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Conserved domains on  [gi|227497884|ref|NP_001153003|]
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brain-enriched guanylate kinase-associated protein isoform 1 [Homo sapiens]

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 4.21e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNymaLQRINQELEDKLYRM 81
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 227497884  82 GQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 132
Cdd:COG4372  104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2-132 4.21e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNymaLQRINQELEDKLYRM 81
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 227497884  82 GQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 132
Cdd:COG4372  104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-122 4.70e-06

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: 49.67  E-value: 4.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884     2 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrm 81
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 227497884    82 gQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 122
Cdd:TIGR02168  876 -EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 2-90 6.09e-05

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 42.77  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884    2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELEKVTEKLRRIQSNYMALQrinQELEDKLYRM 81
Cdd:pfam04871   8 SEASSLKNENTELKAELQELSKQYNSLEQKESQAKE-LEAEVKKLEEALKKLKAELSEEKQKEKEKQ---SELDDLLLLL 83


                  ....*....
gi 227497884   82 GQhyEEEKR 90
Cdd:pfam04871  84 GD--LEEKV 90
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-122 1.96e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELEKVTEKLRRIQSny 64
Cdd:PRK03918 563 KKLDELEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK-- 640

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227497884  65 mALQRINQELED--KLYRMGQHYE--EEKRALSHEIVA-------LNSHLLEAKVTIDKLSEDNELYRK 122
Cdd:PRK03918 641 -RLEELRKELEEleKKYSEEEYEElrEEYLELSRELAGlraeleeLEKRREEIKKTLEKLKEELEEREK 708
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 22-139 6.74e-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: 6.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884  22 THKLEKL-ETEFDSTRhylEIELRRAqeeLEKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRALSHEIval 99
Cdd:cd07651   39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 227497884 100 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 139
Cdd:cd07651  110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2-132 4.21e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNymaLQRINQELEDKLYRM 81
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 227497884  82 GQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 132
Cdd:COG4372  104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-154 2.13e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   1 MEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMA----LQRINQE--- 73
Cdd:COG4372   37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARS----ELEQLEEELEELNEQLQAAQAELAQaqeeLESLQEEaee 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884  74 LEDKLYRM---GQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNElyrkdcNLAAQLLQCSQTYGRV------HKVS 144
Cdd:COG4372  113 LQEELEELqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE------SLQEELAALEQELQALseaeaeQALD 186

                        170
                 ....*....|
gi 227497884 145 ELPSDFQERV 154
Cdd:COG4372  187 ELLKEANRNA 196
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-122 4.70e-06

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: 49.67  E-value: 4.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884     2 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrm 81
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 227497884    82 gQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 122
Cdd:TIGR02168  876 -EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 2-118 1.48e-05

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: 46.46  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSN--YMALQ-------RINQ 72
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKE----IKRLELEIEEVEARIKKYEEQLGNVRNNkeYEALQkeieslkRRIS 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 227497884  73 ELEDKLYR-MGQ--HYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNE 118
Cdd:COG1579  107 DLEDEILElMERieELEEELAELEAELAELEAELEEKKAELDEELAELE 155
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-131 2.04e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884    2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR------------HYLEIELRRAQEELEKVTEKLRRIQSNYMALQR 69
Cdd:COG4913   610 AKLAALEAELAELEEELAEAEERLEALEAELDALQerrealqrlaeySWDEIDVASAEREIAELEAELERLDASSDDLAA 689

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227497884   70 INQELEdKLYRMGQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 131
Cdd:COG4913   690 LEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 2-90 6.09e-05

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 42.77  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884    2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELEKVTEKLRRIQSNYMALQrinQELEDKLYRM 81
Cdd:pfam04871   8 SEASSLKNENTELKAELQELSKQYNSLEQKESQAKE-LEAEVKKLEEALKKLKAELSEEKQKEKEKQ---SELDDLLLLL 83


                  ....*....
gi 227497884   82 GQhyEEEKR 90
Cdd:pfam04871  84 GD--LEEKV 90
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2-123 7.19e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 7.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALqrinQELEDKLYRM 81
Cdd:COG4717   95 EELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEEL 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 227497884  82 GQHYEEEKRALSHEIVALN----SHLLEAKVTIDKLSEDNELYRKD 123
Cdd:COG4717  169 EAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEE 214
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-99 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: 44.75  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRM 81
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                         90
                 ....*....|....*...
gi 227497884  82 GQHYEEEKRALSHEIVAL 99
Cdd:COG4942   96 RAELEAQKEELAELLRAL 113
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 4-136 1.34e-04

