NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958784821|ref|XP_038968914|]
View 

brain-enriched guanylate kinase-associated protein isoform X5 [Rattus norvegicus]

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];
10-149 2.50e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.37  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  10 AGRASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNymaLQRINQ 89
Cdd:COG4372    22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQA 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  90 ELEDKLYRMGQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 149
Cdd:COG4372    95 ELAQAQEELES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
10-149 2.50e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.37  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  10 AGRASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNymaLQRINQ 89
Cdd:COG4372    22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQA 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  90 ELEDKLYRMGQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 149
Cdd:COG4372    95 ELAQAQEELES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 19-139 8.09e-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: 49.28  E-value: 8.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821   19 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrm 98
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958784821   99 gQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 139
Cdd:TIGR02168  876 -EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-135 1.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  19 EKLSALQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELDKVTEKLRRIQSny 81
Cdd:PRK03918  563 KKLDELEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK-- 640

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958784821  82 mALQRINQELED--KLYRMGQHYEEEKRAMS---------HEIVALNSHLLEAKVTIDKLSEDNE 135
Cdd:PRK03918  641 -RLEELRKELEEleKKYSEEEYEELREEYLElsrelaglrAELEELEKRREEIKKTLEKLKEELE 704
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 27-140 3.21e-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: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  27 QKGELRKRLsytthklEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYE 103
Cdd:pfam20492   7 EKQELEERL-------KQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEA 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958784821 104 EEKRAMSHEIvalnshlLEAKVTIDKLSEDNElyRKD 140
Cdd:pfam20492  76 EEKEQLEAEL-------AEAQEEIARLEEEVE--RKE 103
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 39-156 4.68e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 42.29  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  39 THKLEKL-ETEFDSTRhylEIELRRAqeeLDKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIval 116
Cdd:cd07651    39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958784821 117 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 156
Cdd:cd07651   110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
10-149 2.50e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.37  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  10 AGRASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNymaLQRINQ 89
Cdd:COG4372    22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQA 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  90 ELEDKLYRMGQhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 149
Cdd:COG4372    95 ELAQAQEELES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 19-139 8.09e-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: 49.28  E-value: 8.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821   19 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrm 98
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958784821   99 gQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 139
Cdd:TIGR02168  876 -EALLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 7-116 2.70e-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: 46.68  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821   7 CVSAGRASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNYMALQR 86
Cdd:COG4942     8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEA 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958784821  87 INQELEDKLYRMGQHYEEEKRAMSHEIVAL 116
Cdd:COG4942    84 ELAELEKEIAELRAELEAQKEELAELLRAL 113
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
19-156 2.94e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  19 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLE---IELRRAQEELDKVTEKLRRIQSnymALQRINQELEDkl 95
Cdd:COG4372    52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQaaqAELAQAQEELESLQEEAEELQE---ELEELQKERQD-- 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958784821  96 yrmgqhYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNElyrkdcNLAAQLLQCSQTYGR 156
Cdd:COG4372   127 ------LEQQRKQLEAQIAELQSEIAEREEELKELEEQLE------SLQEELAALEQELQA 175
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
19-148 6.81e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 6.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821   19 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR------------HYLEIELRRAQEELDKVTEKLRRIQSNYMALQR 86
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQerrealqrlaeySWDEIDVASAEREIAELEAELERLDASSDDLAA 689

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958784821   87 INQELEdKLYRMGQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 148
Cdd:COG4913    690 LEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
19-140 8.23e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  19 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDstRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRM 98
Cdd:COG4717    95 EELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958784821  99 GQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKD 140
Cdd:COG4717   173 AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 19-162 8.55e-05

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 45.72  E-value: 8.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  19 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI-ELRRAQEELDKVTEKLRRIQSNYMALQR-INQELEDKLY 96
Cdd:COG5185   275 ESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLeEQLAAAEAEQELEESKRETETGIQNLTAeIEQGQESLTE 354

