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Conserved domains on  [gi|157820093|ref|NP_001099582|]
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geminin [Rattus norvegicus]

Protein Classification

geminin_CC domain-containing protein( domain architecture ID 10538419)

geminin_CC domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Geminin pfam07412
Geminin; This family contains the eukaryotic protein geminin (approximately 200 residues long). ...
 1-181 3.43e-96

Geminin; This family contains the eukaryotic protein geminin (approximately 200 residues long). Geminin inhibits DNA replication by preventing the incorporation of MCM complex into prereplication complex, and is degraded during the mitotic phase of the cell cycle. It has been proposed that geminin inhibits DNA replication during S, G2, and M phases and that geminin destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle.


:

Pssm-ID: 462159  Cd Length: 194  Bit Score: 277.78  E-value: 3.43e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820093    1 MNLSMKQK-QEGAQENVKS-------SPVPRRTLKMIQPSAAGSLVGRENELPKGLSKRKLWDDQLTSKISSCG----PE 68
Cdd:pfam07412   1 MNSSMKQKlQEESNENIKSfftpqkaSPVPRRTLKMIQPSAAGSLVGRSNELGKGSPKRKLWNDQLGSKRSKVEvkvtPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820093   69 ANEN-NSVGDLTQEACDLMTKENPSSQYWKEVAEQRRKALYEALTENEKLHKEIEQKDSEIARLRKENKDLAEVAEHVQY 147
Cdd:pfam07412  81 HSENkNLPGGVSQEAYDLMVKENPSSQYWKEVAEERRKALYEVLQENEKLHKEIEQKDEEIARLKEENEELAELAQHVQY 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 157820093  148 MAEVIERLSNEPLDNFESPDSQEFDSEKETVEYS 181
Cdd:pfam07412 161 MADMIERLTGQSPDNLEELDSLAFDSEEEAGEES 194
 
Name Accession Description Interval E-value
Geminin pfam07412
Geminin; This family contains the eukaryotic protein geminin (approximately 200 residues long). ...
 1-181 3.43e-96

Geminin; This family contains the eukaryotic protein geminin (approximately 200 residues long). Geminin inhibits DNA replication by preventing the incorporation of MCM complex into prereplication complex, and is degraded during the mitotic phase of the cell cycle. It has been proposed that geminin inhibits DNA replication during S, G2, and M phases and that geminin destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle.


Pssm-ID: 462159  Cd Length: 194  Bit Score: 277.78  E-value: 3.43e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820093    1 MNLSMKQK-QEGAQENVKS-------SPVPRRTLKMIQPSAAGSLVGRENELPKGLSKRKLWDDQLTSKISSCG----PE 68
Cdd:pfam07412   1 MNSSMKQKlQEESNENIKSfftpqkaSPVPRRTLKMIQPSAAGSLVGRSNELGKGSPKRKLWNDQLGSKRSKVEvkvtPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820093   69 ANEN-NSVGDLTQEACDLMTKENPSSQYWKEVAEQRRKALYEALTENEKLHKEIEQKDSEIARLRKENKDLAEVAEHVQY 147
Cdd:pfam07412  81 HSENkNLPGGVSQEAYDLMVKENPSSQYWKEVAEERRKALYEVLQENEKLHKEIEQKDEEIARLKEENEELAELAQHVQY 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 157820093  148 MAEVIERLSNEPLDNFESPDSQEFDSEKETVEYS 181
Cdd:pfam07412 161 MADMIERLTGQSPDNLEELDSLAFDSEEEAGEES 194
geminin_CC cd22589
central coiled-coil domain of geminin; Geminin, together with geminin coiled-coil ...
 93-157 3.39e-30

central coiled-coil domain of geminin; Geminin, together with geminin coiled-coil domain-containing protein 1 (GemC1) and McIdas (also called Idas or multicilin), controls both the cell cycle and differentiation decisions in cells. Geminin is an inhibitor of Cdt1, a key component and crucial regulator of pre-replicative complexes (pre-RC) that function in the duplication of chromosomal DNA. Pre-RC assembly culminates in the recruitment of the hexameric mini-chromosome maintenance complex (MCM) onto chromatin. Geminin tightly binds and sequesters Cdt1 in a complex that is unable to recruit MCM to origins, inhibiting DNA replication. It belongs to the geminin family of proteins that also includes GemC1 and McIdas. They share a homologous central coiled-coil domain that mediates homo- and heterodimerization with other family members; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of geminin.


Pssm-ID: 439143 [Multi-domain]  Cd Length: 65  Bit Score: 105.76  E-value: 3.39e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157820093  93 SQYWKEVAEQRRKALYEALTENEKLHKEIEQKDSEIARLRKENKDLAEVAEHVQYMAEVIERLSN 157
Cdd:cd22589    1 EQYWKELAEERRKALYEALQENEKLHKEIEQLDEEIARLKEENDELEELAEHVQYLAEVIERLTG 65
 
Name Accession Description Interval E-value
Geminin pfam07412
Geminin; This family contains the eukaryotic protein geminin (approximately 200 residues long). ...
 1-181 3.43e-96

Geminin; This family contains the eukaryotic protein geminin (approximately 200 residues long). Geminin inhibits DNA replication by preventing the incorporation of MCM complex into prereplication complex, and is degraded during the mitotic phase of the cell cycle. It has been proposed that geminin inhibits DNA replication during S, G2, and M phases and that geminin destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle.


