ID A0A0B4HU57_METMF Unreviewed; 653 AA.
AC A0A0B4HU57;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Ribosomal protein L37ae {ECO:0000313|EMBL:KIE02941.1};
DE Flags: Fragment;
GN ORFNames=MAJ_01243 {ECO:0000313|EMBL:KIE02941.1};
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143 {ECO:0000313|EMBL:KIE02941.1, ECO:0000313|Proteomes:UP000031176};
RN [1] {ECO:0000313|EMBL:KIE02941.1, ECO:0000313|Proteomes:UP000031176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297 {ECO:0000313|EMBL:KIE02941.1,
RC ECO:0000313|Proteomes:UP000031176};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIE02941.1}.
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DR EMBL; AZNE01000003; KIE02941.1; -; Genomic_DNA.
DR RefSeq; XP_014581934.1; XM_014726448.1.
DR AlphaFoldDB; A0A0B4HU57; -.
DR HOGENOM; CLU_026721_0_0_1; -.
DR OrthoDB; 5490909at2759; -.
DR Proteomes; UP000031176; Unassembled WGS sequence.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR CDD; cd15545; PHD_BAZ2A_like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR047157; PHRF1-like.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR PANTHER; PTHR12618; PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR12618:SF20; PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF12678; zf-rbx1; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031176};
KW Ribonucleoprotein {ECO:0000313|EMBL:KIE02941.1};
KW Ribosomal protein {ECO:0000313|EMBL:KIE02941.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 7..90
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 139..187
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 12..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIE02941.1"
SQ SEQUENCE 653 AA; 73082 MW; 0E72B771AE4B92A8 CRC64;
MDEPEQCIIC LDPLPHPSSL SSPPSPSPSP SHLNGARIKP APETTTETDP LADESNHLNI
VAALDGCEHI IHDACIRSWA QKTNTCPICR TPFHCVRVYN GVDGTAISTY DVIDKKQVAE
FDVQAWLGEN IVDQEEEECN PCPICNSAER EDILLLCDSC DAAYHTHCIG LDHIPEGDWY
CMECAHLFQL TQDQPERTDA EPESPRPQLV QRPHPRDVRG YHVRTRQRLR RARRQARNAE
WQGAWGQFSG RFYEMSDLDL DNHDDEDEDL EQFRRFQQLD RRELDRWRQR MDIANRLGAR
ETFASNIPPQ ISERLQPPPP PVEETRDERR AWGAFDRARE AEVTTSGTRK RKSRSVTASP
AEPVQEPERK LKRPRTRRLP TQAEASASAP SPATSGPSSA RPTTTSTAAT TTGTSGINGT
NGINGTNGSS LRNGLTRMES ATPLVSSLLK ELEPNPLSED ETPVLTPNWR VPPEASSPAL
SPSPSNHSSP RALSLTPPPL PSLNGRPTSP TLSLSTHIEP RYPPANYSPT RSNSDHGDSD
SRSTKVDPRP LELRQPRPRR AHQVPQTEEG SPTRWTMTQE EKKSINDIVK SALRPHWRAQ
KLTTEQYATI NRDISRKLYD EVKGAASLNE ESRRTWEKRA TQEVAQAVAE LSA
//
