NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1867158357|ref|NP_001372018|]
View 

brain-enriched guanylate kinase-associated protein isoform 6 [Homo sapiens]

Protein Classification

COG4372 family protein( domain architecture ID 11468211)

COG4372 family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-151 3.63e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNymaLQRINQELEDKLYRM 100
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1867158357 101 GQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 151
Cdd:COG4372   104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-151 3.63e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNymaLQRINQELEDKLYRM 100
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1867158357 101 GQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 151
Cdd:COG4372   104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-141 4.68e-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: 50.06  E-value: 4.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357   21 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrm 100
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1867158357  101 gQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 141
Cdd:TIGR02168  876 -EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 21-109 6.06e-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: 6.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELEKVTEKLRRIQSNYMALQrinQELEDKLYRM 100
Cdd:pfam04871   8 SEASSLKNENTELKAELQELSKQYNSLEQKESQAKE-LEAEVKKLEEALKKLKAELSEEKQKEKEKQ---SELDDLLLLL 83


                  ....*....
gi 1867158357 101 GQhyEEEKR 109
Cdd:pfam04871  84 GD--LEEKV 90
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-141 1.36e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSY-----------TTHKLEKLETEFDS---TRHYLEIELRR---AQEELEKVTEKLRRIQSny 83
Cdd:PRK03918  563 KKLDELEEELAELLKELEElgfesveeleeRLKELEPFYNEYLElkdAEKELEREEKElkkLEEELDKAFEELAETEK-- 640

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867158357  84 mALQRINQELED--KLYRMGQHYE--EEKRALSHEIVA-------LNSHLLEAKVTIDKLSEDNELYRK 141
Cdd:PRK03918  641 -RLEELRKELEEleKKYSEEEYEElrEEYLELSRELAGlraeleeLEKRREEIKKTLEKLKEELEEREK 708
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 41-158 7.01e-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: 7.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  41 THKLEKL-ETEFDSTRhylEIELRRAqeeLEKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRALSHEIval 118
Cdd:cd07651    39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1867158357 119 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 158
Cdd:cd07651   110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-151 3.63e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNymaLQRINQELEDKLYRM 100
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1867158357 101 GQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 151
Cdd:COG4372   104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-141 4.68e-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: 50.06  E-value: 4.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357   21 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrm 100
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1867158357  101 gQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 141
Cdd:TIGR02168  876 -EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-173 1.19e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLE---IELRRAQEELEKVTEKLRRIQSnymALQRINQELEDkl 97
Cdd:COG4372    52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQaaqAELAQAQEELESLQEEAEELQE---ELEELQKERQD-- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  98 yrmgqhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNElyrkdcNLAAQLLQCSQTYGRV------HKVSELPSDFQE 171
Cdd:COG4372   127 ------LEQQRKQLEAQIAELQSEIAEREEELKELEEQLE------SLQEELAALEQELQALseaeaeQALDELLKEANR 194


                  ..
gi 1867158357 172 RV 173
Cdd:COG4372   195 NA 196
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 14-118 1.27e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.84  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  14 AASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQEL 93
Cdd:COG4942    13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAEL 88

                          90       100
                  ....*....|....*....|....*
gi 1867158357  94 EDKLYRMGQHYEEEKRALSHEIVAL 118
Cdd:COG4942    89 EKEIAELRAELEAQKEELAELLRAL 113
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
21-150 2.19e-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: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357   21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR------------HYLEIELRRAQEELEKVTEKLRRIQSNYMALQR 88
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQerrealqrlaeySWDEIDVASAEREIAELEAELERLDASSDDLAA 689

