NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|665402770|ref|NP_001286716|]
View 

Liprin-gamma, isoform E [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 812-883 8.79e-46

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: 158.37  E-value: 8.79e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665402770  812 DPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 883
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 ...
 648-717 3.14e-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: 136.81  E-value: 3.14e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  648 IDRWRATQVLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEEQRRPE 717
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 ...
 726-790 8.09e-36

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: 129.84  E-value: 8.09e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665402770  726 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 790
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
276-390 1.04e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  276 ASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF---IRNYQERVRETET 352
Cdd:COG4372    92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELeeqLESLQEELAALEQ 171

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 665402770  353 TNAKISGDRDRERF-QLLKQARDEAERSLALAQQLSARD 390
Cdd:COG4372   172 ELQALSEAEAEQALdELLKEANRNAEKEEELAEAEKLIE 210
 
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 ...
 812-883 8.79e-46

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: 158.37  E-value: 8.79e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665402770  812 DPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 883
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 ...
 648-717 3.14e-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: 136.81  E-value: 3.14e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  648 IDRWRATQVLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEEQRRPE 717
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 ...
 726-790 8.09e-36

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: 129.84  E-value: 8.09e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665402770  726 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 790
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 726-790 6.52e-16

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: 73.07  E-value: 6.52e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665402770   726 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKfLGVTRKFHQASIVHGIHVLR 790
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRLK 64
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
813-883 4.80e-10

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 56.51  E-value: 4.80e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665402770   813 PIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEpsFSGDTMAtALGIppSKNIIRRHLNTEFDALI 883
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGI--TSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 735-790 2.49e-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: 51.53  E-value: 2.49e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 665402770    735 EWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 790
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 649-711 5.09e-08

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: 50.73  E-value: 5.09e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665402770   649 DRWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAgLGLAHPMHRKKLRLAIE 711
Cdd:pfam00536    1 DGWSVEDVGEWLE-SIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQ 61
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 649-711 9.52e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 9.52e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665402770    649 DRWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIE 711
Cdd:smart00454    2 SQWSPESVADWLE-SIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQ 63
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
276-390 1.04e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  276 ASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF---IRNYQERVRETET 352
Cdd:COG4372    92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELeeqLESLQEELAALEQ 171

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 665402770  353 TNAKISGDRDRERF-QLLKQARDEAERSLALAQQLSARD 390
Cdd:COG4372   172 ELQALSEAEAEQALdELLKEANRNAEKEEELAEAEKLIE 210
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 274-390 3.51e-06

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: 50.84  E-value: 3.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   274 AVASGEGSAAKERIER------LESELRSVKNQL--LTMRLERKKLRTDKSD-LLGQVKqlcASLQEKEQELRDFIRNYQ 344
Cdd:pfam19220  210 RLRALEGQLAAEQAEReraeaqLEEAVEAHRAERasLRMKLEALTARAAATEqLLAEAR---NQLRDRDEAIRAAERRLK 286

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 665402770   345 ERVRETETTNAKISG-----DRDRERFQLLKQARDEA-ERSLALAQQLSARD 390
Cdd:pfam19220  287 EASIERDTLERRLAGleadlERRTQQFQEMQRARAELeERAEMLTKALAAKD 338
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 263-385 1.96e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   263 VGGVDTAPEMEAVASGEGSAAKERIERLESELRSVKNQLLTMRLER------KKLRTDKSD------------LLGQVKQ 324
Cdd:TIGR02169  162 IAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKREyegyellkekeaLERQKEA 241

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665402770   325 LCASLQEKEQELRDFIRNYQERVRET-------ETTNAKISGDRDRERFQLLKQARD------EAERSLALAQQ 385
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLeeieqllEELNKKIKDLGEEEQLRVKEKIGEleaeiaSLERSIAEKER 315
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
284-390 1.06e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  284 KERIERLES------ELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNY-QERVRETETTNAK 356
Cdd:PRK03918  591 EERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLE 670

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 665402770  357 ISGD--RDRERFQLLKQARDEAERSLA-LAQQLSARD 390
Cdd:PRK03918  671 LSRElaGLRAELEELEKRREEIKKTLEkLKEELEERE 707
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 815-864 1.97e-03

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: 37.66  E-value: 1.97e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 665402770    815 VWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSfsgDTMATALGI 864
Cdd:smart00454    3 QWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGI 49
 
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 ...
 812-883 8.79e-46

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: 158.37  E-value: 8.79e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665402770  812 DPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 883
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 ...
 648-717 3.14e-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: 136.81  E-value: 3.14e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  648 IDRWRATQVLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEEQRRPE 717
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 ...
 726-790 8.09e-36

