ID A0A084QT89_STAC4 Unreviewed; 397 AA.
AC A0A084QT89;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=WLM domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=S40285_05237 {ECO:0000313|EMBL:KFA67174.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA67174.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA67174.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA67174.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL660239; KFA67174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QT89; -.
DR STRING; 1283841.A0A084QT89; -.
DR HOGENOM; CLU_023057_1_1_1; -.
DR InParanoid; A0A084QT89; -.
DR OMA; GTLCEFY; -.
DR OrthoDB; 318145at2759; -.
DR Proteomes; UP000028524; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR013536; WLM_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR46622; DNA-DEPENDENT METALLOPROTEASE WSS1; 1.
DR PANTHER; PTHR46622:SF1; DNA-DEPENDENT METALLOPROTEASE WSS1; 1.
DR Pfam; PF08325; WLM; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR PROSITE; PS51397; WLM; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000028524};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 1..197
FT /note="WLM"
FT /evidence="ECO:0000259|PROSITE:PS51397"
FT DOMAIN 290..319
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 155..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 43536 MW; 9BAD2B0EC3B29ACA CRC64;
MGEHDPLVIS YVHLARFPRA DDALRMLKKV ASLVKPIMRA RGWKVGELAE FYPEQQNLLG
LNVNRGKKIC LRLRFPGDRT LFLPIEHIVD TMLHELSHIV HGPHDSKFHA LWDQLRDEHE
SLVRKGYTGE GFLSDGRRLG GPNMPPREVR RLTREAAEKR KAQPVGTAGG QRLGGAAPRP
GQDIRRVIAR AAEARNKTLK GCATDQLSDT QIHDIADTAT RNGFRTQAEE DKANEEAIAQ
AMWELVQEDE RAKYGKSYIP PSAQNPAGNG GGTVLAGGSS TAAEHAQGKS PKGWACEICT
FHNPPTYLCC GACGIEKTEH QPSRPQPSSS RPTRSAATSS STTIDLTGSP PKGKRPTGQP
KPTASAPQTW HCSFCGTEMA RQWWTCSTCG LMKNNSR
//