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Conserved domains on  [gi|1046888608|ref|XP_006239372|]
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kazrin isoform X2 [Rattus norvegicus]

Protein Classification

SAM domain-containing protein( domain architecture ID 10175987)

SAM (sterile alpha motif) domain-containing protein may be involved in protein-protein interaction and in developmental regulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 630-701 4.81e-43

SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


:

Pssm-ID: 188969  Cd Length: 72  Bit Score: 149.90  E-value: 4.81e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046888608 630 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSTVF 701
Cdd:cd09570     1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 465-534 7.25e-38

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


:

Pssm-ID: 188963  Cd Length: 70  Bit Score: 135.27  E-value: 7.25e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 465 MSHWKAGTVQAWLEVVMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRDAE 534
Cdd:cd09564     1 MSRWKADMVLAWLEVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEEYRDPE 70
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 544-608 2.47e-34

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


:

Pssm-ID: 188966  Cd Length: 65  Bit Score: 125.21  E-value: 2.47e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046888608 544 DLDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 608
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-274 1.33e-09

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  42 NLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQhGAQVLLREEVVQLQEEVHLLRQMKEML 121
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 122 AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR- 200
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRa 394

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888608 201 --NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 274
Cdd:COG1196   395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
 
Name Accession Description Interval E-value
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 630-701 4.81e-43

SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188969  Cd Length: 72  Bit Score: 149.90  E-value: 4.81e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046888608 630 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSTVF 701
Cdd:cd09570     1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 465-534 7.25e-38

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188963  Cd Length: 70  Bit Score: 135.27  E-value: 7.25e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 465 MSHWKAGTVQAWLEVVMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRDAE 534
Cdd:cd09564     1 MSRWKADMVLAWLEVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEEYRDPE 70
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 544-608 2.47e-34

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188966  Cd Length: 65  Bit Score: 125.21  E-value: 2.47e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046888608 544 DLDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 608
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 554-607 4.39e-10

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 56.12  E-value: 4.39e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046888608 554 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIELL 607
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-274 1.33e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  42 NLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQhGAQVLLREEVVQLQEEVHLLRQMKEML 121
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 122 AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR- 200
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRa 394

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888608 201 --NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 274
Cdd:COG1196   395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 553-607 6.98e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 52.68  E-value: 6.98e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1046888608  553 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 607
Cdd:smart00454  11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 38-274 4.87e-08

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: 56.99  E-value: 4.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   38 QEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENhqhgaqvlLREEVVQLQEEVHLLRQM 117
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------LEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  118 KEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDL---VSQMQQLYATLESREEQ 194
Cdd:TIGR02168  763 IEELEERLEEAE-------EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  195 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATD-------HAAALRSQLDLKDNRMKELEAELAMAKQ 267
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRR 915


                   ....*..
gi 1046888608  268 SLATLTK 274
Cdd:TIGR02168  916 ELEELRE 922
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 465-532 9.81e-08

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.60  E-value: 9.81e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046888608  465 MSHWKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRD 532
Cdd:smart00454   1 VSQWSPESVADWLES-IGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 466-531 3.19e-07

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 48.03  E-value: 3.19e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888608 466 SHWKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLElGLGVCSSLHRRKLRLAIEDYR 531
Cdd:pfam00536   1 DGWSVEDVGEWLES-IGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
631-693 9.12e-07

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.88  E-value: 9.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046888608 631 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEptFNAEAMAtALGIPSGKHilRRHL 693
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGITSVGH--RRKI 58
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 141-269 1.04e-05

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: 45.29  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 141 ELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLyatlesreeqlrdfirnyEQHRKESEDAVKALAKEK 220
Cdd:pfam20492  10 ELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL------------------EQKRQEAEEEKERLEESA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1046888608 221 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSL 269
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
99-274 2.65e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.73  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  99 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQ----GGKCSE----------VLSATELRVQLVQKEQELARAREALQAMK 164
Cdd:PRK02224  416 ELREERDELREREAELEATLRTARERVEEAEalleAGKCPEcgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 165 ADRKRLKgektDLVSQMQQLyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAAL 244
Cdd:PRK02224  496 ERLERAE----DLVEAEDRI-ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570

                         170       180       190
                  ....*....|....*....|....*....|
gi 1046888608 245 RSqldlkdnRMKELEAELAMAKQSLATLTK 274
Cdd:PRK02224  571 RE-------EVAELNSKLAELKERIESLER 593
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 631-690 3.02e-04

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 39.59  E-value: 3.02e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  631 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTfnaEAMATALGIPSGKHILR 690
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGITKLGHRKK 57
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 145-273 3.85e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.05  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 145 QLVQKEQELARAREALQAMKAdRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHR---KESEDAVKA-LAKEK 220
Cdd:cd22656    95 EILELIDDLADATDDEELEEA-KKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQtalETLEKALKDlLTDEG 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046888608 221 DLLEREKWE-LRRQAKEAT-DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLT 273
Cdd:cd22656   174 GAIARKEIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
 
Name Accession Description Interval E-value
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 630-701 4.81e-43

SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188969  Cd Length: 72  Bit Score: 149.90  E-value: 4.81e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046888608 630 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSTVF 701
Cdd:cd09570     1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 465-534 7.25e-38

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188963  Cd Length: 70  Bit Score: 135.27  E-value: 7.25e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 465 MSHWKAGTVQAWLEVVMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRDAE 534
Cdd:cd09564     1 MSRWKADMVLAWLEVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEEYRDPE 70
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 544-608 2.47e-34

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188966  Cd Length: 65  Bit Score: 125.21  E-value: 2.47e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046888608 544 DLDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 608
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 630-700 8.87e-24

SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188968  Cd Length: 72  Bit Score: 95.22  E-value: 8.87e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046888608 630 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSTV 700
Cdd:cd09569     1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQL 71
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 638-696 1.80e-21

SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188895  Cd Length: 62  Bit Score: 88.37  E-value: 1.80e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046888608 638 RVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEE 696
Cdd:cd09496     1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETE 59
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 472-529 1.48e-20

SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188893  Cd Length: 58  Bit Score: 85.74  E-value: 1.48e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046888608 472 TVQAWLEVVMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIED 529
Cdd:cd09494     1 RVCAWLEDFGLMPMYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 549-608 3.72e-20

SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188894  Cd Length: 60  Bit Score: 84.51  E-value: 3.72e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 549 WVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 608
Cdd:cd09495     1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 630-698 8.10e-20

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 83.91  E-value: 8.10e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046888608 630 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMS 698
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFN 69
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 544-607 1.14e-17

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188965  Cd Length: 63  Bit Score: 77.73  E-value: 1.14e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046888608 544 DLDHHWVAKaWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEkHLNVSKKFHQVSILLGIELL 607
Cdd:cd09566     1 KLDTHWVLR-WLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVL 62
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 466-529 3.58e-14

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 67.97  E-value: 3.58e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046888608 466 SHWKAGTVQAWLEVVMAMPM-YVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIED 529
Cdd:cd09562     2 ALWNGPTVVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 66
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 545-607 1.95e-13

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 65.57  E-value: 1.95e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046888608 545 LDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 607
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 554-607 4.39e-10

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 56.12  E-value: 4.39e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046888608 554 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIELL 607
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 468-529 4.69e-10

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 56.08  E-value: 4.69e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046888608 468 WKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIED 529
Cdd:cd09563     4 WSTEQVCDWLAE-LGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-274 1.33e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  42 NLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQhGAQVLLREEVVQLQEEVHLLRQMKEML 121
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 122 AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR- 200
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRa 394

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888608 201 --NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 274
Cdd:COG1196   395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 553-607 6.98e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 52.68  E-value: 6.98e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1046888608  553 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 607
Cdd:smart00454  11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
100-276 1.49e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.39  E-value: 1.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  100 LREEVVQLQEEVHLLRQMKEmLAKDLEESQGGKcsEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLvs 179
Cdd:COG4913    240 AHEALEDAREQIELLEPIRE-LAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  180 qmQQLYATLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELE 259
Cdd:COG4913    315 --EARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386

                          170
                   ....*....|....*..
gi 1046888608  260 AELAMAKQSLATLTKDV 276
Cdd:COG4913    387 AEAAALLEALEEELEAL 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 38-274 4.87e-08

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: 56.99  E-value: 4.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   38 QEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENhqhgaqvlLREEVVQLQEEVHLLRQM 117
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------LEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  118 KEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDL---VSQMQQLYATLESREEQ 194
Cdd:TIGR02168  763 IEELEERLEEAE-------EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  195 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATD-------HAAALRSQLDLKDNRMKELEAELAMAKQ 267
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRR 915


                   ....*..
gi 1046888608  268 SLATLTK 274
Cdd:TIGR02168  916 ELEELRE 922
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
102-276 7.84e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 7.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 102 EEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQM 181
Cdd:COG4372     6 EKVGKARLSLFGLRPKTGILIAALSEQLR---KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 182 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKekdlLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAE 261
Cdd:COG4372    83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158

                         170
                  ....*....|....*
gi 1046888608 262 LAMAKQSLATLTKDV 276
Cdd:COG4372   159 LESLQEELAALEQEL 173
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 465-532 9.81e-08

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.60  E-value: 9.81e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046888608  465 MSHWKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRD 532
Cdd:smart00454   1 VSQWSPESVADWLES-IGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 141-275 1.71e-07

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: 53.00  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 141 ELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfIRNYEQhrkesedaVKALAKEK 220
Cdd:COG1579    28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKE--------YEALQKEI 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046888608 221 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 275
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-276 2.00e-07

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: 55.06  E-value: 2.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  100 LREEVVQLQEEVHLLRQMKEMLAKDL---------EESQGGKCSEVLSA-----TELRVQLVQKEQELARAREALQAMKA 165
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQIsalrkdlarLEAEVEQLEERIAQlskelTELEAEIEELEERLEEAEEELAEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  166 DRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAT---- 238
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeie 862

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1046888608  239 ---DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 276
Cdd:TIGR02168  863 eleELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 466-531 3.19e-07

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 48.03  E-value: 3.19e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888608 466 SHWKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLElGLGVCSSLHRRKLRLAIEDYR 531
Cdd:pfam00536   1 DGWSVEDVGEWLES-IGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 141-276 4.05e-07

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: 53.91  E-value: 4.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  141 ELRVQLVQKEQELARAREALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 217
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888608  218 K-------EKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 276
Cdd:TIGR02168  768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 100-274 4.67e-07

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: 53.53  E-value: 4.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  100 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVS 179
Cdd:TIGR02169  700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  180 QMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHAAALRSQLDLK 251
Cdd:TIGR02169  780 ALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859

                          170       180
                   ....*....|....*....|...
gi 1046888608  252 DNRMKELEAELAMAKQSLATLTK 274
Cdd:TIGR02169  860 NGKKEELEEELEELEAALRDLES 882
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 102-278 4.97e-07

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: 52.84  E-value: 4.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 102 EEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQM 181
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKK-------EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 182 QQLYATLESREEQLRDFIRNYEQHRKESEDAV---------------------KALAKEKDLLEREKWELRRQAKEATDH 240
Cdd:COG4942    93 AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1046888608 241 AAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPK 278
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 100-275 7.32e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 7.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHLLR-----QMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEK 174
Cdd:COG1196   218 LKEELKELEAELLLLKlreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 175 TDLVSQM---QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLK 251
Cdd:COG1196   298 ARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180
                  ....*....|....*....|....
gi 1046888608 252 DNRMKELEAELAMAKQSLATLTKD 275
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQ 401
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
631-693 9.12e-07

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.88  E-value: 9.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046888608 631 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEptFNAEAMAtALGIPSGKHilRRHL 693
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGITSVGH--RRKI 58
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-277 3.04e-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: 51.21  E-value: 3.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   83 DSAVATMENHQHGAQvllrEEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQA 162
Cdd:TIGR02168  273 RLEVSELEEEIEELQ----KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  163 MKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAA 242
Cdd:TIGR02168  349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1046888608  243 AlrsqldLKDNRMKELEAELAMAKQSLATLTKDVP 277
Cdd:TIGR02168  429 K------LEEAELKELQAELEELEEELEELQEELE 457
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
100-262 3.18e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 3.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  100 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCS----EVLSATELRV-----QLVQKEQELARAREA---LQAMKADR 167
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEIDVasaerEIAELEAELERLDASsddLAALEEQL 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  168 KRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDH----AAA 243
Cdd:COG4913    695 EELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVerelREN 770