Pssm-ID: 462159  Cd Length: 194  Bit Score: 277.78  E-value: 3.43e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820093    1 MNLSMKQK-QEGAQENVKS-------SPVPRRTLKMIQPSAAGSLVGRENELPKGLSKRKLWDDQLTSKISSCG----PE 68
Cdd:pfam07412   1 MNSSMKQKlQEESNENIKSfftpqkaSPVPRRTLKMIQPSAAGSLVGRSNELGKGSPKRKLWNDQLGSKRSKVEvkvtPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820093   69 ANEN-NSVGDLTQEACDLMTKENPSSQYWKEVAEQRRKALYEALTENEKLHKEIEQKDSEIARLRKENKDLAEVAEHVQY 147
Cdd:pfam07412  81 HSENkNLPGGVSQEAYDLMVKENPSSQYWKEVAEERRKALYEVLQENEKLHKEIEQKDEEIARLKEENEELAELAQHVQY 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 157820093  148 MAEVIERLSNEPLDNFESPDSQEFDSEKETVEYS 181
Cdd:pfam07412 161 MADMIERLTGQSPDNLEELDSLAFDSEEEAGEES 194
geminin_CC cd22589
central coiled-coil domain of geminin; Geminin, together with geminin coiled-coil ...
 93-157 3.39e-30

central coiled-coil domain of geminin; Geminin, together with geminin coiled-coil domain-containing protein 1 (GemC1) and McIdas (also called Idas or multicilin), controls both the cell cycle and differentiation decisions in cells. Geminin is an inhibitor of Cdt1, a key component and crucial regulator of pre-replicative complexes (pre-RC) that function in the duplication of chromosomal DNA. Pre-RC assembly culminates in the recruitment of the hexameric mini-chromosome maintenance complex (MCM) onto chromatin. Geminin tightly binds and sequesters Cdt1 in a complex that is unable to recruit MCM to origins, inhibiting DNA replication. It belongs to the geminin family of proteins that also includes GemC1 and McIdas. They share a homologous central coiled-coil domain that mediates homo- and heterodimerization with other family members; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of geminin.


Pssm-ID: 439143 [Multi-domain]  Cd Length: 65  Bit Score: 105.76  E-value: 3.39e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157820093  93 SQYWKEVAEQRRKALYEALTENEKLHKEIEQKDSEIARLRKENKDLAEVAEHVQYMAEVIERLSN 157
Cdd:cd22589    1 EQYWKELAEERRKALYEALQENEKLHKEIEQLDEEIARLKEENDELEELAEHVQYLAEVIERLTG 65
geminin-like_CC cd21103
coiled-coil domain found in the geminin family; The geminin family includes geminin, geminin ...
 100-155 1.57e-14

coiled-coil domain found in the geminin family; The geminin family includes geminin, geminin coiled-coil domain-containing protein 1 (GemC1), and McIdas. Together, geminin, GemC1, and McIdas (also called Idas or multicilin), controls both the cell cycle and differentiation decisions in cells. They were initially identified as cell cycle regulators associated with the chromosome cycle. Geminin is required to ensure once-per-cell-cycle genome replication, while McIdas and GemC1 bind to geminin and are implicated in DNA replication control. Geminin binds to Cdt1, a key component and crucial regulator of pre-replicative complexes (pre-RC), in a timely manner to inhibit DNA replication. Geminin family members also function as early regulators of multiciliogenesis. GemC1 and McIdas specify the multiciliate cell fate by forming complexes with the E2F4/5 transcription factors, resulting in centriole amplification and cilia formation. Geminin family proteins contain a homologous central coiled-coil domain that mediates homo- and heterodimerization; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of the geminin family.


Pssm-ID: 439141  Cd Length: 58  Bit Score: 65.36  E-value: 1.57e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157820093 100 AEQRRKALYEALTENEKLHKEIEQKDSEIARLRKENKDLAEVAEHVQYMAEVIERL 155
Cdd:cd21103    1 ASWEEAALSSALYENKQLHDTLVQKEEEIARLKEENNHLREYANSALVKAEEEKAL 56
McIdas_CC cd22590
central coiled-coil domain of McIdas (or multicilin); McIdas (also called Idas or multicilin), ...
 96-155 4.61e-09

central coiled-coil domain of McIdas (or multicilin); McIdas (also called Idas or multicilin), together with geminin coiled-coil domain-containing protein 1 (GemC1) and geminin, controls both the cell cycle and differentiation decisions in cells. Idas binds to geminin and is implicated in DNA replication control. It also functions as an early regulator of multiciliogenesis. GemC1 and McIdas specify the multiciliate cell fate by forming complexes with the E2F4/5 transcription factors, resulting in centriole amplification and cilia formation. Idas belongs to the geminin family of proteins that also includes geminin and GemC1. They share a homologous central coiled-coil domain that mediates homo- and heterodimerization with other family members; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of McIdas.


Pssm-ID: 439144  Cd Length: 64  Bit Score: 50.95  E-value: 4.61e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820093  96 WKEVAEQRRKALYEALTENEKLHKEIEQKDSEIARLRKENKDLAEVAEHVQYMAEVIERL 155
Cdd:cd22590    1 WRDVADQHQRALGDALEVNNQLHETLTRKQEEIDSLQERNVQLKELASQAKHLASVLDKL 60
 
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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