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1867158357   89 INQELEdKLYRMGQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 150
Cdd:COG4913    690 LEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 15-137 2.52e-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: 46.07  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  15 ASAADMEKLSALQE----------QKGELRKRLSYTTHKLEKLETEFDSTR---HYLEIELRRAQEELEKVTEKLRRIQS 81
Cdd:COG1579     1 AMPEDLRALLDLQEldseldrlehRLKELPAELAELEDELAALEARLEAAKtelEDLEKEIKRLELEIEEVEARIKKYEE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1867158357  82 N---------YMALQ-------RINQELEDKLYR-MGQ--HYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNE 137
Cdd:COG1579    81 QlgnvrnnkeYEALQkeieslkRRISDLEDEILElMERieELEEELAELEAELAELEAELEEKKAELDEELAELE 155
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 21-109 6.06e-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: 6.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELEKVTEKLRRIQSNYMALQrinQELEDKLYRM 100
Cdd:pfam04871   8 SEASSLKNENTELKAELQELSKQYNSLEQKESQAKE-LEAEVKKLEEALKKLKAELSEEKQKEKEKQ---SELDDLLLLL 83


                  ....*....
gi 1867158357 101 GQhyEEEKR 109
Cdd:pfam04871  84 GD--LEEKV 90
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
21-142 7.14e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 7.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALqrinQELEDKLYRM 100
Cdd:COG4717    95 EELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEEL 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1867158357 101 GQHYEEEKRALSHEIVALN----SHLLEAKVTIDKLSEDNELYRKD 142
Cdd:COG4717   169 EAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEE 214
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 23-155 1.03e-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: 43.74  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  23 LSALQEQKGELRKRLSYTTHKLEKLETE-----------------FDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMA 85
Cdd:pfam15619   6 LSARLHKIKELQNELAELQSKLEELRKEnrllkrlqkrqekalgkYEGTESELPQLIARHNEEVRVLRERLRRLQEKERD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  86 LQRINQELEDKLYRMG---QHYEE--------EKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRK--DCNLAAQLLQC 152
Cdd:pfam15619  86 LERKLKEKEAELLRLRdqlKRLEKlsedknlaEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKsfRRQLAAEKKKH 165


                  ...
gi 1867158357 153 SQT 155
Cdd:pfam15619 166 KEA 168
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-141 1.36e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSY-----------TTHKLEKLETEFDS---TRHYLEIELRR---AQEELEKVTEKLRRIQSny 83
Cdd:PRK03918  563 KKLDELEEELAELLKELEElgfesveeleeRLKELEPFYNEYLElkdAEKELEREEKElkkLEEELDKAFEELAETEK-- 640

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867158357  84 mALQRINQELED--KLYRMGQHYE--EEKRALSHEIVA-------LNSHLLEAKVTIDKLSEDNELYRK 141
Cdd:PRK03918  641 -RLEELRKELEEleKKYSEEEYEElrEEYLELSRELAGlraeleeLEKRREEIKKTLEKLKEELEEREK 708
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-141 1.41e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEiELRRAQEELEKVTEKLRRIQ---SNYMALQRINQELEDKL 97
Cdd:PRK03918  231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDEL 309

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1867158357  98 YRMgqhyEEEKRALSHEIVALNSHLLEAKvtiDKLSEDNELYRK 141
Cdd:PRK03918  310 REI----EKRLSRLEEEINGIEERIKELE---EKEERLEELKKK 346
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 22-161 2.09e-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: 44.67  E-value: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357   22 KLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrmG 101
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL---A 423

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1867158357  102 QHYEEEKRALShEIVALNSHLLEAKVTIDKLSEDNELYRKDC-NLAAQLLQCSQTYGRVHK 161
Cdd:TIGR02169  424 DLNAAIAGIEA-KINELEEEKEDKALEIKKQEWKLEQLAADLsKYEQELYDLKEEYDRVEK 483
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 21-136 2.38e-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: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEfDSTRhylEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDklyrm 100
Cdd:pfam08614  64 EELAELYRSRGELAQRLVDLNEELQELEKK-LRED---ERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD----- 134

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1867158357 101 gqhyeeekralshEIVALNSHLLEAKVTIDKLSEDN 136
Cdd:pfam08614 135 -------------ELVALQLQLNMAEEKLRKLEKEN 157
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 21-164 2.49e-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: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI-ELRRAQEELEKVTEKLRRIQSNYMALQR-INQELEDKLY 98
Cdd:COG5185   275 ESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLeEQLAAAEAEQELEESKRETETGIQNLTAeIEQGQESLTE 354