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: 43.35  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884    4 LSALQEQKGELRKRLSYTTHKLEKLETE-----------------FDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMA 66
Cdd:pfam15619   6 LSARLHKIKELQNELAELQSKLEELRKEnrllkrlqkrqekalgkYEGTESELPQLIARHNEEVRVLRERLRRLQEKERD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   67 LQRINQELEDKLYRMG---QHYEE--------EKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRK--DCNLAAQLLQC 133
Cdd:pfam15619  86 LERKLKEKEAELLRLRdqlKRLEKlsedknlaEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKsfRRQLAAEKKKH 165


                  ...
gi 227497884  134 SQT 136
Cdd:pfam15619 166 KEA 168
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-122 1.96e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELEKVTEKLRRIQSny 64
Cdd:PRK03918 563 KKLDELEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK-- 640

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227497884  65 mALQRINQELED--KLYRMGQHYE--EEKRALSHEIVA-------LNSHLLEAKVTIDKLSEDNELYRK 122
Cdd:PRK03918 641 -RLEELRKELEEleKKYSEEEYEElrEEYLELSRELAGlraeleeLEKRREEIKKTLEKLKEELEEREK 708
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 2-117 2.25e-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: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884    2 EKLSALQEQKGELRKRLSYTTHKLEKLETEfDSTRhylEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDklyrm 81
Cdd:pfam08614  64 EELAELYRSRGELAQRLVDLNEELQELEKK-LRED---ERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD----- 134

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 227497884   82 gqhyeeekralshEIVALNSHLLEAKVTIDKLSEDN 117
Cdd:pfam08614 135 -------------ELVALQLQLNMAEEKLRKLEKEN 157
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-142 2.37e-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: 44.29  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884     3 KLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrmG 82
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL---A 423

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227497884    83 QHYEEEKRALShEIVALNSHLLEAKVTIDKLSEDNELYRKDC-NLAAQLLQCSQTYGRVHK 142
Cdd:TIGR02169  424 DLNAAIAGIEA-KINELEEEKEDKALEIKKQEWKLEQLAADLsKYEQELYDLKEEYDRVEK 483
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 2-145 2.39e-04

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 44.18  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI-ELRRAQEELEKVTEKLRRIQSNYMALQR-INQELEDKLY 79
Cdd:COG5185  275 ESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLeEQLAAAEAEQELEESKRETETGIQNLTAeIEQGQESLTE 354

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227497884  80 RMGQHYEEEKRALSHEIVALNSHLLE-AKVTIDKLSEDNELYRKDCNLAAQLL--QCSQTYGRVHKVSE 145
Cdd:COG5185  355 NLEAIKEEIENIVGEVELSKSSEELDsFKDTIESTKESLDEIPQNQRGYAQEIlaTLEDTLKAADRQIE 423
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 24-123 3.72e-04

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: 40.67  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   24 KLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYEEEKRALSHEIvaln 100
Cdd:pfam20492  14 RLKQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEAEEKEQLEAEL---- 85

                          90       100
                  ....*....|....*....|...
gi 227497884  101 shlLEAKVTIDKLSEDNElyRKD 123
Cdd:pfam20492  86 ---AEAQEEIARLEEEVE--RKE 103
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-122 4.35e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEiELRRAQEELEKV---TEKLRRIQSNYMALQRINQELEDKL 78
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE-ELKKEIEELEEKvkeLKELKEKAEEYIKLSEFYEEYLDEL 309

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 227497884  79 YRMgqhyEEEKRALSHEIVALNSHLLEAKvtiDKLSEDNELYRK 122
Cdd:PRK03918 310 REI----EKRLSRLEEEINGIEERIKELE---EKEERLEELKKK 346
Tup_N pfam08581
Tup N-terminal; The N-terminal domain of the Tup protein has been shown to interact with the ...
 25-96 4.45e-04

Tup N-terminal; The N-terminal domain of the Tup protein has been shown to interact with the Ssn6 transcriptional co-repressor.


Pssm-ID: 400755 [Multi-domain]  Cd Length: 77  Bit Score: 39.03  E-value: 4.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227497884   25 LEKLETEFDS-TRHYLEIELRRaqEELEkvteklRRIQSNYMALQRINQ---ELEDKLYRMGQHYEEEKRALSHEI 96
Cdd:pfam08581   6 LDAIKQEFDNlSQEANSYKAQR--DEYE------HKINQQINELQQIRQtlyELERAHRKIKQQYEEEIARLKAEL 73
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 22-139 6.74e-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: 6.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884  22 THKLEKL-ETEFDSTRhylEIELRRAqeeLEKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRALSHEIval 99
Cdd:cd07651   39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 227497884 100 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 139
Cdd:cd07651  110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-122 7.25e-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: 7.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884     2 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKL----RRIQSNYMALQRINQELEDK 77
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLE----KEYLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEELEEL 873