                          170
                   ....*....|....*....
gi 1046888608  244 LRSQLDLKDNRMKELEAEL 262
Cdd:COG4913    771 LEERIDALRARLNRAEEEL 789
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
99-265 3.29e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 3.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   99 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKE-QELARAREALQAMKADRKRLKGEKTDL 177
Cdd:COG4913    292 LLEAELEELRAELARLEAELERLEARLDALRE-------ELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  178 VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKE 257
Cdd:COG4913    365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444


                   ....*...
gi 1046888608  258 LEAELAMA 265
Cdd:COG4913    445 LRDALAEA 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 20-271 4.13e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  20 EDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQHGAQVL 99
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHLLRQMKEML---------AKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRL 170
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLerlerleeeLEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 171 KGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQH---RKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQ 247
Cdd:COG1196   472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551

                         250       260
                  ....*....|....*....|....
gi 1046888608 248 LDLKDNRMKELEAELAMAKQSLAT 271
Cdd:COG1196   552 VVEDDEVAAAAIEYLKAAKAGRAT 575
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 9-219 4.14e-06

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: 49.76  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   9 MDAQAKILSMMEDNKQLALR----IDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVtvads 84
Cdd:COG4942    36 IAELEKELAALKKEEKALLKqlaaLERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL----- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  85 AVATMENHQHGAQVLLR-EEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsevlsatELRVQLVQKEQELARAREALQAM 163
Cdd:COG4942   111 RALYRLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELR-----------ADLAELAALRAELEAERAELEAL 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888608 164 KADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 219
Cdd:COG4942   180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 552-605 4.97e-06

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 44.15  E-value: 4.97e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046888608 552 KAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIE 605
Cdd:cd09487     3 AEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAIQ 55
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
102-273 7.63e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 7.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 102 EEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQM 181
Cdd:COG4717    88 EEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 182 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRM--KELE 259
Cdd:COG4717   163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALE 242

                         170
                  ....*....|....
gi 1046888608 260 AELAMAKQSLATLT 273
Cdd:COG4717   243 ERLKEARLLLLIAA 256
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 141-276 8.94e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 8.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  141 ELRVQLVQKEQELARAReaLQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQL---RDFIRNYEQHRKESEDAVKALA 217
Cdd:TIGR02168  217 ELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAELQELEEKLeelRLEVSELEEEIEELQKELYALA 294

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046888608  218 KEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 276
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 141-269 1.04e-05

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: 45.29  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 141 ELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLyatlesreeqlrdfirnyEQHRKESEDAVKALAKEK 220
Cdd:pfam20492  10 ELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL------------------EQKRQEAEEEKERLEESA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1046888608 221 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSL 269
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
100-270 1.44e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVS 179
Cdd:COG4372    64 LEEELEQARSELEQLEEELEELNEQLQAAQA-------ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 180 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAK-EKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKEL 258
Cdd:COG4372   137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216

                         170
                  ....*....|..
gi 1046888608 259 EAELAMAKQSLA 270
Cdd:COG4372   217 AEELLEAKDSLE 228
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 100-365 2.08e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKEQELARAREALQAMKADRKRlKGEKTDLVS 179
Cdd:COG3883    35 AQAELDALQAELEELNEEYNELQAELEALQA-------EIDKLQAEIAEAEAEIEERREELGERARALYR-SGGSVSYLD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 180 QM--QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKE 257
Cdd:COG3883   107 VLlgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 258 LEAELAMAKQSLATL--TKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQAVRVSPCH 335
Cdd:COG3883   187 LSAEEAAAEAQLAELeaELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266

                         250       260       270
                  ....*....|....*....|....*....|
gi 1046888608 336 SRQPSVISDASAAEGDRSSTPSDINSPRHR 365
Cdd:COG3883   267 AAAGAAGAGAAAASAAGGGAGGAGGGGGGG 296
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
141-276 2.15e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 141 ELRVQLVQKEQELARAREALQAMKADRKRLKGEKT--DLVSQMQQLYATLESREEQLRDfIRNYEQHRKESEDAVKALAK 218
Cdd:COG4717    92 ELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEA 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046888608 219 EKDLLEREKWELRRQAKEATDHAAA-LRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 276
Cdd:COG4717   171 ELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
99-274 2.65e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.73  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  99 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQ----GGKCSE----------VLSATELRVQLVQKEQELARAREALQAMK 164
Cdd:PRK02224  416 ELREERDELREREAELEATLRTARERVEEAEalleAGKCPEcgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 165 ADRKRLKgektDLVSQMQQLyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAAL 244
Cdd:PRK02224  496 ERLERAE----DLVEAEDRI-ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570

                         170       180       190
                  ....*....|....*....|....*....|
gi 1046888608 245 RSqldlkdnRMKELEAELAMAKQSLATLTK 274
Cdd:PRK02224  571 RE-------EVAELNSKLAELKERIESLER 593
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
141-263 2.96e-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: 2.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  141 ELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLvSQMQQLY------ATLESREEQLRDFIRNYEqhrkESEDAVK 214
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSwdeidvASAEREIAELEAELERLD----ASSDDLA 688

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1046888608  215 ALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELA 263
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
100-287 3.44e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkcSEVLSATElrvQLVQKEQELARAREALQAMKADRKRLKGEKTDLVS 179
Cdd:COG4372    43 LQEELEQLREELEQAREELEQLEEELEQAR----SELEQLEE---ELEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 180 QMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAalrsqldlkDNRMK 256
Cdd:COG4372   116 ELEELqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA---------EQALD 186

