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Conserved domains on  [gi|1907157322|ref|XP_036020338|]
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kazrin isoform X8 [Mus musculus]

Protein Classification

SAM domain-containing protein; ACK family non-receptor tyrosine-protein kinase( domain architecture ID 10175987)

SAM (sterile alpha motif) domain-containing protein may be involved in protein-protein interaction and in developmental regulation| ACK (activated Cdc42-associated kinase) family non-receptor tyrosine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates; such as TNK1

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 ...
 601-672 1.58e-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: 151.44  E-value: 1.58e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907157322 601 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSTIF 672
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 ...
 436-505 1.25e-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: 137.58  E-value: 1.25e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 436 MSHWKAGTVQAWLEVVMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRDAE 505
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 ...
 515-579 5.93e-35

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: 126.76  E-value: 5.93e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907157322 515 DLDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 579
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
74-248 4.24e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 59.15  E-value: 4.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  74 EEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 153
Cdd:COG4372     6 EKVGKARLSLFGLRPKTGILIAALSEQLR---KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 154 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKekdlLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAE 233
Cdd:COG4372    83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158

                         170
                  ....*....|....*
gi 1907157322 234 LAMAKQSLATLTKDV 248
Cdd:COG4372   159 LESLQEELAALEQEL 173
 
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 ...
 601-672 1.58e-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: 151.44  E-value: 1.58e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907157322 601 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSTIF 672
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 ...
 436-505 1.25e-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: 137.58  E-value: 1.25e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 436 MSHWKAGTVQAWLEVVMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRDAE 505
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 ...
 515-579 5.93e-35

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: 126.76  E-value: 5.93e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907157322 515 DLDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 579
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 525-578 1.93e-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: 56.89  E-value: 1.93e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907157322 525 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIELL 578
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 524-578 2.60e-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: 53.84  E-value: 2.60e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907157322  524 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 578
Cdd:smart00454  11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
74-248 4.24e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 59.15  E-value: 4.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  74 EEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 153
Cdd:COG4372     6 EKVGKARLSLFGLRPKTGILIAALSEQLR---KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 154 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKekdlLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAE 233
Cdd:COG4372    83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158

                         170
                  ....*....|....*
gi 1907157322 234 LAMAKQSLATLTKDV 248
Cdd:COG4372   159 LESLQEELAALEQEL 173
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 436-503 3.73e-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: 50.76  E-value: 3.73e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157322  436 MSHWKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRD 503
Cdd:smart00454   1 VSQWSPESVADWLES-IGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 72-246 4.28e-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: 4.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   72 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDL-- 149
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAE-------EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLne 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  150 -VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATD-------HAAALRSQLD 221
Cdd:TIGR02168  818 eAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRSELE 897

                          170       180
                   ....*....|....*....|....*
gi 1907157322  222 LKDNRMKELEAELAMAKQSLATLTK 246
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEELRE 922
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 437-502 1.46e-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: 48.80  E-value: 1.46e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157322 437 SHWKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLElGLGVCSSLHRRKLRLAIEDYR 502
Cdd:pfam00536   1 DGWSVEDVGEWLES-IGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
602-664 3.26e-07

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 48.03  E-value: 3.26e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907157322 602 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEptFNAEAMAtALGIPSGKHilRRHL 664
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 ...
 113-241 1.13e-06

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: 47.99  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 113 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLyatlesreeqlrdfirnyEQHRKESEDAVKALAKEK 192
Cdd:pfam20492  10 ELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL------------------EQKRQEAEEEKERLEESA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907157322 193 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSL 241
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
71-246 1.31e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.88  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  71 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQ----GGKCSE----------VLSATELRVQLVQKEQELARAKEALQAMK 136
Cdd:PRK02224  416 ELREERDELREREAELEATLRTARERVEEAEalleAGKCPEcgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 137 ADRKRLKgektDLVSQMQQLyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAAL 216
Cdd:PRK02224  496 ERLERAE----DLVEAEDRI-ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570

                         170       180       190
                  ....*....|....*....|....*....|
gi 1907157322 217 RSqldlkdnRMKELEAELAMAKQSLATLTK 246
Cdd:PRK02224  571 RE-------EVAELNSKLAELKERIESLER 593
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 602-661 1.34e-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: 40.74  E-value: 1.34e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  602 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTfnaEAMATALGIPSGKHILR 661
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGITKLGHRKK 57
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 120-245 4.25e-04

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: 43.13  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 120 QKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLERE 198
Cdd:cd22656   111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIARK 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907157322 199 KWE-LRRQAKEAT-DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLT 245
Cdd:cd22656   180 EIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 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 ...
 601-672 1.58e-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: 151.44  E-value: 1.58e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907157322 601 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSTIF 672
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 ...
 436-505 1.25e-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: 137.58  E-value: 1.25e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 436 MSHWKAGTVQAWLEVVMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRDAE 505
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 ...
 515-579 5.93e-35

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: 126.76  E-value: 5.93e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907157322 515 DLDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 579
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 ...
 601-671 2.96e-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: 96.76  E-value: 2.96e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907157322 601 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSTI 671
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 ...
 609-667 8.69e-22

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: 89.14  E-value: 8.69e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907157322 609 RVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEE 667
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 ...
 443-500 6.54e-21

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: 86.51  E-value: 6.54e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157322 443 TVQAWLEVVMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIED 500
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 ...
 520-579 1.04e-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: 86.05  E-value: 1.04e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 520 WVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 579
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 ...
 601-669 2.98e-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: 85.06  E-value: 2.98e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907157322 601 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMS 669
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 ...
 515-578 3.47e-18

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: 78.89  E-value: 3.47e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907157322 515 DLDHHWVAKaWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEkHLNVSKKFHQVSILLGIELL 578
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 ...
 437-500 2.14e-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: 68.36  E-value: 2.14e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907157322 437 SHWKAGTVQAWLEVVMAMPM-YVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIED 500
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 ...
 516-578 8.86e-14

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: 66.73  E-value: 8.86e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907157322 516 LDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 578
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 525-578 1.93e-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: 56.89  E-value: 1.93e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907157322 525 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIELL 578
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 ...
 439-500 3.00e-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: 56.47  E-value: 3.00e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907157322 439 WKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIED 500
Cdd:cd09563     4 WSTEQVCDWLAE-LGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 524-578 2.60e-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: 53.84  E-value: 2.60e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907157322  524 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 578
Cdd:smart00454  11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
74-248 4.24e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 59.15  E-value: 4.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  74 EEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 153
Cdd:COG4372     6 EKVGKARLSLFGLRPKTGILIAALSEQLR---KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 154 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKekdlLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAE 233
Cdd:COG4372    83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158