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: 129.84  E-value: 8.09e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665402770  726 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 790
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 820-881 3.45e-32

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: 119.18  E-value: 3.45e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665402770  820 RFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDA 881
Cdd:cd09496     1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 816-883 6.31e-28

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: 107.54  E-value: 6.31e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665402770  816 WTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 883
Cdd:cd09569     5 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 731-790 8.45e-23

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: 92.60  E-value: 8.45e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  731 WVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 790
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 ...
 812-883 3.76e-22

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: 90.84  E-value: 3.76e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665402770  812 DPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 883
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 656-712 1.12e-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: 89.21  E-value: 1.12e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665402770  656 VLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEE 712
Cdd:cd09494     2 VCAWLEDFGLMPMYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
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 ...
 727-792 4.20e-19

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: 82.14  E-value: 4.20e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665402770  727 LGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLRIV 792
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 726-790 3.35e-17

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 76.58  E-value: 3.35e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665402770  726 QLGHTWVaTEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEkFLGVTRKFHQASIVHGIHVLR 790
Cdd:cd09566     1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
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 ...
 649-712 3.52e-16

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: 74.14  E-value: 3.52e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665402770  649 DRWRATQVLAWLEVALGMPQ-YSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEE 712
Cdd:cd09562     2 ALWNGPTVVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 726-790 6.52e-16

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: 73.07  E-value: 6.52e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665402770   726 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKfLGVTRKFHQASIVHGIHVLR 790
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRLK 64
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 650-711 2.02e-14

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: 68.79  E-value: 2.02e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665402770  650 RWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIE 711
Cdd:cd09563     3 EWSTEQVCDWLA-ELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
813-883 4.80e-10

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 56.51  E-value: 4.80e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665402770   813 PIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEpsFSGDTMAtALGIppSKNIIRRHLNTEFDALI 883
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGI--TSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 735-790 2.49e-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: 51.53  E-value: 2.49e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 665402770    735 EWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 790
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 649-711 5.09e-08

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: 50.73  E-value: 5.09e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665402770   649 DRWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAgLGLAHPMHRKKLRLAIE 711
Cdd:pfam00536    1 DGWSVEDVGEWLE-SIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQ 61
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 731-786 8.37e-08

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: 49.55  E-value: 8.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 665402770  731 WVAtEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKfLGVTRKFHQASIVHGI 786
Cdd:cd09487     1 DVA-EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAI 54
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 649-711 9.52e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 9.52e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665402770    649 DRWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIE 711
Cdd:smart00454    2 SQWSPESVADWLE-SIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQ 63
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
276-390 1.04e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  276 ASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF---IRNYQERVRETET 352
Cdd:COG4372    92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELeeqLESLQEELAALEQ 171

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 665402770  353 TNAKISGDRDRERF-QLLKQARDEAERSLALAQQLSARD 390
Cdd:COG4372   172 ELQALSEAEAEQALdELLKEANRNAEKEEELAEAEKLIE 210
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 655-712 2.49e-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: 45.69  E-value: 2.49e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 665402770  655 QVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAgLGLAHPMHRKKLRLAIEE 712
Cdd:cd09487     1 DVAEWLE-SLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAIQR 56
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 274-390 3.51e-06

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: 50.84  E-value: 3.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   274 AVASGEGSAAKERIER------LESELRSVKNQL--LTMRLERKKLRTDKSD-LLGQVKqlcASLQEKEQELRDFIRNYQ 344
Cdd:pfam19220  210 RLRALEGQLAAEQAEReraeaqLEEAVEAHRAERasLRMKLEALTARAAATEqLLAEAR---NQLRDRDEAIRAAERRLK 286

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 665402770   345 ERVRETETTNAKISG-----DRDRERFQLLKQARDEA-ERSLALAQQLSARD 390
Cdd:pfam19220  287 EASIERDTLERRLAGleadlERRTQQFQEMQRARAELeERAEMLTKALAAKD 338
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 282-389 5.84e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 5.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  282 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETEttnakisgDR 361
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE--------EL 384

                          90       100
                  ....*....|....*....|....*...
gi 665402770  362 DRERFQLLKQARDEAERSLALAQQLSAR 389
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEAL 412
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
282-448 1.05e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  282 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKS--DLLGQVKQLCASLQEKEQELRDF------IRNYQERVRETETT 353
Cdd:COG4717    92 ELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELeerleeLRELEEELEELEAE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  354 NAKISGDRDRERFQLLKQARDEAERSL----ALAQQLSARDLQLQRLQEQLQEARRQLTGCLSDQESLHSFAPLTPPSAA 429
Cdd:COG4717   172 LAELQEELEELLEQLSLATEEELQDLAeeleELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251