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 227497884    78 LYRMGQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRK 122
Cdd:TIGR02169  874 EAALRD-LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-118 7.70e-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: 7.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884     2 EKLSALQEQKGELRKRLSYTthKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrm 81
Cdd:TIGR02168  213 ERYKELKAELRELELALLVL--RLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI--- 283

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 227497884    82 gQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNE 118
Cdd:TIGR02168  284 -EELQKELYALANEISRLEQQKQILRERLANLERQLE 319
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 2-135 1.10e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884    2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEiELRRAQEELEKVTEKLRR----IQSNymaLQRINQELEDK 77
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-DLKKQKEELENELNLLEKeklnIQKN---IDKIKNKLLKL 199

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227497884   78 LYRMG--QHYEEEKRALSHEIVALNSHLLEAKVTIDKLSED-NELYRKDCNLAAQLLQCSQ 135
Cdd:TIGR04523 200 ELLLSnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEiNEKTTEISNTQTQLNQLKD 260
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-132 1.18e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrm 81
Cdd:COG1196  239 AELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERR--- 311

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 227497884  82 gQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 132
Cdd:COG1196  312 -RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-133 1.62e-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: 41.59  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884     2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLeiELRRAQEELEkVTEKLRRIQSNYMALQRINQELEDkLYRM 81
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ--ALLKEKREYE-GYELLKEKEALERQKEAIERQLAS-LEEE 252

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 227497884    82 GQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSED--NELYRKDCNLAAQLLQC 133
Cdd:TIGR02169  253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqLRVKEKIGELEAEIASL 306
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-84 1.73e-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: 40.90  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR----------HYLEIELRRAQEELEKVTEKLRRIQSNYMALQRIN 71
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALErriaalarriRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106

                         90
                 ....*....|...
gi 227497884  72 QELEDKLYRMGQH 84
Cdd:COG4942  107 AELLRALYRLGRQ 119
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
9-122 2.35e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   9 EQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKlyrmgqhyEEE 88
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELERE--------EKE 620

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 227497884  89 KRALSHEIVALNSHLLEAKVTIDKLSED-NELYRK 122
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKElEELEKK 655
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1-113 2.51e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   1 MEKLSALQEQKGELRKRLSYTTHKLEKLEtefdsTRHYLEIELRRAQEELEKVTEKLrriqSNYmALQRINQELEdKLYR 80
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELE-----ERHELYEEAKAKKEELERLKKRL----TGL-TPEKLEKELE-ELEK 398

                         90       100       110
                 ....*....|....*....|....*....|...
gi 227497884  81 MGQHYEEEKRALSHEIVALNSHLLEAKVTIDKL 113
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 2-145 2.52e-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: 39.75  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884    2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleIELRRAQEElekvteklRRIQSNYMALQRINQELEDKLYRM 81
Cdd:pfam14988  40 ELASRYTQQTAELQTQLLQKEKEQASLKKELQALRP---FAKLKESQE--------REIQDLEEEKEKVRAETAEKDREA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   82 GQHYEEEKRALSHEIVALNSHLL-----------------EAKVTIDKLSEDneLYRKDCNLAAQLLQCSQTYGRVHKVS 144
Cdd:pfam14988 109 HLQFLKEKALLEKQLQELRILELgeratrelkrkaqalklAAKQALSEFCRS--IKRENRQLQKELLQLIQETQALEAIK 186


                  .
gi 227497884  145 E 145
Cdd:pfam14988 187 S 187
PRK01156 PRK01156
chromosome segregation protein; Provisional
 4-160 2.56e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.04  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   4 LSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQ 83
Cdd:PRK01156 582 IETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAE 661

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227497884  84 HYEEEKR--ALSHEIVALNSHLLEAKVTIDKLSEDneLYRKDcNLAAQLLQcsqtygRVHKVSELPSDFQERVSlHMEK 160
Cdd:PRK01156 662 IDSIIPDlkEITSRINDIEDNLKKSRKALDDAKAN--RARLE-STIEILRT------RINELSDRINDINETLE-SMKK 730
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-111 2.96e-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: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884     2 EKLSALQEQKGELRkrLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRM 81
Cdd:TIGR02169  211 ERYQALLKEKREYE--GYELLKEKEALERQ----KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL 284

                           90       100       110
                   ....*....|....*....|....*....|
gi 227497884    82 GqhyEEEKRALSHEIVALNSHLLEAKVTID 111
Cdd:TIGR02169  285 G---EEEQLRVKEKIGELEAEIASLERSIA 311
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1-122 3.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   1 MEKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYR 80
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINE----ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 227497884  81 MGQhYEEEKRALSHEIVALNSHL--LEAKVT-IDKLSEDNELYRK 122
Cdd:PRK03918 254 KRK-LEEKIRELEERIEELKKEIeeLEEKVKeLKELKEKAEEYIK 297
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-131 4.61e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   1 MEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELEKVTEKLRRiqsnymALQRINQELEDKLYR 80
Cdd:COG4717  124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEE------LLEQLSLATEEELQD 196

