ID A0A1S3JF56_LINUN Unreviewed; 1025 AA.
AC A0A1S3JF56;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=RNA-binding protein 5 {ECO:0000313|RefSeq:XP_013408781.1};
GN Name=LOC106172558 {ECO:0000313|RefSeq:XP_013408781.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013408781.1};
RN [1] {ECO:0000313|RefSeq:XP_013408781.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26383154;
RA Luo Y.J., Takeuchi T., Koyanagi R., Yamada L., Kanda M., Khalturina M.,
RA Fujie M., Yamasaki S.I., Endo K., Satoh N.;
RT "The Lingula genome provides insights into brachiopod evolution and the
RT origin of phosphate biomineralization.";
RL Nat. Commun. 6:8301-8301(2015).
RN [2] {ECO:0000313|RefSeq:XP_013408781.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_013408781.1; XM_013553327.1.
DR AlphaFoldDB; A0A1S3JF56; -.
DR STRING; 7574.A0A1S3JF56; -.
DR EnsemblMetazoa; XM_013553327.1; XP_013408781.1; LOC106172558.
DR GeneID; 106172558; -.
DR KEGG; lak:106172558; -.
DR InParanoid; A0A1S3JF56; -.
DR OrthoDB; 298711at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd16167; OCRE_RBM10; 1.
DR CDD; cd12313; RRM1_RRM2_RBM5_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR041591; OCRE.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR035618; RBM10_OCRE.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR13948:SF3; FI21118P1; 1.
DR PANTHER; PTHR13948; RNA-BINDING PROTEIN; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF17780; OCRE; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 271..352
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 377..410
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 430..514
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 862..887
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 952..998
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT REGION 119..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1025 AA; 115450 MW; 0863AD84706D5B73 CRC64;
MDSQISQFLA QQKQQSLFPR PPLRGAGFVV ARPGQGGFIG VRQPGLMPIP IAGHFGQPEI
PGNFPQHDFQ RAFPPQHEIA ANFGGQREMP GNFGQPNIPA DMRQLERDMQ GKMGQREMLG
NIPHRDDFGQ GEMHHDSFDD RGFGNQVEED HDRHYQNRTR DRDRDRRRDR DRDRDRDRRR
NRDRDRDRNR DRSMERSRGG EGNFDNSYDY GNYEEYDDDG YNYDGGRQDV NNSMGRDRRE
GRGYDRGDHY GRDGRGHNRE GEKWLTDNPT NTIMLRGLPQ KIDEKDIRAE LMMFGVPIKE
VRLMKKKDTG ASRGFAFVEF QNTTDAQRWM EHNQGQLYML NQYAVSMHYS QPKTPGMGGG
SGRDGGPSGG GMGPMDRNGD HKTDWICSKC GVHNFKRRDY CFKCSISREE SEKSGKEGDG
FDQVGTNPCN TLIFRGLDAL TTEESIMAAL VKVTALTVKN CRVMRDSLTN TSQGYAFIEM
NLAAEASQLL ESLGRLNPPL EIDGKQVLMS YSKNTFTTVL ATLQQNSTYD YSQYYDSTYY
QGQEAQQTGY YDQNGQYYEY SQGQYVQAAA PPTQTDSTNA AAAVAQAAIQ QAQAVKHFQK
QQEQYQKQVI EQIQHQQKLA DMSPEQRLAH QAQQWSTTQT DGAEPAPQPG EPNASGEYTT
YPVPDVSTYT YDEASGYYYD PQTGLYYDAN SQYYYNASTA KFLYWDSERS TYLAAPTAEN
QGEQKDDKTK KEKDKKEKVK IAKKIAKDME KWAKTLNAQK DAMKDGFKKS MQSLGGGPER
ESASADAGFA VLEKGMGEKP VDQSLMPPPP LPGGGKQAPG QGQPSGALVA SYGGDSDEED
EDDTQQMSPG MVEEKMTDWT KMACLLCKRQ FPSKEALQRH QQLSDLHKQN LDKLKASQAA
QAGPSAGQYR DRAKERRQKY GSTDPPINKK KQQQLRQQAT AYEEPTKAGL GQDNIGNKLL
QKMGWSQGKG LGRTNQGIVD PIQAQRRTMT AGLGARGSSY DINPGDTYKD SVKKVMYARF
HEMGE
//
