Full text data of ZZZZ
Q86U75
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q86U75
ID Q86U75_HUMAN Unreviewed; 619 AA.
AC Q86U75;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
read moreDT 22-JAN-2014, entry version 48.
DE SubName: Full=Dihydropyrimidinase-like 2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) System Donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; BT006944; AAP35590.1; -; mRNA.
DR ProteinModelPortal; Q86U75; -.
DR SMR; Q86U75; 15-396.
DR REPRODUCTION-2DPAGE; IPI00106642; -.
DR PRIDE; Q86U75; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:InterPro.
DR GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IEA:InterPro.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR016093; MIR_motif.
DR Pfam; PF02815; MIR; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF82109; SSF82109; 1.
DR TIGRFAMs; TIGR02033; D-hydantoinase; 1.
DR PROSITE; PS50919; MIR; 3.
PE 2: Evidence at transcript level;
SQ SEQUENCE 619 AA; 67017 MW; 3EFF0DED0930C9CE CRC64;
MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI VPGGVKTIEA
HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGTSLLAAF
DQWREWADSK SCCDYSLHVD ISEWHKGIQE EMEALVKDHG VNSFLVYMAF KDRFQLTDCQ
IYEVLSVIRD IGAIAQVHAE NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRAI
TIANQTNCPL YITKVMSKSS AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA
FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL IPEGTNGTEE
RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPGAMW SAGRGGAAWP VLLGLLLALL
VPGGGAAKTG AELVTCGSVL KLLNTHHRVR LHSHDIKYGS GSGQQSVTGV EASDDANSYW
RIRGGSEGGC PRGSPVRCGQ AVRLTHVLTG KNLHTHHFPS PLSNNQEVSA FGEDGEGDDL
DLWTVRCSGQ HWEREAAVRF QHVGTSVFLS VTGEQYGSPI RGQHEVHGMP SANTHNTWKA
MEGIFIKPSV EPSAGHDEL
//
ID Q86U75_HUMAN Unreviewed; 619 AA.
AC Q86U75;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
read moreDT 22-JAN-2014, entry version 48.
DE SubName: Full=Dihydropyrimidinase-like 2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) System Donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; BT006944; AAP35590.1; -; mRNA.
DR ProteinModelPortal; Q86U75; -.
DR SMR; Q86U75; 15-396.
DR REPRODUCTION-2DPAGE; IPI00106642; -.
DR PRIDE; Q86U75; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:InterPro.
DR GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IEA:InterPro.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR016093; MIR_motif.
DR Pfam; PF02815; MIR; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF82109; SSF82109; 1.
DR TIGRFAMs; TIGR02033; D-hydantoinase; 1.
DR PROSITE; PS50919; MIR; 3.
PE 2: Evidence at transcript level;
SQ SEQUENCE 619 AA; 67017 MW; 3EFF0DED0930C9CE CRC64;
MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI VPGGVKTIEA
HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGTSLLAAF
DQWREWADSK SCCDYSLHVD ISEWHKGIQE EMEALVKDHG VNSFLVYMAF KDRFQLTDCQ
IYEVLSVIRD IGAIAQVHAE NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRAI
TIANQTNCPL YITKVMSKSS AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA
FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL IPEGTNGTEE
RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPGAMW SAGRGGAAWP VLLGLLLALL
VPGGGAAKTG AELVTCGSVL KLLNTHHRVR LHSHDIKYGS GSGQQSVTGV EASDDANSYW
RIRGGSEGGC PRGSPVRCGQ AVRLTHVLTG KNLHTHHFPS PLSNNQEVSA FGEDGEGDDL
DLWTVRCSGQ HWEREAAVRF QHVGTSVFLS VTGEQYGSPI RGQHEVHGMP SANTHNTWKA
MEGIFIKPSV EPSAGHDEL
//