(data stored in ACNUC941 zone)

HOGENOM: BOVIN21_58_PE6

ID   BOVIN21_58_PE6                       STANDARD;      PRT;   421 AA.
AC   BOVIN21_58_PE6; Q9TTK8; Q3ZCF8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Creatine kinase U-type, mitochondrial; EC=2.7.3 2;AltName:
DE   Full=Acidic-type mitochondrial creatine kinase; Short=Mia-CK;AltName:
DE   Full=Ubiquitous mitochondrial creatine kinase; Short=U-MtCK;Flags:
DE   Precursor; (BOVIN21_58.PE6).
GN   Name=CKMT1;
OS   BOS TAURUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BOVIN21_58.PE6.
CC       Bos taurus chromosome 21 Btau_4.0 partial sequence 55582871..56525353
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:KCRU_BOVIN
CC   -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC       ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC       kinase isoenzymes play a central role in energy transduction in
CC       tissues with large, fluctuating energy demands, such as skeletal
CC       muscle, heart, brain and spermatozoa (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC   -!- SUBUNIT: Exists as an octamer composed of four MTCK homodimers (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Intermembrane side (By similarity).
CC   -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC   -!- SIMILARITY: Contains 1 phosphagen kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 phosphagen kinase N-terminal domain.
CC   -!- GENE_FAMILY: HOG000232165 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Bos_taurus;ENSBTAG00000007502;ENSBTAT00000009871;ENSBTAP00000009871.
DR   EMBL; AB003307; - ;
DR   EMBL; BC102422; - ;
DR   UniProtKB/Swiss-Prot; Q9TTK8; Q3ZCF8; -.
DR   EMBL; AB003307; BAA88431.1; -; mRNA.
DR   EMBL; BC102422; AAI02423.1; -; mRNA.
DR   IPI; IPI00692034; -.
DR   RefSeq; NP_776700.1; NM_174275.2.
DR   UniGene; Bt.49713; -.
DR   ProteinModelPortal; Q9TTK8; -.
DR   SMR; Q9TTK8; 39-412.
DR   PRIDE; Q9TTK8; -.
DR   GeneID; 281692; -.
DR   KEGG; bta:281692; -.
DR   CTD; 12716; -.
DR   eggNOG; maNOG10765; -.
DR   GeneTree; ENSGT00550000074561; -.
DR   InParanoid; Q9TTK8; -.
DR   OrthoDB; EOG40VVPN; -.
DR   PhylomeDB; Q9TTK8; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; IEA:EC.
DR   InterPro; IPR000749; ATP-guanido_PTrfase.
DR   InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR   InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR   InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   Gene3D; G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
DR   Gene3D; G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
DR   PANTHER; PTHR11547; ATP-gua_Ptrans; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   SUPFAM; SSF48034; ATP-gua_Ptrans; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR   PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
DR   HOGENOMDNA; BOVIN21_58.PE6; -.
KW   ENSBTAG00000007502fold_1320000031; ENSBTAP00000009871fold_1320000031;
KW   AB003307; BC102422;
KW   ATP-binding; Complete proteome; Kinase; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase; Transit peptide.
SQ   SEQUENCE   421 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAGPFSRLLS ARPGLRLLAL AGAGSLAAGF LLRSEPVRAA SERRRLYPPR YPLPSAEYPD
     LRKHNNCMAS HLTPAVYARL CDKTTPTGWT LDQCIQTGVD NPGHPFIKTV GMVAGDEETY
     EVFAELFDPV IQERHNGYDP RTMKHTTDLD ASKIRSGYFD ERYVLSSRVR TGRSIRGLSL
     PPACTRAERR EVERVVVDAL SGLKGDLAGR YYRLSEMTEA EQQQLIDDHF LFDKPVSPLL
     TAAGMARDWP DARGIWHNNE KSFLIWVNEE DHTRVISMEK GGNMKKVFER FCRGLKEVER
     LIQERGWEFM WNERLGYILT CPSNLGTGLR AGVHIKLPLL SKDSRFPKIL ENLRLQKRGT
     GGVDTAATGS VFDISNLDRL GKSEVELVQL VIDGVNFLID CERRLERGQD IRIPPPLPNK
     H
//

If you have problems or comments...

PBIL Back to PBIL home page