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867158357  99 RMGQHYEEEKRALSHEIVALNSHLLE-AKVTIDKLSEDNELYRKDCNLAAQLL--QCSQTYGRVHKVSE 164
Cdd:COG5185   355 NLEAIKEEIENIVGEVELSKSSEELDsFKDTIESTKESLDEIPQNQRGYAQEIlaTLEDTLKAADRQIE 423
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 43-142 3.85e-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: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  43 KLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYEEEKRALSHEIvaln 119
Cdd:pfam20492  14 RLKQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEAEEKEQLEAEL---- 85

                          90       100
                  ....*....|....*....|...
gi 1867158357 120 shlLEAKVTIDKLSEDNElyRKD 142
Cdd:pfam20492  86 ---AEAQEEIARLEEEVE--RKE 103
Tup_N pfam08581
Tup N-terminal; The N-terminal domain of the Tup protein has been shown to interact with the ...
 44-115 3.97e-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: 39.42  E-value: 3.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1867158357  44 LEKLETEFDS-TRHYLEIELRRaqEELEkvteklRRIQSNYMALQRINQ---ELEDKLYRMGQHYEEEKRALSHEI 115
Cdd:pfam08581   6 LDAIKQEFDNlSQEANSYKAQR--DEYE------HKINQQINELQQIRQtlyELERAHRKIKQQYEEEIARLKAEL 73
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 15-137 4.70e-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: 43.51  E-value: 4.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357   15 ASAAdmEKLSALQEQKGELRKRLSYTthKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELE 94
Cdd:TIGR02168  209 AEKA--ERYKELKAELRELELALLVL--RLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1867158357   95 DKLyrmgQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNE 137
Cdd:TIGR02168  281 EEI----EELQKELYALANEISRLEQQKQILRERLANLERQLE 319
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 41-158 7.01e-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: 7.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  41 THKLEKL-ETEFDSTRhylEIELRRAqeeLEKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRALSHEIval 118
Cdd:cd07651    39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1867158357 119 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 158
Cdd:cd07651   110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 21-141 7.07e-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: 7.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357   21 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKL----RRIQSNYMALQRINQELEDK 96
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLE----KEYLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEELEEL 873

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1867158357   97 LYRMGQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRK 141
Cdd:TIGR02169  874 EAALRD-LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 21-154 1.15e-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: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEiELRRAQEELEKVTEKLRR----IQSNymaLQRINQELEDK 96
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-DLKKQKEELENELNLLEKeklnIQKN---IDKIKNKLLKL 199

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1867158357  97 LYRMG--QHYEEEKRALSHEIVALNSHLLEAKVTIDKLSED-NELYRKDCNLAAQLLQCSQ 154
Cdd:TIGR04523 200 ELLLSnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEiNEKTTEISNTQTQLNQLKD 260
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 21-152 1.51e-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: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357   21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLeiELRRAQEELEkVTEKLRRIQSNYMALQRINQELEDkLYRM 100
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ--ALLKEKREYE-GYELLKEKEALERQKEAIERQLAS-LEEE 252

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1867158357  101 GQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSED--NELYRKDCNLAAQLLQC 152
Cdd:TIGR02169  253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqLRVKEKIGELEAEIASL 306
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
20-132 1.89e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  20 MEKLSALQEQKGELRKRLSYTTHKLEKLEtefdsTRHYLEIELRRAQEELEKVTEKLrriqSNYmALQRINQELEdKLYR 99
Cdd:PRK03918  330 IKELEEKEERLEELKKKLKELEKRLEELE-----ERHELYEEAKAKKEELERLKKRL----TGL-TPEKLEKELE-ELEK 398

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1867158357 100 MGQHYEEEKRALSHEIVALNSHLLEAKVTIDKL 132
Cdd:PRK03918  399 AKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-141 2.08e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  28 EQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKlyrmgqhyEEE 107
Cdd:PRK03918  549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELERE--------EKE 620

