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Database: UniProt
Entry: A1C5C9_ASPCL
LinkDB: A1C5C9_ASPCL
Original site: A1C5C9_ASPCL 
ID   A1C5C9_ASPCL            Unreviewed;       613 AA.
AC   A1C5C9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=RNA binding protein (Arp), putative {ECO:0000313|EMBL:EAW14897.1};
GN   ORFNames=ACLA_003080 {ECO:0000313|EMBL:EAW14897.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW14897.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW14897.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RRM TET family.
CC       {ECO:0000256|ARBA:ARBA00008448}.
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DR   EMBL; DS027004; EAW14897.1; -; Genomic_DNA.
DR   RefSeq; XP_001276323.1; XM_001276322.1.
DR   AlphaFoldDB; A1C5C9; -.
DR   STRING; 344612.A1C5C9; -.
DR   EnsemblFungi; EAW14897; EAW14897; ACLA_003080.
DR   GeneID; 4708466; -.
DR   KEGG; act:ACLA_003080; -.
DR   VEuPathDB; FungiDB:ACLA_003080; -.
DR   eggNOG; KOG4198; Eukaryota.
DR   HOGENOM; CLU_022834_2_0_1; -.
DR   OMA; NLDRYVV; -.
DR   OrthoDB; 228305at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140453; C:protein aggregate center; IEA:EnsemblFungi.
DR   GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071502; P:cellular response to temperature stimulus; IEA:EnsemblFungi.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0031445; P:regulation of heterochromatin formation; IEA:EnsemblFungi.
DR   CDD; cd06133; ERI-1_3'hExo_like; 1.
DR   CDD; cd12452; RRM_ARP_like; 1.
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; IPR047201; ERI-1_3'hExo-like.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR034351; Nrp1_RRM.
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; IPR034870; TET_fam.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR23238:SF31; GH13594P-RELATED; 1.
DR   PANTHER; PTHR23238; RNA BINDING PROTEIN; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00641; zf-RanBP; 2.
DR   SMART; SM00360; RRM; 1.
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   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00322}.
FT   DOMAIN          253..331
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          352..381
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          426..457
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   REGION          593..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  65715 MW;  696B23386740720D CRC64;
     MATVSAPTPK LDRYIVIHVA TTCDEHGVYV TKDSAEVIEL GWILLDTKTC EELHRESVLV
     KPVNTPITPL CTSLTTLTWE HVRSAGTFRD AINRFDAFAQ EHLISKNLEF AFVTLDSWDL
     RVQLPREARD KAVVLPPYLQ HSRTFDLRTE YQRWQTHHPE SLPFGPSSLS NICAALEVEP
     VQSSAPIKHN LPFHLQALAP ASPRRAMEEA ITLARVLRGL IRKSQPPHEH PEILTRPMDA
     RADVRAFLTE RSKVLHLSGL PHDTTQSELE SWFTQFGGRP IAFWTLRTPD QHKPTGTGFA
     VFSSHEEAAE SLCMNGRALN EKAIEVSPSS SRVLDRAAEI LTPFPPSKNR PRPGDWTCPS
     CGFSNFQRRT ACFRCSFPAM AAAPDPMGYG AYGYGPPSMM PPHMGHNHGM GHSRGLGGNG
     GVVPFRAGDW KCGSEGCGYH NFAKNINCLR CGAPRSGAAV VADSAFPSPM DPPAGFGMGP
     NSMTSTPAPA PFTSAAGGFG GFSQQFAAPP NNYALPSGLG SAPGAYPPMG QVNAGYGSTN
     ASHTASSFSN PATQAAFSGA DHASSTSASN GAFYGTDGSN DPFAFLSTGL GGLTVSDDSH
     SRRNGTGASK SPA
//
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