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Conserved domains on  [gi|13162365|ref|NP_077077|]
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brain-enriched guanylate kinase-associated protein isoform 2 [Rattus norvegicus]

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];
21-151 7.85e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 7.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNymaLQRINQELEDKLYRM 100
Cdd:COG4372  31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13162365 101 GQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 151
Cdd:COG4372 104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-151 7.85e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 7.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNymaLQRINQELEDKLYRM 100
Cdd:COG4372  31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13162365 101 GQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 151
Cdd:COG4372 104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-141 2.13e-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: 47.74  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365     21 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrm 100
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 13162365    101 gQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 141
Cdd:TIGR02168  876 -EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-141 3.85e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365   21 EKLSALQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELDKVTEKLRRIQSny 83
Cdd:PRK03918 563 KKLDELEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK-- 640

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13162365   84 mALQRINQELED--KLYRMGQHYEEEKRAMS---------HEIVALNSHLLEAKVTIDKLSEDNELYRK 141
Cdd:PRK03918 641 -RLEELRKELEEleKKYSEEEYEELREEYLElsrelaglrAELEELEKRREEIKKTLEKLKEELEEREK 708
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 41-158 4.65e-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: 4.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365  41 THKLEKL-ETEFDSTRhylEIELRRAqeeLDKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIval 118
Cdd:cd07651  39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13162365 119 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 158
Cdd:cd07651 110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 21-136 1.27e-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: 39.92  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365    21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDklyrm 100
Cdd:pfam08614  64 EELAELYRSRGELAQRLVDLNEELQELEKKLRE----DERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD----- 134

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 13162365   101 gqhyeeekramshEIVALNSHLLEAKVTIDKLSEDN 136
Cdd:pfam08614 135 -------------ELVALQLQLNMAEEKLRKLEKEN 157
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-151 7.85e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 7.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNymaLQRINQELEDKLYRM 100
Cdd:COG4372  31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13162365 101 GQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 151
Cdd:COG4372 104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-141 2.13e-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: 47.74  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365     21 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrm 100
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 13162365    101 gQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 141
Cdd:TIGR02168  876 -EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 14-118 5.09e-05

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: 45.91  E-value: 5.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365  14 AASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQEL 93
Cdd:COG4942  13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAEL 88

                        90       100
                ....*....|....*....|....*
gi 13162365  94 EDKLYRMGQHYEEEKRAMSHEIVAL 118
Cdd:COG4942  89 EKEIAELRAELEAQKEELAELLRAL 113
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 21-174 5.42e-05

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: 46.10  E-value: 5.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI-ELRRAQEELDKVTEKLRRIQSNYMALQR-INQELEDKLY 98
Cdd:COG5185 275 ESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLeEQLAAAEAEQELEESKRETETGIQNLTAeIEQGQESLTE 354

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365  99 RMGQHYEEEKRAMSHEIVALNSHLLE-AKVTIDKLSEDNELYRKDCNLAAQLL--QCSQTYGRV-HKVSELPSDFQQRVS 174
Cdd:COG5185 355 NLEAIKEEIENIVGEVELSKSSEELDsFKDTIESTKESLDEIPQNQRGYAQEIlaTLEDTLKAAdRQIEELQRQIEQATS 434
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
21-150 1.36e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365   21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR------------HYLEIELRRAQEELDKVTEKLRRIQSNYMALQR 88
Cdd:COG4913  610 AKLAALEAELAELEEELAEAEERLEALEAELDALQerrealqrlaeySWDEIDVASAEREIAELEAELERLDASSDDLAA 689

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13162365   89 INQELEdKLYRMGQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 150
Cdd:COG4913  690 LEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
21-142 2.39e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRM 100
Cdd:COG4717  95 EELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13162365 101 GQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKD 142
Cdd:COG4717 173 AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-173 3.13e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 3.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLE---IELRRAQEELDKVTEKLRRIQSnymALQRINQELEDkl 97
Cdd:COG4372  52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQaaqAELAQAQEELESLQEEAEELQE---ELEELQKERQD-- 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365  98 yrmgqhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNElyrkdcNLAAQLLQCSQTYGRV------HKVSELPSDFQQ 171
Cdd:COG4372 127 ------LEQQRKQLEAQIAELQSEIAEREEELKELEEQLE------SLQEELAALEQELQALseaeaeQALDELLKEANR 194


