ID A0A2Y9PQU2_DELLE Unreviewed; 1059 AA.
AC A0A2Y9PQU2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=RNA-binding protein 27 isoform X1 {ECO:0000313|RefSeq:XP_022445722.1};
GN Name=RBM27 {ECO:0000313|RefSeq:XP_022445722.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022445722.1};
RN [1] {ECO:0000313|RefSeq:XP_022445722.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022445722.1};
RG RefSeq;
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_022445722.1; XM_022590014.2.
DR AlphaFoldDB; A0A2Y9PQU2; -.
DR STRING; 9749.A0A2Y9PQU2; -.
DR Ensembl; ENSDLET00000004669; ENSDLEP00000004167; ENSDLEG00000003245.
DR KEGG; dle:111183053; -.
DR InParanoid; A0A2Y9PQU2; -.
DR OrthoDB; 5406435at2759; -.
DR Proteomes; UP000248483; Unplaced.
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:UP000248483};
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 274..302
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 599..673
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 274..302
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 79..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 811..885
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 88..140
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..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1051
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1059 AA; 118573 MW; 51E4D4104BF70F66 CRC64;
MLIEDVDALK SWLAKLLEPI CDADPSALAN YVVALVKKDK PEKELKAFCA DQLDVFLQKE
TSGFVDKLFE SLYTKNYLPP LEPVKPEPKP PVQEKEEVKE EVFQEPAEEE RDGRKKKYPS
PQKTRSESSE RRTREKKRDD GKWRDYDRYY ERTEMYREKY DWRRGRSKSR SKSRGLSRSR
SRSRGRSKDR DPNRNVAEHR ERSKFKSERN DLESSYVSVS APPPNSSEQY SSGAQSIPST
VTVIAPAHHS ENTTESWSNY YNNHSSSNSF GRNPPPKRRC RDYDERGFCV LGDLCQFDHG
NDPLVVDEVA LPSMIPFPPP PPGLPPPPPP GMLMPPMPGP GPGPGPGPGP GPGPGPGHSM
RLPVPQGHGQ PPPSVVLPIP RPPITQSSLI NNRDQPGTSA VPNLAPVGAR LPPPLPQNLL
YTVSERQPMY SREHGAAASE RLQLGTPPPL LAARLVPPRN LMGSSIGYHT SVSSPTPLVP
DTYEPDGYNP EAPSITSSGR SQYRQFFSRT QTQRPNLIGL TSGDMDANPR AANIVIQTEP
PVPVSINSNI TRVVLEPDSR KRAMSGLEGP LAKKPWLGKQ GNNNQSKPGF LRKNQYTNTK
LEVKKIPQEL NNITKLNEHF SKFGTIVNIQ VAFKGDPEAA LIQYLTNEEA RKAISSTEAV
LNNRFIRVLW HRENNEQPAL QSPTQLLLQQ QQTLSHLSQQ HHHLPQHLHQ QQVLVAQSPP
STVHGGIQKM MNKPQTSGTY VLNKVPVKHR LGHASGNQSD AAHLLNQSGG AGDDCQIFST
PGHPKMIYSS SNLKTPSKLC SGSKSHDVQE VLKKKQEAMK LQQDMRKKRQ EMLEKQIECQ
KMLISKLEKN KNMKPEERAN IMKTLKELGE KISQLKDELK TSSAVSTPSK VKTKTEAQKE
LLDTELDLHK RLSSGEDTTE LRKKLSQLQV EAARLGILPV GRGKTMSSQG RGRGRGRGGR
GRGSLNHMVV DHRPKALTVG GFIEEEKDDL LQHFSPANQG SKFKDRRLQI SWHKAKVPSV
STETEEEEVK EEETETSDLF LHDDDDEDED EYESRSWRR
//