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1046888608 257 ELEAELAMAKQSLATLTKDVPKRHSLAMPGE 287
Cdd:COG4372   187 ELLKEANRNAEKEEELAEAEKLIESLPRELA 217
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
143-276 4.12e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 4.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  143 RVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQmQQLYATLESREEQLRDfIRNYEQHRKESEDAVKALAKEKDL 222
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEID-VASAEREIAELEAELERLDASSDD 686

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1046888608  223 LErekwELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 276
Cdd:COG4913    687 LA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 553-613 4.63e-05

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 42.30  E-value: 4.63e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046888608 553 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLYQVNFS 613
Cdd:cd09505    12 TWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELKMKSDS 72
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 10-389 5.87e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  10 DAQAKILSMmedNKQLAlRIDGAVQSASQEVTNLRAELTATNRRLAElsgggggpgsgpgaatsasaaavtvadsavatm 89
Cdd:COG3883    34 AAQAELDAL---QAELE-ELNEEYNELQAELEALQAEIDKLQAEIAE--------------------------------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  90 enhqhgaqvlLREEVVQLQEEV-HLLRQMKEmlakdlEESQGGKCSEVLSATEL-----RVQLVQKEQElaRAREALQAM 163
Cdd:COG3883    77 ----------AEAEIEERREELgERARALYR------SGGSVSYLDVLLGSESFsdfldRLSALSKIAD--ADADLLEEL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 164 KADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfirnYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAA 243
Cdd:COG3883   139 KADKAELEAKKAELEAKLAELEALKAELEAAKAE----LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 244 LRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHP 323
Cdd:COG3883   215 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGG 294

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888608 324 ADRQAVRVSPCHSRQPSVISDASAAEGDRSSTPSDINSPRHRTHSLCNGDSPGPVQKSLHNPIVQS 389
Cdd:COG3883   295 GGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSS 360
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 107-284 6.64e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.35  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 107 LQEEVHLLRQMKE----MLAK------DLEESQGGKCSEV------LSATELRVQLVQKEQE--LARAREALQAMKADRK 168
Cdd:pfam10174 343 LQTEVDALRLRLEekesFLNKktkqlqDLTEEKSTLAGEIrdlkdmLDVKERKINVLQKKIEnlQEQLRDKDKQLAGLKE 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 169 RLKGEKTDlVSQMQQLYATLES---------------REEQLRDFIRNYEQHRKESEDAvkalaKEK-DLLEREKWELRR 232
Cdd:pfam10174 423 RVKSLQTD-SSNTDTALTTLEEalsekeriierlkeqREREDRERLEELESLKKENKDL-----KEKvSALQPELTEKES 496

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046888608 233 QAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAM 284
Cdd:pfam10174 497 SLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 139-272 6.68e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 6.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 139 ATELRVQLVQKEQELARAReaLQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDA------ 212
Cdd:COG1196   215 YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeye 292

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046888608 213 ----VKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATL 272
Cdd:COG1196   293 llaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
100-235 8.61e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 8.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkCSEVLSATELRV-QLVQKEQELARAREALQAMKADRKRLKGEKTDLV 178
Cdd:COG4717   107 LEAELEELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLeELEERLEELRELEEELEELEAELAELQEELEELL 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046888608 179 SQ----MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAK 235
Cdd:COG4717   184 EQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 145-299 8.74e-05

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: 46.17  E-value: 8.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 145 QLVQKEQELARAREALQamKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA-KEKDLL 223
Cdd:TIGR04523 422 ELLEKEIERLKETIIKN--NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKsKEKELK 499

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046888608 224 E--REKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLtKDVPKRHSLampgETVLNGNQEWVVQ 299
Cdd:TIGR04523 500 KlnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-DFELKKENL----EKEIDEKNKEIEE 572
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 102-272 1.26e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.73  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  102 EEVVQLQEEVHLLrqmkemLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQm 181
Cdd:pfam02463  278 EKEKKLQEEELKL------LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK- 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  182 qqlYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQA----KEATDHAAALRSQLDLKDNRMKE 257
Cdd:pfam02463  351 ---REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKseeeKEAQLLLELARQLEDLLKEEKKE 427

                          170
                   ....*....|....*
gi 1046888608  258 LEAELAMAKQSLATL 272
Cdd:pfam02463  428 ELEILEEEEESIELK 442
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
100-262 1.26e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCS-EVLSAT--ELRVQLVQKEQELARAREALQAMKADRKRLKGEKTD 176
Cdd:PRK02224  218 LDEEIERYEEQREQARETRDEADEVLEEHEERREElETLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 177 LVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRS 246
Cdd:PRK02224  298 LLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377

                         170
                  ....*....|....*.
gi 1046888608 247 QLDLKDNRMKELEAEL 262
Cdd:PRK02224  378 AVEDRREEIEELEEEI 393
PTZ00121 PTZ00121
MAEBL; Provisional
 96-261 1.86e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   96 AQVLLREEVVQLQEEVHLLRQMKEmlAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKT 175
Cdd:PTZ00121  1548 ADELKKAEELKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  176 DLVSQMQQLYATLESREEQLrdfIRNYEQHRKESEDAVKALAKEKDLLEREK---WELRRQAKEATDHAAALRSQLD--L 250
Cdd:PTZ00121  1626 KKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKkkaEEAKKAEEDEKKAAEALKKEAEeaK 1702

                          170
                   ....*....|.
gi 1046888608  251 KDNRMKELEAE 261
Cdd:PTZ00121  1703 KAEELKKKEAE 1713
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
100-271 2.12e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsEVLSATElrvqlvQKEQELARAREALQAMKADRKRLKGEKTDLVS 179
Cdd:PRK02224  211 LESELAELDEEIERYEEQREQARETRDEAD-----EVLEEHE------ERREELETLEAEIEDLRETIAETEREREELAE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 180 QMQQLYATLESREEQLRDFIRNYEQHRKESEdavkALAKEKDLLEREKWELRR--------------QAKEATDHAAALR 245
Cdd:PRK02224  280 EVRDLRERLEELEEERDDLLAEAGLDDADAE----AVEARREELEDRDEELRDrleecrvaaqahneEAESLREDADDLE 355