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958784821  97 RMGQHYEEEKRAMSHEIVALNSHLLE-AKVTIDKLSEDNELYRKDCNLAAQLL--QCSQTYGRVHKVSE 162
Cdd:COG5185   355 NLEAIKEEIENIVGEVELSKSSEELDsFKDTIESTKESLDEIPQNQRGYAQEIlaTLEDTLKAADRQIE 423
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-135 1.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  19 EKLSALQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELDKVTEKLRRIQSny 81
Cdd:PRK03918  563 KKLDELEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK-- 640

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958784821  82 mALQRINQELED--KLYRMGQHYEEEKRAMS---------HEIVALNSHLLEAKVTIDKLSEDNE 135
Cdd:PRK03918  641 -RLEELRKELEEleKKYSEEEYEELREEYLElsrelaglrAELEELEKRREEIKKTLEKLKEELE 704
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 3-101 1.45e-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: 44.37  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821   3 FPSSCVSAGRASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR----------HYLEIELRRAQEELDKVTE 72
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALErriaalarriRALEQELAALEAELAELEK 90

                          90       100
                  ....*....|....*....|....*....
gi 1958784821  73 KLRRIQSNYMALQRINQELEDKLYRMGQH 101
Cdd:COG4942    91 EIAELRAELEAQKEELAELLRALYRLGRQ 119
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 12-159 2.45e-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: 2.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821   12 RASAADMEKLS-ALQEQKG----------ELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSN 80
Cdd:TIGR02169  332 DKLLAEIEELErEIEEERKrrdklteeyaELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRE 407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821   81 YMALQRINQELEDKLyrmGQHYEEEKRAMShEIVALNSHLLEAKVTIDK-------LSEDNELYRKdcnlaaQLLQCSQT 153
Cdd:TIGR02169  408 LDRLQEELQRLSEEL---ADLNAAIAGIEA-KINELEEEKEDKALEIKKqewkleqLAADLSKYEQ------ELYDLKEE 477


                   ....*.
gi 1958784821  154 YGRVHK 159
Cdd:TIGR02169  478 YDRVEK 483
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 27-140 3.21e-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: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  27 QKGELRKRLsytthklEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYE 103
Cdd:pfam20492   7 EKQELEERL-------KQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEA 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958784821 104 EEKRAMSHEIvalnshlLEAKVTIDKLSEDNElyRKD 140
Cdd:pfam20492  76 EEKEQLEAEL-------AEAQEEIARLEEEVE--RKE 103
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 9-134 3.24e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 41.84  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821   9 SAGRASAADME-KLSALQEQ-------KGELRKRLSYTTHKLEKLETEfDSTRhylEIELRRAQEELDKVTEKLRRIQSN 80
Cdd:pfam08614  46 SPQSASIQSLEqLLAQLREElaelyrsRGELAQRLVDLNEELQELEKK-LRED---ERRLAALEAERAQLEEKLKDREEE 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958784821  81 YMALQRINQELEDklyrmgqhyeeekramshEIVALNSHLLEAKVTIDKLSEDN 134
Cdd:pfam08614 122 LREKRKLNQDLQD------------------ELVALQLQLNMAEEKLRKLEKEN 157
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 39-156 4.68e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 42.29  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  39 THKLEKL-ETEFDSTRhylEIELRRAqeeLDKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIval 116
Cdd:cd07651    39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958784821 117 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 156
Cdd:cd07651   110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 19-155 8.57e-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: 8.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821   19 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDstrhylEIELRRAQEELDKVTEKLRRI----QSNYMALQRINQELEDK 94
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKLEEALN------DLEARLSHSRIPEIQAELSKLeeevSRIEARLREIEQKLNRL 824

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958784821   95 LYRmgQHYEEEKRAmshEIVALNSHLLEAKVTI-DKLSEDN----ELYRKDCNLAAQLLQCSQTYG 155
Cdd:TIGR02169  825 TLE--KEYLEKEIQ---ELQEQRIDLKEQIKSIeKEIENLNgkkeELEEELEELEAALRDLESRLG 885
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 19-162 1.47e-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: 40.52  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  19 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleIELRRAQEEldkvteklRRIQSNYMALQRINQELEDKLYRM 98
Cdd:pfam14988  40 ELASRYTQQTAELQTQLLQKEKEQASLKKELQALRP---FAKLKESQE--------REIQDLEEEKEKVRAETAEKDREA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  99 GQHYEEEKRAMSHEIVALNSHLL-----------------EAKVTIDKLSEDneLYRKDCNLAAQLLQCSQTYGRVHKVS 161
Cdd:pfam14988 109 HLQFLKEKALLEKQLQELRILELgeratrelkrkaqalklAAKQALSEFCRS--IKRENRQLQKELLQLIQETQALEAIK 186


