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Database: UniProt
Entry: Q5CY84_CRYPI
LinkDB: Q5CY84_CRYPI
Original site: Q5CY84_CRYPI 
ID   Q5CY84_CRYPI            Unreviewed;       873 AA.
AC   Q5CY84;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=E3 ubiquitin-protein ligase CHFR {ECO:0000256|ARBA:ARBA00017908};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=cgd7_3320 {ECO:0000313|EMBL:EAK90333.1};
OS   Cryptosporidium parvum (strain Iowa II).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK90333.1, ECO:0000313|Proteomes:UP000006726};
RN   [1] {ECO:0000313|EMBL:EAK90333.1, ECO:0000313|Proteomes:UP000006726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX   PubMed=15044751; DOI=10.1126/science.1094786;
RA   Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA   Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA   Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA   Anantharaman V., Aravind L., Kapur V.;
RT   "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL   Science 304:441-445(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- SIMILARITY: Belongs to the CHFR family.
CC       {ECO:0000256|ARBA:ARBA00005797}.
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:EAK90333.1}.
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DR   EMBL; AAEE01000001; EAK90333.1; -; Genomic_DNA.
DR   RefSeq; XP_628496.1; XM_628494.1.
DR   AlphaFoldDB; Q5CY84; -.
DR   STRING; 353152.Q5CY84; -.
DR   EnsemblProtists; EAK90333; EAK90333; cgd7_3320.
DR   GeneID; 3372048; -.
DR   KEGG; cpv:cgd7_3320; -.
DR   VEuPathDB; CryptoDB:cgd7_3320; -.
DR   InParanoid; Q5CY84; -.
DR   OMA; YNIEETH; -.
DR   OrthoDB; 5479648at2759; -.
DR   Proteomes; UP000006726; Chromosome 7.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00060; FHA; 1.
DR   Gene3D; 2.60.200.20; -; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
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   PANTHER; PTHR23328:SF0; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR23328; UNCHARACTERIZED; 1.
DR   Pfam; PF00498; FHA; 2.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00240; FHA; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 2.
DR   PROSITE; PS50006; FHA_DOMAIN; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006726};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          80..118
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          573..647
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
SQ   SEQUENCE   873 AA;  99450 MW;  FD39DDB1977145B7 CRC64;
     MINNNMIKRE VVNERKQDCE HGSDIINNKD NMFNITVNTE PYDVLENDIM KNKSRKVNNS
     SKNGFESTNI SNKILSEFTC PVCLDYYMLP VTIPCGHTFC RYCITHNRLL GKKCPVCRQL
     IGYNFRINMT IHNVIVSLGI FKQIENSSQD ERLYNEILLT NNELIGQNRP KWWQLCFCKP
     IISVTLFARI ISDEILGIGI VFAEDLTRCI IDHLSKLSSI IQDKKLKSMI WSNGIYMIGP
     LEVNLLTKWM GCPPLPFKLD DKETGNLEKN SDFTLNNNAI FKNQVKKWVE ECIALKPTIL
     NIGQSPFTKT STYPILRILS DRIHRVESKI YDLGALRSPL PWDLGRHSKS TIQVSHSSVS
     TNHLLIVNIK EHDQVAQELK YKSNTSHKFD ESSPIEKDWG IGVIDLGSSI GTMLKIQPKH
     RLATDEVIHL ADRVEIIVKI RKIEEITNED NLNGDSRILI NEWKKLRWSN KLNLVINIDD
     YNKGEHKTIN RAKNSDFEDL FGICNDKDKL DSSELSQESK IVQVPLEELE IEEIKECLEV
     YIPIGSKSFV PCEGAKKTEN GMYWSVIVHP SGMVFGRGKN GALGLRKVEV TESNGYISRE
     HCIFYYSSIR NREYEGLDYL SRSNGCLSNW FVKDVSTSGT FLRLKPFSYP VRVLPGMVLK
     VGQCKMEILP YMIGALYSGQ PNSSVRNNSI NLVSQDFQPI QTNLTEVESS QTHVSNTNQI
     PIPYLSNSAL FTQTLNDQYL SNINNNVIAQ LNILAAYNYI NSSSITNLVN SNNIVEFNNQ
     TYEDRIIQRQ NSSFDNIILQ SILRNSIVNN NILSAGHYLG NIQTSEDNSI TGGSIGSLEV
     NSILNYDRRP REPRVTQEVD VSFQIESFEN EDC
//
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