                         170       180
                  ....*....|....*....|....*.
gi 1046888608 246 SQLDLKDNRMKELEAELAMAKQSLAT 271
Cdd:PRK02224  356 ERAEELREEAAELESELEEAREAVED 381
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-277 2.14e-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: 45.06  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   33 VQSASQEVTNLRAELTATNRRLAELSGGGGGPGSgpgaatsasaaavtvadsAVATMENHQHGAQVllrEEVVQLQEEVH 112
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEE------------------ALNDLEARLSHSRI---PEIQAELSKLE 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  113 LLRQMKEMLAKDLEESqggkcsevLSATELRVQLVQKE-QELARAREALQAMKADRKRlkgEKTDLVSQMQQLYATLESR 191
Cdd:TIGR02169  805 EEVSRIEARLREIEQK--------LNRLTLEKEYLEKEiQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEEL 873

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  192 EEQLRDFirnyeqhrkesEDAVKALAKEKDLLEREKWELRRQAKEatdhaaaLRSQLDLKDNRMKELEAELAMAKQSLAT 271
Cdd:TIGR02169  874 EAALRDL-----------ESRLGDLKKERDELEAQLRELERKIEE-------LEAQIEKKRKRLSELKAKLEALEEELSE 935


                   ....*.
gi 1046888608  272 LTKDVP 277
Cdd:TIGR02169  936 IEDPKG 941
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 547-607 2.32e-04

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 40.09  E-value: 2.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046888608 547 HHWVAK---AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 607
Cdd:cd09507     3 TNWTTEevgAWLESLQLGEYRDIFARNDIRGSELLHLERRDL-KDLGITKVGHVKRILQAIKDL 65
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
150-266 2.59e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 43.28  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 150 EQELARAREALQAMKADRKRLKgektdlvSQMQQLYATLESREEQLRDFIrnyeqhRKESEDAVKALAKEKDLLEREKWE 229
Cdd:COG1842    36 EEDLVEARQALAQVIANQKRLE-------RQLEELEAEAEKWEEKARLAL------EKGREDLAREALERKAELEAQAEA 102

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1046888608 230 LRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAK 266
Cdd:COG1842   103 LEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLK 139
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
100-278 2.90e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHLLRQMKEMLA-----KDLEESQGGKCSEVLSATELRV-QLVQKEQELARAREALQAMKADRK---RL 170
Cdd:PRK03918  219 LREELEKLEKEVKELEELKEEIEelekeLESLEGSKRKLEEKIRELEERIeELKKEIEELEEKVKELKELKEKAEeyiKL 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 171 KGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQhRKESEDAVKALAKEKDLLEREKWELRRQAKEATDhAAALRSQLD- 249
Cdd:PRK03918  299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELEr 376

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1046888608 250 ----LKDNRMKELEAELAMAKQSLATLTKDVPK 278
Cdd:PRK03918  377 lkkrLTGLTPEKLEKELEELEKAKEEIEEEISK 409
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 631-690 3.02e-04

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 39.59  E-value: 3.02e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  631 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTfnaEAMATALGIPSGKHILR 690
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGITKLGHRKK 57
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
125-276 3.40e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 125 LEESQGGKCSEVLSATE-LRVQLVQKEQELARAREALQAMKADRK--RLKGEKTDLVSQMQQL---YATLESREEQLRDF 198
Cdd:COG3206   162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELesqLAEARAELAEAEAR 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046888608 199 IRNYEQHRKESEDAVKALAKEKDLLErekweLRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 276
Cdd:COG3206   242 LAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 143-276 4.47e-04

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 43.52  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 143 RVQLVQKEQELARAREALQAMKADRKRLkgekTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDL 222
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGL----TRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046888608 223 LEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 276
Cdd:pfam19220 123 LERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQEN 176
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 547-607 4.47e-04

SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK-delta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. In particular DGK-delta is involved in the regulation of clathrin-dependent endocytosis. The SAM domain of DGK-delta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-eta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it inhibits the translocation of the protein to the plasma membrane from the cytoplasm. The SAM domain also can bind Zn at multiple (not conserved) sites driving the formation of highly ordered large sheets of polymers, thus suggesting that Zn may play important role in the function of DCK-delta.


Pssm-ID: 188974  Cd Length: 65  Bit Score: 39.16  E-value: 4.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046888608 547 HHWVAK---AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 607
Cdd:cd09575     3 HLWGTEevaAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 100-277 4.68e-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: 43.90  E-value: 4.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  100 LREEVVQLQEEVHLLRQMKEMLAKDleesqggkcsevlsATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVS 179
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKE--------------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  180 QMQQLYATLESREEQLrdfirnyeqhrKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELE 259
Cdd:TIGR02169  421 ELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489

                          170
                   ....*....|....*...
gi 1046888608  260 AELAMAKQSLATLTKDVP 277
Cdd:TIGR02169  490 RELAEAEAQARASEERVR 507
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
100-264 5.49e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSatELRVQLVQKEQELARARE----------ALQAMKAD-RK 168
Cdd:COG3206   228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSArytpnhpdviALRAQIAAlRA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 169 RLKGEKTDLVSQMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKALAKEKDlLEREkwelrrqakeatdhAAALRSQL 248
Cdd:COG3206   306 QLQQEAQRILASLEAELEALQAREASLQ---AQLAQLEARLAELPELEAELRR-LERE--------------VEVARELY 367

                         170
                  ....*....|....*.
gi 1046888608 249 DLKDNRMKELEAELAM 264
Cdd:COG3206   368 ESLLQRLEEARLAEAL 383
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 553-610 6.77e-04

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.


