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Conserved domains on  [gi|944248194|gb|KQL12459|]
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hypothetical protein AAES_35507 [Amazona aestiva]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYCLIN_CABLES2 cd20603
cyclin box found in CDK5 and ABL1 enzyme substrate 2 (CABLES2); CABLES2, also called ...
 851-971 1.21e-80

cyclin box found in CDK5 and ABL1 enzyme substrate 2 (CABLES2); CABLES2, also called interactor with CDK3 2 (Ik3-2), acts as a proapoptotic factor involved in both p53-mediated and p53-independent apoptotic pathways. CABLES2 contains one cyclin box. The cyclin box is a protein binding domain.


:

Pssm-ID: 410306  Cd Length: 121  Bit Score: 256.73  E-value: 1.21e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194 851 LTLSKIRSLKREMRNLSEECNLEPVTVSMAYVYFEKLVLQGKLNKQNRKLCAGACVLLAAKISSDLRKHEVKHLIDKLEE 930
Cdd:cd20603    1 LTLSKIRSLKREMRNVAEECNLEPVTVAMAYVYFEKLVLQGKLNKQNRKLCAGACVLLAAKISSDLKKHEVKHLIDKLEE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 944248194 931 RFRFNRRDLIGFEFTVLVALELALYLPENQVLPHYRRLTQQ 971
Cdd:cd20603   81 RFRLNRRELISFEFTVLVALELALYLPENQVLPHYRRLTQQ 121
CtIP_N pfam10482
Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that ...
 48-150 7.67e-58

Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that complexes with both BRCA1 and the BRCA1-associated RING domain protein (BARD1). At the protein level, CtIP expression varies with cell cycle progression in a pattern identical to that of BRCA1. Thus, the steady-state levels of CtIP polypeptides, which remain low in resting cells and G1 cycling cells, increase dramatically as Dividing cells traverse the G1/S boundary. CtIP can potentially modulate the functions ascribed to BRCA1 in transcriptional regulation, DNA repair, and/or cell cycle checkpoint control. This N-terminal domain carries a coiled-coil region and is essential for homodimerization of the protein. The C-terminal domain is family pfam08573.


:

Pssm-ID: 463107 [Multi-domain]  Cd Length: 120  Bit Score: 194.12  E-value: 7.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194   48 GLQSKMTELMTEKCRDAQRIEELFAKNHQLREQ*KVLKENVKVLENRLRAGLCDRCMVTQELAKKKQNEYETSHFQSLQH 127
Cdd:pfam10482  18 GLQAKVSELKKERCLDAQRLEELFSKNQQLREQQKALQENIKVLENRLRAGLCDRCAVTQELAKKKQQEFENSQLQSLQH 97

                          90       100
                  ....*....|....*....|...
gi 944248194  128 IFILTNETNRLREENKTLKEELK 150
Cdd:pfam10482  98 ITILTNEMNTLKDENRKLKEELK 120
 
Name Accession Description Interval E-value
CYCLIN_CABLES2 cd20603
cyclin box found in CDK5 and ABL1 enzyme substrate 2 (CABLES2); CABLES2, also called ...
 851-971 1.21e-80

cyclin box found in CDK5 and ABL1 enzyme substrate 2 (CABLES2); CABLES2, also called interactor with CDK3 2 (Ik3-2), acts as a proapoptotic factor involved in both p53-mediated and p53-independent apoptotic pathways. CABLES2 contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410306  Cd Length: 121  Bit Score: 256.73  E-value: 1.21e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194 851 LTLSKIRSLKREMRNLSEECNLEPVTVSMAYVYFEKLVLQGKLNKQNRKLCAGACVLLAAKISSDLRKHEVKHLIDKLEE 930
Cdd:cd20603    1 LTLSKIRSLKREMRNVAEECNLEPVTVAMAYVYFEKLVLQGKLNKQNRKLCAGACVLLAAKISSDLKKHEVKHLIDKLEE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 944248194 931 RFRFNRRDLIGFEFTVLVALELALYLPENQVLPHYRRLTQQ 971
Cdd:cd20603   81 RFRLNRRELISFEFTVLVALELALYLPENQVLPHYRRLTQQ 121
CtIP_N pfam10482
Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that ...
 48-150 7.67e-58

Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that complexes with both BRCA1 and the BRCA1-associated RING domain protein (BARD1). At the protein level, CtIP expression varies with cell cycle progression in a pattern identical to that of BRCA1. Thus, the steady-state levels of CtIP polypeptides, which remain low in resting cells and G1 cycling cells, increase dramatically as Dividing cells traverse the G1/S boundary. CtIP can potentially modulate the functions ascribed to BRCA1 in transcriptional regulation, DNA repair, and/or cell cycle checkpoint control. This N-terminal domain carries a coiled-coil region and is essential for homodimerization of the protein. The C-terminal domain is family pfam08573.


Pssm-ID: 463107 [Multi-domain]  Cd Length: 120  Bit Score: 194.12  E-value: 7.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194   48 GLQSKMTELMTEKCRDAQRIEELFAKNHQLREQ*KVLKENVKVLENRLRAGLCDRCMVTQELAKKKQNEYETSHFQSLQH 127
Cdd:pfam10482  18 GLQAKVSELKKERCLDAQRLEELFSKNQQLREQQKALQENIKVLENRLRAGLCDRCAVTQELAKKKQQEFENSQLQSLQH 97

                          90       100
                  ....*....|....*....|...
gi 944248194  128 IFILTNETNRLREENKTLKEELK 150
Cdd:pfam10482  98 ITILTNEMNTLKDENRKLKEELK 120
CYCLIN smart00385
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ...
 863-947 1.09e-04

domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and TFIIB (twice) and Retinoblastoma (once). A protein recognition domain functioning in cell-cycle and transcription control.


Pssm-ID: 214641 [Multi-domain]  Cd Length: 83  Bit Score: 41.81  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194   863 MRNLSEECNLEPVTVSMAYVYFEKLVLQGKLNKQNRKLCAGACVLLAAKIssdlrkHEVKHLIDKLEERFR-FNRRDLIG 941
Cdd:smart00385   3 LRRVCKALNLDPETLNLAVNLLDRFLSDYKFLKYSPSLIAAAALYLASKT------EETPPWTKELVHYTGyFTEEEILR 76


                   ....*.
gi 944248194   942 FEFTVL 947
Cdd:smart00385  77 MERLLL 82
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 49-161 1.08e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194    49 LQSKMTELMTEKCRDAQRIEELFAKNHQLREQ*KVLKENVKVLENRLRAGLCDRCMVTQELA--KKKQNEYETSHFQSLQ 126
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEelESKLDELAEELAELEE 344

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 944248194   127 HIFILTNETNRLREENKTLKEELKKLRSLEEACRA 161
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEE 379
Cyclin_N pfam00134
Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Swiss:P22674 is a ...
 817-951 2.14e-03

Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Swiss:P22674 is a Uracil-DNA glycosylase that is related to other cyclins. Cyclins contain two domains of similar all-alpha fold, of which this family corresponds with the N-terminal domain.


Pssm-ID: 459686 [Multi-domain]  Cd Length: 127  Bit Score: 39.04  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194  817 IFASYMTTVIEYV-KPSDLKK--DMNETFREkfphIKLTLskirslkreMRNLSEECNLEPVTVSMAYVYFEKLVLQGKL 893
Cdd:pfam00134   2 IFQYLRELELKYLpKPDYMDQqpDINPKMRA----ILIDW---------LVEVHEKFKLLPETLYLAVNYLDRFLSKKSV 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 944248194  894 NKQNRKLCAGACVLLAAKIssdlrkHE-----VKHLIDKLEERFRfnRRDLIGFEFTVLVALE 951
Cdd:pfam00134  69 PKNKLQLVGVTCLFIAAKY------EEiypptVEDLVYITDNAYT--REEILRMERLILETLN 123
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
57-157 9.28e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 9.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194  57 MTEKCRDAQ-RIEELFAKNHQLREQ*KVLKENVKVLENRLRaglcdrcmvtqeLAKKKQNE--YETSHFQSLQH-IFILT 132
Cdd:COG2433  411 EEEEIRRLEeQVERLEAEVEELEAELEEKDERIERLERELS------------EARSEERReiRKDREISRLDReIERLE 478

