ID A5DT36_LODEL Unreviewed; 725 AA.
AC A5DT36;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Asparagine-rich protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LELG_00522 {ECO:0000313|EMBL:EDK42344.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK42344.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK42344.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CH981524; EDK42344.1; -; Genomic_DNA.
DR RefSeq; XP_001528002.1; XM_001527952.1.
DR AlphaFoldDB; A5DT36; -.
DR STRING; 379508.A5DT36; -.
DR GeneID; 5234684; -.
DR KEGG; lel:LELG_00522; -.
DR VEuPathDB; FungiDB:LELG_00522; -.
DR eggNOG; KOG4198; Eukaryota.
DR HOGENOM; CLU_022834_1_0_1; -.
DR InParanoid; A5DT36; -.
DR OMA; NLDRYVV; -.
DR OrthoDB; 228305at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
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 Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23111:SF40; RNA-BINDING PROTEIN INVOLVED IN HETEROCHROMATIN ASSEMBLY-RELATED; 1.
DR PANTHER; PTHR23111; ZINC FINGER PROTEIN; 1.
DR Pfam; PF00641; zf-RanBP; 2.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 2.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 2.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001996};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 297..380
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 401..430
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 536..565
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 234..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..271
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 81746 MW; 167D3476AAB592A9 CRC64;
MGDVYIVFDS ITTCDDTNTY ISKDSTELIY LAWSVIDVAS LEVLSFQSTF IKPLNTPITQ
FCTRKCNLTW EHVRNAGSFK DAIDTLDTYM KLEIIGENRE FTFIVLDDFK LKVQVSREAR
DKGVTLPQYL QFPRYFDLLK EYLKWQKHTG EYKLGDSSFS ANTNASINAG SNTSASASPL
LEEMKNALQI DDTSLNVRDE KLSSSTDNSH EELFESVKLI TKLAIELLKK VSKKEQEKEG
GKTREGEEEI EEEEEEEEEE EEEEEEEEEE SQLHDHPFTK PYDIAQDMKS FLEERSEVLY
LTSLPNGTTH LELEYWFTQY GGRPVAFWKL GYLENANTSG SINSNDGFAV FGSHEETMEA
LKMNGKVLND VAIEVQPSSS KILDAAGDLL VPFPSSKNRP RPGDWTCPSC GFSNFQRRTQ
CFRCSFPASS AVAIQESMHT KAVPVASGNQ SASIESRRDP NVGSYQGLRE LQSNMYTDQI
ETKLAESKSS SPERDPAHKS TNRNGSTPSI GVTSNNKSFS TNANTQKHYN NNVPFRAGDW
KCNLCQYHNF AKNMTCLKCG GATKPIVDYN NLQSTNSIHS VNSTAAAIAA ATASGQPLNL
NNNLIHLHQQ QHIHQNLRTR AFPHQQHQQH QQHQQHQQHQ QHQQFNHSCH YNNLNSQSSV
LPNNVPVGAP LLKNTIRHDS SYTNTPGASQ ADLSRILMHQ HLQKHNRENS PALNDYSRNA
DSLKN
//