Pssm-ID: 188932  Cd Length: 58  Bit Score: 38.45  E-value: 6.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046888608 553 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIellYQV 610
Cdd:cd09533     4 DWLSSLGLPQYEDQFIENGITGDVLVALDHEDL-KEMGITSVGHRLTILKAV---YEL 57
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 115-275 6.79e-04

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: 43.24  E-value: 6.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  115 RQMKEMLAKDlEESQGGKCSEVLSATELRvQLVQKEQELARAREALQamkadrKRLKGEkTDLVSQMQQLYATLESREEQ 194
Cdd:pfam01576    2 RQEEEMQAKE-EELQKVKERQQKAESELK-ELEKKHQQLCEEKNALQ------EQLQAE-TELCAEAEEMRARLAARKQE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  195 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEatDHAAALRSQLD--LKDNRMKELEAELAMAKQSLATL 272
Cdd:pfam01576   73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEkvTTEAKIKKLEEDILLLEDQNSKL 150


                   ...
gi 1046888608  273 TKD 275
Cdd:pfam01576  151 SKE 153
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
96-243 8.14e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 8.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   96 AQVLLREEVVQLQEEVHLLRQMKEMLAKDLEE------SQGGKCSEVLSA--TELRVQLVQKEQELARAREALQAMKADR 167
Cdd:COG4913    296 ELEELRAELARLEAELERLEARLDALREELDEleaqirGNGGDRLEQLEReiERLERELEERERRRARLEALLAALGLPL 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  168 KRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKW-------ELRRQAKEATDH 240
Cdd:COG4913    376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDALAEALGL 455


                   ...
gi 1046888608  241 AAA 243
Cdd:COG4913    456 DEA 458
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-233 8.87e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 8.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   38 QEVTNLRAELTATNRRLAELsgggggpgsgpgaatsasaaavtvaDSAVATMENHQHGAQVLL-----REEVVQLQEEVH 112
Cdd:COG4913    617 AELAELEEELAEAEERLEAL-------------------------EAELDALQERREALQRLAeyswdEIDVASAEREIA 671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  113 LLRQMKEmlakDLEESQggkcSEVlsaTELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESRE 192
Cdd:COG4913    672 ELEAELE----RLDASS----DDL---AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1046888608  193 EQLRDFIRNY--EQHRKESEDAV-----KALAKEKDLLEREKWELRRQ 233
Cdd:COG4913    741 DLARLELRALleERFAAALGDAVerelrENLEERIDALRARLNRAEEE 788
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 473-529 1.10e-03

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 37.60  E-value: 1.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046888608 473 VQAWLEVVmAMPMYVKACAENVKSGKVLLSLSDEDLElGLGVCSSLHRRKLRLAIED 529
Cdd:cd09487     2 VAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 142-277 1.39e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 142 LRVQLVQKEQELARAREALQAMKADRKRLKGEKtDLVSQmqqlyatleSREEQLRDFIrnyEQHRKESEDAvkalakekd 221
Cdd:COG0542   402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ-DEASF---------ERLAELRDEL---AELEEELEAL--------- 459

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888608 222 lleREKWElrrQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 277
Cdd:COG0542   460 ---KARWE---AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 25-277 1.47e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  25 LALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQHGAQVL----- 99
Cdd:COG4942     7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaela 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 -LREEVVQLQEEvhlLRQMKEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAREALQAMKAdrkrlkgektdLV 178
Cdd:COG4942    87 eLEKEIAELRAE---LEAQKEELAELLRALY-------RLGRQPPLALLLSPEDFLDAVRRLQYLKY-----------LA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 179 SQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKEL 258
Cdd:COG4942   146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225

                         250
                  ....*....|....*....
gi 1046888608 259 EAELAMAKQSLATLTKDVP 277
Cdd:COG4942   226 EALIARLEAEAAAAAERTP 244
PTZ00121 PTZ00121
MAEBL; Provisional
 96-261 1.52e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   96 AQVLLREEVVQLQEEVHLLRQMKEMLAKDL--EESQGGKCSEVLSATELR----------------VQLVQKEQELARAR 157
Cdd:PTZ00121  1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKkkveqlkkkeaeekkkAEELKKAEEENKIK 1662

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  158 EALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKA---LAKEKDLLEREKWELRRQA 234
Cdd:PTZ00121  1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA---KKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEA 1739

                          170       180
                   ....*....|....*....|....*..
gi 1046888608  235 KEATDHAAALRSQLDLKdNRMKELEAE 261
Cdd:PTZ00121  1740 EEDKKKAEEAKKDEEEK-KKIAHLKKE 1765
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 100-279 1.54e-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: 41.06  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKEQELARAREALqamKADRKRLKGEKT---- 175
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEAAKT-------ELEDLEKEIKRLELEIEEVEARI---KKYEEQLGNVRNnkey 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 176 -DLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELrrqakeatdhaaalrsqldlkDNR 254
Cdd:COG1579    92 eALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---------------------DEE 150

                         170       180
                  ....*....|....*....|....*
gi 1046888608 255 MKELEAELAMAKQSLATLTKDVPKR 279
Cdd:COG1579   151 LAELEAELEELEAEREELAAKIPPE 175
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 139-313 1.55e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.80  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 139 ATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNY-------EQHRKESED 211
Cdd:pfam07888  29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSrekheelEEKYKELSA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 212 AVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKD---NRMKE------------------LEAELAMAKQSLA 270
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEREtelERMKErakkagaqrkeeeaerkqLQAKLQQTEEELR 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1046888608 271 TLTKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQ 313
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
151-277 1.59e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 151 QELARAREALQAMKADRKRLKgEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRkesedAVKALAKEKDLLEREKWEL 230
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAEL 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1046888608 231 RRQAKEATDHAAALRSQLdlkdNRMKELEAELAMAKQSLATLTKDVP 277
Cdd:COG4717   145 PERLEELEERLEELRELE----EELEELEAELAELQEELEELLEQLS 187
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
101-262 1.66e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 101 REEVVQLQEEVHLLRQMKEMLAKDLEESqggkcsEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGE-----KT 175
Cdd:PRK02224  474 RERVEELEAELEDLEEEVEEVEERLERA------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEelrerAA 547

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 176 DLVSQMQQLYA---TLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLL------EREKWELRRQAKEATDHAAALRS 246
Cdd:PRK02224  548 ELEAEAEEKREaaaEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiadaEDEIERLREKREALAELNDERRE 627

                         170
                  ....*....|....*.
gi 1046888608 247 QLDLKDNRMKELEAEL 262
Cdd:PRK02224  628 RLAEKRERKRELEAEF 643
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 99-276 1.71e-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: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  99 LLREEVVQLQEEVHLLRQ---MKEMLAKDLE---ESQGGKCSEV-LSATELRVQLVQKEQELARAREALQAMKADRKRLK 171
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNqdsVKELIIKNLDntrESLETQLKVLsRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE 509