                         170
                  ....*....|....*....
gi 665402770  430 SGMLSQMAAASGMGGGLAG 448
Cdd:COG4717   252 LLIAAALLALLGLGGSLLS 270
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 651-708 1.88e-05

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: 43.86  E-value: 1.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665402770  651 WRATQVLAWLEVALGMPQYSARCAENVKSGKVLLEL---NDVELEAGLGLAHPMHRKKLRL 708
Cdd:cd09504     5 WTVEDTVEWLVNSVELPQYVEAFKENGVDGSALPRLavnNPSFLTSVLGIKDPIHRQKLSL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
281-390 2.59e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  281 SAAKERIERLESELRSVKNQLLTMRLE----RKKLRTDKSDLL---GQVKQLCASLQEKEQELRDFIRNYQERVRETETT 353
Cdd:COG4372    34 RKALFELDKLQEELEQLREELEQAREEleqlEEELEQARSELEqleEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 665402770  354 NAKISgDRDRERFQLLKQARDEAERSLALAQQLSARD 390
Cdd:COG4372   114 QEELE-ELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 282-385 1.96e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  282 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQElrdfIRNYQERVRETETTNAKISGDR 361
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD----IARLEERRRELEERLEELEEEL 325

                          90       100
                  ....*....|....*....|....*.
gi 665402770  362 DRERFQL--LKQARDEAERSLALAQQ 385
Cdd:COG1196   326 AELEEELeeLEEELEELEEELEEAEE 351
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 263-385 1.96e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   263 VGGVDTAPEMEAVASGEGSAAKERIERLESELRSVKNQLLTMRLER------KKLRTDKSD------------LLGQVKQ 324
Cdd:TIGR02169  162 IAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKREyegyellkekeaLERQKEA 241

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665402770   325 LCASLQEKEQELRDFIRNYQERVRET-------ETTNAKISGDRDRERFQLLKQARD------EAERSLALAQQ 385
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLeeieqllEELNKKIKDLGEEEQLRVKEKIGEleaeiaSLERSIAEKER 315
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 735-789 4.50e-04

SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) subfamily is a putative protein-protein interaction domain. SAM is widespread domain in proteins involved in signal transduction and regulation. In many cases SAM mediates homodimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188929  Cd Length: 67  Bit Score: 39.61  E-value: 4.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665402770  735 EWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKfLGVTRKFHQASIVHGIHVL 789
Cdd:cd09530    10 EWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPR-MGVTDFEHIKAIARKIREL 63
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
268-386 5.09e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  268 TAPEMEAVASGEGSAAKERIERLESELrsvknqlltmrlerKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERV 347
Cdd:COG2433   396 EAEREKEHEERELTEEEEEIRRLEEQV--------------ERLEAEVEELEAELEEKDERIERLERELSEARSEERREI 461

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 665402770  348 RETETTNAkisgdRDRERFQLLKQARDEAERSLALAQQL 386
Cdd:COG2433   462 RKDREISR-----LDREIERLERELEEERERIEELKRKL 495
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
284-377 5.34e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  284 KERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKIsgdrdR 363
Cdd:COG1340    14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL-----N 88

                          90
                  ....*....|....
gi 665402770  364 ERFQLLKQARDEAE 377
Cdd:COG1340    89 ELREELDELRKELA 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 282-385 6.64e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 6.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   282 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQElrdfIRNYQERVRETETTNAKISGDR 361
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ----KQILRERLANLERQLEELEAQL 325

                           90       100
                   ....*....|....*....|....
gi 665402770   362 DRerfqlLKQARDEAERSLALAQQ 385
Cdd:TIGR02168  326 EE-----LESKLDELAEELAELEE 344
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
734-790 8.45e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 38.79  E-value: 8.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 665402770   734 TEWLPDIGLPQYAEPFVQSLVD-ARMLDTLSKKELEKfLGVTRKFHQASIVHGIHVLR 790
Cdd:pfam07647   10 ADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKR-LGITSVGHRRKILKKIQELK 66
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 284-424 9.03e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.57  E-value: 9.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   284 KERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELrDFIRNYQERVRETETTNAkISGDRDR 363
Cdd:pfam15921  341 EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL-SLEKEQNKRLWDRDTGNS-ITIDHLR 418

