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Conserved domains on  [gi|1388876039|ref|NP_001350172|]
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calmodulin-regulated spectrin-associated protein 3 isoform 10 [Mus musculus]

Protein Classification

CAMSAP_CH and CAMSAP_CKK domain-containing protein( domain architecture ID 10571890)

protein containing domains CAMSAP_CH, DUF4670, Smc, and CAMSAP_CKK

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 723-851 1.30e-76

Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.


:

Pssm-ID: 198119  Cd Length: 129  Bit Score: 244.57  E-value: 1.30e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039  723 GPRLYKEPSAKSNKFIIHNALSHCCLAGKVNEPQKNRILEEIEKSKANHFLILFRDSSCQFRALYTLSGETEELSRLAGY 802
Cdd:smart01051   1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1388876039  803 GPRTVTPAMVEGIYKYNSDRKRFTQIPAKTMSMSVDAFTIQGHLWQSKK 851
Cdd:smart01051  81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 241-323 4.27e-33

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


:

Pssm-ID: 432229  Cd Length: 85  Bit Score: 122.41  E-value: 4.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 241 RAIARRAPCFPNVTTL-QDLASGAALAATIHCYCPQLLRLEEVCLKDPMSVADSLYNLQLVQDFCASHLP-RGCPLSLED 318
Cdd:pfam11971   1 PLSQRSLPLSPPVEDLlRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLGnRCCHLTLED 80


                  ....*
gi 1388876039 319 LLYVP 323
Cdd:pfam11971  81 LLYAR 85
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 346-551 2.05e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 346 PDFVQAKDLPDGHAVSPRntetvPSQNNSGSSSPVFNfRHPLLsPGGPQSPLRGSTGSLKSSPSMSHmealgkawnrqlS 425
Cdd:pfam03154 432 PVLTQSQSLPPPAASHPP-----TSGLHQVPSQSPFP-QHPFV-PGGPPPITPPSGPPTSTSSAMPG------------I 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 426 QVPVQTRSSIllsEGTPPEEPTTKPALIEIPLASLGEPAADEegdgSPPGAEDSLEEEASSEGEPR--SGLGFFYKDEDK 503
Cdd:pfam03154 493 QPPSSASVSS---SGPVPAAVSCPLPPVQIKEEALDEAEEPE----SPPPPPRSPSPEPTVVNTPShaSQSARFYKHLDR 565

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388876039 504 ---------------PEDEMAQKRASLLERQQRRVEEARRRKQWQEAEKEQKREEAARLAQEA 551
Cdd:pfam03154 566 gynscartdlyfmplAGSKLAKKREEALEKAKREAEQKAREEKEREKEKEKEREREREREREA 628
PRK02224 super family cl32023
DNA double-strand break repair Rad50 ATPase;
505-603 3.19e-03

DNA double-strand break repair Rad50 ATPase;


The actual alignment was detected with superfamily member PRK02224:

Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 505 EDEMAQKRASLlERQQRRVEEARRRKQWQEAEKEQKREEAARLAQEAPGLAFT--------TPVVASAAPVATLAPTTRA 576
Cdd:PRK02224  522 EELIAERRETI-EEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEvaelnsklAELKERIESLERIRTLLAA 600

                          90       100       110
                  ....*....|....*....|....*....|
gi 1388876039 577 MAPAEEEVG---PRRGDFTRLEYERRAQLK 603
Cdd:PRK02224  601 IADAEDEIErlrEKREALAELNDERRERLA 630
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 723-851 1.30e-76

Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.


Pssm-ID: 198119  Cd Length: 129  Bit Score: 244.57  E-value: 1.30e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039  723 GPRLYKEPSAKSNKFIIHNALSHCCLAGKVNEPQKNRILEEIEKSKANHFLILFRDSSCQFRALYTLSGETEELSRLAGY 802
Cdd:smart01051   1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1388876039  803 GPRTVTPAMVEGIYKYNSDRKRFTQIPAKTMSMSVDAFTIQGHLWQSKK 851
Cdd:smart01051  81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 724-842 1.49e-76

Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.