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 172 GEKTDLVSQMqqlyATLESREEQLRDFIRNYEQHRKESEDAVKAL--AKEKDLLEREKWELRRQAKEATDHAAALRSQLD 249
Cdd:TIGR04523 510 EKVKDLTKKI----SSLKEKIEKLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQE 585

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1046888608 250 LKDNRMKELEAE-------LAMAKQSLATLTKDV 276
Cdd:TIGR04523 586 EKQELIDQKEKEkkdlikeIEEKEKKISSLEKEL 619
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 634-687 1.80e-03

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 37.70  E-value: 1.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046888608 634 WTNQRVLKW-VRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKH 687
Cdd:cd09504     5 WTVEDTVEWlVNSVELPQYVEAFKENGVDGSALPRLAVNNPSFLTSVLGIKDPIH 59
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 141-273 1.89e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 41.25  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 141 ELRVQLVQKEQELARA---REALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHR----------K 207
Cdd:pfam00529  62 SAEAQLAKAQAQVARLqaeLDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiggisrE 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 208 ESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDN----RMKELEAELAMAKQSLATLT 273
Cdd:pfam00529 142 SLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlQIAEAEAELKLAKLDLERTE 211
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
102-227 2.38e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 102 EEVVQLQEEVHLLRQMKEMLAKDLEESqggkcSEVLSATELrvqlvqkEQELARAREALQAMKADRKRLKGEKTDLVSQM 181
Cdd:COG4717   395 EEYQELKEELEELEEQLEELLGELEEL-----LEALDEEEL-------EEELEELEEELEELEEELEELREELAELEAEL 462

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1046888608 182 QQL-----YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREK 227
Cdd:COG4717   463 EQLeedgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 100-259 2.45e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 41.28  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHL---LRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKE-----QELARAREALQAMKADRKRLK 171
Cdd:pfam07111 486 LREERNRLDAELQLsahLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESlasvgQQLEVARQGQQESTEEAASLR 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 172 GEKTdlvsQMQQLY--------ATLESR-EEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREK---WELRRQAKEATD 239
Cdd:pfam07111 566 QELT----QQQEIYgqalqekvAEVETRlREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKernQELRRLQDEARK 641

                         170       180
                  ....*....|....*....|
gi 1046888608 240 HAAALRSQldlkdnRMKELE 259
Cdd:pfam07111 642 EEGQRLAR------RVQELE 655
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
101-270 3.20e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 101 REEvvqLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSAT-------ELRVQLVQKEQELARAREALQAMKADRKRLKGE 173
Cdd:PRK02224  274 REE---LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEavearreELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 174 KTDLvsqmqqlyatlESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRR-------QAKEATDHAAALRS 246
Cdd:PRK02224  351 ADDL-----------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDFLEELRE 419

                         170       180
                  ....*....|....*....|....
gi 1046888608 247 QLDLKDNRMKELEAELAMAKQSLA 270
Cdd:PRK02224  420 ERDELREREAELEATLRTARERVE 443
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 554-592 3.53e-03

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.90  E-value: 3.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1046888608 554 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVS 592
Cdd:cd09501    12 WLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMS 50
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 22-315 3.55e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 3.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   22 NKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQHGAQVLLR 101
Cdd:TIGR00618  526 LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE 605

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  102 EEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQM 181
Cdd:TIGR00618  606 AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKM 685

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  182 QQLYATL--------------ESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQ 247
Cdd:TIGR00618  686 QSEKEQLtywkemlaqcqtllRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFN 765

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046888608  248 LDLK-------DNRMKELEAELAM---AKQSLATLTKDVPKRHSLAMP-GETVLNGNQEWVVQADLPLTAAIRQSQQTL 315
Cdd:TIGR00618  766 NNEEvtaalqtGAELSHLAAEIQFfnrLREEDTHLLKTLEAEIGQEIPsDEDILNLQCETLVQEEEQFLSRLEEKSATL 844
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
100-266 3.71e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 100 LREEVVQLQEEVHLLRQMKEMLAKDLEEsQGGKCSEVLSAT--ELRvQLVQKEQELARAREALQAMKADRKRLKGEKTDL 177
Cdd:PRK03918  554 LKKKLAELEKKLDELEEELAELLKELEE-LGFESVEELEERlkELE-PFYNEYLELKDAEKELEREEKELKKLEEELDKA 631

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 178 VSQMQQLYATLESREEQLRDFIRNY--EQHRKESEDAVKaLAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRM 255
Cdd:PRK03918  632 FEELAETEKRLEELRKELEELEKKYseEEYEELREEYLE-LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710

                         170
                  ....*....|..
gi 1046888608 256 KELEA-ELAMAK 266
Cdd:PRK03918  711 KELEKlEKALER 722
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 145-273 3.85e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.05  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 145 QLVQKEQELARAREALQAMKAdRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHR---KESEDAVKA-LAKEK 220
Cdd:cd22656    95 EILELIDDLADATDDEELEEA-KKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQtalETLEKALKDlLTDEG 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046888608 221 DLLEREKWE-LRRQAKEAT-DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLT 273
Cdd:cd22656   174 GAIARKEIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 93-250 4.72e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.71  E-value: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   93 QHGAQVLLREEVVQLQEEVHLLRQM------KEMLAKDLEESQGGKCSevlSATELRVQLVQKEQELARAREALQAMKAD 166
Cdd:COG3096    503 RYRSQQALAQRLQQLRAQLAELEQRlrqqqnAERLLEEFCQRIGQQLD---AAEELEELLAELEAQLEELEEQAAEAVEQ 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  167 RKRLKGEKTDLVSQMQQLYA------TLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREkwelrRQAKEATDH 240
Cdd:COG3096    580 RSELRQQLEQLRARIKELAArapawlAAQDALERLR------EQSGEALADSQEVTAAMQQLLERE-----REATVERDE 648

                          170
                   ....*....|
gi 1046888608  241 AAALRSQLDL 250
Cdd:COG3096    649 LAARKQALES 658
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 547-585 5.10e-03

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.


