ID I1CSN5_RHIO9 Unreviewed; 305 AA.
AC I1CSN5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=BAH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=RO3G_16176 {ECO:0000313|EMBL:EIE91465.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE91465.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE91465.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
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DR EMBL; CH476750; EIE91465.1; -; Genomic_DNA.
DR AlphaFoldDB; I1CSN5; -.
DR STRING; 246409.I1CSN5; -.
DR VEuPathDB; FungiDB:RO3G_16176; -.
DR eggNOG; KOG0955; Eukaryota.
DR InParanoid; I1CSN5; -.
DR OMA; CAYCTRQ; -.
DR OrthoDB; 1409291at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15497; PHD1_Snt2p_like; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR029617; Snt2.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47672; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR PANTHER; PTHR47672:SF1; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 19..137
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 174..226
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 231..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 305 AA; 34869 MW; 5635E7D13FF0F2EB CRC64;
MSDVKSAPHI ESTTLADGVT IRINDHVYIA PEHLGEPYYV GRIMEFCTSH KSKGLQVRLA
WFNRPKDVIN RNLADRCLLV ATMHSDINLV SSIRGKCVVT HKHYIPKDQL EDYRKKENHF
YYNQLYDRYI QRVYDVVPCE IVQNVPTDIL EALKERYQFI IVEQGKASDL TVARRICCIC
QEWCSSTASV KCAACHKSYH MACLKPPLAR KPPKGFAWQC ALCTRQEVLA SSPSDSDMSN
QNDTNKNTPK KRQIRTTRSQ LPKSQAQPQQ QIITSTSLTS TIKPKASHSK KMSSKLKNNI
FFFKA
//