                ..
gi 13162365 172 RV 173
Cdd:COG4372 195 NA 196
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-141 3.85e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365   21 EKLSALQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELDKVTEKLRRIQSny 83
Cdd:PRK03918 563 KKLDELEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK-- 640

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13162365   84 mALQRINQELED--KLYRMGQHYEEEKRAMS---------HEIVALNSHLLEAKVTIDKLSEDNELYRK 141
Cdd:PRK03918 641 -RLEELRKELEEleKKYSEEEYEELREEYLElsrelaglrAELEELEKRREEIKKTLEKLKEELEEREK 708
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 41-158 4.65e-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: 4.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365  41 THKLEKL-ETEFDSTRhylEIELRRAqeeLDKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIval 118
Cdd:cd07651  39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13162365 119 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 158
Cdd:cd07651 110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 22-161 7.30e-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: 42.75  E-value: 7.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365     22 KLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrmG 101
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL---A 423

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13162365    102 QHYEEEKRAMShEIVALNSHLLEAKVTIDKLSEDNELYRKDC-NLAAQLLQCSQTYGRVHK 161
Cdd:TIGR02169  424 DLNAAIAGIEA-KINELEEEKEDKALEIKKQEWKLEQLAADLsKYEQELYDLKEEYDRVEK 483
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 21-136 1.27e-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: 39.92  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365    21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDklyrm 100
Cdd:pfam08614  64 EELAELYRSRGELAQRLVDLNEELQELEKKLRE----DERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD----- 134

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 13162365   101 gqhyeeekramshEIVALNSHLLEAKVTIDKLSEDN 136
Cdd:pfam08614 135 -------------ELVALQLQLNMAEEKLRKLEKEN 157
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 43-142 2.55e-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: 37.98  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365    43 KLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYEEEKRAMSHEIvaln 119
Cdd:pfam20492  14 RLKQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEAEEKEQLEAEL---- 85

                          90       100
                  ....*....|....*....|...
gi 13162365   120 shlLEAKVTIDKLSEDNElyRKD 142
Cdd:pfam20492  86 ---AEAQEEIARLEEEVE--RKE 103
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 21-157 2.74e-03

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: 40.82  E-value: 2.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365     21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDstrhylEIELRRAQEELDKVTEKLRRI----QSNYMALQRINQELEDK 96
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKLEEALN------DLEARLSHSRIPEIQAELSKLeeevSRIEARLREIEQKLNRL 824

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13162365     97 LYRmgQHYEEEKRAmshEIVALNSHLLEAKVTI-DKLSEDN----ELYRKDCNLAAQLLQCSQTYG 157
Cdd:TIGR02169  825 TLE--KEYLEKEIQ---ELQEQRIDLKEQIKSIeKEIENLNgkkeELEEELEELEAALRDLESRLG 885
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-141 2.92e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365   21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEiELRRAQEELDKVTEKLRRIQ---SNYMALQRINQELEDKL 97
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDEL 309

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 13162365   98 YRMgqhyEEEKRAMSHEIVALNSHLLEAKvtiDKLSEDNELYRK 141
Cdd:PRK03918 310 REI----EKRLSRLEEEINGIEERIKELE---EKEERLEELKKK 346
mukB PRK04863
chromosome partition protein MukB;
16-114 3.05e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365    16 SAADMEKLSALQEQkgeLRKRLsytthklEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELED 95
Cdd:PRK04863  976 AAEMLAKNSDLNEK---LRQRL-------EQAEQERTRARE----QLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQ 1041

                          90       100
                  ....*....|....*....|.
gi 13162365    96 KLYRMGQHY--EEEKRAMSHE 114
Cdd:PRK04863 1042 ELQDLGVPAdsGAEERARARR 1062
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 17-108 3.27e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365   17 AADMEKLsaLQEQKgELRKRLSyttHKLEKLETEFDSTRHYLEIE----LRRAQEELDKVTEKLRRIQSNYMALQRiNQE 92
Cdd:PRK00409 536 AEEAEAL--LKEAE-KLKEELE---EKKEKLQEEEDKLLEEAEKEaqqaIKEAKKEADEIIKELRQLQKGGYASVK-AHE 608