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665402770   364 ERfqlLKQARDEAERSLALAQQLSARdlqlqrlqeQLQEARRQLTGCLSDQESLHSFAPLT 424
Cdd:pfam15921  419 RE---LDDRNMEVQRLEALLKAMKSE---------CQGQMERQMAAIQGKNESLEKVSSLT 467
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 269-390 1.05e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 43.09  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   269 APEMEAVASGEGSAA--------KERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF- 339
Cdd:pfam05701  107 VEEMEQGIADEASVAakaqlevaKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELt 186

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665402770   340 -----IRNYQERVR------ETETTNAKISGDRDRERFQL-LKQARDEAERslaLAQQL-SARD 390
Cdd:pfam05701  187 ieliaTKESLESAHaahleaEEHRIGAALAREQDKLNWEKeLKQAEEELQR---LNQQLlSAKD 247
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
284-390 1.06e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  284 KERIERLES------ELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNY-QERVRETETTNAK 356
Cdd:PRK03918  591 EERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLE 670

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 665402770  357 ISGD--RDRERFQLLKQARDEAERSLA-LAQQLSARD 390
Cdd:PRK03918  671 LSRElaGLRAELEELEKRREEIKKTLEkLKEELEERE 707
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 282-380 1.52e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  282 AAKERIERLESELRSVKN---------QLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETET 352
Cdd:COG1579    70 EVEARIKKYEEQLGNVRNnkeyealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149

                          90       100
                  ....*....|....*....|....*...
gi 665402770  353 TNAKIsgDRDRERfqlLKQARDEAERSL 380
Cdd:COG1579   150 ELAEL--EAELEE---LEAEREELAAKI 172
mukB PRK04863
chromosome partition protein MukB;
265-388 1.56e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  265 GVDTAPEMEAVASgegsAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDL-------------LGQVKQLCASLQE 331
Cdd:PRK04863  549 NLDDEDELEQLQE----ELEARLESLSESVSEARERRMALRQQLEQLQARIQRLaarapawlaaqdaLARLREQSGEEFE 624

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665402770  332 KEQELRDFIRNYQERVRETETTNAKISgdrdRERFQLLKQARD-------EAERSLALAQQLSA 388
Cdd:PRK04863  625 DSQDVTEYMQQLLERERELTVERDELA----ARKQALDEEIERlsqpggsEDPRLNALAERFGG 684
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 285-385 1.94e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  285 ERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDfIRN---YQERVRETETTNAKISgDR 361
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNnkeYEALQKEIESLKRRIS-DL 108

                          90       100
                  ....*....|....*....|....
gi 665402770  362 DRERFQLLKQaRDEAERSLALAQQ 385
Cdd:COG1579   109 EDEILELMER-IEELEEELAELEA 131
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 815-864 1.97e-03

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: 37.66  E-value: 1.97e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 665402770    815 VWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSfsgDTMATALGI 864
Cdd:smart00454    3 QWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGI 49
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 271-377 2.34e-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: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   271 EMEAVASgEGSAAKERIERLESELRSV--KNQLLT---MRLErKKLRTDkSDLLGQVKQLCASLQEKEQELRDFIRNYQE 345
Cdd:pfam01576    6 EMQAKEE-ELQKVKERQQKAESELKELekKHQQLCeekNALQ-EQLQAE-TELCAEAEEMRARLAARKQELEEILHELES 82

                           90       100       110
                   ....*....|....*....|....*....|....
gi 665402770   346 RVRETETTNAKISGDRDR--ERFQLLKQARDEAE 377
Cdd:pfam01576   83 RLEEEEERSQQLQNEKKKmqQHIQDLEEQLDEEE 116
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 285-386 3.20e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   285 ERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF---IRNYQERVRETETTNAKISGDR 361
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELeeeLEELEAALRDLESRLGDLKKER 891

                           90       100
                   ....*....|....*....|....*..
gi 665402770   362 DRERFQL--LKQARDEAERSLALAQQL 386
Cdd:TIGR02169  892 DELEAQLreLERKIEELEAQIEKKRKR 918
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 655-714 3.42e-03

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: 36.91  E-value: 3.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  655 QVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAgLGLAHPMHRKKLRLAIEEQR 714
Cdd:cd09533     1 DVADWLS-SLGLPQYEDQFIENGITGDVLVALDHEDLKE-MGITSVGHRLTILKAVYELK 58
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
280-435 3.52e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  280 GSAAKERIERLESELRSVKNQLLTMRLERKKLRtDKSDLLGQVKQLCASLQEKEQELRDfIRNYQERVRETETTNAKIsg 359
Cdd:COG4913   605 GFDNRAKLAALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERL-- 680

