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Database: UniProt
Entry: A0A3Q0GZX3_ALLSI
LinkDB: A0A3Q0GZX3_ALLSI
Original site: A0A3Q0GZX3_ALLSI 
ID   A0A3Q0GZX3_ALLSI        Unreviewed;      1011 AA.
AC   A0A3Q0GZX3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=RNA-binding protein 27 isoform X2 {ECO:0000313|RefSeq:XP_025065306.1};
GN   Name=RBM27 {ECO:0000313|RefSeq:XP_025065306.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025065306.1};
RN   [1] {ECO:0000313|RefSeq:XP_025065306.1}
RP   IDENTIFICATION.
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_025065306.1; XM_025209521.1.
DR   AlphaFoldDB; A0A3Q0GZX3; -.
DR   Proteomes; UP000189705; 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   Gene3D; 3.30.70.330; -; 2.
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; 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   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705};
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          287..315
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          538..612
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          897..966
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   ZN_FING         287..315
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          95..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          798..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          945..1011
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..195
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..535
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        800..814
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..1004
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1011 AA;  114496 MW;  09C3AAB6A5DF03A9 CRC64;
     MVRNFPTVPK PGIAVNFTGW QNNIKRRKLY ASLICDADPS ALANYVVALV KKDKPEKELK
     AFCADQLDVF LQKETSGFVD KLFESLYTKS YLPSPEPAKV ELKPAGQEKE EIKEETFQES
     LEEERESKKK KHCSPQKNRS DSNEQRTREK KRDDGKWRDY DRYYDRNDLY RDKYDWRRGR
     SKSRSKSRGL SRSRSRSRGR SKDRDANRTI AEHRERSKFK SERNDVESSY NPVSLSPSNS
     TEQYSSAQSI PSAVTVIAPA HHLENTTESW SNYYNNHNAP NSFGRNPPPK RRCRDYDERG
     FCVLGDLCQF DHGNDPLVVD EVSLPSMIPF PPPPPGLPPP GMLMPPMPGP AHNMRMPVPQ
     AHPQPPPPVV LPVPRPPLTQ SSLINNRDQP GTSAVPNLAP VGARLPPPLP HNLLYTVSEH
     TYEPDGYNPE APSITGAGRS QYRQFFTRTQ TQRPNLIGLT SGEMDTNPRA ANIIIQTEPP
     IPMINNSNVT RVVLEPDSRK RPPSSMEGPS VKKPWIGKQT NNNQNKPGFL KKNQYTNTKL
     EVRKIPPELN NITRLNEHFS KFGTIVNIQV AFQNDPEAAL IQYLTNDEAR KAISSTEAVL
     NNRFIRVLWH RENEQQPSLQ QQQPPQSLHH QLHPHPQSLT AQPPAVTVHS NVSKVMTKPL
     AAGAYVLNKV SVKRRLGVVG GNQTDLNQSS SIAEDSQTFP TSTSHAKMIY SPSNLKTSMK
     PGTGSKSHDV QEALKKKQEA MKLQQDMRKK KQEMLEKQIE YQKMLISKLE KNKAMKPEER
     AEIMKTLNEL TEKISQLKDE LKTSSTASTP SKLKSKTEAQ KEILDAELDL HKRLSSGEDT
     TELRKKLNQL QVEAARLGIL PVGRGKVMSV QGRGRGRGRG GRGRGMLNHM VVDHRPKALT
     VGGFVEEEKD ELLQHFSKFG DIEDLQEEES PLSVVLTFKS RSEAENAANQ GSKFKDRKLQ
     ISWHKPKVPS VSTEIEEEES KEEETETSDL FLHEDDDDDD EDEDESRSWR R
//
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