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Database: UniProt
Entry: Q5CQB6_CRYPI
LinkDB: Q5CQB6_CRYPI
Original site: Q5CQB6_CRYPI 
ID   Q5CQB6_CRYPI            Unreviewed;       686 AA.
AC   Q5CQB6;
DT   12-APR-2005, integrated into UniProtKB/TrEMBL.
DT   12-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=cgd4_1360 {ECO:0000313|EMBL:EAK87615.1};
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:EAK87615.1, ECO:0000313|Proteomes:UP000006726};
RN   [1] {ECO:0000313|EMBL:EAK87615.1, 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   -!- 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:EAK87615.1}.
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DR   EMBL; AAEE01000009; EAK87615.1; -; Genomic_DNA.
DR   RefSeq; XP_625732.1; XM_625732.1.
DR   AlphaFoldDB; Q5CQB6; -.
DR   STRING; 353152.Q5CQB6; -.
DR   EnsemblProtists; EAK87615; EAK87615; cgd4_1360.
DR   GeneID; 3372642; -.
DR   KEGG; cpv:cgd4_1360; -.
DR   VEuPathDB; CryptoDB:cgd4_1360; -.
DR   InParanoid; Q5CQB6; -.
DR   OMA; EIKMLCR; -.
DR   OrthoDB; 5471056at2759; -.
DR   Proteomes; UP000006726; Chromosome 4.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   CDD; cd16649; mRING-HC-C3HC5_CGRF1-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045194; MGRN1/RNF157-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22996; MAHOGUNIN; 1.
DR   PANTHER; PTHR22996:SF0; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006726};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   TRANSMEM        29..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          635..672
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   COILED          160..217
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   686 AA;  79275 MW;  64A0FC436BD809E3 CRC64;
     MEDISIIECS KLYPALCFDL YGSPGFHNIY VGLLVIISGI WLVSRLAKIV EFYEMIRIIQ
     EEGKVINIPS LGPYSNDLKK LIKSHISQII RERCSISPIN VKKLQVMNIM EESTLKTRLI
     PNSSSSSSPD ESYSLEVSFK VDSFVPHSIQ LFWGVDYFAA KELLIEERKV ENELNTISNK
     MSRRMALGSS ISMFDQLKLK EKNNENLEEN KIEKNTNIGL EYNNNVNNST RLFENMEIDH
     DEKERTDLNV PFDFSPSESM KSLANINPIL YTTEISNRRY YNYFGNSHDR DYFDYHTNMS
     RRGIFNIGPR ITRIVLKIKQ ILRDNIVVNT ISNSLNYSTW NSSLLGNNAI ILSRSIKRLF
     ENAFFYNTIS NINNNNNNNN NNNNINLGGF SLTKSSLLSS ASVTTELLLD KYHYDQLKSK
     SGSNNKYNID LKKIINQPST NLDEIKYQIL INKLNPMYIT EKKYYEKGLS QDYSEKIKLT
     PEYLTSCNLN SPYYDTQEQE INSKDEHQVL NHGDYYEIQD KCNHKEIFWN SDIINFNKNN
     IDSSILKIKT ENEENKEMPR IPLLILIRAN IGVIEDESIL TNNIIAINFD LIQDHYNIPY
     LMYKPIILKQ AISNSHGILI EPYDTYGLED DELDCLICMS NPKDVILLPC RHCISCESCL
     RSLRQDKCPL CRTTFSGFVV LPIKNS
//
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