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Conserved domains on  [gi|1131247163|ref|XP_019809103|]
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PREDICTED: protein phosphatase 1 regulatory subunit 3B isoform X1 [Bos indicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBM_21 pfam03370
Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic ...
 181-286 1.96e-52

Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.


:

Pssm-ID: 427265  Cd Length: 112  Bit Score: 168.57  E-value: 1.96e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131247163 181 RLQTDHVCLENCVLKD--RSIAGTVKVQNLAFEKTVKVRMTFDTWKSFTDFPCWYVKD---TYAGSDKDTFSFDISL-PE 254
Cdd:pfam03370   1 RLQGQPVCLERLFLSDdkKSLVGTVRVKNLAFEKRVAVRYTFDNWKTISDVPAEYVPDarsSLDGDNYDRFKFKIPLpPL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1131247163 255 KIQSYERMEFAVCYECNGQTYWDSNKGKNYRI 286
Cdd:pfam03370  81 LNLEGKTLEFCIRYEVNGQEYWDNNNGKNYQV 112
PBD_PPP1R3B cd22814
PP1C binding domain found in protein phosphatase 1 regulatory subunit 3B (PPP1R3B); PPP1R3B, ...
 86-158 4.14e-40

PP1C binding domain found in protein phosphatase 1 regulatory subunit 3B (PPP1R3B); PPP1R3B, also called hepatic glycogen-targeting protein phosphatase 1 (PP1) regulatory subunit GL, protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, or protein phosphatase 1 subunit GL, acts as a glycogen-targeting subunit for PP1. It facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. PPP1R3B suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by glycogen phosphorylase liver form (PYGL), resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. It can dramatically increase basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes. PPP1R3B interacts with glycogen, the PPP1CC catalytic subunit of PP1, and PYGL. It associates with glycogen particles. This model corresponds to the protein phosphatase 1 catalytic subunit (PP1C) binding domain of PPP1R3B, which contains a RVxF PP1C-binding motif that mediates interactions with PP1C.


:

Pssm-ID: 439279  Cd Length: 74  Bit Score: 135.75  E-value: 4.14e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131247163  86 KPLRPCIQLSGKNEASGTVAPT-VQEKKVKKRVSFADNQGLALTMVKVFSEFDDPLDIPLNITELLDSIVSLTT 158
Cdd:cd22814     1 KPLRPCIQLNSKNKLSGGMSEPsVQENKVKKHVSFADHKGLALTMVKVFSEFDDPLDIPFNITELIDNIVSLTT 74
 
Name Accession Description Interval E-value
CBM_21 pfam03370
Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic ...
 181-286 1.96e-52

Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.


Pssm-ID: 427265  Cd Length: 112  Bit Score: 168.57  E-value: 1.96e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131247163 181 RLQTDHVCLENCVLKD--RSIAGTVKVQNLAFEKTVKVRMTFDTWKSFTDFPCWYVKD---TYAGSDKDTFSFDISL-PE 254
Cdd:pfam03370   1 RLQGQPVCLERLFLSDdkKSLVGTVRVKNLAFEKRVAVRYTFDNWKTISDVPAEYVPDarsSLDGDNYDRFKFKIPLpPL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1131247163 255 KIQSYERMEFAVCYECNGQTYWDSNKGKNYRI 286
Cdd:pfam03370  81 LNLEGKTLEFCIRYEVNGQEYWDNNNGKNYQV 112
PBD_PPP1R3B cd22814
PP1C binding domain found in protein phosphatase 1 regulatory subunit 3B (PPP1R3B); PPP1R3B, ...
 86-158 4.14e-40

PP1C binding domain found in protein phosphatase 1 regulatory subunit 3B (PPP1R3B); PPP1R3B, also called hepatic glycogen-targeting protein phosphatase 1 (PP1) regulatory subunit GL, protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, or protein phosphatase 1 subunit GL, acts as a glycogen-targeting subunit for PP1. It facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. PPP1R3B suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by glycogen phosphorylase liver form (PYGL), resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. It can dramatically increase basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes. PPP1R3B interacts with glycogen, the PPP1CC catalytic subunit of PP1, and PYGL. It associates with glycogen particles. This model corresponds to the protein phosphatase 1 catalytic subunit (PP1C) binding domain of PPP1R3B, which contains a RVxF PP1C-binding motif that mediates interactions with PP1C.


