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PR00104

Identifier
CGMPKINASE  [View Relations]  [View Alignment]  
Accession
PR00104
No. of Motifs
6
Creation Date
27-JUL-1991  (UPDATE 06-JUN-1999)
Title
cGMP-dependent protein kinase signature
Database References

PROSITE; PS00888 CNMP_BINDING_1; PS00889 CNMP_BINDING_2
BLOCKS; BL00888
INTERPRO; IPR002374
Literature References
1. KALDERON. D. AND RUBIN, G.M.
cGMP-Dependent protein kinase genes in Drosophila.
J.BIOL.CHEM. 264 10738-10748 (1989).
 
2. TAKIO, K., WADE, R.D., SMITH, S.B., KREBS, E.G., WALSH, K.A.
AND TITANI, K.
Guanosine cyclase 3',5'-phosphate dependent protein kinase, a chimeric
protein homologous with two separate protein families.
BIOCHEMISTRY 23 4207-4218 (1984).

Documentation
Little is known in detail about the biological functions of cGMP-dependent
protein kinases, but they are known to play a role in smooth muscle
relaxation, ion fluxes in kidneys and intestines, and neuronal function.
In recent years, identification of genes coding for these proteins has
made their isolation easier, leading to an increase in our understanding
of the cells in which they are present and the functions they possess.
 
The predominant form of cGMP-dependent protein kinase is a dimer of
identical 75kDa subunits, although larger subunits of 86 and 130kDa have
been found [1]. The enzyme is kept in an inactive form by the interaction
of the catalytic domain of one subunit with the region on the other subunit
that precedes the cGMP binding domain. Each subunit contains 2 cGMP-binding
regions, found together in the sequence: binding of 2 molecules of cGMP
precipitates a conformational change in the active site that allows the
substrate to bind.
 
Although cGMP- and cAMP-dependent protein kinases are similar both in
structure and sequence around the nucleotide binding site, and in the 
method of activation and inactivation, there are some basic contrasts. The
major difference is that all of the functional domains of the cGMP-
dependent enzymes are found on a single polypeptide chain, whereas cAMP-
dependent protein kinases have separate regulatory (cAMP binding) and
catalytic chains. 
 
CGMPKINASE is a 6-element fingerprint that provides a signature for the 
cGMP-dependent protein kinases. The fingerprint was derived from an 
initial alignment of 4 sequences: the motifs were drawn from the second
cGMP-binding region (see Takio et al. [2]). Two iterations on OWL11.0 were
required to reach convergence, at which point a true set comprising 11
sequences was identified. 
 
An update on SPTR37_9f identified a true set of 11 sequences, and 5
partial matches.
Summary Information
  11 codes involving  6 elements
0 codes involving 5 elements
2 codes involving 4 elements
3 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
6111111111111
5000000
4220220
3300330
2000000
123456
True Positives
KGP1_DROME    KGP2_DROME    KGP3_DROME    KGPA_BOVIN    
KGPB_BOVIN KGPB_HUMAN O77676 Q24302
Q24303 Q24304 Q24566
True Positive Partials
Codes involving 4 elements
O00125 Q13237
Codes involving 3 elements
O17474 Q61410 Q64595
Sequence Titles
KGP1_DROME  CGMP-DEPENDENT PROTEIN KINASE, ISOZYME 1 (EC 2.7.1.-) (CGK) - DROSOPHILA MELANOGASTER (FRUIT FLY). 
KGP2_DROME CGMP-DEPENDENT PROTEIN KINASE, ISOZYME 2 FORMS T1/T3 (EC 2.7.1.37) (CGK) (PROTEIN FORAGING) - DROSOPHILA MELANOGASTER (FRUIT FLY).
KGP3_DROME CGMP-DEPENDENT PROTEIN KINASE, ISOZYME 2 FORMS T2/CD5 (EC 2.7.1.-) (CGK) (PROTEIN FORAGING) - DROSOPHILA MELANOGASTER (FRUIT FLY).
KGPA_BOVIN CGMP-DEPENDENT PROTEIN KINASE, ALPHA ISOZYME (CGK) (EC 2.7.1.37) - BOS TAURUS (BOVINE).
KGPB_BOVIN CGMP-DEPENDENT PROTEIN KINASE, BETA ISOZYME (CGK) (EC 2.7.1.37) - BOS TAURUS (BOVINE).
KGPB_HUMAN CGMP-DEPENDENT PROTEIN KINASE, BETA ISOZYME (CGK) (EC 2.7.1.37) - HOMO SAPIENS (HUMAN).
O77676 CGMP-DEPENDENT PROTEIN KINASE TYPE 1 ALPHA - ORYCTOLAGUS CUNICULUS (RABBIT).
Q24302 CGMP-DEPENDENT PROTEIN KINASE (DG2;CD5) - DROSOPHILA MELANOGASTER (FRUIT FLY).
Q24303 CGMP-DEPENDENT PROTEIN KINASE (DG2;T2) - DROSOPHILA MELANOGASTER (FRUIT FLY).
Q24304 CGMP-DEPENDENT PROTEIN KINASE (DG2;T3) - DROSOPHILA MELANOGASTER (FRUIT FLY).
Q24566 CGMP-DEPENDENT PROTEIN KINASE - DROSOPHILA MELANOGASTER (FRUIT FLY).