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 227497884  81 MGQHYEE---EKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 131
Cdd:COG4717  197 LAEELEElqqRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-75 4.89e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR-HYLEIELRRAQEELEKVTEKLRRIQSNYMALQR----INQELE 75
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAeigaVENELE 691
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 2-89 5.35e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.81  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGE---LRKRLSyttHKLEKLETEFDSTRHYLEIE----LRRAQEELEKVTEKLRRIQSNYMALQRiNQEL 74
Cdd:PRK00409 534 QKAEEAEALLKEaekLKEELE---EKKEKLQEEEDKLLEEAEKEaqqaIKEAKKEADEIIKELRQLQKGGYASVK-AHEL 609

                         90
                 ....*....|....*
gi 227497884  75 EDKLYRMGQHYEEEK 89
Cdd:PRK00409 610 IEARKRLNKANEKKE 624
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 7-79 6.00e-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: 6.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227497884    7 LQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYM-ALQRINQELEDKLY 79
Cdd:pfam03938  24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQqELQKKQQELLQPIQ 97
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2-146 6.61e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 6.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETefDSTRHYLEIELRRAQEELEkvtEKLRRIQSNYMALQRINQELEdklyrm 81
Cdd:COG4717  439 EELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELR---ELAEEWAALKLALELLEEARE------ 507

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227497884  82 gqHYEEEKR-ALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNlaaqllqcsqtyGRVHKVSEL 146
Cdd:COG4717  508 --EYREERLpPVLERASEYFSRLTDGRYRLIRIDEDLSLKVDTED------------GRTRPVEEL 559
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-95 7.20e-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: 39.67  E-value: 7.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884     2 EKLSALQEQKGEL-------RKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEE------LEKVTEKLRRIQSNYMALQ 68
Cdd:TIGR02169  896 AQLRELERKIEELeaqiekkRKRLSELKAKLEALEEELSE----IEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRALE 971

                           90       100       110
                   ....*....|....*....|....*....|.
gi 227497884    69 RIN----QELEDKLYRMGQhYEEEKRALSHE 95
Cdd:TIGR02169  972 PVNmlaiQEYEEVLKRLDE-LKEKRAKLEEE 1001
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 39-117 7.22e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.00  E-value: 7.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884  39 LEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDklyrmgqhyeeekralshEIVALNSH--LLEAKvtIDKLSED 116
Cdd:cd22887    9 LEKRLAELEAELASLEEEIKDLEEELKEKNKANEILND------------------ELIALQIEnnLLEEK--LRKLQEE 68


                 .
gi 227497884 117 N 117
Cdd:cd22887   69 N 69
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2-117 7.99e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 7.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKgELRKRLSYTTHKLEKLETEF-----DSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELE- 75
Cdd:COG4717  389 AALEQAEEYQ-ELKEELEELEEQLEELLGELeelleALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEe 467

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 227497884  76 ----DKLYRMGQHYEEEKRALSHEIVALN--SHLLEAkvTIDKLSEDN 117
Cdd:COG4717  468 dgelAELLQELEELKAELRELAEEWAALKlaLELLEE--AREEYREER 513
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-107 8.91e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 8.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884   2 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEiELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRM 81
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK 371

                         90       100
                 ....*....|....*....|....*.
gi 227497884  82 GQHYEEEKRALSHEIVALNSHLLEAK 107
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELE 397
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1-57 9.29e-03

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: 37.98  E-value: 9.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 227497884   1 MEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKL 57
Cdd:COG1579  116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
 1-57 9.79e-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: 9.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 227497884    1 MEKLSALQEQKGELRKRLSytTHKLEKLETEFDSTRHYLEiELRRAQEELEKVTEKL 57
Cdd:pfam17098  91 MAKCRLLQQENEELGRQLS--EGRIAKLEIELALQKKVVE-ELKKSLEELDEFLIEL 144
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 7-113 9.79e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.00  E-value: 9.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227497884     7 LQEqkgELRKRLSYTThKLEKLETEFDSTRHYLEielrraqEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQhYE 86
Cdd:pfam01576  477 LQE---ETRQKLNLST-RLRQLEDERNSLQEQLE-------EEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LE 544

                           90       100
                   ....*....|....*....|....*..
gi 227497884    87 EEKRALSHEIVALNSHLLEAKVTIDKL 113
Cdd:pfam01576  545 EGKKRLQRELEALTQQLEEKAAAYDKL 571
 
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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