Pssm-ID: 439279  Cd Length: 74  Bit Score: 135.75  E-value: 4.14e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131247163  86 KPLRPCIQLSGKNEASGTVAPT-VQEKKVKKRVSFADNQGLALTMVKVFSEFDDPLDIPLNITELLDSIVSLTT 158
Cdd:cd22814     1 KPLRPCIQLNSKNKLSGGMSEPsVQENKVKKHVSFADHKGLALTMVKVFSEFDDPLDIPFNITELIDNIVSLTT 74
 
Name Accession Description Interval E-value
CBM_21 pfam03370
Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic ...
 181-286 1.96e-52

Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.


Pssm-ID: 427265  Cd Length: 112  Bit Score: 168.57  E-value: 1.96e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131247163 181 RLQTDHVCLENCVLKD--RSIAGTVKVQNLAFEKTVKVRMTFDTWKSFTDFPCWYVKD---TYAGSDKDTFSFDISL-PE 254
Cdd:pfam03370   1 RLQGQPVCLERLFLSDdkKSLVGTVRVKNLAFEKRVAVRYTFDNWKTISDVPAEYVPDarsSLDGDNYDRFKFKIPLpPL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1131247163 255 KIQSYERMEFAVCYECNGQTYWDSNKGKNYRI 286
Cdd:pfam03370  81 LNLEGKTLEFCIRYEVNGQEYWDNNNGKNYQV 112
PBD_PPP1R3B cd22814
PP1C binding domain found in protein phosphatase 1 regulatory subunit 3B (PPP1R3B); PPP1R3B, ...
 86-158 4.14e-40

PP1C binding domain found in protein phosphatase 1 regulatory subunit 3B (PPP1R3B); PPP1R3B, also called hepatic glycogen-targeting protein phosphatase 1 (PP1) regulatory subunit GL, protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, or protein phosphatase 1 subunit GL, acts as a glycogen-targeting subunit for PP1. It facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. PPP1R3B suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by glycogen phosphorylase liver form (PYGL), resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. It can dramatically increase basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes. PPP1R3B interacts with glycogen, the PPP1CC catalytic subunit of PP1, and PYGL. It associates with glycogen particles. This model corresponds to the protein phosphatase 1 catalytic subunit (PP1C) binding domain of PPP1R3B, which contains a RVxF PP1C-binding motif that mediates interactions with PP1C.


Pssm-ID: 439279  Cd Length: 74  Bit Score: 135.75  E-value: 4.14e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131247163  86 KPLRPCIQLSGKNEASGTVAPT-VQEKKVKKRVSFADNQGLALTMVKVFSEFDDPLDIPLNITELLDSIVSLTT 158
Cdd:cd22814     1 KPLRPCIQLNSKNKLSGGMSEPsVQENKVKKHVSFADHKGLALTMVKVFSEFDDPLDIPFNITELIDNIVSLTT 74
CBM53 pfam16760
Starch/carbohydrate-binding module (family 53);
207-287 4.27e-15

Starch/carbohydrate-binding module (family 53);


Pssm-ID: 465261 [Multi-domain]  Cd Length: 76  Bit Score: 69.24  E-value: 4.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131247163 207 NLAFEKTVK----VRMTFDTWKSFTDFPCWYVKDTYAGsdkDTFSFDISLPEKIqsyERMEFAVCyecNGQTYWDSNKGK 282
Cdd:pfam16760   1 NIYYNGSLAkevyIHGGFNGWKNVQDVPMEKLPPTGGG---DWFSATVPVPEDA---YVLDFVFK---DGAGNWDNNNGQ 71


                  ....*
gi 1131247163 283 NYRII 287
Cdd:pfam16760  72 NYHIP 76
PBD_PPP1R3C cd22815
PP1C binding domain found in protein phosphatase 1 regulatory subunit 3C (PPP1R3C); PPP1R3C, ...
 86-156 1.93e-13

PP1C binding domain found in protein phosphatase 1 regulatory subunit 3C (PPP1R3C); PPP1R3C, also called protein phosphatase 1 regulatory subunit 5 (PPP1R5), PP1 subunit R5, or protein targeting to glycogen (PTG), acts as a glycogen-targeting subunit for protein phosphatase 1 (PP1) and regulates its activity. It activates glycogen synthase, reduces glycogen phosphorylase activity, and limits glycogen breakdown. It can dramatically increase basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types. PPP1R3C interacts with the PPP1CC catalytic subunit of PP1 and associates with glycogen. This model corresponds to protein phosphatase 1 catalytic subunit (PP1C) binding domain of PPP1R3C, which contains a RVxF PP1C-binding motif that mediates interactions with PP1C.