O00125 CGMP-DEPENDENT PROTEIN KINASE II - HOMO SAPIENS (HUMAN).
Q13237 TYPE II CGMP-DEPENDENT PROTEIN KINASE - HOMO SAPIENS (HUMAN).

O17474 CYCLIC GMP-DEPENDENT PROTEIN KINASE - HYDRA OLIGACTIS (HYDRA).
Q61410 PROTEIN KINASE, CGMP-DEPENDENT, TYPE II (CYCLIC GMP-DEPENDENT PROTEIN KINASE II) - MUS MUSCULUS (MOUSE).
Q64595 CGMP DEPENDENT PROTEIN KINASE II (EC 2.7.1.37) (PHOSPHORYLASE B KINASE KINASE) (GLYCOGEN SYNTHASE A KINASE) (HYDROXYALKYL-PROTEIN KINASE) (SERINE(THREONINE) PROTEIN KINASE) - RATTUS NORVEGICUS (RAT).
Scan History
OWL11_0    2  50   NSINGLE    
OWL17_1 1 30 NSINGLE
OWL18_0 1 30 NSINGLE
OWL19_1 1 30 NSINGLE
OWL26_0 1 100 NSINGLE
SPTR37_9f 2 47 NSINGLE
Initial Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
EDTLIKISDVLEETH DRODG2T3A 298 298 -
EELLAKIADVLELEF DRODG1A2 310 310 -
EEILSKLADVLEETH OKBOG 226 226 -
EEILSKLADVLEETH KGPB_HUMAN 242 242 -

Motif 2 width=10
Element Seqn Id St Int Rpt
SQGNVRVTQK DRODG1A2 345 20 -
SKGKVNVTRE OKBOG 261 20 -
SKGKVRVTIK DRODG2T3A 333 20 -
SKGTVNVTRE KGPB_HUMAN 277 20 -

Motif 3 width=8
Element Seqn Id St Int Rpt
FLRTLGKG KGPB_HUMAN 295 8 -
FLRTLGKG OKBOG 279 8 -
ELRTLSRG DRODG1A2 364 9 -
FIRMLGKG DRODG2T3A 351 8 -

Motif 4 width=10
Element Seqn Id St Int Rpt
DDLRTANIIC DRODG2T3A 369 10 -
EDKRTANIIA DRODG1A2 382 10 -
EDVRTANVIA OKBOG 297 10 -
EDVRTANVIA KGPB_HUMAN 313 10 -

Motif 5 width=10
Element Seqn Id St Int Rpt
VTCLVIDRDS OKBOG 310 3 -
VECLTLDRDS DRODG1A2 396 4 -
VSCLVIDRET DRODG2T3A 384 5 -
VTCLVIDRDS KGPB_HUMAN 326 3 -