                  .
gi 1958784821 162 E 162
Cdd:pfam14988 187 S 187
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 21-153 1.58e-03

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


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 40.27  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  21 LSALQEQKGELRKRLSYTTHKLEKLETE-----------------FDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMA 83
Cdd:pfam15619   6 LSARLHKIKELQNELAELQSKLEELRKEnrllkrlqkrqekalgkYEGTESELPQLIARHNEEVRVLRERLRRLQEKERD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  84 LQRINQELEDKLYRMG---QHYEE--------EKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRK--DCNLAAQLLQC 150
Cdd:pfam15619  86 LERKLKEKEAELLRLRdqlKRLEKlsedknlaEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKsfRRQLAAEKKKH 165


                  ...
gi 1958784821 151 SQT 153
Cdd:pfam15619 166 KEA 168
mukB PRK04863
chromosome partition protein MukB;
14-112 1.72e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821   14 SAADMEKLSALQEQkgeLRKRLsytthklEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELED 93
Cdd:PRK04863   976 AAEMLAKNSDLNEK---LRQRL-------EQAEQERTRARE----QLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQ 1041

                           90       100
                   ....*....|....*....|.
gi 1958784821   94 KLYRMGQHY--EEEKRAMSHE 112
Cdd:PRK04863  1042 ELQDLGVPAdsGAEERARARR 1062
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 13-135 2.55e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821   13 ASAAdmEKLSALQEQKGELRKRLSYTthKLEKLETEFDStrhyLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELE 92
Cdd:TIGR02168  209 AEKA--ERYKELKAELRELELALLVL--RLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958784821   93 DKLyrmgQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNE 135
Cdd:TIGR02168  281 EEI----EELQKELYALANEISRLEQQKQILRERLANLERQLE 319
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
 18-74 3.08e-03

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


Pssm-ID: 465345 [Multi-domain]  Cd Length: 155  Bit Score: 38.82  E-value: 3.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958784821  18 MEKLSALQEQKGELRKRLSytTHKLEKLETEFDSTRHYLEiELRRAQEELDKVTEKL 74
Cdd:pfam17098  91 MAKCRLLQQENEELGRQLS--EGRIAKLEIELALQKKVVE-ELKKSLEELDEFLIEL 144
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 15-106 3.52e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  15 AADMEKLsaLQEQKgELRKRLSyttHKLEKLETEFDSTRHYLEIE----LRRAQEELDKVTEKLRRIQSNYMALQRiNQE 90
Cdd:PRK00409  536 AEEAEAL--LKEAE-KLKEELE---EKKEKLQEEEDKLLEEAEKEaqqaIKEAKKEADEIIKELRQLQKGGYASVK-AHE 608

                          90
                  ....*....|....*.
gi 1958784821  91 LEDKLYRMGQHYEEEK 106
Cdd:PRK00409  609 LIEARKRLNKANEKKE 624
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 12-110 3.55e-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: 40.13  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  12 RASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQEL 91
Cdd:COG4942   146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225

                          90
                  ....*....|....*....
gi 1958784821  92 EDKLYRMGQHYEEEKRAMS 110
Cdd:COG4942   226 EALIARLEAEAAAAAERTP 244
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
18-110 4.24e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  18 MEKLSALQEQKGELRKRLSYTTHKLEKLET---EFDSTRHYLE----IELRRAQEELDKVTEKLRRIQSNYMALQRINQE 90
Cdd:PRK03918  330 IKELEEKEERLEELKKKLKELEKRLEELEErheLYEEAKAKKEelerLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK 409