                         90
                 ....*....|....*.
gi 13162365   93 LEDKLYRMGQHYEEEK 108
Cdd:PRK00409 609 LIEARKRLNKANEKKE 624
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 15-137 6.11e-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: 39.65  E-value: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365     15 ASAAdmEKLSALQEQKGELRKRLSYTthKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELE 94
Cdd:TIGR02168  209 AEKA--ERYKELKAELRELELALLVL--RLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 13162365     95 DKLyrmgQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNE 137
Cdd:TIGR02168  281 EEI----EELQKELYALANEISRLEQQKQILRERLANLERQLE 319
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 23-155 7.70e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 37.96  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365    23 LSALQEQKGELRKRLSYTTHKLEKLETE-----------------FDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMA 85
Cdd:pfam15619   6 LSARLHKIKELQNELAELQSKLEELRKEnrllkrlqkrqekalgkYEGTESELPQLIARHNEEVRVLRERLRRLQEKERD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365    86 LQRINQELEDKLYRMG---QHYEE--------EKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRK--DCNLAAQLLQC 152
Cdd:pfam15619  86 LERKLKEKEAELLRLRdqlKRLEKlsedknlaEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKsfRRQLAAEKKKH 165


                  ...
gi 13162365   153 SQT 155
Cdd:pfam15619 166 KEA 168
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
 20-76 8.47e-03

WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.


Pssm-ID: 465345 [Multi-domain]  Cd Length: 155  Bit Score: 37.27  E-value: 8.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 13162365    20 MEKLSALQEQKGELRKRLSytTHKLEKLETEFDSTRHYLEiELRRAQEELDKVTEKL 76
Cdd:pfam17098  91 MAKCRLLQQENEELGRQLS--EGRIAKLEIELALQKKVVE-ELKKSLEELDEFLIEL 144
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 21-164 8.50e-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: 37.83  E-value: 8.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365    21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleIELRRAQEEldkvteklRRIQSNYMALQRINQELEDKLYRM 100
Cdd:pfam14988  40 ELASRYTQQTAELQTQLLQKEKEQASLKKELQALRP---FAKLKESQE--------REIQDLEEEKEKVRAETAEKDREA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365   101 GQHYEEEKRAMSHEIVALNSHLL-----------------EAKVTIDKLSEDneLYRKDCNLAAQLLQCSQTYGRVHKVS 163
Cdd:pfam14988 109 HLQFLKEKALLEKQLQELRILELgeratrelkrkaqalklAAKQALSEFCRS--IKRENRQLQKELLQLIQETQALEAIK 186


                  .
gi 13162365   164 E 164
Cdd:pfam14988 187 S 187
PRK01156 PRK01156
chromosome segregation protein; Provisional
 14-141 8.75e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.11  E-value: 8.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365   14 AASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQEL 93
Cdd:PRK01156 573 ALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKI 652

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 13162365   94 EDKLYRMGQHYEEEKR--AMSHEIVALNSHLLEAKVTIDKLSEDneLYRK 141
Cdd:PRK01156 653 DNYKKQIAEIDSIIPDlkEITSRINDIEDNLKKSRKALDDAKAN--RARL 700
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
20-112 8.88e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 8.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365   20 MEKLSALQEQKGELRKRLSYTTHKLEKLET---EFDSTRHYLE----IELRRAQEELDKVTEKLRRIQSNYMALQRINQE 92
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEErheLYEEAKAKKEelerLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK 409

                         90       100
                 ....*....|....*....|
gi 13162365   93 LEDKLYRMGQHYEEEKRAMS 112
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIE 429
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 26-98 8.91e-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: 8.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13162365    26 LQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYM-ALQRINQELEDKLY 98
Cdd:pfam03938  24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQqELQKKQQELLQPIQ 97
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-141 9.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 9.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162365   28 EQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRMgQHYEEE 107
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKEL-KKLEEE 627

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 13162365  108 KRAMSHEIVALNSHLLEAKVTIDKLSE--DNELYRK 141
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKkySEEEYEE 663
 
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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