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1867158357 108 KRALSHEIVALNSHLLEAKVTIDKLSED-NELYRK 141
Cdd:PRK03918  621 LKKLEEELDKAFEELAETEKRLEELRKElEELEKK 655
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-138 2.17e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrm 100
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEE----LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL--- 318

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1867158357 101 gQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNEL 138
Cdd:COG1196   319 -EELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 21-164 2.18e-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: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleIELRRAQEElekvteklRRIQSNYMALQRINQELEDKLYRM 100
Cdd:pfam14988  40 ELASRYTQQTAELQTQLLQKEKEQASLKKELQALRP---FAKLKESQE--------REIQDLEEEKEKVRAETAEKDREA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357 101 GQHYEEEKRALSHEIVALNSHLL-----------------EAKVTIDKLSEDneLYRKDCNLAAQLLQCSQTYGRVHKVS 163
Cdd:pfam14988 109 HLQFLKEKALLEKQLQELRILELgeratrelkrkaqalklAAKQALSEFCRS--IKRENRQLQKELLQLIQETQALEAIK 186


                  .
gi 1867158357 164 E 164
Cdd:pfam14988 187 S 187
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
14-136 2.24e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  14 AASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEF-----DSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQR 88
Cdd:COG4717   381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeelleALDEEELEEELEELEEELEELEEELEELREELAELEA 460

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1867158357  89 INQELE-----DKLYRMGQHYEEEKRALSHEIVALN--SHLLEAkvTIDKLSEDN 136
Cdd:COG4717   461 ELEQLEedgelAELLQELEELKAELRELAEEWAALKlaLELLEE--AREEYREER 513
PRK01156 PRK01156
chromosome segregation protein; Provisional
 14-179 2.29e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.04  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  14 AASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQEL 93
Cdd:PRK01156  573 ALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKI 652

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  94 EDKLYRMGQHYEEEKR--ALSHEIVALNSHLLEAKVTIDKLSEDneLYRKDcNLAAQLLQcsqtygRVHKVSELPSDFQE 171
Cdd:PRK01156  653 DNYKKQIAEIDSIIPDlkEITSRINDIEDNLKKSRKALDDAKAN--RARLE-STIEILRT------RINELSDRINDINE 723


                  ....*...
gi 1867158357 172 RVSlHMEK 179
Cdd:PRK01156  724 TLE-SMKK 730
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 18-130 2.41e-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: 41.21  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357   18 ADMEKLSALQEQKGELRkrLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKL 97
Cdd:TIGR02169  208 EKAERYQALLKEKREYE--GYELLKEKEALERQ----KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1867158357   98 YRMGqhyEEEKRALSHEIVALNSHLLEAKVTID 130
Cdd:TIGR02169  282 KDLG---EEEQLRVKEKIGELEAEIASLERSIA 311
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
20-141 2.64e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  20 MEKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYR 99
Cdd:PRK03918  178 IERLEKFIKRTENIEELIKEKEKELEEVLREINE----ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1867158357 100 MGQhYEEEKRALSHEIVALNSHL--LEAKVT-IDKLSEDNELYRK 141
Cdd:PRK03918  254 KRK-LEEKIRELEERIEELKKEIeeLEEKVKeLKELKEKAEEYIK 297
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
15-150 4.19e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  15 ASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELEKVTEKLRRiqsnymALQRINQELE 94
Cdd:COG4717   119 EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEE------LLEQLSLATE 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1867158357  95 DKLYRMGQHYEE---EKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 150
Cdd:COG4717   192 EELQDLAEELEElqqRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 17-108 4.54e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  17 AADMEKLsaLQEQKgELRKRLSyttHKLEKLETEFDSTRHYLEIE----LRRAQEELEKVTEKLRRIQSNYMALQRiNQE 92
Cdd:PRK00409  536 AEEAEAL--LKEAE-KLKEELE---EKKEKLQEEEDKLLEEAEKEaqqaIKEAKKEADEIIKELRQLQKGGYASVK-AHE 608

