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Conserved domains on  [gi|568980006|ref|XP_006516107|]
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brain-enriched guanylate kinase-associated protein isoform X4 [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];
2-132 1.27e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNymaLQRINQELEDKLYRM 81
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568980006  82 GQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 132
Cdd:COG4372  104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2-132 1.27e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNymaLQRINQELEDKLYRM 81
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568980006  82 GQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 132
Cdd:COG4372  104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-122 2.36e-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: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006     2 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrm 81
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 568980006    82 gQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 122
Cdd:TIGR02168  876 -EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 22-139 5.97e-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: 41.90  E-value: 5.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006  22 THKLEKL-ETEFDSTRhylEIELRRAqeeLDKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIval 99
Cdd:cd07651   39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568980006 100 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 139
Cdd:cd07651  110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-118 8.76e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 8.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   2 EKLSALQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELDKVTEKLRRIQSny 64
Cdd:PRK03918 563 KKLDELEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK-- 640

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980006  65 mALQRINQELED--KLYRMGQHYEEEKRAMS---------HEIVALNSHLLEAKVTIDKLSEDNE 118
Cdd:PRK03918 641 -RLEELRKELEEleKKYSEEEYEELREEYLElsrelaglrAELEELEKRREEIKKTLEKLKEELE 704
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 2-117 1.05e-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: 40.30  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006    2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDklyrm 81
Cdd:pfam08614  64 EELAELYRSRGELAQRLVDLNEELQELEKKLRE----DERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD----- 134

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568980006   82 gqhyeeekramshEIVALNSHLLEAKVTIDKLSEDN 117
Cdd:pfam08614 135 -------------ELVALQLQLNMAEEKLRKLEKEN 157
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2-132 1.27e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNymaLQRINQELEDKLYRM 81
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568980006  82 GQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 132
Cdd:COG4372  104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-122 2.36e-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: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006     2 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrm 81
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 568980006    82 gQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 122
Cdd:TIGR02168  876 -EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 2-155 5.29e-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: 5.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI-ELRRAQEELDKVTEKLRRIQSNYMALQR-INQELEDKLY 79
Cdd:COG5185  275 ESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLeEQLAAAEAEQELEESKRETETGIQNLTAeIEQGQESLTE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006  80 RMGQHYEEEKRAMSHEIVALNSHLLE-AKVTIDKLSEDNELYRKDCNLAAQLL--QCSQTYGRV-HKVSELPSDFQQRVS 155
Cdd:COG5185  355 NLEAIKEEIENIVGEVELSKSSEELDsFKDTIESTKESLDEIPQNQRGYAQEIlaTLEDTLKAAdRQIEELQRQIEQATS 434
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-154 7.41e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 7.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   1 MEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMA----LQRINQE--- 73
Cdd:COG4372   37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARS----ELEQLEEELEELNEQLQAAQAELAQaqeeLESLQEEaee 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006  74 LEDKLYRM---GQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNElyrkdcNLAAQLLQCSQTYGRV------HKVS 144
Cdd:COG4372  113 LQEELEELqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE------SLQEELAALEQELQALseaeaeQALD 186

                        170
                 ....*....|
gi 568980006 145 ELPSDFQQRV 154
Cdd:COG4372  187 ELLKEANRNA 196
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 2-118 1.29e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.76  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELDKVTEKLRRIQSN--YMALQ-------RINQ 72
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKE----IKRLELEIEEVEARIKKYEEQLGNVRNNkeYEALQkeieslkRRIS 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568980006  73 ELEDKLYR-MGQ--HYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNE 118
Cdd:COG1579  107 DLEDEILElMERieELEEELAELEAELAELEAELEEKKAELDEELAELE 155
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-131 1.36e-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: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006    2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR------------HYLEIELRRAQEELDKVTEKLRRIQSNYMALQR 69
Cdd:COG4913   610 AKLAALEAELAELEEELAEAEERLEALEAELDALQerrealqrlaeySWDEIDVASAEREIAELEAELERLDASSDDLAA 689