Pssm-ID: 462558  Cd Length: 119  Bit Score: 244.11  E-value: 1.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 724 PRLYKEPSAKSNKFIIHNALSHCCLAGKVNEPQKNRILEEIEKSKANHFLILFRDSSCQFRALYTLSGETEELSRLAGYG 803
Cdd:pfam08683   1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1388876039 804 PRTVTPAMVEGIYKYNSDRKRFTQIPAKTMSMSVDAFTI 842
Cdd:pfam08683  81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 241-323 4.27e-33

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


Pssm-ID: 432229  Cd Length: 85  Bit Score: 122.41  E-value: 4.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 241 RAIARRAPCFPNVTTL-QDLASGAALAATIHCYCPQLLRLEEVCLKDPMSVADSLYNLQLVQDFCASHLP-RGCPLSLED 318
Cdd:pfam11971   1 PLSQRSLPLSPPVEDLlRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLGnRCCHLTLED 80


                  ....*
gi 1388876039 319 LLYVP 323
Cdd:pfam11971  81 LLYAR 85
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 346-551 2.05e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 346 PDFVQAKDLPDGHAVSPRntetvPSQNNSGSSSPVFNfRHPLLsPGGPQSPLRGSTGSLKSSPSMSHmealgkawnrqlS 425
Cdd:pfam03154 432 PVLTQSQSLPPPAASHPP-----TSGLHQVPSQSPFP-QHPFV-PGGPPPITPPSGPPTSTSSAMPG------------I 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 426 QVPVQTRSSIllsEGTPPEEPTTKPALIEIPLASLGEPAADEegdgSPPGAEDSLEEEASSEGEPR--SGLGFFYKDEDK 503
Cdd:pfam03154 493 QPPSSASVSS---SGPVPAAVSCPLPPVQIKEEALDEAEEPE----SPPPPPRSPSPEPTVVNTPShaSQSARFYKHLDR 565

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388876039 504 ---------------PEDEMAQKRASLLERQQRRVEEARRRKQWQEAEKEQKREEAARLAQEA 551
Cdd:pfam03154 566 gynscartdlyfmplAGSKLAKKREEALEKAKREAEQKAREEKEREKEKEKEREREREREREA 628
PIN_FEN1 cd09867
FEN-like PIN domains of Flap endonuclease-1, a structure-specific, divalent-metal-ion ...
 511-549 2.48e-03

FEN-like PIN domains of Flap endonuclease-1, a structure-specific, divalent-metal-ion dependent, 5' nuclease and homologs; Flap endonuclease-1 (FEN1) is involved in multiple DNA metabolic pathways, including DNA replication processes (5' flap DNA endonuclease activity and double stranded DNA 5'-exonuclease activity) and DNA repair processes (long-patch base excision repair) in eukaryotes and archaea. Interaction between FEN1 and PCNA (Proliferating cell nuclear antigen) is an essential prerequisite to FEN1's DNA replication functionality and stimulates FEN1 nuclease activity by 10-50 fold. FEN1 belongs to the FEN1-EXO1-like subfamily of structure-specific, 5' nucleases (FEN-like family). Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. FEN1 has a C-terminal extension containing residues forming the consensus PIP-box - Qxx(M/L/I)xxF(Y/F) which serves to anchor FEN1 to PCNA.


Pssm-ID: 350215 [Multi-domain]  Cd Length: 251  Bit Score: 40.46  E-value: 2.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1388876039 511 KRASLLERQQRRvEEARrrKQWQEAEKEQKREEAARLAQ 549
Cdd:cd09867    85 KSGELEKRRERR-EEAE--EKLEEALEEGDLEEARKYAK 120
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
505-603 3.19e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 505 EDEMAQKRASLlERQQRRVEEARRRKQWQEAEKEQKREEAARLAQEAPGLAFT--------TPVVASAAPVATLAPTTRA 576
Cdd:PRK02224  522 EELIAERRETI-EEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEvaelnsklAELKERIESLERIRTLLAA 600

