ID A0A0J6YEM1_COCIT Unreviewed; 900 AA.
AC A0A0J6YEM1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CIRG_05170 {ECO:0000313|EMBL:KMP05489.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP05489.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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DR EMBL; DS028095; KMP05489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6YEM1; -.
DR STRING; 404692.A0A0J6YEM1; -.
DR Proteomes; UP000054565; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 15..66
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 834..895
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 88..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 900 AA; 101283 MW; 28973D7893F1A1B1 CRC64;
MANTGLVDLE KELTCSICTE LLYQPLTLLD CLHTFCGYCL KEWFSWQGSN PGDRRRYPQF
TCPSCRASVR DTRHDAKVTT LLDLFLRSHP EKEKPTEEKN QIAEKYKPGD GVLPVGVSSS
QPPSDGDDEE DRRLLEEVRE MSLRDSQGRG RHMETQIRVP PSLVQRGAVA ERTPEHQRIE
DARRRRRATR QMNATSRSRS PLDGSSQRAR QVEHQSSLRS LLSNPDFTET AIQEEILRQI
AEEGLLDGID LQSLDPDQEE ELTERIAEAF RRRQRRRVRS GGRSNEAHSI QASSGSRSHS
VSQPNTERSR QSEAVQEQYL SSSGHATASG HRRSASDRGI GRRRTSPVPT SSEERIYPAR
RSATDVSNPT RVRRESHSRI AVDDEANSRS TAADQTPSHT RQRPASSRSD RREILVRQRA
EPTSVAESPV STTHSQSSRI LDSRACQGHR HRSNSRSSTN NQSDRLAVPS SRPPPSRQAV
IARSVPSSFV EPSISCERCG KKNLEYELHK LCTRCNNGTY HLCLRCYRLD LGCLHWFGFG
DSAHSRFKKS QDSLPPEQRS EEAPHKFRSR RFLAPAKESV LPTTGEGGTQ ITNSDPSGRL
QDGLFCDMCQ FFSDDCYWNC GECNDGEWGF CNSWFSALLQ HPLPVPGSSI TVDTREYRIL
TFSTRCNICT YPIPPSVTRY HCPTCNDGDY DICRNCYVKL CAMGKISRDN GRNGWRRCLQ
NHRMVIVGFE DHENGQRRVI VSGLVGGYAM KDDLDPTTPN SLNRPDTGSP NSPLSRQDSD
PWEWPEGSNS NNPDAADLAK GTRRKLNRSR HHLSGSSGDS PKSPLAPRFP PSGGIGLRLV
AIWSYYPDPE ETDEIMFPRG AEITEAENIN DDWFWGCYAG QKGLFPGYYA NVVEAVDILN
//