Pssm-ID: 188914  Cd Length: 70  Bit Score: 36.46  E-value: 5.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1046888608 547 HHW----VAKaWLNDIGLSQYSQAF-QNHLVDGRMLNSLMKRDL 585
Cdd:cd09515     2 HEWtcedVAK-WLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDL 44
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 141-274 5.22e-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: 40.39  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 141 ELRVQLVQKEQELararealqamkadrKRLKGEKTDLVSQMQQLyatlESREEQLRDFIRNYEQHRKESEDAVKALAKEK 220
Cdd:TIGR04523 360 EKQRELEEKQNEI--------------EKLKKENQSYKQEIKNL----ESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046888608 221 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 274
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 97-274 5.45e-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: 40.54  E-value: 5.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608   97 QVLLREEVVQLQEevhlLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAREALQAMKADRKRLKGEKTD 176
Cdd:pfam01576  193 EERLKKEEKGRQE----LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  177 LVSQMQQLYATLESR-------EEQLRDFIRNYEQHRKESEDAVKALAKEKDL---LEREKWELRRQAKEATDHAAALRS 246
Cdd:pfam01576  269 LEAQISELQEDLESEraarnkaEKQRRDLGEELEALKTELEDTLDTTAAQQELrskREQEVTELKKALEEETRSHEAQLQ 348

                          170       180
                   ....*....|....*....|....*....
gi 1046888608  247 QLDLKDNR-MKELEAELAMAKQSLATLTK 274
Cdd:pfam01576  349 EMRQKHTQaLEELTEQLEQAKRNKANLEK 377
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-208 6.77e-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: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  25 LALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPGAATSASAAAVTVADSAVATMENHQHGAQVLLREEV 104
Cdd:COG1196   653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 105 VQLQEEVHLLRQMKEMLAKDLEESQggkcsEVLSATELRVQLvqkeQELARAREALQA--MKADR--KRLKGEKTDLVSQ 180
Cdd:COG1196   733 EREELLEELLEEEELLEEEALEELP-----EPPDLEELEREL----ERLEREIEALGPvnLLAIEeyEELEERYDFLSEQ 803

                         170       180
                  ....*....|....*....|....*...
gi 1046888608 181 mqqlYATLESREEQLRDFIRNYEQHRKE 208
Cdd:COG1196   804 ----REDLEEARETLEEAIEEIDRETRE 827
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
554-607 7.09e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 35.71  E-value: 7.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046888608 554 WLNDIGLSQYSQAFQNHLVDG-RMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 607
Cdd:pfam07647  12 WLRSIGLEQYTDNFRDQGITGaELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 464-529 7.33e-03

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 35.85  E-value: 7.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888608 464 PMSHWKAGTVQAWLEvVMAMPMYVKACAENVKSGKVLLSLSDEDLElGLGVCSSLHRRKLRLAIED 529
Cdd:cd09507     1 PVTNWTTEEVGAWLE-SLQLGEYRDIFARNDIRGSELLHLERRDLK-DLGITKVGHVKRILQAIKD 64
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 87-262 8.52e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.81  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608  87 ATMENHQHgaqvlLREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSA--TELRVQLVQKEQE-LARAREALqam 163
Cdd:pfam10174  64 VTQEENQH-----LQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPelTEENFRRLQSEHErQAKELFLL--- 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 164 kadRKRLKGEKTDLVSQMQqlyaTLESREEQLRDFIRNYEQhrkesedavKALAKEkdlLEREKWELRRQAKEATDHAAA 243
Cdd:pfam10174 136 ---RKTLEEMELRIETQKQ----TLGARDESIKKLLEMLQS---------KGLPKK---SGEEDWERTRRIAEAEMQLGH 196

                         170
                  ....*....|....*....
gi 1046888608 244 LRSQLDLKDNRMKELEAEL 262
Cdd:pfam10174 197 LEVLLDQKEKENIHLREEL 215
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
138-271 9.05e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 9.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 138 SATELRVQLVQKEQE-----LARAREALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQlRDFIRNYEQHRKESEDA 212
Cdd:PRK02224  188 SLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELETLEAEIEDLRET 266

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888608 213 VKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKD-------NRMKELEAELAMAKQSLAT 271
Cdd:PRK02224  267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDadaeaveARREELEDRDEELRDRLEE 332
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 116-231 9.47e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 38.81  E-value: 9.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 116 QMKEMLAKDLEESQGgkCSEVLSATElrVQLVQKEQELARAREALQAMKADRKRLKGEKTDLVSQMQ-----------QL 184
Cdd:pfam02841 173 KAEEVLQEFLQSKEA--VEEAILQTD--QALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEaqersyqehvkQL 248

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1046888608 185 YATLES-REEQLRDFIRNYEQHRKESEDAVKA-LAKEKDLLEREKWELR 231
Cdd:pfam02841 249 IEKMEAeREQLLAEQERMLEHKLQEQEELLKEgFKTEAESLQKEIQDLK 297
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 547-577 9.57e-03

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 35.77  E-value: 9.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1046888608 547 HHWVAK---AWL-NDIGLSQYSQAFQNHLVDGRML 577
Cdd:cd09504     3 HNWTVEdtvEWLvNSVELPQYVEAFKENGVDGSAL 37
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 553-600 9.67e-03

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 35.37  E-value: 9.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1046888608 553 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSI 600
Cdd:cd09506    12 DWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTE-LGVTRVGHRMNI 58
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 134-224 9.75e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 37.96  E-value: 9.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888608 134 SEVLSATELRVQLVQKEQE-LARAREALQAMKADRKRLKGEKtdLVSQMQQLYATLESREEQLRDFIRNYEqhrkeseda 212
Cdd:pfam10368  57 DEALENVEEREELLEKEKEsIEEAKEEFKKIKEIIEEIEDEE--LKKEAEELIDAMEERYEAYDELYDAYK--------- 125

                          90
                  ....*....|..
gi 1046888608 213 vKALAKEKDLLE 224
Cdd:pfam10368 126 -KALELDKELYE 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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