                          90       100       110
                  ....*....|....*....|....*....|
gi 1388876039 577 MAPAEEEVG---PRRGDFTRLEYERRAQLK 603
Cdd:PRK02224  601 IADAEDEIErlrEKREALAELNDERRERLA 630
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 499-582 3.60e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 499 KDEDKPEDEMAQKRAsllERQQRRVEEARRRKQWQEAEKEQkrEEAARLAQEAPGLAftTPVVASAAPVATLAPTTRAMA 578
Cdd:PRK09510   83 KKEQQQAEELQQKQA---AEQERLKQLEKERLAAQEQKKQA--EEAAKQAALKQKQA--EEAAAKAAAAAKAKAEAEAKR 155


                  ....
gi 1388876039 579 PAEE 582
Cdd:PRK09510  156 AAAA 159
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
499-551 7.66e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 39.64  E-value: 7.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1388876039 499 KDEDKPEDEMAQKRASLLERQQRRVEEARRRKQWQEAEKEQKREEAARLAQEA 551
Cdd:COG3064     4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEE 56
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 723-851 1.30e-76

Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.


Pssm-ID: 198119  Cd Length: 129  Bit Score: 244.57  E-value: 1.30e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039  723 GPRLYKEPSAKSNKFIIHNALSHCCLAGKVNEPQKNRILEEIEKSKANHFLILFRDSSCQFRALYTLSGETEELSRLAGY 802
Cdd:smart01051   1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1388876039  803 GPRTVTPAMVEGIYKYNSDRKRFTQIPAKTMSMSVDAFTIQGHLWQSKK 851
Cdd:smart01051  81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 724-842 1.49e-76

Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.


Pssm-ID: 462558  Cd Length: 119  Bit Score: 244.11  E-value: 1.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 724 PRLYKEPSAKSNKFIIHNALSHCCLAGKVNEPQKNRILEEIEKSKANHFLILFRDSSCQFRALYTLSGETEELSRLAGYG 803
Cdd:pfam08683   1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1388876039 804 PRTVTPAMVEGIYKYNSDRKRFTQIPAKTMSMSVDAFTI 842
Cdd:pfam08683  81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 241-323 4.27e-33

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


Pssm-ID: 432229  Cd Length: 85  Bit Score: 122.41  E-value: 4.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 241 RAIARRAPCFPNVTTL-QDLASGAALAATIHCYCPQLLRLEEVCLKDPMSVADSLYNLQLVQDFCASHLP-RGCPLSLED 318
Cdd:pfam11971   1 PLSQRSLPLSPPVEDLlRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLGnRCCHLTLED 80


                  ....*
gi 1388876039 319 LLYVP 323
Cdd:pfam11971  81 LLYAR 85
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 346-551 2.05e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 346 PDFVQAKDLPDGHAVSPRntetvPSQNNSGSSSPVFNfRHPLLsPGGPQSPLRGSTGSLKSSPSMSHmealgkawnrqlS 425
Cdd:pfam03154 432 PVLTQSQSLPPPAASHPP-----TSGLHQVPSQSPFP-QHPFV-PGGPPPITPPSGPPTSTSSAMPG------------I 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 426 QVPVQTRSSIllsEGTPPEEPTTKPALIEIPLASLGEPAADEegdgSPPGAEDSLEEEASSEGEPR--SGLGFFYKDEDK 503
Cdd:pfam03154 493 QPPSSASVSS---SGPVPAAVSCPLPPVQIKEEALDEAEEPE----SPPPPPRSPSPEPTVVNTPShaSQSARFYKHLDR 565

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388876039 504 ---------------PEDEMAQKRASLLERQQRRVEEARRRKQWQEAEKEQKREEAARLAQEA 551
Cdd:pfam03154 566 gynscartdlyfmplAGSKLAKKREEALEKAKREAEQKAREEKEREKEKEKEREREREREREA 628
PIN_FEN1 cd09867
FEN-like PIN domains of Flap endonuclease-1, a structure-specific, divalent-metal-ion ...
 511-549 2.48e-03

