ID K1Q8K9_CRAGI Unreviewed; 885 AA.
AC K1Q8K9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=KRR1 small subunit processome component homolog {ECO:0000256|ARBA:ARBA00020053};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
DE AltName: Full=KRR-R motif-containing protein 1 {ECO:0000256|ARBA:ARBA00032993};
GN ORFNames=CGI_10024541 {ECO:0000313|EMBL:EKC30308.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC30308.1};
RN [1] {ECO:0000313|EMBL:EKC30308.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC30308.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(2012).
CC -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other
CC proteins. {ECO:0000256|ARBA:ARBA00002035}.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}. Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the KRR1 family.
CC {ECO:0000256|ARBA:ARBA00009344}.
CC -!- SIMILARITY: Belongs to the P4HA family.
CC {ECO:0000256|ARBA:ARBA00006511}.
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DR EMBL; JH818600; EKC30308.1; -; Genomic_DNA.
DR AlphaFoldDB; K1Q8K9; -.
DR HOGENOM; CLU_325779_0_0_1; -.
DR InParanoid; K1Q8K9; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd22393; KH-I_KRR1_rpt1; 1.
DR CDD; cd22394; KH-I_KRR1_rpt2; 1.
DR Gene3D; 6.10.140.1460; -; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 2.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR041174; KRR1-like_KH1.
DR InterPro; IPR048550; KRR1-like_KH1_euk.
DR InterPro; IPR048548; KRR1-like_KH2.
DR InterPro; IPR048549; KRR1-like_KH2_euk.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR013547; Pro_4_hyd_alph_N.
DR InterPro; IPR024166; rRNA_assembly_KRR1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR12581; HIV-1 REV BINDING PROTEIN 2, 3; 1.
DR PANTHER; PTHR12581:SF0; KRR1 SMALL SUBUNIT PROCESSOME COMPONENT HOMOLOG; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF17903; KH_8; 1.
DR Pfam; PF21800; KRR1-like_KH2; 1.
DR Pfam; PF08336; P4Ha_N; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
SQ SEQUENCE 885 AA; 101311 MW; 3192418C89C0366D CRC64;
MDFPVNKGKQ KGKKTVNQEE LLEVPDGWKE PGIAKEQNPH GVVSESSFAT LFPKYRENYI
NECWPLVKKT LGDHNIKAEL DLVEGSMTVR TTKKTWDPYI IIKARDLLKL LARSVPYEQA
VRVLEDDTAC DIIKIGSLTR NKERFVKRRQ RLIGPNGSTL KAIEILTDCY ILVQGNTVSA
LGPYKGLREV RKIVEDTMKN IHPIYNIKTL MIKKELAKDP ELRNENWERF IPKFKSKNIS
KRKQPKKKRV KKPYTPFPPP QPESKVDKEL ASGEYFLKPH QKKAKIQQEK KEKQLKAVQK
SQEKRAKAFV APKEDAAPPK KKQKVSEAVN VEELKKKIKK SQCDFFSALY KLQDLLREEE
KLQLDLSRYI SSVQENEQDV PLEILRFSES LKIKRKTIND GSAYIEHPVN DFHLLYRFVV
EWQSVFDIIF CKDCEETEAA KGAKGSPFAT VIQLPMHLDG HLGEKGDFNF TVQLVSKRLG
LWPSSYDLDG ASSALLRLWK VYKLDLNEFI NGIVQTYTAD QPMSDDEVLT VAKFADSVKD
DYSEMRWLKA LYKRLQTEDG FSHNQTTVIR FPKKGIFILE PFQSLENRDI NSDVAFYLSN
ATSDENETIP EPATEDAMYE ALCREEQKSL HELAKLRCFL RDTVIPYYKA KEEVVNYEPR
IAIFHDVISS TSIEHLKSIA SKGLTRSTVF LENTGPNGQV TITYGKQDNI RVSQTCWIRT
DEYPELLRLE NRIQLITGLS AEYKPVRSHS EKFQVVNYGV GGMYTAHHDY TGYKLGIISN
PMDSEDISTS GDRMATWMFY MNDAKAGGAT VFPEVRTRIP VAKGGAAFWF NLRPSGATDP
RTLHGGCPVL VGSKWVTNKW IREEGQMDRR LCGLTEDAVE DFPKI
//
