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Conserved domains on  [gi|161077383|ref|NP_001097414|]
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Liprin-gamma, isoform C [Drosophila melanogaster]

Protein Classification

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 ...
 882-953 1.41e-45

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: 157.99  E-value: 1.41e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077383  882 DPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 953
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 ...
 718-787 3.16e-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: 3.16e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  718 IDRWRATQVLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEEQRRPE 787
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 ...
 796-860 8.62e-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: 8.62e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077383  796 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 860
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
346-460 6.22e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.06  E-value: 6.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  346 ASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF---IRNYQERVRETET 422
Cdd:COG4372    92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELeeqLESLQEELAALEQ 171

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 161077383  423 TNAKISGDRDRERF-QLLKQARDEAERSLALAQQLSARD 460
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 ...
 882-953 1.41e-45

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: 157.99  E-value: 1.41e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077383  882 DPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 953
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 ...
 718-787 3.16e-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: 3.16e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  718 IDRWRATQVLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEEQRRPE 787
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 ...
 796-860 8.62e-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: 8.62e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077383  796 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 860
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 796-860 6.95e-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: 6.95e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077383   796 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKfLGVTRKFHQASIVHGIHVLR 860
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRLK 64
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
883-953 5.12e-10

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 56.51  E-value: 5.12e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077383   883 PIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEpsFSGDTMAtALGIppSKNIIRRHLNTEFDALI 953
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGI--TSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 805-860 2.65e-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: 2.65e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 161077383    805 EWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 860
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 719-781 5.43e-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: 5.43e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077383   719 DRWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAgLGLAHPMHRKKLRLAIE 781
Cdd:pfam00536    1 DGWSVEDVGEWLE-SIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQ 61
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
346-460 6.22e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.06  E-value: 6.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  346 ASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF---IRNYQERVRETET 422
Cdd:COG4372    92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELeeqLESLQEELAALEQ 171

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 161077383  423 TNAKISGDRDRERF-QLLKQARDEAERSLALAQQLSARD 460
Cdd:COG4372   172 ELQALSEAEAEQALdELLKEANRNAEKEEELAEAEKLIE 210
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 719-781 1.02e-07

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: 1.02e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077383    719 DRWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIE 781
Cdd:smart00454    2 SQWSPESVADWLE-SIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQ 63
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 344-460 2.69e-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: 51.22  E-value: 2.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   344 AVASGEGSAAKERIER------LESELRSVKNQL--LTMRLERKKLRTDKSD-LLGQVKqlcASLQEKEQELRDFIRNYQ 414
Cdd:pfam19220  210 RLRALEGQLAAEQAEReraeaqLEEAVEAHRAERasLRMKLEALTARAAATEqLLAEAR---NQLRDRDEAIRAAERRLK 286

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 161077383   415 ERVRETETTNAKISG-----DRDRERFQLLKQARDEA-ERSLALAQQLSARD 460
Cdd:pfam19220  287 EASIERDTLERRLAGleadlERRTQQFQEMQRARAELeERAEMLTKALAAKD 338
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 333-455 1.65e-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: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   333 VGGVDTAPEMEAVASGEGSAAKERIERLESELRSVKNQLLTMRLER------KKLRTDKSD------------LLGQVKQ 394
Cdd:TIGR02169  162 IAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKREyegyellkekeaLERQKEA 241

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161077383   395 LCASLQEKEQELRDFIRNYQERVRET-------ETTNAKISGDRDRERFQLLKQARD------EAERSLALAQQ 455
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLeeieqllEELNKKIKDLGEEEQLRVKEKIGEleaeiaSLERSIAEKER 315
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
354-460 1.15e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  354 KERIERLES------ELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNY-QERVRETETTNAK 426
Cdd:PRK03918  591 EERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLE 670

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 161077383  427 ISGD--RDRERFQLLKQARDEAERSLA-LAQQLSARD 460
Cdd:PRK03918  671 LSRElaGLRAELEELEKRREEIKKTLEkLKEELEERE 707
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 885-934 2.10e-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: 2.10e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 161077383    885 VWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSfsgDTMATALGI 934
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 ...
 882-953 1.41e-45

