ID M2QLX5_CERS8 Unreviewed; 268 AA.
AC M2QLX5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=SWIM-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CERSUDRAFT_134570 {ECO:0000313|EMBL:EMD38028.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD38028.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD38028.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD38028.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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DR EMBL; KB445795; EMD38028.1; -; Genomic_DNA.
DR AlphaFoldDB; M2QLX5; -.
DR STRING; 914234.M2QLX5; -.
DR HOGENOM; CLU_037984_2_0_1; -.
DR OrthoDB; 140984at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR007527; Znf_SWIM.
DR InterPro; IPR039903; Zswim2.
DR PANTHER; PTHR21540:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZSWIM2; 1.
DR PANTHER; PTHR21540; RING FINGER AND SWIM DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF04434; SWIM; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 61..93
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 164..210
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 268 AA; 29842 MW; C79D4A5C881DB785 CRC64;
MDPDALAPEK RGAVFKKKCP KNILERLDRV ISQRFFLVDR RRDGHELREE FNVLGSTGNV
YTVVVDKKPS CNCPDALKGN HCKHILFIFL KVLQVTQESG YWYQKGLLTS ELDDIFARAP
PAPNSVANAR VREAYACATG RPSESTSAAD SGQKKRIPGS EDDCPVCYEN MHGAKENTLT
FCQACGNGLH KECFQQWARS ATKMTCVFCR AEWVMPTAAG NRSSGTVHSS EGYVNLAGVA
GLSPVRDTST YYHGPRRGER HYGYQDYC
//