                          90
                  ....*....|....*.
gi 1867158357  93 LEDKLYRMGQHYEEEK 108
Cdd:PRK00409  609 LIEARKRLNKANEKKE 624
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
21-94 4.81e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR-HYLEIELRRAQEELEKVTEKLRRIQSNYMALQR----INQELE 94
Cdd:PRK02224  613 EKREALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAeigaVENELE 691
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 26-98 6.21e-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: 6.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867158357  26 LQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYM-ALQRINQELEDKLY 98
Cdd:pfam03938  24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQqELQKKQQELLQPIQ 97
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 21-114 6.38e-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: 6.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357   21 EKLSALQEQKGEL-------RKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEE------LEKVTEKLRRIQSNYMALQ 87
Cdd:TIGR02169  896 AQLRELERKIEELeaqiekkRKRLSELKAKLEALEEELSE----IEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRALE 971

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1867158357   88 RIN----QELEDKLYRMGQhYEEEKRALSHE 114
Cdd:TIGR02169  972 PVNmlaiQEYEEVLKRLDE-LKEKRAKLEEE 1001
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 14-110 6.59e-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: 39.36  E-value: 6.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  14 AASAADMEKLSALQEQKGEL---RKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRIN 90
Cdd:COG4942   143 YLAPARREQAEELRADLAELaalRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222

                          90       100
                  ....*....|....*....|
gi 1867158357  91 QELEDKLYRMGQHYEEEKRA 110
Cdd:COG4942   223 EELEALIARLEAEAAAAAER 242
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
21-165 6.83e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 6.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETefDSTRHYLEIELRRAQEELEkvtEKLRRIQSNYMALQRINQELEdklyrm 100
Cdd:COG4717   439 EELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELR---ELAEEWAALKLALELLEEARE------ 507

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1867158357 101 gqHYEEEKR-ALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNlaaqllqcsqtyGRVHKVSEL 165
Cdd:COG4717   508 --EYREERLpPVLERASEYFSRLTDGRYRLIRIDEDLSLKVDTED------------GRTRPVEEL 559
FlgN pfam05130
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ...
 16-91 7.33e-03

FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.


Pssm-ID: 428323 [Multi-domain]  Cd Length: 140  Bit Score: 37.34  E-value: 7.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867158357  16 SAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI-ELRRAQEELEKVTEKLRRIQSNYMALQRINQ 91
Cdd:pfam05130  29 KAGDIEALEELTEEKQELLQKLAQLEKERRELLAELGLSPEEATLsELLAKEEEDPELRELWQELLELLERLKELNE 105
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 58-136 7.46e-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: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  58 LEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDklyrmgqhyeeekralshEIVALNSH--LLEAKvtIDKLSED 135
Cdd:cd22887     9 LEKRLAELEAELASLEEEIKDLEEELKEKNKANEILND------------------ELIALQIEnnLLEEK--LRKLQEE 68


                  .
gi 1867158357 136 N 136
Cdd:cd22887    69 N 69
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-126 7.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEiELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRM 100
Cdd:PRK03918  293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK 371

                          90       100
                  ....*....|....*....|....*.
gi 1867158357 101 GQHYEEEKRALSHEIVALNSHLLEAK 126
Cdd:PRK03918  372 EELERLKKRLTGLTPEKLEKELEELE 397
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 26-132 8.83e-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: 39.39  E-value: 8.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867158357   26 LQEqkgELRKRLSYTThKLEKLETEFDSTRHYLEielrraqEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQhYE 105
Cdd:pfam01576  477 LQE---ETRQKLNLST-RLRQLEDERNSLQEQLE-------EEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LE 544

                           90       100
                   ....*....|....*....|....*..
gi 1867158357  106 EEKRALSHEIVALNSHLLEAKVTIDKL 132
Cdd:pfam01576  545 EGKKRLQRELEALTQQLEEKAAAYDKL 571
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 20-76 9.15e-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: 9.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1867158357  20 MEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKL 76
Cdd:COG1579   116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
 20-76 9.24e-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: 9.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1867158357  20 MEKLSALQEQKGELRKRLSytTHKLEKLETEFDSTRHYLEiELRRAQEELEKVTEKL 76
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH