ID A0A0B7NAG9_9FUNG Unreviewed; 831 AA.
AC A0A0B7NAG9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CEP12019.1};
GN Name=PARPA_05926.1 scaffold 20170 {ECO:0000313|EMBL:CEP12019.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP12019.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP12019.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP12019.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; LN727224; CEP12019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NAG9; -.
DR STRING; 35722.A0A0B7NAG9; -.
DR OrthoDB; 228305at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 CDD; cd06133; ERI-1_3'hExo_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; 5.
DR InterPro; IPR047201; ERI-1_3'hExo-like.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
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; PF00929; RNase_T; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 5.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00547; ZnF_RBZ; 5.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 5.
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; 5.
DR PROSITE; PS50199; ZF_RANBP2_2; 5.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107};
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 332..410
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 433..462
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 477..506
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 568..599
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 739..768
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 786..817
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..548
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 90786 MW; A9D9711875F8DEF5 CRC64;
MEVDRKRKAE GQDKLIEEET PSKRPLLDSD HKSTENDETV TAGTEQVVDL QNPEESYYDA
VAETKEEKSS QDIVNDNQQE CGVIKDENAV ENNTLVKVEA TPAAPLETLV PFDRLILVHL
EATCDENPTN PAAVQVTKEN SEIIELSFVV VDAFNMEVLH KQQIFVKPER TPLTAFCSEV
TGIKSSMLES AGSLSDAITT FDNYIQTEIE PKSFCFVTHG GWPLRIQLSR EARDKNITLP
SYLSFCRMFD LKQEIQRWQV HHPEVSLRST SLRDLCEIFD LTRVTDQTVG LNNALTTVAV
LRYLLGFRHT DVFIHPIDTN ADLKQFKKEE SQVIHLAGLP FEVTQGELEA WFSSNGLRPT
TMWMIQPPDN SKPSISGFVV FQQHDDAMRA LSLNGRCLGD RPIEVCPSSA RVIEAAGNML
VPFPLQAKSR QLRPGDWNCF NCSFHNFASR LYCFKCNAEN PNPGPQAGQG PPPQPFSHGD
WMCPSCNFHN YSSRMHCKKC TGPKPLKALK GNKKLVNGPQ MQQAPPSHPQ PYPNIHNGSV
PGGPPPPNAG YHGGYNSGGR PHHHISFRPG DWYCPNTVCG FQNFASRNTC FRCHTPNPNQ
QQQQQQQQQQ QQQPPLNQQH IQQQHTQYSP HQPSYGYSPE PTNNQPGYSN IGYAQGNGGV
NGGGGGGFGY GGQPNGGYGG QNSSGYAPPG GGYAGGGNGG GYSYGGGHPP SGGGYAYGGV
HQGGPPGGAS SGLHNTQFRA GDWICPSCSS HNFASRFQCL KCSTAKPYNP TGAPPAGYTP
SVPPMKPGDW MCRNENCSFH NFAKRTHCAK CGMANPNMQE GSGVGGGYGG N
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