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Conserved domains on  [gi|1738644122|ref|NP_001361131|]
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brain-enriched guanylate kinase-associated protein isoform 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-135 1.27e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122    5 QSSQASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRIN 84
Cdd:TIGR02168  793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1738644122   85 QELEDKLyrmgQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 135
Cdd:TIGR02168  869 EELESEL----EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-135 1.27e-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: 48.51  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122    5 QSSQASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRIN 84
Cdd:TIGR02168  793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1738644122   85 QELEDKLyrmgQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 135
Cdd:TIGR02168  869 EELESEL----EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
15-145 1.38e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122  15 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNymaLQRINQELEDKLYRM 94
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1738644122  95 GQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 145
Cdd:COG4372   104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 1-130 2.24e-04

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: 42.23  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122   1 MGSHQSSQASAADMEKLSALQEQ-------KGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRI 73
Cdd:pfam08614  43 SKASPQSASIQSLEQLLAQLREElaelyrsRGELAQRLVDLNEELQELEKKLRE----DERRLAALEAERAQLEEKLKDR 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1738644122  74 QSNYMALQRINQELEDklyrmgqhyeeekramshEIVALNSHLLEAKVTIDKLSEDN 130
Cdd:pfam08614 119 EEELREKRKLNQDLQD------------------ELVALQLQLNMAEEKLRKLEKEN 157
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
15-135 5.59e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122  15 EKLSALQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELDKVTEKLRRIQSny 77
Cdd:PRK03918  563 KKLDELEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK-- 640

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1738644122  78 mALQRINQELED--KLYRMGQHYEEEKRAMS---------HEIVALNSHLLEAKVTIDKLSEDNELYRK 135
Cdd:PRK03918  641 -RLEELRKELEEleKKYSEEEYEELREEYLElsrelaglrAELEELEKRREEIKKTLEKLKEELEEREK 708
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 35-152 6.53e-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: 41.52  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122  35 THKLEKL-ETEFDSTRhylEIELRRAqeeLDKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIval 112
Cdd:cd07651    39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1738644122 113 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 152
Cdd:cd07651   110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-135 1.27e-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: 48.51  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122    5 QSSQASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRIN 84
Cdd:TIGR02168  793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1738644122   85 QELEDKLyrmgQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 135
Cdd:TIGR02168  869 EELESEL----EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
15-145 1.38e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122  15 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNymaLQRINQELEDKLYRM 94
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1738644122  95 GQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 145
Cdd:COG4372   104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
6-167 2.60e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122   6 SSQASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMA----LQ 81
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARS----ELEQLEEELEELNEQLQAAQAELAQaqeeLE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122  82 RINQE---LEDKLYRM---GQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNElyrkdcNLAAQLLQCSQTYGRV-- 153
Cdd:COG4372   105 SLQEEaeeLQEELEELqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE------SLQEELAALEQELQALse 178

                         170
                  ....*....|....*...
gi 1738644122 154 ----HKVSELPSDFQQRV 167
Cdd:COG4372   179 aeaeQALDELLKEANRNA 196
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 15-168 5.45e-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: 5.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122  15 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI-ELRRAQEELDKVTEKLRRIQSNYMALQR-INQELEDKLY 92
Cdd:COG5185   275 ESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLeEQLAAAEAEQELEESKRETETGIQNLTAeIEQGQESLTE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122  93 RMGQHYEEEKRAMSHEIVALNSHLLE-AKVTIDKLSEDNELYRKDCNLAAQLL--QCSQTYGRV-HKVSELPSDFQQRVS 168
Cdd:COG5185   355 NLEAIKEEIENIVGEVELSKSSEELDsFKDTIESTKESLDEIPQNQRGYAQEIlaTLEDTLKAAdRQIEELQRQIEQATS 434
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 9-112 1.01e-04

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: 45.14  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122   9 ASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELE 88
Cdd:COG4942    14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELE 89

                          90       100
                  ....*....|....*....|....
gi 1738644122  89 DKLYRMGQHYEEEKRAMSHEIVAL 112
Cdd:COG4942    90 KEIAELRAELEAQKEELAELLRAL 113
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
15-144 1.42e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122   15 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR------------HYLEIELRRAQEELDKVTEKLRRIQSNYMALQR 82
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQerrealqrlaeySWDEIDVASAEREIAELEAELERLDASSDDLAA 689

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738644122   83 INQELEdKLYRMGQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 144
Cdd:COG4913    690 LEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 1-130 2.24e-04

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: 42.23  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122   1 MGSHQSSQASAADMEKLSALQEQ-------KGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRI 73
Cdd:pfam08614  43 SKASPQSASIQSLEQLLAQLREElaelyrsRGELAQRLVDLNEELQELEKKLRE----DERRLAALEAERAQLEEKLKDR 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1738644122  74 QSNYMALQRINQELEDklyrmgqhyeeekramshEIVALNSHLLEAKVTIDKLSEDN 130
Cdd:pfam08614 119 EEELREKRKLNQDLQD------------------ELVALQLQLNMAEEKLRKLEKEN 157
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
15-136 2.90e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122  15 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRM 94
Cdd:COG4717    95 EELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1738644122  95 GQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKD 136
Cdd:COG4717   173 AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
15-135 5.59e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122  15 EKLSALQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELDKVTEKLRRIQSny 77
Cdd:PRK03918  563 KKLDELEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK-- 640