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665402770  360 DRDRERFQLLKQARDEAERSL-ALAQQLSARDLQLQRLQEQLQEARRQLTGCLSDQESLHSFAPLTPPSAASGMLSQ 435
Cdd:COG4913   681 DASSDDLAALEEQLEELEAELeELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 282-389 5.07e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 5.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   282 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQElrdfIRNYQERVRETETTNAKISGDR 361
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELEAEI 763

                           90       100
                   ....*....|....*....|....*...
gi 665402770   362 dRERFQLLKQARDEAERSLALAQQLSAR 389
Cdd:TIGR02168  764 -EELEERLEEAEEELAEAEAEIEELEAQ 790
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
273-379 5.63e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  273 EAVASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQvkQLCASLQEKEQELRDFIRNYQERVRETET 352
Cdd:COG4717   420 ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAELRELAEEWAALKL 497

                          90       100
                  ....*....|....*....|....*..
gi 665402770  353 TnakisgdrdrerFQLLKQARDEAERS 379
Cdd:COG4717   498 A------------LELLEEAREEYREE 512
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
269-381 5.86e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  269 APEMEAVAS---GEGSAAKERIERLESELRSVKNQLltMRLERKK----LRTDKSDLLGQVKQLCASLQEKEQELRDFIR 341
Cdd:PRK02224  553 AEEKREAAAeaeEEAEEAREEVAELNSKLAELKERI--ESLERIRtllaAIADAEDEIERLREKREALAELNDERRERLA 630

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 665402770  342 NYQERVRETEttnakisGDRDRERFQLLKQARDEAERSLA 381
Cdd:PRK02224  631 EKRERKRELE-------AEFDEARIEEAREDKERAEEYLE 663
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 285-390 6.02e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.87  E-value: 6.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   285 ERIERLESELRSVKNQL--LTMRLERKKLRTDKSDLlgQVKQLCASLQEKEqelrdfirnyqervRETETTNAKISGDRD 362
Cdd:pfam15921  461 EKVSSLTAQLESTKEMLrkVVEELTAKKMTLESSER--TVSDLTASLQEKE--------------RAIEATNAEITKLRS 524

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 665402770   363 RE--RFQLLKQARDEAE--RSL-----ALAQQLSARD 390
Cdd:pfam15921  525 RVdlKLQELQHLKNEGDhlRNVqteceALKLQMAEKD 561
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
271-397 6.19e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  271 EMEAVASgEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFirnyQERVRET 350
Cdd:COG4372    39 ELDKLQE-ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL----QEEAEEL 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 665402770  351 ETTNAKISGDRDR--ERFQLLKQARDEAERSLALAQ-QLSARDLQLQRLQ 397
Cdd:COG4372   114 QEELEELQKERQDleQQRKQLEAQIAELQSEIAEREeELKELEEQLESLQ 163
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 285-390 6.75e-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: 40.49  E-value: 6.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   285 ERIErLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTN-AKIsgdrdr 363
Cdd:pfam05557    3 ELIE-SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALrEQA------ 75

                           90       100
                   ....*....|....*....|....*....
gi 665402770   364 ERFQLLKQARDEAERSLA--LAQQLSARD 390
Cdd:pfam05557   76 ELNRLKKKYLEALNKKLNekESQLADARE 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 282-396 7.17e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770   282 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLcasLQEKEQELRDFIRN----YQERVRETETTNAKI 357
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL---QQEIEELLKKLEEAelkeLQAELEELEEELEEL 452

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 665402770   358 SGDRD---------RERFQLLKQARDEAERSLalaQQLSARDLQLQRL 396
Cdd:TIGR02168  453 QEELErleealeelREELEEAEQALDAAEREL---AQLQARLDSLERL 497
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
287-415 8.31e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 8.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  287 IERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKISGDRDRerf 366
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--- 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 665402770  367 qlLKQARDEAERSLALAQQLSARDLQLQRLQEQLQEARRQLTGCLSDQE 415
Cdd:COG4372   103 --LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
305-385 8.88e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 37.96  E-value: 8.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402770  305 RLER-KKLRTDKSD----LLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKISGDRDRERF-QLLKQARDEAER 378
Cdd:COG2882     6 RLQTlLDLAEKEEDeaarELGQAQQALEQAEEQLEQLEQYREEYEQRLQQKLQQGLSAAQLRNYQQFiARLDEAIEQQQQ 85


                  ....*..
gi 665402770  379 SLALAQQ 385
Cdd:COG2882    86 QVAQAEQ 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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