                         90       100
                 ....*....|....*....|....*
gi 944248194 133 NETNRLREENKTLKEELKKLRSLEE 157
Cdd:COG2433  479 RELEEERERIEELKRKLERLKELWK 503
 
Name Accession Description Interval E-value
CYCLIN_CABLES2 cd20603
cyclin box found in CDK5 and ABL1 enzyme substrate 2 (CABLES2); CABLES2, also called ...
 851-971 1.21e-80

cyclin box found in CDK5 and ABL1 enzyme substrate 2 (CABLES2); CABLES2, also called interactor with CDK3 2 (Ik3-2), acts as a proapoptotic factor involved in both p53-mediated and p53-independent apoptotic pathways. CABLES2 contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410306  Cd Length: 121  Bit Score: 256.73  E-value: 1.21e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194 851 LTLSKIRSLKREMRNLSEECNLEPVTVSMAYVYFEKLVLQGKLNKQNRKLCAGACVLLAAKISSDLRKHEVKHLIDKLEE 930
Cdd:cd20603    1 LTLSKIRSLKREMRNVAEECNLEPVTVAMAYVYFEKLVLQGKLNKQNRKLCAGACVLLAAKISSDLKKHEVKHLIDKLEE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 944248194 931 RFRFNRRDLIGFEFTVLVALELALYLPENQVLPHYRRLTQQ 971
Cdd:cd20603   81 RFRLNRRELISFEFTVLVALELALYLPENQVLPHYRRLTQQ 121
CYCLIN_CABLES1 cd20602
cyclin box found in CDK5 and ABL1 enzyme substrate 1 (CABLES1); CABLES1, also called ...
 842-972 4.38e-70

cyclin box found in CDK5 and ABL1 enzyme substrate 1 (CABLES1); CABLES1, also called interactor with CDK3 1 (Ik3-1), is a cyclin-dependent kinase binding protein that enhances cyclin-dependent kinase tyrosine phosphorylation by non-receptor tyrosine kinases, such as that of CDK5 by activated ABL1, which leads to increased CDK5 activity and is critical for neuronal development, and that of CDK2 by WEE1, which leads to decreased CDK2 activity and growth inhibition. CABLES1 contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410305  Cd Length: 132  Bit Score: 228.77  E-value: 4.38e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194 842 FREKFPHIKLTLSKIRSLKREMRNLS-EECNLEPVTVSMAYVYFEKLVLQGKLNKQNRKLCAGACVLLAAKISSDLRKHE 920
Cdd:cd20602    1 FKEKFPHIKLTLSKIRSLKREMRKLAqEECGYEEPTVAMAFVYFEKLALKGKLNKQNRKLCAGACVLLAAKIGSDLKKHE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 944248194 921 VKHLIDKLEERFRFNRRDLIGFEFTVLVALELALYLPENQVLPHYRRLTQQS 972
Cdd:cd20602   81 VKHLIDKLEEKFRLNRRELIAFEFPVLVALEFALHLPEHEVMPHYRRLVQNS 132
CYCLIN_CABLES cd20556
cyclin box found in CDK5 and ABL1 enzyme substrate (CABLES) family; The CABLES family includes ...
 851-968 4.31e-59

