ID M7AXQ9_CHEMY Unreviewed; 890 AA.
AC M7AXQ9;
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=Heterogeneous nuclear ribonucleoprotein L {ECO:0000313|EMBL:EMP27835.1};
GN ORFNames=UY3_15082 {ECO:0000313|EMBL:EMP27835.1};
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:EMP27835.1, 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).
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
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DR EMBL; KB566783; EMP27835.1; -; Genomic_DNA.
DR AlphaFoldDB; M7AXQ9; -.
DR STRING; 8469.M7AXQ9; -.
DR eggNOG; KOG1681; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR CDD; cd06558; crotonase-like; 1.
DR CDD; cd12780; RRM1_hnRNPL; 1.
DR CDD; cd12699; RRM3_hnRNPL; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR045002; Ech1-like.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR InterPro; IPR006536; HnRNP-L/PTB.
DR InterPro; IPR034816; hnRNP-L_RRM3.
DR InterPro; IPR035005; hnRNPL_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR NCBIfam; TIGR01649; hnRNP-L_PTB; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43149:SF1; DELTA(3,5)-DELTA(2,4)-DIENOYL-COA ISOMERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43149; ENOYL-COA HYDRATASE; 1.
DR Pfam; PF00025; Arf; 1.
DR Pfam; PF00378; ECH_1; 1.
DR Pfam; PF13893; RRM_5; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 3.
DR PROSITE; PS51417; ARF; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
DR PROSITE; PS50102; RRM; 2.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Ribonucleoprotein {ECO:0000313|EMBL:EMP27835.1};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 174..248
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 420..489
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 321..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..416
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 99040 MW; 8259706DA2A9F780 CRC64;
MRILMLGLDA AGKTTILYKL KLGQSVTTIP TVGFNVETVT YKNVKFNVWD VGGQDKIRPL
WRHYYTGTQG LIFVVDCADR DRIDEGRQEL HRIINDREMR DAIILIFANK QDLPDAMKPH
EIQEKLGLTR IRDRNCPRIL DILVLLEPPG PTRTCVIPSI QENYDDPHKT PASPVVHIRG
LIDGVVEADL VEALQEFGPI SYVVVMPKKR QALVEFEDIL GACNAVNYAA DNQIYIAGHP
AFVNYSTSQK ISRPGDTDDS RGVNNVLLFT ILNPIYSITT SAQRAKASLN GADIYSGCCT
LKIEYAKPTR LNVFKNDQDT WDYTNPNLSG QGDPGGNPNK RQRQPPLLGD HPAEYGGPHG
GYHSHYHDEG YGPPPPHYEG RRMGPPVGGH RRGPSRYGPQ YGHPPPPPPP PEYGPHADSP
VLMVYGLDQS KMNCDRVFNV FCLYGNVEKV KFMKSKPGAA MVEMADGYAV DRAITHLNNN
FMFGQKLNVW WVSFQMLCGL DVCVSKQQAI MPGQSYGLED GSCSYKDFSG SRNNRFSTPE
QAAKNRIQHP SNVLHFFNAP LEVTEDNFYE ICDELGAKRP ASVKVFSGKK PSAQFQPLLS
FRAMSSTPEQ PHASHSYETL KVSRVREKVF HVELNRPDKR NAMNAVFWRE MVECFNKIAQ
DSDCHAVVVS GAGKLFTAGI DLMEMGSAFM MVEGDDTARK AWNMRKKIRE YQESFTVLER
CPKPVIAAVH GACIGGGVDL ISACDIRYCT QDAWFQVKEV DIGLAADVGT LQRLPKIIGN
QSLVNELAFT ARKMMAPEAE SSGLVSRVFQ DKQAMLEGAF ELAADIAGKS PVAVQGTKVN
LVYSRDHSVS EGLRYMATWN MSMLQTEDLV KSAQAALEKK STKDIVYSKM
//