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1738644122  78 mALQRINQELED--KLYRMGQHYEEEKRAMS---------HEIVALNSHLLEAKVTIDKLSEDNELYRK 135
Cdd:PRK03918  641 -RLEELRKELEEleKKYSEEEYEELREEYLElsrelaglrAELEELEKRREEIKKTLEKLKEELEEREK 708
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 35-152 6.53e-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: 41.52  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122  35 THKLEKL-ETEFDSTRhylEIELRRAqeeLDKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIval 112
Cdd:cd07651    39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1738644122 113 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 152
Cdd:cd07651   110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 8-131 7.40e-04

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: 42.74  E-value: 7.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122    8 QASAAdmEKLSALQEQKGELRKRLSYTthKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQEL 87
Cdd:TIGR02168  208 QAEKA--ERYKELKAELRELELALLVL--RLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1738644122   88 EDKLyrmgQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNE 131
Cdd:TIGR02168  280 EEEI----EELQKELYALANEISRLEQQKQILRERLANLERQLE 319
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-155 9.39e-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: 42.36  E-value: 9.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122   16 KLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrmG 95
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL---A 423

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1738644122   96 QHYEEEKRAMShEIVALNSHLLEAKVTIDKLSEDNELYRKDC-NLAAQLLQCSQTYGRVHK 155
Cdd:TIGR02169  424 DLNAAIAGIEA-KINELEEEKEDKALEIKKQEWKLEQLAADLsKYEQELYDLKEEYDRVEK 483
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 5-102 1.10e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122   5 QSSQASAADME-KLSALQEQKGE---LRKRLSyttHKLEKLETEFDSTRHYLEIE----LRRAQEELDKVTEKLRRIQSN 76
Cdd:PRK00409  523 ASLEELERELEqKAEEAEALLKEaekLKEELE---EKKEKLQEEEDKLLEEAEKEaqqaIKEAKKEADEIIKELRQLQKG 599

                          90       100
                  ....*....|....*....|....*.
gi 1738644122  77 YMALQRiNQELEDKLYRMGQHYEEEK 102
Cdd:PRK00409  600 GYASVK-AHELIEARKRLNKANEKKE 624
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-97 1.44e-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: 41.29  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122   1 MGSHQSSQASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR----------HYLEIELRRAQEELDKVTEKL 70
Cdd:COG4942    13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALErriaalarriRALEQELAALEAELAELEKEI 92

                          90       100
                  ....*....|....*....|....*..
gi 1738644122  71 RRIQSNYMALQRINQELEDKLYRMGQH 97
Cdd:COG4942    93 AELRAELEAQKEELAELLRALYRLGRQ 119
mukB PRK04863
chromosome partition protein MukB;
4-108 1.78e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122    4 HQSSQASAADMEKLSALQEQkgeLRKRLsytthklEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRI 83
Cdd:PRK04863   970 HFSYEDAAEMLAKNSDLNEK---LRQRL-------EQAEQERTRARE----QLRQAQAQLAQYNQVLASLKSSYDAKRQM 1035

                           90       100
                   ....*....|....*....|....*..
gi 1738644122   84 NQELEDKLYRMGQHY--EEEKRAMSHE 108
Cdd:PRK04863  1036 LQELKQELQDLGVPAdsGAEERARARR 1062
PRK01156 PRK01156
chromosome segregation protein; Provisional
 7-127 3.68e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122   7 SQASAADMEklsALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQE 86
Cdd:PRK01156  575 AVISLIDIE---TNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGK 651

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1738644122  87 LEDKLYRMGQHYEEEKRAMSheivaLNSHLLEAKVTIDKLS 127
Cdd:PRK01156  652 IDNYKKQIAEIDSIIPDLKE-----ITSRINDIEDNLKKSR 687
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 15-151 4.11e-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: 40.44  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122   15 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDstrhylEIELRRAQEELDKVTEKLRRI----QSNYMALQRINQELEDK 90
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKLEEALN------DLEARLSHSRIPEIQAELSKLeeevSRIEARLREIEQKLNRL 824

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1738644122   91 LYRmgQHYEEEKRAmshEIVALNSHLLEAKVTI-DKLSEDN----ELYRKDCNLAAQLLQCSQTYG 151
Cdd:TIGR02169  825 TLE--KEYLEKEIQ---ELQEQRIDLKEQIKSIeKEIENLNgkkeELEEELEELEAALRDLESRLG 885
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 37-136 4.39e-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: 37.59  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122  37 KLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYEEEKRAMSHEIvaln 113
Cdd:pfam20492  14 RLKQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEAEEKEQLEAEL---- 85

                          90       100
                  ....*....|....*....|...
gi 1738644122 114 shlLEAKVTIDKLSEDNElyRKD 136
Cdd:pfam20492  86 ---AEAQEEIARLEEEVE--RKE 103
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 7-106 4.54e-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: 39.75  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122   7 SQASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQE 86
Cdd:COG4942   145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224

                          90       100
                  ....*....|....*....|
gi 1738644122  87 LEDKLYRMGQHYEEEKRAMS 106
Cdd:COG4942   225 LEALIARLEAEAAAAAERTP 244
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
 7-70 4.65e-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: 38.04  E-value: 4.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1738644122   7 SQASAADMEKLSALQEQKGELRKRLSytTHKLEKLETEFDSTRHYLEiELRRAQEELDKVTEKL 70
Cdd:pfam17098  84 STTGKRLMAKCRLLQQENEELGRQLS--EGRIAKLEIELALQKKVVE-ELKKSLEELDEFLIEL 144
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 5-92 5.99e-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: 37.56  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738644122   5 QSSQASAAdMEKLSALQEQ-KGELRKRlsytTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYM-ALQR 82
Cdd:pfam03938  13 ESPEGKAA-QAQLEKKFKKrQAELEAK----QKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQqELQK 87

                          90
                  ....*....|
gi 1738644122  83 INQELEDKLY 92
Cdd:pfam03938  88 KQQELLQPIQ 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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