cyclin box found in CDK5 and ABL1 enzyme substrate (CABLES) family; The CABLES family includes CABLES1 and CABLES2. CABLES1, also called interactor with CDK3 1 (Ik3-1), is a cyclin-dependent kinase binding protein that enhances cyclin-dependent kinase tyrosine phosphorylation by non-receptor tyrosine kinases, such as that of CDK5 by activated ABL1, which leads to increased CDK5 activity and is critical for neuronal development, and that of CDK2 by WEE1, which leads to decreased CDK2 activity and growth inhibition. CABLES2, also called interactor with CDK3 2 (Ik3-2), acts as a proapoptotic factor involved in both p53-mediated and p53-independent apoptotic pathways. Both, CABLES1 and CABLES2, contain one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410259  Cd Length: 119  Bit Score: 197.79  E-value: 4.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194 851 LTLSKIRSLKREMRNL-SEECNLEPVTVSMAYVYFEKLVLQGKLNKQNRKLCAGACVLLAAKISSDLRKHEVKHLIDKLE 929
Cdd:cd20556    1 LTLSKLRSLKREMLKIaLKLCGLDVSTVALAYVYFEKLVLKGLVNKSNRKLIAGACLLLAAKFNDDVKKEDLKSLLEEIE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 944248194 930 ERFRFNRRDLIGFEFTVLVALELALYLPENQVLPHYRRL 968
Cdd:cd20556   81 DVFRLTRKELIAFEFPVLVALEFSLHVPDEEILPHLQRL 119
CtIP_N pfam10482
Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that ...
 48-150 7.67e-58

Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that complexes with both BRCA1 and the BRCA1-associated RING domain protein (BARD1). At the protein level, CtIP expression varies with cell cycle progression in a pattern identical to that of BRCA1. Thus, the steady-state levels of CtIP polypeptides, which remain low in resting cells and G1 cycling cells, increase dramatically as Dividing cells traverse the G1/S boundary. CtIP can potentially modulate the functions ascribed to BRCA1 in transcriptional regulation, DNA repair, and/or cell cycle checkpoint control. This N-terminal domain carries a coiled-coil region and is essential for homodimerization of the protein. The C-terminal domain is family pfam08573.


Pssm-ID: 463107 [Multi-domain]  Cd Length: 120  Bit Score: 194.12  E-value: 7.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194   48 GLQSKMTELMTEKCRDAQRIEELFAKNHQLREQ*KVLKENVKVLENRLRAGLCDRCMVTQELAKKKQNEYETSHFQSLQH 127
Cdd:pfam10482  18 GLQAKVSELKKERCLDAQRLEELFSKNQQLREQQKALQENIKVLENRLRAGLCDRCAVTQELAKKKQQEFENSQLQSLQH 97

                          90       100
                  ....*....|....*....|...
gi 944248194  128 IFILTNETNRLREENKTLKEELK 150
Cdd:pfam10482  98 ITILTNEMNTLKDENRKLKEELK 120
CYCLIN_SF cd00043
Cyclin box fold superfamily; The cyclin box is a protein binding domain that functions in ...
 858-943 2.00e-08

Cyclin box fold superfamily; The cyclin box is a protein binding domain that functions in cell-cycle and transcriptional control. It is about 100 amino acids in length, composed of five helices, and is present in cyclins, transcription initiation factor IIB (TFIIB), and retinoblastoma tumour suppressor protein (Rb). Cyclins consist of 8 classes of cell cycle regulators that function as regulatory subunits of cyclin-dependent kinases (CDKs), which are serine/threonine kinases. The catalytic activities of CDKs are modulated not only by their interactions with cyclins but also by CDK inhibitors (CKIs). CDKs, cyclins and CKIs play key roles in transcription, epigenetic regulation, metabolism, stem cell self-renewal, neuronal functions, and spermatogenesis. TFIIB is a transcription factor that binds the TATA box. Members in this superfamily contain one or two copies of the cyclin box.


Pssm-ID: 410207 [Multi-domain]  Cd Length: 82  Bit Score: 52.41  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194 858 SLKREMRNLSEECNLEPVTVSMAYVYFEKLVLQGKLNKQNRKLCAGACVLLAAKIssdlrkHEVKHLIDKLEERFRFNRR 937
Cdd:cd00043    1 KAVDFIRRLCSKLGLPEEVLELAIELLDRFLSKGLLLGRSPELIAAACLYLACKL------EELPRTLKEIAKVSGVSEK 74


                 ....*.
gi 944248194 938 DLIGFE 943
Cdd:cd00043   75 ELRKAE 80
CYCLIN smart00385
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ...
 863-947 1.09e-04

domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and TFIIB (twice) and Retinoblastoma (once). A protein recognition domain functioning in cell-cycle and transcription control.