Pssm-ID: 439280  Cd Length: 79  Bit Score: 64.70  E-value: 1.93e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131247163  86 KPLRPCiqLSGKNEA-SGTVAPTVQEKKVKKRVSFADNQGLALTMVKVFSEFDDPL--DIPLNITELLDSIVSL 156
Cdd:cd22815     6 KPLRPC--LSSKSESeSITNEWKRSKSKAKKKVVFADSKGLSLTAVHVFSEFEDDLtsDLQFDLSDLEDITSGL 77
PBD_PPP1R3 cd22813
PP1C binding domain found in protein phosphatase 1 regulatory subunit 3 (PPP1R3) family; The ...
 108-138 4.74e-12

PP1C binding domain found in protein phosphatase 1 regulatory subunit 3 (PPP1R3) family; The PPP1R3 family includes three protein phosphatase 1 regulatory subunits, PPP1R3A, PPP1R3B and PPP1R3C, that act as glycogen-targeting subunits for protein phosphatase 1 (PP1). PPP1R3A, also called protein phosphatase 1 glycogen-associated regulatory subunit (PP1G), protein phosphatase type-1 glycogen targeting subunit, or RG1, is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility, and protein synthesis. PPP1R3A plays an important role in glycogen synthesis but is not essential for insulin activation of glycogen synthase. PPP1R3B, also called hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL, protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, or protein phosphatase 1 subunit GL, facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. PPP1R3B suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by glycogen phosphorylase liver form (PYGL), resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. PPP1R3C, also called protein phosphatase 1 regulatory subunit 5 (PPP1R5), PP1 subunit R5, or protein targeting to glycogen (PTG), activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. It can dramatically increase basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types. This model corresponds to protein phosphatase 1 catalytic subunit (PP1C) binding domain, which contains a RVxF PP1C-binding motif that mediates interactions with PP1C.


Pssm-ID: 439278  Cd Length: 31  Bit Score: 59.54  E-value: 4.74e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1131247163 108 VQEKKVKKRVSFADNQGLALTMVKVFSEFDD 138
Cdd:cd22813     1 TSPNKAKKRVSFADSKGLSLTSVKLFDEWED 31
KNL1_NTD cd21853
N-terminal domain found in kinetochore scaffold 1 (KNL1) and similar proteins; Kinetochore ...
 86-136 3.64e-03

N-terminal domain found in kinetochore scaffold 1 (KNL1) and similar proteins; Kinetochore scaffold 1 (KNL1), also called ALL1-fused gene from chromosome 15q14 protein (AF15q14), Bub-linking kinetochore protein (Blinkin), cancer susceptibility candidate gene 5 protein (CASC5), cancer/testis antigen 29 (CT29), kinetochore-null protein 1, or protein D40/AF15q14, plays crucial roles during mitosis. It is essential for spindle-assembly checkpoint (SAC) signaling and for correct chromosome alignment. It is required for attachment of the kinetochores to the spindle microtubules. KNL1 directly links BUB1 and BUB1B to kinetochores. It is part of the MIS12 complex, which may be fundamental for kinetochore formation and proper chromosome segregation during mitosis. KNL1 also acts in coordination with CENPK to recruit the NDC80 complex to the outer kinetochore. This model corresponds to a small conserved region at the N-terminus of KNL1, which is responsible for the binding of protein phosphatase 1 (PP1). PP1 regulates SAC silencing and mitotic exit, and is targeted to kinetochores, in part, by KNL1.


Pssm-ID: 439316  Cd Length: 56  Bit Score: 35.40  E-value: 3.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1131247163  86 KPLRPCIQLSGKNEASGTVAPTVQEKKVKKRVSFADNqglalTMVKVFSEF 136
Cdd:cd21853     9 KPPRSPLLDLDEGNEQNQDLNKKKKRRSSRRVSFADT-----IQVKEFEKD 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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