                         170
                  ....*....|....*
gi 1907157322 234 LAMAKQSLATLTKDV 248
Cdd:COG4372   159 LESLQEELAALEQEL 173
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
72-248 6.75e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.54  E-value: 6.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   72 LREEVVQLQEEVHLLRQMKEmLAKDLEESQGGKcsEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLvs 151
Cdd:COG4913    240 AHEALEDAREQIELLEPIRE-LAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  152 qmQQLYATLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELE 231
Cdd:COG4913    315 --EARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386

                          170
                   ....*....|....*..
gi 1907157322  232 AELAMAKQSLATLTKDV 248
Cdd:COG4913    387 AEAAALLEALEEELEAL 403
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 71-244 2.82e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  71 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLV 150
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 151 SQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKEL 230
Cdd:COG1196   316 ERLEELEEELAELEEELEEL----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170
                  ....*....|....
gi 1907157322 231 EAELAMAKQSLATL 244
Cdd:COG1196   392 LRAAAELAAQLEEL 405
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 436-503 3.73e-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: 50.76  E-value: 3.73e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157322  436 MSHWKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRD 503
Cdd:smart00454   1 VSQWSPESVADWLES-IGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 72-246 4.28e-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: 4.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   72 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDL-- 149
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAE-------EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLne 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  150 -VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATD-------HAAALRSQLD 221
Cdd:TIGR02168  818 eAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRSELE 897

                          170       180
                   ....*....|....*....|....*
gi 1907157322  222 LKDNRMKELEAELAMAKQSLATLTK 246
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEELRE 922
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 113-247 4.70e-08

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: 54.55  E-value: 4.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 113 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfIRNYEQhrkesedaVKALAKEK 192
Cdd:COG1579    28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKE--------YEALQKEI 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907157322 193 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 247
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 437-502 1.46e-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: 48.80  E-value: 1.46e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157322 437 SHWKAGTVQAWLEVvMAMPMYVKACAENVKSGKVLLSLSDEDLElGLGVCSSLHRRKLRLAIEDYR 502
Cdd:pfam00536   1 DGWSVEDVGEWLES-IGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 72-248 1.47e-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: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   72 LREEVVQLQEEVHLLRQMKEMLAKDL---------EESQGGKCSEVLSA-----TELRVQLVQKEQELARAKEALQAMKA 137
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQIsalrkdlarLEAEVEQLEERIAQlskelTELEAEIEELEERLEEAEEELAEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  138 DRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAT---- 210
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeie 862

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1907157322  211 ---DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:TIGR02168  863 eleELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 72-246 1.54e-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: 55.07  E-value: 1.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   72 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:TIGR02169  700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  152 QMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHAAALRSQLDLK 223
Cdd:TIGR02169  780 ALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859

                          170       180
                   ....*....|....*....|...
gi 1907157322  224 DNRMKELEAELAMAKQSLATLTK 246
Cdd:TIGR02169  860 NGKKEELEEELEELEAALRDLES 882
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 74-250 1.88e-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: 54.00  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  74 EEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 153
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKK-------EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 154 QQLYATLESREEQLRDFIRNYEQ-----------HRKESEDAVK----------ALAKEKDLLEREKWELRRQAKEATDH 212
Cdd:COG4942    93 AELRAELEAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRrlqylkylapARREQAEELRADLAELAALRAELEAE 172

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907157322 213 AAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPK 250
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 113-248 2.45e-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: 54.68  E-value: 2.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  113 ELRVQLVQKEQELARAKEALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 189
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157322  190 K-------EKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:TIGR02168  768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
602-664 3.26e-07

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 48.03  E-value: 3.26e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907157322 602 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEptFNAEAMAtALGIPSGKHilRRHL 664
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGITSVGH--RRKI 58
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 72-247 8.18e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 8.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHLLR-----QMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEK 146
Cdd:COG1196   218 LKEELKELEAELLLLKlreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 147 TDLVSQM---QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLK 223
Cdd:COG1196   298 ARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180
                  ....*....|....*....|....
gi 1907157322 224 DNRMKELEAELAMAKQSLATLTKD 247
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQ 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 72-246 8.28e-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: 52.75  E-value: 8.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   72 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  152 QMQQLYATLESREEQLRDFIRNYEQHRKESEDA----------VKALAKEKDLLEREKWELRRQAKEAtdHAAALRSQLD 221
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLnneierlearLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELE 443

                          170       180
                   ....*....|....*....|....*
gi 1907157322  222 LKDNRMKELEAELAMAKQSLATLTK 246
Cdd:TIGR02168  444 ELEEELEELQEELERLEEALEELRE 468
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
71-237 9.93e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 9.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   71 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQGgkcsevlSATELRVQLVQKE-QELARAKEALQAMKADRKRLKGEKTDL 149
Cdd:COG4913    292 LLEAELEELRAELARLEAELERLEARLDALRE-------ELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  150 VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKE 229
Cdd:COG4913    365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444


                   ....*...
gi 1907157322  230 LEAELAMA 237
Cdd:COG4913    445 LRDALAEA 452
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 113-241 1.13e-06

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: 47.99  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 113 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLyatlesreeqlrdfirnyEQHRKESEDAVKALAKEK 192
Cdd:pfam20492  10 ELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL------------------EQKRQEAEEEKERLEESA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907157322 193 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSL 241
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
66-248 1.33e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.69  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  66 GIQPVLLREEVVQLQEEVHLLRQMKEMLAKDLEESQggKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGE 145
Cdd:COG4717    63 GRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 146 KTDLVSQMQQLYATLESREEQLRDfIRNYEQHRKESEDAVKALakekdlLEREKWELRRQAKEATDHAAALRsqldlkdN 225
Cdd:COG4717   141 LAELPERLEELEERLEELRELEEE-LEELEAELAELQEELEEL------LEQLSLATEEELQDLAEELEELQ-------Q 206

                         170       180
                  ....*....|....*....|...
gi 1907157322 226 RMKELEAELAMAKQSLATLTKDV 248
Cdd:COG4717   207 RLAELEEELEEAQEELEELEEEL 229
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 523-576 2.10e-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: 45.31  E-value: 2.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907157322 523 KAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIE 576
Cdd:cd09487     3 AEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAIQ 55
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
74-245 2.21e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  74 EEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 153
Cdd:COG4717    88 EEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 154 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRM--KELE 231
Cdd:COG4717   163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALE 242

                         170
                  ....*....|....
gi 1907157322 232 AELAMAKQSLATLT 245
Cdd:COG4717   243 ERLKEARLLLLIAA 256
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
72-234 3.11e-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: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   72 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCS----EVLSATELRV-----QLVQKEQELARAKEA---LQAMKADR 139
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEIDVasaerEIAELEAELERLDASsddLAALEEQL 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  140 KRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDH----AAA 215
Cdd:COG4913    695 EELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVerelREN 770

                          170
                   ....*....|....*....
gi 1907157322  216 LRSQLDLKDNRMKELEAEL 234
Cdd:COG4913    771 LEERIDALRARLNRAEEEL 789
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 113-248 3.79e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 3.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  113 ELRVQLVQKEQELA-----RAKEALQAMKADRKRLKGEKTDLVSQMQqlyaTLESREEQLRDFIRNYEQHRKESEDAVKA 187
Cdd:TIGR02168  217 ELKAELRELELALLvlrleELREELEELQEELKEAEEELEELTAELQ----ELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907157322  188 LAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 79-256 4.48e-06

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: 50.21  E-value: 4.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  79 LQEEVHLLRQMKE----MLAK------DLEESQGGKCSEV------LSATELRVQLVQKE----QELARAKEalQAMKAD 138
Cdd:pfam10174 343 LQTEVDALRLRLEekesFLNKktkqlqDLTEEKSTLAGEIrdlkdmLDVKERKINVLQKKienlQEQLRDKD--KQLAGL 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 139 RKRLKGEKTDlVSQMQQLYATLES---------------REEQLRDFIRNYEQHRKESEDAvkalaKEK-DLLEREKWEL 202
Cdd:pfam10174 421 KERVKSLQTD-SSNTDTALTTLEEalsekeriierlkeqREREDRERLEELESLKKENKDL-----KEKvSALQPELTEK 494

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907157322 203 RRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAM 256
Cdd:pfam10174 495 ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 74-244 6.44e-06

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: 49.97  E-value: 6.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   74 EEVVQLQEEVHLLrqmkemLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQm 153
Cdd:pfam02463  278 EKEKKLQEEELKL------LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK- 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  154 qqlYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQA----KEATDHAAALRSQLDLKDNRMKE 229
Cdd:pfam02463  351 ---REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKseeeKEAQLLLELARQLEDLLKEEKKE 427

                          170
                   ....*....|....*
gi 1907157322  230 LEAELAMAKQSLATL 244
Cdd:pfam02463  428 ELEILEEEEESIELK 442
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 111-339 7.52e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 7.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 111 ATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR-NYEQHR----------- 178
Cdd:COG3883    32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaLYRSGGsvsyldvllgs 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 179 ------------------------KESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAEL 234
Cdd:COG3883   112 esfsdfldrlsalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 235 AMAKQSLATLTKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQVRVSPCHSRQPSVIS 314
Cdd:COG3883   192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271

                         250       260
                  ....*....|....*....|....*
gi 1907157322 315 DASAAEGDRSSTPSDINSPRHRTHS 339
Cdd:COG3883   272 AGAGAAAASAAGGGAGGAGGGGGGG 296
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 107-248 1.06e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 107 EVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVK 186
Cdd:COG1196   223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907157322 187 ALAKEKDL-------LEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:COG1196   303 DIARLEERrreleerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 120-271 1.13e-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: 48.86  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 120 QKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA-KEKDLLE-- 196
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKsKEKELKKln 502

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907157322 197 REKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLtKDVPKRHSLampgETVLNGNQEWVVQ 271
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-DFELKKENL----EKEIDEKNKEIEE 572
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
71-246 1.31e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.88  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  71 LLREEVVQLQEEVHLLRQMKEMLAKDLEESQ----GGKCSE----------VLSATELRVQLVQKEQELARAKEALQAMK 136
Cdd:PRK02224  416 ELREERDELREREAELEATLRTARERVEEAEalleAGKCPEcgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 137 ADRKRLKgektDLVSQMQQLyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAAL 216
Cdd:PRK02224  496 ERLERAE----DLVEAEDRI-ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570

                         170       180       190
                  ....*....|....*....|....*....|
gi 1907157322 217 RSqldlkdnRMKELEAELAMAKQSLATLTK 246
Cdd:PRK02224  571 RE-------EVAELNSKLAELKERIESLER 593
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
113-235 1.49e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  113 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLvSQMQQLY------ATLESREEQLRDFIRNYEqhrkESEDAVK 186
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSwdeidvASAEREIAELEAELERLD----ASSDDLA 688

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907157322  187 ALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELA 235
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
72-259 1.62e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkcSEVLSA----TELRVQLVQKEQELARAKEALQAMKADRKRLKGEkt 147
Cdd:COG4372    43 LQEELEQLREELEQAREELEQLEEELEQAR----SELEQLeeelEELNEQLQAAQAELAQAQEELESLQEEAEELQEE-- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 148 dlVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAalrsqldlkDNRM 227
Cdd:COG4372   117 --LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA---------EQAL 185

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907157322 228 KELEAELAMAKQSLATLTKDVPKRHSLAMPGE 259
Cdd:COG4372   186 DELLKEANRNAEKEEELAEAEKLIESLPRELA 217
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 113-252 2.24e-05

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: 48.14  E-value: 2.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  113 ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALA 189
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907157322  190 KEKDLLEREKWELRRQAKEATDHAAalRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRH 252
Cdd:TIGR02169  765 ARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 524-584 2.55e-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: 42.69  E-value: 2.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907157322 524 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLYQVNFS 584
Cdd:cd09505    12 TWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELKMKSDS 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 111-244 3.11e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 111 ATELRVQLVQKEQELARAKeaLQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDA------ 184
Cdd:COG1196   215 YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeye 292

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907157322 185 ----VKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATL 244
Cdd:COG1196   293 llaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
72-243 3.20e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsEVLSATElrvqlvQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:PRK02224  211 LESELAELDEEIERYEEQREQARETRDEAD-----EVLEEHE------ERREELETLEAEIEDLRETIAETEREREELAE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 152 QMQQLYATLESREEQLRDFIRNYEQHRKESEdavkALAKEKDLLEREKWELRR--------------QAKEATDHAAALR 217
Cdd:PRK02224  280 EVRDLRERLEELEEERDDLLAEAGLDDADAE----AVEARREELEDRDEELRDrleecrvaaqahneEAESLREDADDLE 355

                         170       180
                  ....*....|....*....|....*.
gi 1907157322 218 SQLDLKDNRMKELEAELAMAKQSLAT 243
Cdd:PRK02224  356 ERAEELREEAAELESELEEAREAVED 381
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 72-249 4.94e-05

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: 46.98  E-value: 4.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   72 LREEVVQLQEEVHLLRQMKEMLAKDleesqggkcsevlsATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKE--------------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  152 QMQQLYATLESREEQLrdfirnyeqhrKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELE 231
Cdd:TIGR02169  421 ELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489

                          170
                   ....*....|....*...
gi 1907157322  232 AELAMAKQSLATLTKDVP 249
Cdd:TIGR02169  490 RELAEAEAQARASEERVR 507
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
72-234 5.12e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCS-EVLSAT--ELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTD 148
Cdd:PRK02224  218 LDEEIERYEEQREQARETRDEADEVLEEHEERREElETLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 149 LVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRS 218
Cdd:PRK02224  298 LLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377

                         170
                  ....*....|....*.
gi 1907157322 219 QLDLKDNRMKELEAEL 234
Cdd:PRK02224  378 AVEDRREEIEELEEEI 393
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 87-247 8.28e-05

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: 46.32  E-value: 8.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   87 RQMKEMLAKDlEESQGGKCSEVLSATELRvQLVQKEQELARAKEALQamkadrKRLKGEkTDLVSQMQQLYATLESREEQ 166
Cdd:pfam01576    2 RQEEEMQAKE-EELQKVKERQQKAESELK-ELEKKHQQLCEEKNALQ------EQLQAE-TELCAEAEEMRARLAARKQE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  167 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEatDHAAALRSQLD--LKDNRMKELEAELAMAKQSLATL 244
Cdd:pfam01576   73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEkvTTEAKIKKLEEDILLLEDQNSKL 150


                   ...
gi 1907157322  245 TKD 247
Cdd:pfam01576  151 SKE 153
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 602-661 1.34e-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: 40.74  E-value: 1.34e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  602 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTfnaEAMATALGIPSGKHILR 661
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGITKLGHRKK 57
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
97-248 1.35e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  97 LEESQGGKCSEVLSATE-LRVQLVQKEQELARAKEALQAMKADRK--RLKGEKTDLVSQMQQL---YATLESREEQLRDF 170
Cdd:COG3206   162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELesqLAEARAELAEAEAR 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157322 171 IRNYEQHRKESEDAVKALAKEKDLLErekweLRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:COG3206   242 LAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
50-236 1.43e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  50 REQQGAGAVPDAADGFGIQPVLLREEVVQLQEEV----HLLRQMKEMLAKDLEESQGGKCSEVLSatELRVQLVQKEQEL 125
Cdd:COG3206   202 RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELaeaeARLAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAEL 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 126 ARAKE----------ALQAMKAD-RKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQhrkeseDAVKALAKEKDL 194
Cdd:COG3206   280 AELSArytpnhpdviALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA------RLAELPELEAEL 353

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907157322 195 LerekwELRRQAKeatdhaaALRSQLDLKDNRMKELEAELAM 236
Cdd:COG3206   354 R-----RLEREVE-------VARELYESLLQRLEEARLAEAL 383
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 518-578 1.48e-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: 40.47  E-value: 1.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907157322 518 HHWVAK---AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 578
Cdd:cd09507     3 TNWTTEevgAWLESLQLGEYRDIFARNDIRGSELLHLERRDL-KDLGITKVGHVKRILQAIKDL 65
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 72-251 1.73e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.76  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHLLRQMKEMLAKDLEEsqggkcsevlsateLRVQLVQKEQELARAKEALQAMKADRKRLKG------- 144
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEA--------------AKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrn 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 145 --EKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELrrqakeatdhaaalrsqldl 222
Cdd:COG1579    88 nkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL-------------------- 147

                         170       180
                  ....*....|....*....|....*....
gi 1907157322 223 kDNRMKELEAELAMAKQSLATLTKDVPKR 251
Cdd:COG1579   148 -DEELAELEAELEELEAEREELAAKIPPE 175
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
72-250 1.76e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHLLRQMKEMLA-----KDLEESQGGKCSEVLSATELRV-QLVQKEQELARAKEALQAMKADRK---RL 142
Cdd:PRK03918  219 LREELEKLEKEVKELEELKEEIEelekeLESLEGSKRKLEEKIRELEERIeELKKEIEELEEKVKELKELKEKAEeyiKL 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 143 KGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQhRKESEDAVKALAKEKDLLEREKWELRRQAKEATDhAAALRSQLD- 221
Cdd:PRK03918  299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELEr 376

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907157322 222 ----LKDNRMKELEAELAMAKQSLATLTKDVPK 250
Cdd:PRK03918  377 lkkrLTGLTPEKLEKELEELEKAKEEIEEEISK 409
PTZ00121 PTZ00121
MAEBL; Provisional
 71-233 1.77e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   71 LLREEVVQLQEEVHLLRQMKEmlAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLV 150
Cdd:PTZ00121  1551 LKKAEELKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  151 SQMQQLYATLESREEQLrdfIRNYEQHRKESEDAVKALAKEKDLLEREKW---ELRRQAKEATDHAAALRSQLD--LKDN 225
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEALKKEAEeaKKAE 1705


                   ....*...
gi 1907157322  226 RMKELEAE 233
Cdd:PTZ00121  1706 ELKKKEAE 1713
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
74-199 2.40e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  74 EEVVQLQEEVHLLRQMKEMLAKDLEESqggkcSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQm 153
Cdd:COG4717   395 EEYQELKEELEELEEQLEELLGELEEL-----LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED- 468

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907157322 154 qQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREK 199
Cdd:COG4717   469 -GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 78-246 2.71e-04

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: 44.63  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  78 QLQEEVHLLRQMKEMLAKdLEESQGGKCSEVLsatELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqly 157
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQ-LKKELTNSESENS---EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK----- 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 158 atlesreeqlrdfIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMA 237
Cdd:TIGR04523 400 -------------IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466


                  ....*....
gi 1907157322 238 KQSLATLTK 246
Cdd:TIGR04523 467 ETQLKVLSR 475
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 518-578 3.36e-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: 39.55  E-value: 3.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907157322 518 HHWVAK---AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 578
Cdd:cd09575     3 HLWGTEevaAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 524-581 4.14e-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: 38.84  E-value: 4.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157322 524 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIellYQV 581
Cdd:cd09533     4 DWLSSLGLPQYEDQFIENGITGDVLVALDHEDL-KEMGITSVGHRLTILKAV---YEL 57
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 120-245 4.25e-04

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: 43.13  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 120 QKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLERE 198
Cdd:cd22656   111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIARK 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907157322 199 KWE-LRRQAKEAT-DHAAALRSQLDLKDNRMKELEAELAMAKQSLATLT 245
Cdd:cd22656   180 EIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 444-500 4.77e-04

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: 38.76  E-value: 4.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907157322 444 VQAWLEVVmAMPMYVKACAENVKSGKVLLSLSDEDLElGLGVCSSLHRRKLRLAIED 500
Cdd:cd09487     2 VAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 115-248 4.90e-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: 43.13  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 115 RVQLVQKEQELARAKEALQAMKADRKRLkgekTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDL 194
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGL----TRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907157322 195 LEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 248
Cdd:pfam19220 123 LERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQEN 176
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
72-215 5.21e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 5.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   72 LREEVVQLQEEVHLLRQMKEMLAKDLEE------SQGGKCSEVLSA--TELRVQLVQKEQELARAKEALQAMKADRKRLK 143
Cdd:COG4913    300 LRAELARLEAELERLEARLDALREELDEleaqirGNGGDRLEQLEReiERLERELEERERRRARLEALLAALGLPLPASA 379

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907157322  144 GEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKW-------ELRRQAKEATDHAAA 215
Cdd:COG4913    380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDALAEALGLDEA 458
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 74-285 5.30e-04

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: 43.35  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  74 EEVVQLQEEVHLlrqmkemlakdlEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 153
Cdd:pfam07888   4 DELVTLEEESHG------------EEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 154 QQLYATLESREEQLRDFIRNY-------EQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKD-- 224
Cdd:pfam07888  72 ERQRRELESRVAELKEELRQSrekheelEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEREte 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 225 -NRMKE------------------LEAELAMAKQSLATLTKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQ 285
Cdd:pfam07888 152 lERMKErakkagaqrkeeeaerkqLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 72-231 6.02e-04

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: 43.20  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHL---LRQMKEMLAKDLEESQGGKCSEVlsATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTD 148
Cdd:pfam07111 486 LREERNRLDAELQLsahLIQQEVGRAREQGEAERQQLSEV--AQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAAS 563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 149 L---VSQMQQLY--------ATLESR-EEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREK---WELRRQAKEATDHA 213
Cdd:pfam07111 564 LrqeLTQQQEIYgqalqekvAEVETRlREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKernQELRRLQDEARKEE 643

                         170
                  ....*....|....*...
gi 1907157322 214 AALRSQldlkdnRMKELE 231
Cdd:pfam07111 644 GQRLAR------RVQELE 655
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
123-249 6.25e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 6.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 123 QELARAKEALQAMKADRKRLKgEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRkesedAVKALAKEKDLLEREKWEL 202
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAEL 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907157322 203 RRQAKEATDHAAALRSQLdlkdNRMKELEAELAMAKQSLATLTKDVP 249
Cdd:COG4717   145 PERLEELEERLEELRELE----EELEELEAELAELQEELEELLEQLS 187
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
72-238 7.44e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 7.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHLLRQMKEMLAKDLEEsQGGKCSEVLSAT--ELRvQLVQKEQELARAKEALQAMKADRKRLKGEKTDL 149
Cdd:PRK03918  554 LKKKLAELEKKLDELEEELAELLKELEE-LGFESVEELEERlkELE-PFYNEYLELKDAEKELEREEKELKKLEEELDKA 631

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 150 VSQMQQLYATLESREEQLRDFIRNY--EQHRKESEDAVKaLAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRM 227
Cdd:PRK03918  632 FEELAETEKRLEELRKELEELEKKYseEEYEELREEYLE-LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710

                         170
                  ....*....|..
gi 1907157322 228 KELEA-ELAMAK 238
Cdd:PRK03918  711 KELEKlEKALER 722
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 72-249 9.45e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 9.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkcsevLSATELRVQLVQKEQELARAKEALQAM-KADRKRLKGEKTD-- 148
Cdd:COG4942    60 LERRIAALARRIRALEQELAALEAELAELE-------KEIAELRAELEAQKEELAELLRALYRLgRQPPLALLLSPEDfl 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 149 -----------LVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALR 217
Cdd:COG4942   133 davrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907157322 218 SQLDLKDNRMKELEAELAMAKQSLATLTKDVP 249
Cdd:COG4942   213 AELAELQQEAEELEALIARLEAEAAAAAERTP 244
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 106-196 1.19e-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: 40.65  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 106 SEVLSATELRVQLVQKEQE-LARAKEALQAMKADRKRLKGEKtdLVSQMQQLYATLESREEQLRDFIRNYEqhrkeseda 184
Cdd:pfam10368  57 DEALENVEEREELLEKEKEsIEEAKEEFKKIKEIIEEIEDEE--LKKEAEELIDAMEERYEAYDELYDAYK--------- 125

                          90
                  ....*....|..
gi 1907157322 185 vKALAKEKDLLE 196
Cdd:pfam10368 126 -KALELDKELYE 136
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 605-658 1.19e-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: 38.08  E-value: 1.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907157322 605 WTNQRVLKW-VRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKH 658
Cdd:cd09504     5 WTVEDTVEWlVNSVELPQYVEAFKENGVDGSALPRLAVNNPSFLTSVLGIKDPIH 59
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 117-220 1.19e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 117 QLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEkdlle 196
Cdd:COG4942   161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE----- 235

                          90       100
                  ....*....|....*....|....
gi 1907157322 197 rekwELRRQAKEATDHAAALRSQL 220
Cdd:COG4942   236 ----AAAAAERTPAAGFAALKGKL 255
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 114-249 1.40e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 114 LRVQLVQKEQELARAKEALQAMKADRKRLKGEKtDLVSQmqqlyatleSREEQLRDFIrnyEQHRKESEDAvkalakekd 193
Cdd:COG0542   402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ-DEASF---------ERLAELRDEL---AELEEELEAL--------- 459