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980006   70 INQELEdKLYRMGQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 131
Cdd:COG4913   690 LEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2-123 2.94e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRM 81
Cdd:COG4717   95 EELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568980006  82 GQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKD 123
Cdd:COG4717  173 AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-99 4.57e-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: 42.83  E-value: 4.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRM 81
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                         90
                 ....*....|....*...
gi 568980006  82 GQHYEEEKRAMSHEIVAL 99
Cdd:COG4942   96 RAELEAQKEELAELLRAL 113
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 22-139 5.97e-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: 41.90  E-value: 5.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006  22 THKLEKL-ETEFDSTRhylEIELRRAqeeLDKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIval 99
Cdd:cd07651   39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568980006 100 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 139
Cdd:cd07651  110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-118 8.76e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 8.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   2 EKLSALQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELDKVTEKLRRIQSny 64
Cdd:PRK03918 563 KKLDELEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK-- 640

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980006  65 mALQRINQELED--KLYRMGQHYEEEKRAMS---------HEIVALNSHLLEAKVTIDKLSEDNE 118
Cdd:PRK03918 641 -RLEELRKELEEleKKYSEEEYEELREEYLElsrelaglrAELEELEKRREEIKKTLEKLKEELE 704
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 2-117 1.05e-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: 40.30  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006    2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDklyrm 81
Cdd:pfam08614  64 EELAELYRSRGELAQRLVDLNEELQELEKKLRE----DERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD----- 134

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568980006   82 gqhyeeekramshEIVALNSHLLEAKVTIDKLSEDN 117
Cdd:pfam08614 135 -------------ELVALQLQLNMAEEKLRKLEKEN 157
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-142 1.05e-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: 42.36  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006     3 KLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrmG 82
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL---A 423

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980006    83 QHYEEEKRAMShEIVALNSHLLEAKVTIDKLSEDNELYRKDC-NLAAQLLQCSQTYGRVHK 142
Cdd:TIGR02169  424 DLNAAIAGIEA-KINELEEEKEDKALEIKKQEWKLEQLAADLsKYEQELYDLKEEYDRVEK 483
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 2-89 3.92e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   2 EKLSALQEQKGE---LRKRLSyttHKLEKLETEFDSTRHYLEIE----LRRAQEELDKVTEKLRRIQSNYMALQRiNQEL 74
Cdd:PRK00409 534 QKAEEAEALLKEaekLKEELE---EKKEKLQEEEDKLLEEAEKEaqqaIKEAKKEADEIIKELRQLQKGGYASVK-AHEL 609

                         90
                 ....*....|....*
gi 568980006  75 EDKLYRMGQHYEEEK 89
Cdd:PRK00409 610 IEARKRLNKANEKKE 624
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-138 4.13e-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: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006     2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDstrhylEIELRRAQEELDKVTEKLRRI----QSNYMALQRINQELEDK 77
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKLEEALN------DLEARLSHSRIPEIQAELSKLeeevSRIEARLREIEQKLNRL 824

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980006    78 LYRmgQHYEEEKRAmshEIVALNSHLLEAKVTI-DKLSEDN----ELYRKDCNLAAQLLQCSQTYG 138
Cdd:TIGR02169  825 TLE--KEYLEKEIQ---ELQEQRIDLKEQIKSIeKEIENLNgkkeELEEELEELEAALRDLESRLG 885
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-84 4.19e-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: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR----------HYLEIELRRAQEELDKVTEKLRRIQSNYMALQRIN 71
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALErriaalarriRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106

                         90
                 ....*....|...
gi 568980006  72 QELEDKLYRMGQH 84
Cdd:COG4942  107 AELLRALYRLGRQ 119
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 24-123 4.37e-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: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980006   24 KLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYEEEKRAMSHEIvaln 100
Cdd:pfam20492  14 RLKQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEAEEKEQLEAEL---- 85

                          90       100
                  ....*....|....*....|...
gi 568980006  101 shlLEAKVTIDKLSEDNElyRKD 123
Cdd:pfam20492  86 ---AEAQEEIARLEEEVE--RKE 103
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
 1-57 9.74e-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: 9.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568980006    1 MEKLSALQEQKGELRKRLSytTHKLEKLETEFDSTRHYLEiELRRAQEELDKVTEKL 57
Cdd:pfam17098  91 MAKCRLLQQENEELGRQLS--EGRIAKLEIELALQKKVVE-ELKKSLEELDEFLIEL 144
 
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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