLCPFD HGNDPLIVDD VTLPAMIPFP PPPGMPPPRM GMPPMVEPPS NMRIPPMPPH
GQPTPPGMFP VPGPPLIPAS AVDAREHSGT SSVSALAPPG VGPPPALPPH PQYTLSEYNY
DPEAYNPEAP GITAPGRPQY RQFIPRIQTQ RPNLIGLTSS DMDTQNSRAM TNNNARYSND
QDNRKRSMAN TEGPQAKKPW MDKQNFNNQH KPAFQKKNHY ANTKLEVRKI PRDLNNITKL
NEHFSKFGTI VNIQVVFGGD PEAALIQYTT NEEARRAISS TEAVLNNRFI RVYWHRENNE
QQQQQQQHQA QTQTAPVALQ HTSVHKKMTP KHRLGNATGN KGDAPQPSTE VSPAMPASMS
LQKGAYSSAV MKMTSKPMVK ATKALEAHEA MKKKQEALKL QQDMRKKKQE MLEKQIECQK
VLINRLEKNK NMKPEDRSSI MKTLKDLTEK ISQLKDEMKP SCNTLAKSAQ LKTKIDAQKE
LLDAELDFHK KLSSGEDTTD LKKKLSQLQV EAARLGLIPA GRGKVTPVRG RGRGRGRTLR
GRGAGNHMVV DHRPRALAIL GVTKEEKDEL MPHFVKFGEI EELRDHDATS VVMTFKTRSE
AENAANQGAK FKGRTLQISW YKPKTPSVST EPEEEESKEE EEAECSLLHP EEEEEDDDEE
DEDESRSWRR
//