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: 157.99  E-value: 1.41e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077383  882 DPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 953
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 ...
 718-787 3.16e-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: 3.16e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  718 IDRWRATQVLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEEQRRPE 787
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 ...
 796-860 8.62e-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: 8.62e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077383  796 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 860
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 ...
 890-951 6.03e-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: 118.80  E-value: 6.03e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077383  890 RFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDA 951
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 ...
 886-953 9.09e-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: 107.16  E-value: 9.09e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161077383  886 WTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 953
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 ...
 801-860 9.00e-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: 9.00e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  801 WVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 860
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 ...
 882-953 4.05e-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: 4.05e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077383  882 DPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 953
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 ...
 726-782 1.19e-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: 1.19e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 161077383  726 VLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEE 782
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 ...
 797-862 4.48e-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: 4.48e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161077383  797 LGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLRIV 862
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 ...
 796-860 3.57e-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: 3.57e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077383  796 QLGHTWVaTEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEkFLGVTRKFHQASIVHGIHVLR 860
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 ...
 719-782 3.44e-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: 3.44e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077383  719 DRWRATQVLAWLEVALGMPQ-YSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEE 782
Cdd:cd09562     2 ALWNGPTVVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 796-860 6.95e-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: 6.95e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077383   796 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKfLGVTRKFHQASIVHGIHVLR 860
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 ...
 720-781 2.15e-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: 2.15e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077383  720 RWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIE 781
Cdd:cd09563     3 EWSTEQVCDWLA-ELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
883-953 5.12e-10

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 56.51  E-value: 5.12e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077383   883 PIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEpsFSGDTMAtALGIppSKNIIRRHLNTEFDALI 953
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGI--TSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 805-860 2.65e-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: 2.65e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 161077383    805 EWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 860
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 719-781 5.43e-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: 5.43e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077383   719 DRWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAgLGLAHPMHRKKLRLAIE 781
Cdd:pfam00536    1 DGWSVEDVGEWLE-SIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQ 61
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
346-460 6.22e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.06  E-value: 6.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  346 ASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF---IRNYQERVRETET 422
Cdd:COG4372    92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELeeqLESLQEELAALEQ 171

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 161077383  423 TNAKISGDRDRERF-QLLKQARDEAERSLALAQQLSARD 460
Cdd:COG4372   172 ELQALSEAEAEQALdELLKEANRNAEKEEELAEAEKLIE 210
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 801-856 8.92e-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: 8.92e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161077383  801 WVAtEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKfLGVTRKFHQASIVHGI 856
Cdd:cd09487     1 DVA-EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAI 54
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 719-781 1.02e-07

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: 1.02e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077383    719 DRWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIE 781
Cdd:smart00454    2 SQWSPESVADWLE-SIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQ 63
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 725-782 2.65e-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: 2.65e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 161077383  725 QVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAgLGLAHPMHRKKLRLAIEE 782
Cdd:cd09487     1 DVAEWLE-SLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAIQR 56
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 344-460 2.69e-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: 51.22  E-value: 2.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   344 AVASGEGSAAKERIER------LESELRSVKNQL--LTMRLERKKLRTDKSD-LLGQVKqlcASLQEKEQELRDFIRNYQ 414
Cdd:pfam19220  210 RLRALEGQLAAEQAEReraeaqLEEAVEAHRAERasLRMKLEALTARAAATEqLLAEAR---NQLRDRDEAIRAAERRLK 286

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 161077383   415 ERVRETETTNAKISG-----DRDRERFQLLKQARDEA-ERSLALAQQLSARD 460
Cdd:pfam19220  287 EASIERDTLERRLAGleadlERRTQQFQEMQRARAELeERAEMLTKALAAKD 338
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 352-459 4.97e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 4.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  352 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETEttnakisgDR 431
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE--------EL 384

                          90       100
                  ....*....|....*....|....*...
gi 161077383  432 DRERFQLLKQARDEAERSLALAQQLSAR 459
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEAL 412
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
352-518 1.05e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  352 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKS--DLLGQVKQLCASLQEKEQELRDF------IRNYQERVRETETT 423
Cdd:COG4717    92 ELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELeerleeLRELEEELEELEAE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  424 NAKISGDRDRERFQLLKQARDEAERSL----ALAQQLSARDLQLQRLQEQLQEARRQLTGCLSDQESLHSFAPLTPPSAA 499
Cdd:COG4717   172 LAELQEELEELLEQLSLATEEELQDLAeeleELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251

                         170
                  ....*....|....*....
gi 161077383  500 SGMLSQMAAASGMGGGLAG 518
Cdd:COG4717   252 LLIAAALLALLGLGGSLLS 270
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
351-460 1.60e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  351 SAAKERIERLESELRSVKNQLLTMRLE----RKKLRTDKSDLL---GQVKQLCASLQEKEQELRDFIRNYQERVRETETT 423
Cdd:COG4372    34 RKALFELDKLQEELEQLREELEQAREEleqlEEELEQARSELEqleEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 161077383  424 NAKISgDRDRERFQLLKQARDEAERSLALAQQLSARD 460
Cdd:COG4372   114 QEELE-ELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 721-778 2.00e-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: 2.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077383  721 WRATQVLAWLEVALGMPQYSARCAENVKSGKVLLEL---NDVELEAGLGLAHPMHRKKLRL 778
Cdd:cd09504     5 WTVEDTVEWLVNSVELPQYVEAFKENGVDGSALPRLavnNPSFLTSVLGIKDPIHRQKLSL 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 352-455 1.62e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  352 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQElrdfIRNYQERVRETETTNAKISGDR 431
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD----IARLEERRRELEERLEELEEEL 325

                          90       100
                  ....*....|....*....|....*.
gi 161077383  432 DRERFQL--LKQARDEAERSLALAQQ 455
Cdd:COG1196   326 AELEEELeeLEEELEELEEELEEAEE 351
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 333-455 1.65e-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: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   333 VGGVDTAPEMEAVASGEGSAAKERIERLESELRSVKNQLLTMRLER------KKLRTDKSD------------LLGQVKQ 394
Cdd:TIGR02169  162 IAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKREyegyellkekeaLERQKEA 241

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161077383   395 LCASLQEKEQELRDFIRNYQERVRET-------ETTNAKISGDRDRERFQLLKQARD------EAERSLALAQQ 455
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLeeieqllEELNKKIKDLGEEEQLRVKEKIGEleaeiaSLERSIAEKER 315
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 805-859 4.80e-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: 4.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 161077383  805 EWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKfLGVTRKFHQASIVHGIHVL 859
Cdd:cd09530    10 EWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPR-MGVTDFEHIKAIARKIREL 63
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
338-456 5.12e-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: 5.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  338 TAPEMEAVASGEGSAAKERIERLESELrsvknqlltmrlerKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERV 417
Cdd:COG2433   396 EAEREKEHEERELTEEEEEIRRLEEQV--------------ERLEAEVEELEAELEEKDERIERLERELSEARSEERREI 461

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 161077383  418 RETETTNAkisgdRDRERFQLLKQARDEAERSLALAQQL 456
Cdd:COG2433   462 RKDREISR-----LDREIERLERELEEERERIEELKRKL 495
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
354-447 5.74e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 5.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  354 KERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKIsgdrdR 433
Cdd:COG1340    14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL-----N 88

                          90
                  ....*....|....
gi 161077383  434 ERFQLLKQARDEAE 447
Cdd:COG1340    89 ELREELDELRKELA 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 352-459 5.83e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 5.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  352 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKISGDR 431
Cdd:COG1196   327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406

                          90       100
                  ....*....|....*....|....*...
gi 161077383  432 DRERFQLLKQARDEAERSLALAQQLSAR 459
Cdd:COG1196   407 EAEEALLERLERLEEELEELEEALAELE 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 352-455 5.89e-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: 44.28  E-value: 5.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   352 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQElrdfIRNYQERVRETETTNAKISGDR 431
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ----KQILRERLANLERQLEELEAQL 325

                           90       100
                   ....*....|....*....|....
gi 161077383   432 DRerfqlLKQARDEAERSLALAQQ 455
Cdd:TIGR02168  326 EE-----LESKLDELAEELAELEE 344
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 339-460 8.26e-04

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: 43.48  E-value: 8.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   339 APEMEAVASGEGSAA--------KERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF- 409
Cdd:pfam05701  107 VEEMEQGIADEASVAakaqlevaKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELt 186

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161077383   410 -----IRNYQERVR------ETETTNAKISGDRDRERFQL-LKQARDEAERslaLAQQL-SARD 460
Cdd:pfam05701  187 ieliaTKESLESAHaahleaEEHRIGAALAREQDKLNWEKeLKQAEEELQR---LNQQLlSAKD 247
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
804-860 9.00e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 38.79  E-value: 9.00e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 161077383   804 TEWLPDIGLPQYAEPFVQSLVD-ARMLDTLSKKELEKfLGVTRKFHQASIVHGIHVLR 860
Cdd:pfam07647   10 ADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKR-LGITSVGHRRKILKKIQELK 66
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 354-494 9.88e-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: 9.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   354 KERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELrDFIRNYQERVRETETTNAkISGDRDR 433
Cdd:pfam15921  341 EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL-SLEKEQNKRLWDRDTGNS-ITIDHLR 418

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077383   434 ERfqlLKQARDEAERSLALAQQLSARdlqlqrlqeQLQEARRQLTGCLSDQESLHSFAPLT 494
Cdd:pfam15921  419 RE---LDDRNMEVQRLEALLKAMKSE---------CQGQMERQMAAIQGKNESLEKVSSLT 467
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
354-460 1.15e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  354 KERIERLES------ELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNY-QERVRETETTNAK 426
Cdd:PRK03918  591 EERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLE 670

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 161077383  427 ISGD--RDRERFQLLKQARDEAERSLA-LAQQLSARD 460
Cdd:PRK03918  671 LSRElaGLRAELEELEKRREEIKKTLEkLKEELEERE 707
mukB PRK04863
chromosome partition protein MukB;
335-458 1.60e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  335 GVDTAPEMEAVASgegsAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDL-------------LGQVKQLCASLQE 401
Cdd:PRK04863  549 NLDDEDELEQLQE----ELEARLESLSESVSEARERRMALRQQLEQLQARIQRLaarapawlaaqdaLARLREQSGEEFE 624

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161077383  402 KEQELRDFIRNYQERVRETETTNAKISgdrdRERFQLLKQARD-------EAERSLALAQQLSA 458
Cdd:PRK04863  625 DSQDVTEYMQQLLERERELTVERDELA----ARKQALDEEIERlsqpggsEDPRLNALAERFGG 684
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 352-450 1.63e-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: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  352 AAKERIERLESELRSVKN---------QLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETET 422
Cdd:COG1579    70 EVEARIKKYEEQLGNVRNnkeyealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149

                          90       100
                  ....*....|....*....|....*...
gi 161077383  423 TNAKIsgDRDRERfqlLKQARDEAERSL 450
Cdd:COG1579   150 ELAEL--EAELEE---LEAEREELAAKI 172
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 341-447 1.97e-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: 42.47  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   341 EMEAVASgEGSAAKERIERLESELRSV--KNQLLT---MRLErKKLRTDkSDLLGQVKQLCASLQEKEQELRDFIRNYQE 415
Cdd:pfam01576    6 EMQAKEE-ELQKVKERQQKAESELKELekKHQQLCeekNALQ-EQLQAE-TELCAEAEEMRARLAARKQELEEILHELES 82

                           90       100       110
                   ....*....|....*....|....*....|....
gi 161077383   416 RVRETETTNAKISGDRDR--ERFQLLKQARDEAE 447
Cdd:pfam01576   83 RLEEEEERSQQLQNEKKKmqQHIQDLEEQLDEEE 116
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 355-455 2.08e-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: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  355 ERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDfIRN---YQERVRETETTNAKISgDR 431
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNnkeYEALQKEIESLKRRIS-DL 108

                          90       100
                  ....*....|....*....|....
gi 161077383  432 DRERFQLLKQaRDEAERSLALAQQ 455
Cdd:COG1579   109 EDEILELMER-IEELEEELAELEA 131
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 885-934 2.10e-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: 2.10e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 161077383    885 VWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSfsgDTMATALGI 934
Cdd:smart00454    3 QWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGI 49
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 355-456 2.81e-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: 41.98  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   355 ERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF---IRNYQERVRETETTNAKISGDR 431
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELeeeLEELEAALRDLESRLGDLKKER 891

                           90       100
                   ....*....|....*....|....*..
gi 161077383   432 DRERFQL--LKQARDEAERSLALAQQL 456
Cdd:TIGR02169  892 DELEAQLreLERKIEELEAQIEKKRKR 918
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
350-505 3.60e-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: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  350 GSAAKERIERLESELRSVKNQLLTMRLERKKLRtDKSDLLGQVKQLCASLQEKEQELRDfIRNYQERVRETETTNAKIsg 429
Cdd:COG4913   605 GFDNRAKLAALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERL-- 680

