ID A0A024UP00_9STRA Unreviewed; 566 AA.
AC A0A024UP00;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=RanBP2-type domain-containing protein {ECO:0000259|PROSITE:PS50199};
GN ORFNames=H310_02399 {ECO:0000313|EMBL:ETW08024.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW08024.1};
RN [1] {ECO:0000313|EMBL:ETW08024.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW08024.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the rad17/RAD24 family.
CC {ECO:0000256|ARBA:ARBA00006168}.
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DR EMBL; KI913954; ETW08024.1; -; Genomic_DNA.
DR RefSeq; XP_008864117.1; XM_008865895.1.
DR AlphaFoldDB; A0A024UP00; -.
DR EnsemblFungi; H310_02399-t26_2; H310_02399-t26_2-p1; H310_02399.
DR EnsemblProtists; ETW08024; ETW08024; H310_02399.
DR GeneID; 20079449; -.
DR VEuPathDB; FungiDB:H310_02399; -.
DR OrthoDB; 197226at2759; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd18140; HLD_clamp_RFC; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004582; Checkpoint_prot_Rad17_Rad24.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047854; RFC_lid.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR12172; CELL CYCLE CHECKPOINT PROTEIN RAD17; 1.
DR PANTHER; PTHR12172:SF0; CELL CYCLE CHECKPOINT PROTEIN RAD17; 1.
DR Pfam; PF03215; Rad17; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 2.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 7..37
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 62..94
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 99..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 63475 MW; 163D8B4DF405073A CRC64;
MVVVDTPLAI TWSCERCTYI NPAGNKACEL CSTSRFTLKG KTTAPPTPRH LRCKELTKSK
VKAEVSCPWT CQSCTFINDT PSLACSLCDT RRRMIATASN RKPRGQASLM ESIDSSSSDD
CNSIQTSAKS QLSQSFDRSN ASNTVDNALW NDKYQPNDTI EVVMHPKKAQ EVSDWLVHSS
THQRILFLCG PPGTGKSTLV RSLAAKLGMT VKEWHDTTGM VPGYSKLSAS AMDDFGSFLE
RSQRYPSLRF ANAKTNAAKH VILVEEWPSF HSDHRVELQR ILQRRLDVQG SHAFAAPIVI
VYSDVREGKV TANKLAKEFS PQVMQSPLVH IIHCNPIPPG MLKKYVMHVA RKERMALSTQ
DVTNIVESSR GDIRHAINTL QFQRTSTAHT KESGTRDLFL SDFHVIGKIL HQKDSSNDST
RLSHTSLDTS HALGMLHHNF VAFFTDVDDV ARALDYFSFT DVLLQSVYHD RSNSNYFQHT
HELAQTVLER TIHVTNNHAA TSAFRPLHRS QFAAASQRVR DDDPLKHDSS YHRDVRPYLQ
WLPHSSLGPT QAFLADDVDD DIVDSE
//
