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Conserved domains on  [gi|568979998|ref|XP_006516103|]
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brain-enriched guanylate kinase-associated protein isoform X1 [Mus musculus]

Protein Classification

COG4372 family protein( domain architecture ID 11468211)

COG4372 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
30-179 1.46e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  30 LCLGQPRVLPGRLARSLPSLWDSALQEQKgELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQS 109
Cdd:COG4372   13 LSLFGLRPKTGILIAALSEQLRKALFELD-KLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNE 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998 110 NymaLQRINQELEDKLYRMGQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 179
Cdd:COG4372   88 Q---LQAAQAELAQAQEELES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
30-179 1.46e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  30 LCLGQPRVLPGRLARSLPSLWDSALQEQKgELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQS 109
Cdd:COG4372   13 LSLFGLRPKTGILIAALSEQLRKALFELD-KLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNE 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998 110 NymaLQRINQELEDKLYRMGQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 179
Cdd:COG4372   88 Q---LQAAQAELAQAQEELES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-169 9.78e-05

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: 45.82  E-value: 9.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998    52 SALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrmgQH 131
Cdd:TIGR02168  806 DELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EA 877

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568979998   132 YEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 169
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 69-186 4.69e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 42.29  E-value: 4.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  69 THKLEKL-ETEFDSTRhylEIELRRAqeeLDKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIval 146
Cdd:cd07651   39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568979998 147 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 186
Cdd:cd07651  110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 71-170 1.05e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.13  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998   71 KLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYEEEKRAMSHEIvaln 147
Cdd:pfam20492  14 RLKQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEAEEKEQLEAEL---- 85

                          90       100
                  ....*....|....*....|...
gi 568979998  148 shlLEAKVTIDKLSEDNElyRKD 170
Cdd:pfam20492  86 ---AEAQEEIARLEEEVE--RKE 103
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 51-136 2.19e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  51 DSALQEQKgELRKRLSyttHKLEKLETEFDSTRHYLEIE----LRRAQEELDKVTEKLRRIQSNYMALQRiNQELEDKLY 126
Cdd:PRK00409 540 EALLKEAE-KLKEELE---EKKEKLQEEEDKLLEEAEKEaqqaIKEAKKEADEIIKELRQLQKGGYASVK-AHELIEARK 614

                         90
                 ....*....|
gi 568979998 127 RMGQHYEEEK 136
Cdd:PRK00409 615 RLNKANEKKE 624
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
30-179 1.46e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  30 LCLGQPRVLPGRLARSLPSLWDSALQEQKgELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQS 109
Cdd:COG4372   13 LSLFGLRPKTGILIAALSEQLRKALFELD-KLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNE 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998 110 NymaLQRINQELEDKLYRMGQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 179
Cdd:COG4372   88 Q---LQAAQAELAQAQEELES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-169 9.78e-05

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: 45.82  E-value: 9.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998    52 SALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrmgQH 131
Cdd:TIGR02168  806 DELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EA 877

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568979998   132 YEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 169
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 54-202 1.69e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 44.56  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  54 LQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI-ELRRAQEELDKVTEKLRRIQSNYMALQR-INQELEDKLYRMGQH 131
Cdd:COG5185  280 LNENANNLIKQFENTKEKIAEYTKSIDIKKATESLeEQLAAAEAEQELEESKRETETGIQNLTAeIEQGQESLTENLEAI 359

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979998 132 YEEEKRAMSHEIVALNSHLLE-AKVTIDKLSEDNELYRKDCNLAAQLL--QCSQTYGRV-HKVSELPSDFQQRVS 202
Cdd:COG5185  360 KEEIENIVGEVELSKSSEELDsFKDTIESTKESLDEIPQNQRGYAQEIlaTLEDTLKAAdRQIEELQRQIEQATS 434
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 69-186 4.69e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 42.29  E-value: 4.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  69 THKLEKL-ETEFDSTRhylEIELRRAqeeLDKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIval 146
Cdd:cd07651   39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568979998 147 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 186
Cdd:cd07651  110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
52-201 4.79e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  52 SALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSnymALQRINQELEDklyrmgqh 131
Cdd:COG4372   62 EQLEEELEQARSELEQLEEELEELNEQLQAAQA----ELAQAQEELESLQEEAEELQE---ELEELQKERQD-------- 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568979998 132 YEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNElyrkdcNLAAQLLQCSQTYGRV------HKVSELPSDFQQRV 201
Cdd:COG4372  127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLE------SLQEELAALEQELQALseaeaeQALDELLKEANRNA 196
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 53-189 6.26e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 6.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998    53 ALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrmGQHY 132
Cdd:TIGR02169  354 KLTEEYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL---ADLN 426

