ID J3KHD3_COCIM Unreviewed; 786 AA.
AC J3KHD3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Carbon catabolite repression protein B {ECO:0000256|ARBA:ARBA00041962};
DE AltName: Full=Deubiquitinating enzyme creB {ECO:0000256|ARBA:ARBA00042958};
DE AltName: Full=Ubiquitin thioesterase creB {ECO:0000256|ARBA:ARBA00041772};
DE AltName: Full=Ubiquitin-hydrolyzing enzyme creB {ECO:0000256|ARBA:ARBA00041870};
DE AltName: Full=Ubiquitin-specific-processing protease creB {ECO:0000256|ARBA:ARBA00042086};
GN ORFNames=CIMG_00618 {ECO:0000313|EMBL:EAS35264.3};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS35264.3, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
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 -!- FUNCTION: Ubiquitin thioesterase component of the regulatory network
CC controlling carbon source utilization through ubiquitination and
CC deubiquitination involving creA, creB, creC, creD and acrB.
CC Deubiquitinates the creA catabolic repressor and the quinate permease
CC qutD. Also plays a role in response to carbon starvation and the
CC control of extracellular proteases activity.
CC {ECO:0000256|ARBA:ARBA00037075}.
CC -!- SUBUNIT: Interacts with creA, creC and qutD.
CC {ECO:0000256|ARBA:ARBA00038752}.
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DR EMBL; GG704911; EAS35264.3; -; Genomic_DNA.
DR RefSeq; XP_001246847.1; XM_001246846.2.
DR AlphaFoldDB; J3KHD3; -.
DR STRING; 246410.J3KHD3; -.
DR GeneID; 4565582; -.
DR KEGG; cim:CIMG_00618; -.
DR VEuPathDB; FungiDB:CIMG_00618; -.
DR InParanoid; J3KHD3; -.
DR OMA; CEKKSQR; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd02663; Peptidase_C19G; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006:SF944; RE52890P; 1.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EAS35264.3};
KW Reference proteome {ECO:0000313|Proteomes:UP000001261}.
FT DOMAIN 55..480
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..130
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 786 AA; 88302 MW; 0EC39B59BF3AB8FD CRC64;
MAILLGKFRG NSASGNGSQS SAPAKRDPVP PPLTPLQKML LDAGPVRDDG SDKFFGMENA
QFGNTCYCNS ILQCLYYSVP FRESVINYPR RSPPDVLQNA LRNNLRYPDP SVPLDELLKP
KPPPTTPGKP SNSPLQVQKP EDKNSAEYKK KVALHTLPLL ETTDNSASYG MKESLFTSLK
DLFEAVIASP ERVGVIRPYH FLEILRREHE MFRTTMHQDA HEFLNLLLNQ VVSNVEDDAV
LLSDADEQSD NSEETSEGTS EETATDGSVS TLPSNGVKSS RNTRWVHQLF EGTLTSETQC
LTCETVSQRD EVFLDLSVDL EEHSSVTACL RKFSEEEVLC ERNKFHCDNC GGLQEAERRM
KIKRLPKILA LHLKRFKYSE DLDRLQKLFH RVTYPYYLRL FNTTDDAEDP DRLYELYAVV
VHIGGGPYHG HYVAIIKTED RGWLLFDDEM VEPVDKSFVQ NFFGDRPTLT SAYILFYQET
TDEAMQQELA KENAASARDT PETKDGVAPL VKPNGHPVRP MKLDRSQTAT DAVPTLDSAH
LSPIKPTPTA PSQLPRSSEE PSSSPPSNGL SRPSLSSLIP KVDLHIKRQR TKNDKEQVKE
ERDRKAAEKE QAKLDKQKAK RQEFQRKQDE KREQAYIKAA MEESKITKAE EDRRNGVKGD
KESGFFGLNK IKLRNRSASQ SKLFLRAKEN DVPDLPPLPP PNSLPESATD VSSRVPPSNE
STDDDKADSA NATAVSLQEQ QPLASHVEAL PPIPTSDTPD SRETPQTPAT PKKTRFNIRK
RSFNVF
//