                          90       100
                  ....*....|....*....|
gi 1958784821  91 LEDKLYRMGQHYEEEKRAMS 110
Cdd:PRK03918  410 ITARIGELKKEIKELKKAIE 429
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
26-139 4.62e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  26 EQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRMgQHYEEE 105
Cdd:PRK03918  549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKEL-KKLEEE 627

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958784821 106 KRAMSHEIVALNSHLLEAKVTIDKLSE--DNELYRK 139
Cdd:PRK03918  628 LDKAFEELAETEKRLEELRKELEELEKkySEEEYEE 663
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-149 6.21e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  19 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLyrm 98
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERR--- 311

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958784821  99 gQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 149
Cdd:COG1196   312 -RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
19-136 7.08e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 7.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  19 EKLSALQEQKGELRKRLSYTTHKLEKLETefDSTRHYLEIELRRAQEELdkvTEKLRRIQSNYMALQRINQELEdklyrm 98
Cdd:COG4717   439 EELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAEL---RELAEEWAALKLALELLEEARE------ 507

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958784821  99 gqHYEEEKR-AMSHEIVALNSHLLEAKVTIDKLSEDNEL 136
Cdd:COG4717   508 --EYREERLpPVLERASEYFSRLTDGRYRLIRIDEDLSL 544
Tup_N pfam08581
Tup N-terminal; The N-terminal domain of the Tup protein has been shown to interact with the ...
 42-113 7.09e-03

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: 35.95  E-value: 7.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958784821  42 LEKLETEFDS-TRHYLEIELRRaqEELDkvteklRRIQSNYMALQRINQ---ELEDKLYRMGQHYEEEKRAMSHEI 113
Cdd:pfam08581   6 LDAIKQEFDNlSQEANSYKAQR--DEYE------HKINQQINELQQIRQtlyELERAHRKIKQQYEEEIARLKAEL 73
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 10-96 7.20e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.17  E-value: 7.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  10 AGRASAADMEKLSalQEQKGELRKRlsytTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYM-ALQRIN 88
Cdd:pfam03938  16 EGKAAQAQLEKKF--KKRQAELEAK----QKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQqELQKKQ 89


                  ....*...
gi 1958784821  89 QELEDKLY 96
Cdd:pfam03938  90 QELLQPIQ 97
PRK01156 PRK01156
chromosome segregation protein; Provisional
 14-139 7.34e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.50  E-value: 7.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  14 SAADMEklsALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELED 93
Cdd:PRK01156  578 SLIDIE---TNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDN 654

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958784821  94 KLYRMGQHYEEEKR--AMSHEIVALNSHLLEAKVTIDKLSEDneLYRK 139
Cdd:PRK01156  655 YKKQIAEIDSIIPDlkEITSRINDIEDNLKKSRKALDDAKAN--RARL 700
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 19-150 7.40e-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: 7.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821   19 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLeiELRRAQEELdKVTEKLRRIQSNYMALQRINQELEDkLYRM 98
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ--ALLKEKREY-EGYELLKEKEALERQKEAIERQLAS-LEEE 252

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958784821   99 GQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSED--NELYRKDCNLAAQLLQC 150
Cdd:TIGR02169  253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqLRVKEKIGELEAEIASL 306
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
10-134 8.55e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 8.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  10 AGRASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEF-----DSTRHYLEIELRRAQEELDKVTEKLRRIQSnymAL 84
Cdd:COG4717   379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeelleALDEEELEEELEELEEELEELEEELEELRE---EL 455

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  85 QRINQELE--------DKLYRMGQHYEEEKRAMSHEIVALN--SHLLEAkvTIDKLSEDN 134
Cdd:COG4717   456 AELEAELEqleedgelAELLQELEELKAELRELAEEWAALKlaLELLEE--AREEYREER 513
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
12-148 9.40e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784821  12 RASAADMEKLSALQE---QKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELDKVTEKLRRiqsnymALQRIN 88
Cdd:COG4717   115 REELEKLEKLLQLLPlyqELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEE------LLEQLS 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958784821  89 QELEDKLYRMGQHYEE---EKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 148
Cdd:COG4717   188 LATEEELQDLAEELEElqqRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
 
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