Pssm-ID: 214641 [Multi-domain]  Cd Length: 83  Bit Score: 41.81  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194   863 MRNLSEECNLEPVTVSMAYVYFEKLVLQGKLNKQNRKLCAGACVLLAAKIssdlrkHEVKHLIDKLEERFR-FNRRDLIG 941
Cdd:smart00385   3 LRRVCKALNLDPETLNLAVNLLDRFLSDYKFLKYSPSLIAAAALYLASKT------EETPPWTKELVHYTGyFTEEEILR 76


                   ....*.
gi 944248194   942 FEFTVL 947
Cdd:smart00385  77 MERLLL 82
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 49-161 1.08e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194    49 LQSKMTELMTEKCRDAQRIEELFAKNHQLREQ*KVLKENVKVLENRLRAGLCDRCMVTQELA--KKKQNEYETSHFQSLQ 126
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEelESKLDELAEELAELEE 344

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 944248194   127 HIFILTNETNRLREENKTLKEELKKLRSLEEACRA 161
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEE 379
Cyclin_N pfam00134
Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Swiss:P22674 is a ...
 817-951 2.14e-03

Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Swiss:P22674 is a Uracil-DNA glycosylase that is related to other cyclins. Cyclins contain two domains of similar all-alpha fold, of which this family corresponds with the N-terminal domain.


Pssm-ID: 459686 [Multi-domain]  Cd Length: 127  Bit Score: 39.04  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194  817 IFASYMTTVIEYV-KPSDLKK--DMNETFREkfphIKLTLskirslkreMRNLSEECNLEPVTVSMAYVYFEKLVLQGKL 893
Cdd:pfam00134   2 IFQYLRELELKYLpKPDYMDQqpDINPKMRA----ILIDW---------LVEVHEKFKLLPETLYLAVNYLDRFLSKKSV 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 944248194  894 NKQNRKLCAGACVLLAAKIssdlrkHE-----VKHLIDKLEERFRfnRRDLIGFEFTVLVALE 951
Cdd:pfam00134  69 PKNKLQLVGVTCLFIAAKY------EEiypptVEDLVYITDNAYT--REEILRMERLILETLN 123
CYCLIN_CCNM_CCNQ_rpt1 cd20534
first cyclin box found in cyclin-M (CCNM) family; The CCNM family proteins, also called ...
 863-918 4.71e-03

first cyclin box found in cyclin-M (CCNM) family; The CCNM family proteins, also called ancient conserved domain proteins (ACDPs), are evolutionarily conserved Mg2+ transporters. CCNM, also called cyclin-Q (CCNQ), or CDK10-activating cyclin, or cyclin-related protein FAM58A, associates with CDK10 to promote its kinase activity. Members of this family contain two cyclin boxes. This model corresponds to the first one. The cyclin box is a protein binding domain.


Pssm-ID: 410237 [Multi-domain]  Cd Length: 110  Bit Score: 37.92  E-value: 4.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 944248194 863 MRNLSEECNLEPVTVSMAYVYFEKLVLQGKLNKQNRKLCAGACVLLAAKISSDLRK 918
Cdd:cd20534    9 IREAGLKLELSSVTIATACVLYHRFYRELSLEDYDPYLVAMACLYLAGKAEEQPRR 64
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
57-157 9.28e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 9.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 944248194  57 MTEKCRDAQ-RIEELFAKNHQLREQ*KVLKENVKVLENRLRaglcdrcmvtqeLAKKKQNE--YETSHFQSLQH-IFILT 132
Cdd:COG2433  411 EEEEIRRLEeQVERLEAEVEELEAELEEKDERIERLERELS------------EARSEERReiRKDREISRLDReIERLE 478

                         90       100
                 ....*....|....*....|....*
gi 944248194 133 NETNRLREENKTLKEELKKLRSLEE 157
Cdd:COG2433  479 RELEEERERIEELKRKLERLKELWK 503
 
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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