FEN-like PIN domains of Flap endonuclease-1, a structure-specific, divalent-metal-ion dependent, 5' nuclease and homologs; Flap endonuclease-1 (FEN1) is involved in multiple DNA metabolic pathways, including DNA replication processes (5' flap DNA endonuclease activity and double stranded DNA 5'-exonuclease activity) and DNA repair processes (long-patch base excision repair) in eukaryotes and archaea. Interaction between FEN1 and PCNA (Proliferating cell nuclear antigen) is an essential prerequisite to FEN1's DNA replication functionality and stimulates FEN1 nuclease activity by 10-50 fold. FEN1 belongs to the FEN1-EXO1-like subfamily of structure-specific, 5' nucleases (FEN-like family). Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. FEN1 has a C-terminal extension containing residues forming the consensus PIP-box - Qxx(M/L/I)xxF(Y/F) which serves to anchor FEN1 to PCNA.


Pssm-ID: 350215 [Multi-domain]  Cd Length: 251  Bit Score: 40.46  E-value: 2.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1388876039 511 KRASLLERQQRRvEEARrrKQWQEAEKEQKREEAARLAQ 549
Cdd:cd09867    85 KSGELEKRRERR-EEAE--EKLEEALEEGDLEEARKYAK 120
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
505-603 3.19e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 505 EDEMAQKRASLlERQQRRVEEARRRKQWQEAEKEQKREEAARLAQEAPGLAFT--------TPVVASAAPVATLAPTTRA 576
Cdd:PRK02224  522 EELIAERRETI-EEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEvaelnsklAELKERIESLERIRTLLAA 600

                          90       100       110
                  ....*....|....*....|....*....|
gi 1388876039 577 MAPAEEEVG---PRRGDFTRLEYERRAQLK 603
Cdd:PRK02224  601 IADAEDEIErlrEKREALAELNDERRERLA 630
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 499-582 3.60e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039 499 KDEDKPEDEMAQKRAsllERQQRRVEEARRRKQWQEAEKEQkrEEAARLAQEAPGLAftTPVVASAAPVATLAPTTRAMA 578
Cdd:PRK09510   83 KKEQQQAEELQQKQA---AEQERLKQLEKERLAAQEQKKQA--EEAAKQAALKQKQA--EEAAAKAAAAAKAKAEAEAKR 155


                  ....
gi 1388876039 579 PAEE 582
Cdd:PRK09510  156 AAAA 159
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 482-550 3.69e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 3.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388876039 482 EEASSEGEPRSGLGFFYKDEDKPEDEMAQKrasllER--QQRRVEEARRRKQWQEAEKEQKREEAARLAQE 550
Cdd:pfam15709 445 ERAEAEKQRQKELEMQLAEEQKRLMEMAEE-----ERleYQRQKQEAEEKARLEAEERRQKEEEAARLALE 510
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 507-546 6.06e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.93  E-value: 6.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1388876039 507 EMAQKRASLLER-QQRRVEEARRRKQWQEAEKEQKREEAAR 546
Cdd:pfam15709 369 ERAEKMREELELeQQRRFEEIRLRKQRLEEERQRQEEEERK 409
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 377-580 6.57e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 6.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039  377 SSPVFNFRHPLLSPGGPQSPLRGSTGslKSSPSMSHMEALGKAWNRQLSQVPVQTRSSILLSEGTPPEEPTTKPALIEIP 456
Cdd:PRK10263   387 AQPAVQYNEPLQQPVQPQQPYYAPAA--EQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQT 464

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388876039  457 LASLGEPAADEEGDGSPPgaedSLEEEASSEGEPRSglgffykDEDKPedemaqKRASLL---ERQQRRVEEARRRKQWQ 533
Cdd:PRK10263   465 EQTYQQPAAQEPLYQQPQ----PVEQQPVVEPEPVV-------EETKP------ARPPLYyfeEVEEKRAREREQLAAWY 527

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1388876039  534 EAEKEQKREEAARLAQEAPGLAFTTPVVASAAPVATLAPTTRAMAPA 580
Cdd:PRK10263   528 QPIPEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVSPLASGVKKATLA 574
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
499-551 7.66e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 39.64  E-value: 7.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1388876039 499 KDEDKPEDEMAQKRASLLERQQRRVEEARRRKQWQEAEKEQKREEAARLAQEA 551
Cdd:COG3064     4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEE 56
 
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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