Motif 6 width=15
Element Seqn Id St Int Rpt
FKRLIGDLCELKEKD DRODG1A2 406 0 -
FKHLIGGLDDVSNKA OKBOG 320 0 -
FKHLIGGLDDVSNKA KGPB_HUMAN 336 0 -
FNQLISNLDEIKHRY DRODG2T3A 394 0 -
Final Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
EDTLIKISDVLEETH KGP2_DROME 644 644 -
EDTLIKISDVLEETH Q24304 298 298 -
EDTLIKISDVLEETH Q24303 450 450 -
EDTLIKISDVLEETH Q24302 490 490 -
EDTLIKISDVLEETH KGP3_DROME 489 489 -
EEILSKLADVLEETH KGPA_BOVIN 226 226 -
EEILSKLADVLEETH O77676 227 227 -
EEILSKLADVLEETH KGPB_BOVIN 242 242 -
EEILSKLADVLEETH KGPB_HUMAN 242 242 -
EELLAKIADVLELEF KGP1_DROME 310 310 -
EELLAKIADVLELEF Q24566 310 310 -

Motif 2 width=10
Element Seqn Id St Int Rpt
SKGKVRVTIK KGP2_DROME 679 20 -
SKGKVRVTIK Q24304 333 20 -
SKGKVRVTIK Q24303 485 20 -
SKGKVRVTIK Q24302 525 20 -
SKGKVRVTIK KGP3_DROME 524 20 -
SKGKVNVTRE KGPA_BOVIN 261 20 -
SKGKVNVTRE O77676 262 20 -
SKGKVNVTRE KGPB_BOVIN 277 20 -
SKGTVNVTRE KGPB_HUMAN 277 20 -
SQGNVRVTQK KGP1_DROME 345 20 -
SQGNVRVTQK Q24566 345 20 -

Motif 3 width=8
Element Seqn Id St Int Rpt
FIRMLGKG KGP2_DROME 697 8 -
FIRMLGKG Q24304 351 8 -
FIRMLGKG Q24303 503 8 -
FIRMLGKG Q24302 543 8 -
FIRMLGKG KGP3_DROME 542 8 -
FLRTLGKG KGPA_BOVIN 279 8 -
FLRTLGKG O77676 280 8 -
FLRTLGKG KGPB_BOVIN 295 8 -
FLRTLGKG KGPB_HUMAN 295 8 -
ELRTLSRG KGP1_DROME 364 9 -
ELRTLSRG Q24566 364 9 -

Motif 4 width=10
Element Seqn Id St Int Rpt
DDLRTANIIC KGP2_DROME 715 10 -
DDLRTANIIC Q24304 369 10 -
DDLRTANIIC Q24303 521 10 -
DDLRTANIIC Q24302 561 10 -
DDLRTANIIC KGP3_DROME 560 10 -
EDVRTANVIA KGPA_BOVIN 297 10 -
EDVRTANVIA O77676 298 10 -
EDVRTANVIA KGPB_BOVIN 313 10 -
EDVRTANVIA KGPB_HUMAN 313 10 -
EDKRTANIIA KGP1_DROME 382 10 -
EDKRTANIIA Q24566 382 10 -

Motif 5 width=10
Element Seqn Id St Int Rpt
VSCLVIDRET KGP2_DROME 730 5 -
VSCLVIDRET Q24304 384 5 -
VSCLVIDRET Q24303 536 5 -
VSCLVIDRET Q24302 576 5 -
VSCLVIDRET KGP3_DROME 575 5 -
VTCLVIDRDS KGPA_BOVIN 310 3 -
VTCLVIDRDS O77676 311 3 -
VTCLVIDRDS KGPB_BOVIN 326 3 -
VTCLVIDRDS KGPB_HUMAN 326 3 -
VECLTLDRDS KGP1_DROME 396 4 -
VECLTLDRDS Q24566 396 4 -

Motif 6 width=15
Element Seqn Id St Int Rpt
FNQLISNLDEIKHRY KGP2_DROME 740 0 -
FNQLISNLDEIKHRY Q24304 394 0 -
FNQLISNLDEIKHRY Q24303 546 0 -
FNQLISNLDEIKHRY Q24302 586 0 -
FNQLISNLDEIKHRY KGP3_DROME 585 0 -
FKHLIGGLDDVSNKA KGPA_BOVIN 320 0 -
FKHLIGGLDDVSNKA O77676 321 0 -
FKHLIGGLDDVSNKA KGPB_BOVIN 336 0 -
FKHLIGGLDDVSNKA KGPB_HUMAN 336 0 -
FKRLIGDLCELKEKD KGP1_DROME 406 0 -
FKRLIGDLCELKEKD Q24566 406 0 -