ID D4AT44_ARTBC Unreviewed; 668 AA.
AC D4AT44;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=RING finger protein, putative {ECO:0000313|EMBL:EFE33944.1};
GN ORFNames=ARB_07408 {ECO:0000313|EMBL:EFE33944.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE33944.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE33944.1}.
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DR EMBL; ABSU01000008; EFE33944.1; -; Genomic_DNA.
DR RefSeq; XP_003014847.1; XM_003014801.1.
DR AlphaFoldDB; D4AT44; -.
DR STRING; 663331.D4AT44; -.
DR GeneID; 9520384; -.
DR KEGG; abe:ARB_07408; -.
DR eggNOG; KOG1812; Eukaryota.
DR HOGENOM; CLU_009961_3_1_1; -.
DR OMA; HWGKEDN; -.
DR OrthoDB; 3354811at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd20339; BRcat_RBR_RNF216; 1.
DR CDD; cd16630; RING-HC_RBR_RNF216; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR InterPro; IPR047545; BRcat_RBR_RNF216.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047544; RING-HC_RBR_RNF216.
DR InterPro; IPR044066; TRIAD_supradom.
DR PANTHER; PTHR22770:SF47; E3 UBIQUITIN-PROTEIN LIGASE RNF216; 1.
DR PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51873; TRIAD; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008866};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 277..496
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
SQ SEQUENCE 668 AA; 76954 MW; 2A8401D07D54B55F CRC64;
MSRTILRPLQ RLTLSVLRRD QSSNGFTKDK AKLQDPYFID EYDLTSPGEN SVAEDGDDDG
MAFLESLLVL GEDDKRTSSQ GLTAAGLANI LTLFPDICPR YVTTLYQPML ARKPENFEGA
LIDAILKEAT YTTVSGSRQK REDMAKDVHW GKEDNLTRNS RKALLKLDFP LVPTDYIKEY
LEVTNDCLYN AYLRLYEVES TYETSDPKPY SRNTDVKREK LMASFRKVVA KYPNRDIDLE
IKDARAERKR RIVAQTLRKQ AFEDEKRNLA YYTSIGGIIE CHCCFSDTPL NRVVYCAAAA
AHPFCWECIK SNAKAQVGMM RHSIKCMDIN GCDAGFSRED LINSAGDSLM NKLFDLQQLE
EIQQADLTDL EECPFCEYKA IYPPVEENCE FRCLKPGCMR MSCRRCQRPS HIPITCAESR
REDSKNLRKH VEEAMSKAVI RICPNKKCKA PIIKEDGCNT LKCRKCSTVM CYVCKKNISR
AKDSHFDMVG SCPVEDDRYL LERHERERMT ARNEAVESLL KDKPELNEED LGVELIKRRT
VRDGLPIVYP EGTPDTSEMP LWVFGERVSG RPDRQLQRWP QLRVRFPPAN QDTQLPINYE
YQAIETIGVL PAPSQNPQDS HYQQTQWFSF YAYAPYPLPP DLPVVRYERE QNPHWFKGLR
RAQPSRTK
//
