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Database: UniProt
Entry: I3M0B1_ICTTR
LinkDB: I3M0B1_ICTTR
Original site: I3M0B1_ICTTR 
ID   I3M0B1_ICTTR            Unreviewed;      1005 AA.
AC   I3M0B1;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=RNA binding motif protein 27 {ECO:0000313|Ensembl:ENSSTOP00000002129.3};
GN   Name=RBM27 {ECO:0000313|Ensembl:ENSSTOP00000002129.3};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000002129.3, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000002129.3}
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   EMBL; AGTP01032987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01032988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01032989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01032990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01032991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01032992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; I3M0B1; -.
DR   Ensembl; ENSSTOT00000002382.3; ENSSTOP00000002129.3; ENSSTOG00000002378.3.
DR   GeneTree; ENSGT00510000046929; -.
DR   HOGENOM; CLU_031853_0_0_1; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
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; -; 1.
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; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
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:UP000005215};
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          273..301
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          545..619
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   ZN_FING         273..301
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          79..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          959..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          757..831
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        88..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..181
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..360
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..381
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..750
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        971..997
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1005 AA;  112974 MW;  3355543DD39F71E2 CRC64;
     MLIEDVDALK SWLAKLLEPI CDADPSALAN YVVALVKKDK PEKELKAFCA DQLDVFLQKE
     TSGFVDKLFE SLYTKNYLPP LEPVKPEPKP LVQEKEEIKE EVFQEPAEEE RDGRKKKYPS
     PQKTRSESSE RRTREKKRED GKWRDYDRYY ERNELYREKY DWRRGRSKSR SKSRGLSRSR
     SRSRGRSKDR DPNRNVEHRE RSKFKSERND LESSYVPVSA PPPNSSEQYS SGAQSIPSTV
     TVIAPAHHSE NTTESWSNYY NNHSSSNSFG RNPPPKRRCR DYDERGFCVL GDLCQFDHGN
     DPLVVDEVAL PSMIPFPPPP PGLPPPPPPG MLMPPMPGPG PGPGPGPGPG PGPGPGPGHS
     MRLPVPQGHG QPPPSVVLPI PRPPISQSSL INSRDQPGTS AVPNLAPVGA RLPPPLPQNL
     LYTVSEHTYE PDGYNPEAPS ITSSGRSQYR QFFSRTQTQR PNLIGLTSGD MDANPRAANI
     VIQTEPPVPV SINSNITRVV LEPDSRKRAM SGLEGPLTKK PWLGKQGNNN QSKPGFLRKN
     QYTNTKLEVK KIPQELNNIT KLNEHFSKFG TIVNIQVAFK GDPEAALIQY LTNEEARKAI
     SSTEAVLNNR FIRVLWHREN NEQPALQSPT QLLLQQQQTL SHLSQQHHHL PQHLHPQQVL
     VPQSPPSSVH GGIQKMMGKP QTSGAYVLNK VPVKHRLGHA SGNQSDASHL LNQSGGAGED
     CQIFPSPSHP KTIYSSSNLK TPSKLCSGSK SHDVQEVLKK KQEAMKLQQD MRKKRQEMLE
     KQIECQKMLI SKLEKNKNMK PEERANIMKT LKELGEKISQ LKDELKTSSA VSTPSKVKTK
     TEAQKELLDT ELDLHKRLSS GEDTTELRKK LNQLQVEAAR LGILPVGRGK TMSSQSRGRG
     RGRGGRGRGS LNHMVVDHRP KALTVRGFIE EEKDELLQHF SAANQGSKFK DRRLQISWHK
     PKVPSISTET EEEEVKEEET ETSDLFLHDD DDEDEDEYES RSWRR
//
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