GenomeNet

Database: UniProt
Entry: G3U002_LOXAF
LinkDB: G3U002_LOXAF
Original site: G3U002_LOXAF 
ID   G3U002_LOXAF            Unreviewed;      1065 AA.
AC   G3U002;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=RNA binding motif protein 27 {ECO:0000313|Ensembl:ENSLAFP00000021160.1};
GN   Name=RBM27 {ECO:0000313|Ensembl:ENSLAFP00000021160.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000021160.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000021160.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000021160.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000021160.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000021160.1};
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   RefSeq; XP_010589828.1; XM_010591526.1.
DR   AlphaFoldDB; G3U002; -.
DR   STRING; 9785.ENSLAFP00000021160; -.
DR   Ensembl; ENSLAFT00000023062.2; ENSLAFP00000021160.1; ENSLAFG00000022447.2.
DR   GeneID; 100660063; -.
DR   KEGG; lav:100660063; -.
DR   CTD; 54439; -.
DR   eggNOG; KOG2135; Eukaryota.
DR   GeneTree; ENSGT00510000046929; -.
DR   InParanoid; G3U002; -.
DR   OMA; CPMEHGL; -.
DR   OrthoDB; 5406435at2759; -.
DR   TreeFam; TF319253; -.
DR   Proteomes; UP000007646; 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:UP000007646};
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          606..680
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..144
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..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          947..974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1009..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          818..892
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        88..144
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..366
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..387
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1012..1030
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1057
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1065 AA;  119062 MW;  D5EA876D7FF72725 CRC64;
     MLIEDVDALK SWLAKLLEPI CDADPSALAN YVVALVKKDK PEKELKAFCA DQLDVFLQKE
     TSGFVDKLFE SLYTKNYLPP LEPVKPEPKP SVQEKEEIKE EVFQEPAEEE RDSRKKKYPS
     PQKTRSESSE RRTREKKRED GKWRDYDRYY ERNELYREKY DWRRGRSKSR SKSRGLSRSR
     SRSRGRSKDR DPNRNVEHRE RSKFKSERND LESSYVPVSA PPPNSSEQYS SGTQSIPSTV
     TVIAPAHHSE NTTESWSNYY NNHSSSNSFG RNPPPKRRCR DYDERGFCVL GDLCQFDHGN
     DPLVVDEVAL PSMIPFPPPP PGLPPPPPPG ILMPPMPGPG PGPGPGPGPG PGPGPGPGPG
     PGPGHSMRLP VPQGHGQPPP SVVLPIPRPP ITQSNLINNR DQPGTSAVPN LAPVGARLPP
     PLPQNLLYTV SERQPMYSRE HGAAASERLQ LGTPPPLLAA RLVPPRNLMG SSIGYHTSVS
     SPTPLVPDTY EPDGYNPEAP SITSSGRSQY RQFFSRTQTQ RPNLIGLTSG DMDANPRAAN
     IVIQTEPPVP VSINSNITRV VLEPDSRKRA MSGLEGPLTK KPWLGKQGNN NQSKPGFLRK
     NQYTNTKLEV KKIPQELNNI TKLNEHFSKF GTIVNIQVAF KGDPEAALIQ YLTNEEARKA
     ISSTEAVLNN RFIRVLWHRE NNEQPALQSP TQLLLQQQQT LSHLSQQHHH LPQHLHQQQV
     LATQSPPSAV HGGIQKMMNK PQTSGAYVLN KVPVKHRLGH ASGNQSDAAH LLNQSGGAGE
     DCQIFSAPGH PKMIYSSSNL KTPSKLCSGS KSHDVQEVLK KKQEAMKLQQ DMRKKRQEVL
     EKQIECQKML ISKLEKNKNM KPEERANIMK TLKELGEKIS QLKDELKTSS AVSTPSKVKT
     KTEAQKELLD TELDLHKRLS SGEDTTELRK KLSQLQVEAA RLGILPVGRG KTMSSQGRGR
     GRGRGGRGRG SLNHMVVDHR PKALTVGGFN EEEKDELLQH FSAANQGSKF KDRRLQVWHK
     PKVPSISTET EEEEVKEEET ETSDLFLHDD DDEDEDEYES RSWRR
//
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