ID M7ASV0_CHEMY Unreviewed; 890 AA.
AC M7ASV0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Polyadenylate-binding protein 4 {ECO:0000313|EMBL:EMP28441.1};
GN ORFNames=UY3_14472 {ECO:0000313|EMBL:EMP28441.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP28441.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB563787; EMP28441.1; -; Genomic_DNA.
DR AlphaFoldDB; M7ASV0; -.
DR STRING; 8469.M7ASV0; -.
DR eggNOG; KOG0123; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR CDD; cd12378; RRM1_I_PABPs; 1.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR CDD; cd12380; RRM3_I_PABPs; 1.
DR CDD; cd12381; RRM4_I_PABPs; 1.
DR CDD; cd12347; RRM_PPIE; 1.
DR Gene3D; 3.30.70.330; -; 5.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR034364; PABP_RRM1.
DR InterPro; IPR034168; PPIE_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR NCBIfam; TIGR01628; PABP-1234; 1.
DR PANTHER; PTHR24012; RNA BINDING PROTEIN; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00076; RRM_1; 5.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 5.
DR SMART; SM00361; RRM_1; 4.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF63570; PABC (PABP) domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 3.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 5.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}.
FT DOMAIN 11..89
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 99..175
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 191..268
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 294..370
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 553..631
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 732..888
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 434..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 98705 MW; 4457F36482BFEC8B CRC64;
MNTAASSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPVLSI RVCRDMITRR SLGYAYVNFQ
QPADAERALD TMNFDVIKGK PIRIMWSQRD PSLRKSGVGN VFIKNLDKSI DNKALYDTFS
AFGNILSCKV VCDENGSKGY AFVHFETQDA ADRAIEKMNG MLLNDRKVFV GRFKSRKERE
AELGAKAKEF TNVYIKNFGD DMDDERLKEL FSKYGKTLSV KVMTDPTGKS KGFGFVSFEK
HEDANKAVEE MNGKDINGKM VFVGRAQKKV ERQAELKRKF EQLKQERISR YQGVNLYIKN
LDDTIDDEKL RKEFSPFGSI TSAKVMLEDG RSKGFGFVCF SSPEEATKAV TEMNGRIVGS
KPLYVALAQR KEERKAHLTN QYMQRIAGMR ALPANTIINQ FQPAAGGYFM PAVPQAQSRP
TYYAPNQMTQ MRPNPRWQQG GRPQGFQGMP NAMRQSGPRP ALRHLAPTGN AQASRGLPAA
QRVGVATAAQ NLAPRPPVTA PAPRAVPPYK YASAVRSPHP AVQPLQAPQP AVHVQGQEPL
TASMLAAAPP QEQKQMLGGL AEEVDERVLH AAFIPFGDIT DIQIPLDYET EKHRGFAFIE
FELAEDAAAA IDNMNESELF GRTIRVNLAK PMRIKEGSSR PVWSDDDWLK KFSGKTLEEN
AEEEGAEPSK SETQELQKFL SDATDTENGE FKASSSHESR VRGHGLDSGA QPCPAPRGEP
PAKKSRANPQ VYMDIKIGNK PAGRIQILLR SDIVPMTAEN FRCLCTHEKN FGFKGSSFHR
IIPQFMCQAG DFTNHNGTGG KSIYGKKFDD ENFILKHTGP GLLSMANSGP NTNGSQFFIT
CDKTDWLDGK HVVFGEVTEG IEVVRQIEAQ GSKDGKPKEK VIISDCGEYV
//