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568979998   133 EEEKRAMShEIVALNSHLLEAKVTIDKLSEDNELYRKDC-NLAAQLLQCSQTYGRVHK 189
Cdd:TIGR02169  427 AAIAGIEA-KINELEEEKEDKALEIKKQEWKLEQLAADLsKYEQELYDLKEEYDRVEK 483
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 71-170 1.05e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.13  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998   71 KLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYEEEKRAMSHEIvaln 147
Cdd:pfam20492  14 RLKQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEAEEKEQLEAEL---- 85

                          90       100
                  ....*....|....*....|...
gi 568979998  148 shlLEAKVTIDKLSEDNElyRKD 170
Cdd:pfam20492  86 ---AEAQEEIARLEEEVE--RKE 103
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 52-146 1.12e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  52 SALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRMGQH 131
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90
                 ....*....|....*
gi 568979998 132 YEEEKRAMSHEIVAL 146
Cdd:COG4942   99 LEAQKEELAELLRAL 113
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
53-178 1.63e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998   53 ALQEQKGELRKRLSYTTHKLEKLETEFDSTR------------HYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQE 120
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQerrealqrlaeySWDEIDVASAEREIAELEAELERLDASSDDLAALEEQ 693

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568979998  121 LEdKLYRMGQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 178
Cdd:COG4913   694 LE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
52-170 2.15e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  52 SALQEQKGELRKRLSYTTHKLEKLETEFDstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRMGQH 131
Cdd:COG4717   98 EELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL 175

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568979998 132 YEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKD 170
Cdd:COG4717  176 QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 51-136 2.19e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  51 DSALQEQKgELRKRLSyttHKLEKLETEFDSTRHYLEIE----LRRAQEELDKVTEKLRRIQSNYMALQRiNQELEDKLY 126
Cdd:PRK00409 540 EALLKEAE-KLKEELE---EKKEKLQEEEDKLLEEAEKEaqqaIKEAKKEADEIIKELRQLQKGGYASVK-AHELIEARK 614

                         90
                 ....*....|
gi 568979998 127 RMGQHYEEEK 136
Cdd:PRK00409 615 RLNKANEKKE 624
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
54-165 3.10e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  54 LQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELDKVTEKLRRIQSnymALQR 116
Cdd:PRK03918 568 LEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK---RLEE 644

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998 117 INQELED--KLYRMGQHYEEEKRAMS---------HEIVALNSHLLEAKVTIDKLSEDNE 165
Cdd:PRK03918 645 LRKELEEleKKYSEEEYEELREEYLElsrelaglrAELEELEKRREEIKKTLEKLKEELE 704
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 52-164 5.07e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 38.37  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998   52 SALQEQKGELRKRLSYTTHKLEKLETEfDSTRhylEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDklyrmgqh 131
Cdd:pfam08614  67 AELYRSRGELAQRLVDLNEELQELEKK-LRED---ERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD-------- 134

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568979998  132 yeeekramshEIVALNSHLLEAKVTIDKLSEDN 164
Cdd:pfam08614 135 ----------ELVALQLQLNMAEEKLRKLEKEN 157
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 48-192 5.51e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 38.60  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998   48 SLWDSALQE-----------------QKGELRKRLSYTTHKLEKLETEFDSTRHyleIELRRAQEEldkvteklRRIQSN 110
Cdd:pfam14988  22 KLWNQYVQEceeierrrqelasrytqQTAELQTQLLQKEKEQASLKKELQALRP---FAKLKESQE--------REIQDL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  111 YMALQRINQELEDKLYRMGQHYEEEKRAMSHEIVALNSHLL-----------------EAKVTIDKLSEDneLYRKDCNL 173
Cdd:pfam14988  91 EEEKEKVRAETAEKDREAHLQFLKEKALLEKQLQELRILELgeratrelkrkaqalklAAKQALSEFCRS--IKRENRQL 168

                         170
                  ....*....|....*....
gi 568979998  174 AAQLLQCSQTYGRVHKVSE 192
Cdd:pfam14988 169 QKELLQLIQETQALEAIKS 187
mukB PRK04863
chromosome partition protein MukB;
51-142 7.51e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998   51 DSALQEQkgeLRKRLsytthklEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRMGQ 130
Cdd:PRK04863  983 NSDLNEK---LRQRL-------EQAEQERTRARE----QLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGV 1048

                          90
                  ....*....|....
gi 568979998  131 HY--EEEKRAMSHE 142
Cdd:PRK04863 1049 PAdsGAEERARARR 1062
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
56-169 7.66e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979998  56 EQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRMgQHYEEE 135
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKEL-KKLEEE 627

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568979998 136 KRAMSHEIVALNSHLLEAKVTIDKLSE--DNELYRK 169
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKkySEEEYEE 663
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 54-126 9.06e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.17  E-value: 9.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568979998   54 LQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYM-ALQRINQELEDKLY 126
Cdd:pfam03938  24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQqELQKKQQELLQPIQ 97
 
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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