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157322 194 lleREKWElrrQAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 249
Cdd:COG0542   460 ---KARWE---AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
PTZ00121 PTZ00121
MAEBL; Provisional
 74-233 1.41e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   74 EEVVQLQEEVHLLRQMK--EMLAKDLEESQGGKCSEVLSATELRvqlvqKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:PTZ00121  1610 EEAKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEELK-----KAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  152 QMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKA---LAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKdNRMK 228
Cdd:PTZ00121  1685 EDEKKAAEALKKEAEEA---KKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-KKIA 1760


                   ....*
gi 1907157322  229 ELEAE 233
Cdd:PTZ00121  1761 HLKKE 1765
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 72-243 1.54e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHLLRQMKEMLAKDLEESQggkcSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:COG1196   405 LEEAEEALLERLERLEEELEELEEALAELE----EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 152 QMQQLYATLESREEQLRDFIRNYEQH---RKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMK 228
Cdd:COG1196   481 ELLEELAEAAARLLLLLEAEADYEGFlegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560

                         170
                  ....*....|....*
gi 1907157322 229 ELEAELAMAKQSLAT 243
Cdd:COG1196   561 AAIEYLKAAKAGRAT 575
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 72-246 1.62e-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: 42.08  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   72 LREEVVQLQEevhlLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVS 151
Cdd:pfam01576  196 LKKEEKGRQE----LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEA 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  152 QMQQLYATLESR-------EEQLRDFIRNYEQHRKESEDAVKALAKEKDL---LEREKWELRRQAKEATDHAAALRSQLD 221
Cdd:pfam01576  272 QISELQEDLESEraarnkaEKQRRDLGEELEALKTELEDTLDTTAAQQELrskREQEVTELKKALEEETRSHEAQLQEMR 351

                          170       180
                   ....*....|....*....|....*.
gi 1907157322  222 LKDNR-MKELEAELAMAKQSLATLTK 246
Cdd:pfam01576  352 QKHTQaLEELTEQLEQAKRNKANLEK 377
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 113-245 2.19e-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: 40.87  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 113 ELRVQLVQKEQELARA---KEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHR----------K 179
Cdd:pfam00529  62 SAEAQLAKAQAQVARLqaeLDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiggisrE 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 180 ESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDN----RMKELEAELAMAKQSLATLT 245
Cdd:pfam00529 142 SLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlQIAEAEAELKLAKLDLERTE 211
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 72-222 2.39e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 38.77  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHLLRQMKEMLAKDLEEsqggkcsEVLSATElrvqlVQK--EQEL---ARAKEALQAMKADRKRLKGEK 146
Cdd:pfam07926   6 LQSEIKRLKEEAADAEAQLQKLQEDLEK-------QAEIARE-----AQQnyERELvlhAEDIKALQALREELNELKAEI 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157322 147 TDLVSQMQQLYATLESREEqlrdfirnyeqhrkesedavkALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDL 222
Cdd:pfam07926  74 AELKAEAESAKAELEESEE---------------------SWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 72-246 2.49e-03

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 40.04  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHLLRQMKEMLAKDLEEsqggkcsevlsateLRVQLVQKEQELARAKEALQAmkaDRKRLKGEKTDLVS 151
Cdd:pfam05010  13 ARNEIEEKELEINELKAKYEELRRENLE--------------MRKIVAEFEKTIAQMIEEKQK---QKELEHAEIQKVLE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 152 QMQQLYATLESREEQLRDFIRNYEQHR------KESE---------------------DAVKALAKEKdlLEREKWELRR 204
Cdd:pfam05010  76 EKDQALADLNSVEKSFSDLFKRYEKQKevisgyKKNEeslkkcaqdylarikkeeqryQALKAHAEEK--LDQANEEIAQ 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907157322 205 QAKEATDHAAALRSQLDLKDNRMKELEAELAMAKQSLATLTK 246
Cdd:pfam05010 154 VRSKAKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTK 195
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 93-240 2.57e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.26  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  93 LAKDLEESqggkcSEVLSATELRVQLVQKEQELAraKEALQAMkADRKRLKGEKTDLVSQMQQlyaTLESREEQLRDFIR 172
Cdd:pfam05557  39 LKRQLDRE-----SDRNQELQKRIRLLEKREAEA--EEALREQ-AELNRLKKKYLEALNKKLN---EKESQLADAREVIS 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157322 173 N-------YEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDL---KDNRMKELEAELAMAKQS 240
Cdd:pfam05557 108 ClknelseLRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSlaeAEQRIKELEFEIQSQEQD 185
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
160-248 2.60e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 40.19  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 160 LESREEQLRDFIRNYEQHRKESEDAV-KALAKEKdLLEREKWELRRQAKEATDHA-------------AALRSQLDLkDN 225
Cdd:COG1842    21 AEDPEKMLDQAIRDMEEDLVEARQALaQVIANQK-RLERQLEELEAEAEKWEEKArlalekgredlarEALERKAEL-EA 98

                          90       100
                  ....*....|....*....|...
gi 1907157322 226 RMKELEAELAMAKQSLATLTKDV 248
Cdd:COG1842    99 QAEALEAQLAQLEEQVEKLKEAL 121
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 525-563 2.71e-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: 2.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907157322 525 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVS 563
Cdd:cd09501    12 WLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMS 50
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
113-238 3.11e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.81  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 113 ELRVQLVQKEQELARAkealqamKADRKRLKgektdlvSQMQQLYATLESREEQLRDFIrnyeqhRKESEDAVKALAKEK 192
Cdd:COG1842    34 DMEEDLVEARQALAQV-------IANQKRLE-------RQLEELEAEAEKWEEKARLAL------EKGREDLAREALERK 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907157322 193 DLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAELAMAK 238
Cdd:COG1842    94 AELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLK 139
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
73-234 3.14e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  73 REEVVQLQEEVHLLRQMKEMLAKDLEESqggkcsEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGE-----KT 147
Cdd:PRK02224  474 RERVEELEAELEDLEEEVEEVEERLERA------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEelrerAA 547

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 148 DLVSQMQQLYA---TLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLL------EREKWELRRQAKEATDHAAALRS 218
Cdd:PRK02224  548 ELEAEAEEKREaaaEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiadaEDEIERLREKREALAELNDERRE 627

                         170
                  ....*....|....*.
gi 1907157322 219 QLDLKDNRMKELEAEL 234
Cdd:PRK02224  628 RLAEKRERKRELEAEF 643
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
525-578 3.29e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 36.48  E-value: 3.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907157322 525 WLNDIGLSQYSQAFQNHLVDG-RMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 578
Cdd:pfam07647  12 WLRSIGLEQYTDNFRDQGITGaELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 154-244 3.36e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 154 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAE 233
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90
                  ....*....|.
gi 1907157322 234 LAMAKQSLATL 244
Cdd:COG4942    99 LEAQKEELAEL 109
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
72-233 3.49e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  72 LREEVVQLQEEVHLLRQMKEmLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRL--KGEKTDL 149
Cdd:COG4717   352 LLREAEELEEELQLEELEQE-IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELleALDEEEL 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 150 VSQMQQLYATLESREEQLRDFIrnyeQHRKESEDAVKALAKEKDL--LEREKWELRRQAKEATDHAAALRSQLDLKDNRM 227
Cdd:COG4717   431 EEELEELEEELEELEEELEELR----EELAELEAELEQLEEDGELaeLLQELEELKAELRELAEEWAALKLALELLEEAR 506


                  ....*.
gi 1907157322 228 KELEAE 233
Cdd:COG4717   507 EEYREE 512
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 518-556 3.58e-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: 36.84  E-value: 3.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907157322 518 HHW----VAKaWLNDIGLSQYSQAF-QNHLVDGRMLNSLMKRDL 556
Cdd:cd09515     2 HEWtcedVAK-WLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDL 44
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 79-234 4.01e-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: 40.58  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  79 LQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSA--TELRVQLVQKEQE-LARAKEALqamkadRKRLKGEKTDLVSQMQq 155
Cdd:pfam10174  79 LQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPelTEENFRRLQSEHErQAKELFLL------RKTLEEMELRIETQKQ- 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907157322 156 lyaTLESREEQLRDFIRNYEQhrkesedavKALAKEkdlLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAEL 234
Cdd:pfam10174 152 ---TLGARDESIKKLLEMLQS---------KGLPKK---SGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREEL 215
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 74-234 4.10e-03

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.71  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  74 EEVVQLQEEVHLLRQMKEMLAKDLEEsqgGKCSEVLSATELRVQLVQKE--QELARAKEALQAMKADRKRLKGE--KTDL 149
Cdd:COG5185   299 AEYTKSIDIKKATESLEEQLAAAEAE---QELEESKRETETGIQNLTAEieQGQESLTENLEAIKEEIENIVGEveLSKS 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 150 VSQMQQLYATLESREEQLRDFIRNYEQHRKEsedAVKALAKEKDLLEREKWELRRQAKEATdhaaalrSQLDLKDNRMKE 229
Cdd:COG5185   376 SEELDSFKDTIESTKESLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQAT-------SSNEEVSKLLNE 445


                  ....*
gi 1907157322 230 LEAEL 234
Cdd:COG5185   446 LISEL 450
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 88-203 4.21e-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: 39.96  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  88 QMKEMLAKDLEESQGgkCSEVLSATElrVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQ-----------QL 156
Cdd:pfam02841 173 KAEEVLQEFLQSKEA--VEEAILQTD--QALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEaqersyqehvkQL 248

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907157322 157 YATLES-REEQLRDFIRNYEQHRKESEDAVKA-LAKEKDLLEREKWELR 203
Cdd:pfam02841 249 IEKMEAeREQLLAEQERMLEHKLQEQEELLKEgFKTEAESLQKEIQDLK 297
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
49-247 4.32e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  49 LREQQGAGAVPDAADGFGIQPVLLREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARA 128
Cdd:COG4717   294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 129 KEALQAMKADRKRLKgEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAvkALAKEKDLLEREKWELRRQAKE 208
Cdd:COG4717   374 ALLAEAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEE 450

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907157322 209 ATDHAAALRSQLD--LKDNRMKELEAELAMAKQSLATLTKD 247
Cdd:COG4717   451 LREELAELEAELEqlEEDGELAELLQELEELKAELRELAEE 491
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 435-500 4.81e-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: 36.24  E-value: 4.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157322 435 PMSHWKAGTVQAWLEvVMAMPMYVKACAENVKSGKVLLSLSDEDLElGLGVCSSLHRRKLRLAIED 500
Cdd:cd09507     1 PVTNWTTEEVGAWLE-SLQLGEYRDIFARNDIRGSELLHLERRDLK-DLGITKVGHVKRILQAIKD 64
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 72-249 5.12e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   72 LREEVVQLQEEVHLLRQM--------KEMLAKDLEE---SQGGKCSEV---LSATELRVQLVQKE-QELARAKEALQAMK 136
Cdd:TIGR02169  770 LEEDLHKLEEALNDLEARlshsripeIQAELSKLEEevsRIEARLREIeqkLNRLTLEKEYLEKEiQELQEQRIDLKEQI 849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  137 ADRKRlkgEKTDLVSQMQQLYATLESREEQLRDFirnyeqhrkesEDAVKALAKEKDLLEREKWELRRQAKEatdhaaaL 216
Cdd:TIGR02169  850 KSIEK---EIENLNGKKEELEEELEELEAALRDL-----------ESRLGDLKKERDELEAQLRELERKIEE-------L 908

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1907157322  217 RSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 249
Cdd:TIGR02169  909 EAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
HAUS-augmin3 pfam14932
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ...
 106-250 5.35e-03

HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.


Pssm-ID: 464384 [Multi-domain]  Cd Length: 261  Bit Score: 39.61  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 106 SEVLSATEL--RVQLVQK------EQELArakEALQAMKADR-KRLKGEKTDLvsqmqqlyatLESREEQLRDFIRNYEq 176
Cdd:pfam14932  22 SNVLSEEELqaFEELQKSgkpileGAALD---EALKTISAESpGLLNQQDVEA----------LEESLEEIREATEDLE- 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157322 177 hrkeseDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKDNRMKELEAEL----AMAKQSLATLTKDVPK 250
Cdd:pfam14932  88 ------AELQELQKTKQLKINRLNKLQAQASSLSQGLRALVAEEEEAAKQLEELQEELaalnAKTNNVLQSLQSEVKE 159
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 113-239 5.44e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 113 ELRVQLVQKEQELARAKEALQAMKAD-------RKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNY-EQHRKESEDA 184
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELRAKlyqeeqeRKERQKEREEAEKKARQRQELQQAREEQIELKERRLaEEAEREEEEF 263

