protein kinase C homolog, partial [Neurospora perkinsii]
Protein Classification
serine/threonine-protein kinase N( domain architecture ID 11128916)
serine/threonine-protein kinase N catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| HR1 super family | cl00087 | Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ... |
117-160 | 9.13e-19 | ||
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region. The actual alignment was detected with superfamily member cd11620: Pssm-ID: 469609 Cd Length: 72 Bit Score: 75.47 E-value: 9.13e-19
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| HR1 | pfam02185 | Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ... |
1-31 | 4.84e-05 | ||
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger. : Pssm-ID: 460478 [Multi-domain] Cd Length: 67 Bit Score: 39.43 E-value: 4.84e-05
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| Name | Accession | Description | Interval | E-value | ||
| HR1_PKC-like_2_fungi | cd11620 | Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of fungal ... |
117-160 | 9.13e-19 | ||
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of fungal Protein Kinase C-like proteins; This subfamily is composed of fungal PKC-like proteins including Pkc1p from Saccharomyces cerevisiae, and Pck1p and Pck2p from Schizosaccharomyces pombe. The yeast PKC-like proteins play a critical role in regulating cell wall biosynthesis and maintaining cell wall integrity. They contain two HR1 domains, C2 and C1 domains, and a kinase domain. This model characterizes the second HR1 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family. The HR1 domains of Pck1p and Pck2p interact with GTP-bound Rho1p and Rho2p. Pssm-ID: 212010 Cd Length: 72 Bit Score: 75.47 E-value: 9.13e-19
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| HR1 | pfam02185 | Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ... |
126-160 | 1.26e-07 | ||
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger. Pssm-ID: 460478 [Multi-domain] Cd Length: 67 Bit Score: 46.36 E-value: 1.26e-07
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| Hr1 | smart00742 | Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ... |
125-160 | 3.17e-05 | ||
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain Pssm-ID: 128981 Cd Length: 57 Bit Score: 39.48 E-value: 3.17e-05
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| HR1 | pfam02185 | Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ... |
1-31 | 4.84e-05 | ||
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger. Pssm-ID: 460478 [Multi-domain] Cd Length: 67 Bit Score: 39.43 E-value: 4.84e-05
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| HR1_PKC-like_1_fungi | cd11621 | First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of fungal ... |
3-31 | 5.55e-03 | ||
First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of fungal Protein Kinase C-like proteins; This subfamily is composed of fungal PKC-like proteins including Pkc1p from Saccharomyces cerevisiae, and Pck1p and Pck2p from Schizosaccharomyces pombe. The yeast PKC-like proteins play a critical role in regulating cell wall biosynthesis and maintaining cell wall integrity. They contain two HR1 domains, C2 and C1 domains, and a kinase domain. This model characterizes the first HR1 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family. The HR1 domains of Pck1p and Pck2p interact with GTP-bound Rho1p and Rho2p. Pssm-ID: 212011 Cd Length: 72 Bit Score: 33.89 E-value: 5.55e-03
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| Name | Accession | Description | Interval | E-value | ||
| HR1_PKC-like_2_fungi | cd11620 | Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of fungal ... |
117-160 | 9.13e-19 | ||
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of fungal Protein Kinase C-like proteins; This subfamily is composed of fungal PKC-like proteins including Pkc1p from Saccharomyces cerevisiae, and Pck1p and Pck2p from Schizosaccharomyces pombe. The yeast PKC-like proteins play a critical role in regulating cell wall biosynthesis and maintaining cell wall integrity. They contain two HR1 domains, C2 and C1 domains, and a kinase domain. This model characterizes the second HR1 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family. The HR1 domains of Pck1p and Pck2p interact with GTP-bound Rho1p and Rho2p. Pssm-ID: 212010 Cd Length: 72 Bit Score: 75.47 E-value: 9.13e-19
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| HR1 | pfam02185 | Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ... |
126-160 | 1.26e-07 | ||
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger. Pssm-ID: 460478 [Multi-domain] Cd Length: 67 Bit Score: 46.36 E-value: 1.26e-07
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| Hr1 | smart00742 | Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ... |
125-160 | 3.17e-05 | ||
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain Pssm-ID: 128981 Cd Length: 57 Bit Score: 39.48 E-value: 3.17e-05
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| HR1 | pfam02185 | Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ... |
1-31 | 4.84e-05 | ||
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger. Pssm-ID: 460478 [Multi-domain] Cd Length: 67 Bit Score: 39.43 E-value: 4.84e-05
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| HR1 | cd00089 | Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ... |
122-160 | 1.87e-04 | ||
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region. Pssm-ID: 212008 [Multi-domain] Cd Length: 68 Bit Score: 37.69 E-value: 1.87e-04
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| HR1_PKC-like_1_fungi | cd11621 | First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of fungal ... |
3-31 | 5.55e-03 | ||
First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of fungal Protein Kinase C-like proteins; This subfamily is composed of fungal PKC-like proteins including Pkc1p from Saccharomyces cerevisiae, and Pck1p and Pck2p from Schizosaccharomyces pombe. The yeast PKC-like proteins play a critical role in regulating cell wall biosynthesis and maintaining cell wall integrity. They contain two HR1 domains, C2 and C1 domains, and a kinase domain. This model characterizes the first HR1 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family. The HR1 domains of Pck1p and Pck2p interact with GTP-bound Rho1p and Rho2p. Pssm-ID: 212011 Cd Length: 72 Bit Score: 33.89 E-value: 5.55e-03
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