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161077383  430 DRDRERFQLLKQARDEAERSL-ALAQQLSARDLQLQRLQEQLQEARRQLTGCLSDQESLHSFAPLTPPSAASGMLSQ 505
Cdd:COG4913   681 DASSDDLAALEEQLEELEAELeELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 725-784 3.64e-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: 3.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  725 QVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAgLGLAHPMHRKKLRLAIEEQR 784
Cdd:cd09533     1 DVADWLS-SLGLPQYEDQFIENGITGDVLVALDHEDLKE-MGITSVGHRLTILKAVYELK 58
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
341-467 3.92e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  341 EMEAVASgEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFirnyQERVRET 420
Cdd:COG4372    39 ELDKLQE-ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL----QEEAEEL 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 161077383  421 ETTNAKISGDRDR--ERFQLLKQARDEAERSLALAQ-QLSARDLQLQRLQ 467
Cdd:COG4372   114 QEELEELQKERQDleQQRKQLEAQIAELQSEIAEREeELKELEEQLESLQ 163
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 352-459 4.72e-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: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   352 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQElrdfIRNYQERVRETETTNAKISGDR 431
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELEAEI 763

                           90       100
                   ....*....|....*....|....*...
gi 161077383   432 dRERFQLLKQARDEAERSLALAQQLSAR 459
Cdd:TIGR02168  764 -EELEERLEEAEEELAEAEAEIEELEAQ 790
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
339-451 5.36e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  339 APEMEAVAS---GEGSAAKERIERLESELRSVKNQLltMRLERKK----LRTDKSDLLGQVKQLCASLQEKEQELRDFIR 411
Cdd:PRK02224  553 AEEKREAAAeaeEEAEEAREEVAELNSKLAELKERI--ESLERIRtllaAIADAEDEIERLREKREALAELNDERRERLA 630

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 161077383  412 NYQERVRETEttnakisGDRDRERFQLLKQARDEAERSLA 451
Cdd:PRK02224  631 EKRERKRELE-------AEFDEARIEEAREDKERAEEYLE 663
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
343-449 5.51e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  343 EAVASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQvkQLCASLQEKEQELRDFIRNYQERVRETET 422
Cdd:COG4717   420 ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAELRELAEEWAALKL 497

                          90       100
                  ....*....|....*....|....*..
gi 161077383  423 TnakisgdrdrerFQLLKQARDEAERS 449
Cdd:COG4717   498 A------------LELLEEAREEYREE 512
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
357-485 6.04e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  357 IERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKISGDRDRerf 436
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--- 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 161077383  437 qlLKQARDEAERSLALAQQLSARDLQLQRLQEQLQEARRQLTGCLSDQE 485
Cdd:COG4372   103 --LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 355-460 6.47e-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: 6.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   355 ERIERLESELRSVKNQL--LTMRLERKKLRTDKSDLlgQVKQLCASLQEKEqelrdfirnyqervRETETTNAKISGDRD 432
Cdd:pfam15921  461 EKVSSLTAQLESTKEMLrkVVEELTAKKMTLESSER--TVSDLTASLQEKE--------------RAIEATNAEITKLRS 524

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 161077383   433 RE--RFQLLKQARDEAE--RSL-----ALAQQLSARD 460
Cdd:pfam15921  525 RVdlKLQELQHLKNEGDhlRNVqteceALKLQMAEKD 561
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 352-466 6.51e-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: 40.81  E-value: 6.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   352 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLcasLQEKEQELRDFIRN----YQERVRETETTNAKI 427
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL---QQEIEELLKKLEEAelkeLQAELEELEEELEEL 452

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 161077383   428 SGDRD---------RERFQLLKQARDEAERSLalaQQLSARDLQLQRL 466
Cdd:TIGR02168  453 QEELErleealeelREELEEAEQALDAAEREL---AQLQARLDSLERL 497
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 355-460 6.55e-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: 6.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383   355 ERIErLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTN-AKIsgdrdr 433
Cdd:pfam05557    3 ELIE-SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALrEQA------ 75

                           90       100
                   ....*....|....*....|....*....
gi 161077383   434 ERFQLLKQARDEAERSLA--LAQQLSARD 460
Cdd:pfam05557   76 ELNRLKKKYLEALNKKLNekESQLADARE 104
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
375-455 9.50e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 37.96  E-value: 9.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077383  375 RLER-KKLRTDKSD----LLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKISGDRDRERF-QLLKQARDEAER 448
Cdd:COG2882     6 RLQTlLDLAEKEEDeaarELGQAQQALEQAEEQLEQLEQYREEYEQRLQQKLQQGLSAAQLRNYQQFiARLDEAIEQQQQ 85


                  ....*..
gi 161077383  449 SLALAQQ 455
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.
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