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157322 185 VKALAKEKDLLEREKWELRRQAKEATDHAAALRSQLDLKD-NRMKELEAELAMAKQ 239
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREeQRAAEREEELEEGER 319
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
145-254 5.60e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 145 EKTDLVSQMQqlyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQL-DLK 223
Cdd:COG1340     1 SKTDELSSSL---EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkELK 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907157322 224 DNR------MKELEAELAMAKQSLATLTKDVPKRHSL 254
Cdd:COG1340    78 EERdelnekLNELREELDELRKELAELNKAGGSIDKL 114
mukB PRK04863
chromosome partition protein MukB;
72-234 5.61e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 5.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   72 LREEVVQLQEEVHLLRQMKEMLAKDLEESQGGKCSEVlsatelrvqlvqkEQELARAKEALQAMKADRKRLkgektdlvS 151
Cdd:PRK04863   863 QRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEI-------------REQLDEAEEAKRFVQQHGNAL--------A 921

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  152 QMQQLYATLESREEQLRDFIRNYEQHRKES----------------------EDAVKALAKEKDL----------LEREK 199
Cdd:PRK04863   922 QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQrdakqqafaltevvqrrahfsyEDAAEMLAKNSDLneklrqrleqAEQER 1001

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907157322  200 WELRRQAKEATDHA-------AALRSQLDLKDNRMKELEAEL 234
Cdd:PRK04863  1002 TRAREQLRQAQAQLaqynqvlASLKSSYDAKRQMLQELKQEL 1043
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 435-505 5.98e-03

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: 36.14  E-value: 5.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907157322 435 PMSHWKAGTVQAWLEVVMaMPMYVKACAENVKSGKVLLSLSDEDLELGLGVCSSLHRRKLRLAIEDYRDAE 505
Cdd:cd09505     1 SLQDWSEEDVCTWLRSIG-LEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELKMKS 70
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
73-231 6.10e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  73 REEVVQLQEEVHLLRQMKEMLAKDLEESQggKCSEVLSATELRVQLVQKE-QELARAKEALQAMKADRKRLKGEKTDLvS 151
Cdd:PRK03918  282 VKELKELKEKAEEYIKLSEFYEEYLDELR--EIEKRLSRLEEEINGIEERiKELEEKEERLEELKKKLKELEKRLEEL-E 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 152 QMQQLYATLESREEQLrdfirnyEQHRKESED-AVKALAKEKDLLEREKWELRRQAKEATDHAAALRSQL-DLKDNrMKE 229
Cdd:PRK03918  359 ERHELYEEAKAKKEEL-------ERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIkELKKA-IEE 430


                  ..
gi 1907157322 230 LE 231
Cdd:PRK03918  431 LK 432
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 118-231 6.19e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.16  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 118 LVQKEQELARAKEALQAMKADRKRLKgektdlvSQMQQLYATLESREEQLRDFIRNYEQHRKESED----AVKALAKE-- 191
Cdd:pfam13863   1 LLEKKREMFLVQLALDAKREEIERLE-------ELLKQREEELEKKEQELKEDLIKFDKFLKENDAkrrrALKKAEEEtk 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907157322 192 -KDLLEREkwelrrqAKEATDHAAALRSQLDLKDNRMKELE 231
Cdd:pfam13863  74 lKKEKEKE-------IKKLTAQIEELKSEISKLEEKLEEYK 107
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 518-548 6.28e-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: 36.16  E-value: 6.28e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907157322 518 HHWVAK---AWL-NDIGLSQYSQAFQNHLVDGRML 548
Cdd:cd09504     3 HNWTVEdtvEWLvNSVELPQYVEAFKENGVDGSAL 37
PRK12704 PRK12704
phosphodiesterase; Provisional
 106-234 6.75e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 106 SEVLSATELRVQLVQKEQELARA--KEALQAMKADRKRLK----GEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRK 179
Cdd:PRK12704   31 AKIKEAEEEAKRILEEAKKEAEAikKEALLEAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157322 180 ESEDAVKALAKEKDLLEREKWELRRQAKEATD---HAAALrSQLDLKDNRMKELEAEL 234
Cdd:PRK12704  111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQeleRISGL-TAEEAKEILLEKVEEEA 167
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
73-242 6.87e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 6.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  73 REEvvqLQEEVHLLRQMKEMLAKDLEESQGGKCSEVLSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQ 152
Cdd:PRK02224  274 REE---LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 153 MqqlyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRR-------QAKEATDHAAALRSQLDLKDN 225
Cdd:PRK02224  351 A----DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDFLEELREERDELRE 426

                         170
                  ....*....|....*..
gi 1907157322 226 RMKELEAELAMAKQSLA 242
Cdd:PRK02224  427 REAELEATLRTARERVE 443
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 84-273 7.26e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.81  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322  84 HLLRQMKEMLAKDLEesqggKCSEVLSATE-LRVQLVQKEQELARAKEALQAMKADrkrlkgektdlvsqMQQLYATLES 162
Cdd:PRK00409  502 NIIEEAKKLIGEDKE-----KLNELIASLEeLERELEQKAEEAEALLKEAEKLKEE--------------LEEKKEKLQE 562

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322 163 REEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAtdhaaalrsqldLKDNRMKELEAELAMAKQSLA 242
Cdd:PRK00409  563 EEDKLL------EEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAS------------VKAHELIEARKRLNKANEKKE 624

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907157322 243 TLTKDVPKRHSLAMPGETV-------------LNGNQEWVVQAD 273
Cdd:PRK00409  625 KKKKKQKEKQEELKVGDEVkylslgqkgevlsIPDDKEAIVQAG 668
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 524-571 7.28e-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: 35.76  E-value: 7.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907157322 524 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSI 571
Cdd:cd09506    12 DWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTE-LGVTRVGHRMNI 58
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 78-222 8.09e-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: 39.94  E-value: 8.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157322   78 QLQEEVHLLRQMK--EMLAKDLEESQGGKCSevlSATELRVQLVQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQ 155
Cdd:COG3096    520 QLAELEQRLRQQQnaERLLEEFCQRIGQQLD---AAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907157322  156 LYA------TLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREkwelrRQAKEATDHAAALRSQLDL 222
Cdd:COG3096    597 LAArapawlAAQDALERLR------EQSGEALADSQEVTAAMQQLLERE-----REATVERDELAARKQALES 658
 
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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