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Conserved domains on  [gi|161077381|ref|NP_995922|]
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Liprin-gamma, isoform B [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 ...
 753-824 9.18e-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: 9.18e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077381  753 DPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 824
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 ...
 589-658 2.94e-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: 2.94e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  589 IDRWRATQVLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEEQRRPE 658
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 ...
 667-731 1.24e-35

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


:

Pssm-ID: 188966  Cd Length: 65  Bit Score: 129.07  E-value: 1.24e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077381  667 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 731
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
217-331 5.62e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.06  E-value: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  217 ASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF---IRNYQERVRETET 293
Cdd:COG4372    92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELeeqLESLQEELAALEQ 171

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 161077381  294 TNAKISGDRDRERF-QLLKQARDEAERSLALAQQLSARD 331
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 ...
 753-824 9.18e-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: 9.18e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077381  753 DPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 824
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 ...
 589-658 2.94e-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: 2.94e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  589 IDRWRATQVLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEEQRRPE 658
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 ...
 667-731 1.24e-35

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 129.07  E-value: 1.24e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077381  667 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 731
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 667-731 6.16e-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: 6.16e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077381   667 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKfLGVTRKFHQASIVHGIHVLR 731
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRLK 64
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
754-824 4.54e-10

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 56.51  E-value: 4.54e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077381   754 PIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEpsFSGDTMAtALGIppSKNIIRRHLNTEFDALI 824
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGI--TSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 676-731 2.35e-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: 2.35e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 161077381    676 EWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 731
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 590-652 4.81e-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: 4.81e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077381   590 DRWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAgLGLAHPMHRKKLRLAIE 652
Cdd:pfam00536    1 DGWSVEDVGEWLE-SIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQ 61
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
217-331 5.62e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.06  E-value: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  217 ASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF---IRNYQERVRETET 293
Cdd:COG4372    92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELeeqLESLQEELAALEQ 171

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 161077381  294 TNAKISGDRDRERF-QLLKQARDEAERSLALAQQLSARD 331
Cdd:COG4372   172 ELQALSEAEAEQALdELLKEANRNAEKEEELAEAEKLIE 210
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 590-652 8.99e-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: 8.99e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077381    590 DRWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIE 652
Cdd:smart00454    2 SQWSPESVADWLE-SIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQ 63
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 215-331 2.98e-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: 2.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   215 AVASGEGSAAKERIER------LESELRSVKNQL--LTMRLERKKLRTDKSD-LLGQVKqlcASLQEKEQELRDFIRNYQ 285
Cdd:pfam19220  210 RLRALEGQLAAEQAEReraeaqLEEAVEAHRAERasLRMKLEALTARAAATEqLLAEAR---NQLRDRDEAIRAAERRLK 286

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 161077381   286 ERVRETETTNAKISG-----DRDRERFQLLKQARDEA-ERSLALAQQLSARD 331
Cdd:pfam19220  287 EASIERDTLERRLAGleadlERRTQQFQEMQRARAELeERAEMLTKALAAKD 338
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 204-326 1.56e-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: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   204 VGGVDTAPEMEAVASGEGSAAKERIERLESELRSVKNQLLTMRLER------KKLRTDKSD------------LLGQVKQ 265
Cdd:TIGR02169  162 IAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKREyegyellkekeaLERQKEA 241

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161077381   266 LCASLQEKEQELRDFIRNYQERVRET-------ETTNAKISGDRDRERFQLLKQARD------EAERSLALAQQ 326
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLeeieqllEELNKKIKDLGEEEQLRVKEKIGEleaeiaSLERSIAEKER 315
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
225-331 9.97e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 9.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  225 KERIERLES------ELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNY-QERVRETETTNAK 297
Cdd:PRK03918  591 EERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLE 670

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 161077381  298 ISGD--RDRERFQLLKQARDEAERSLA-LAQQLSARD 331
Cdd:PRK03918  671 LSRElaGLRAELEELEKRREEIKKTLEkLKEELEERE 707
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 756-805 1.86e-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: 1.86e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 161077381    756 VWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSfsgDTMATALGI 805
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 ...
 753-824 9.18e-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: 9.18e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077381  753 DPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 824
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 ...
 589-658 2.94e-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: 2.94e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  589 IDRWRATQVLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEEQRRPE 658
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 ...
 667-731 1.24e-35

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 129.07  E-value: 1.24e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077381  667 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 731
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 ...
 761-822 5.56e-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: 5.56e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077381  761 RFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDA 822
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 ...
 757-824 7.53e-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: 7.53e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161077381  757 WTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 824
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 ...
 672-731 7.98e-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: 7.98e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  672 WVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 731
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 ...
 753-824 4.11e-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: 4.11e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077381  753 DPIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSFSGDTMATALGIPPSKNIIRRHLNTEFDALI 824
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 ...
 597-653 1.05e-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: 1.05e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 161077381  597 VLAWLEVALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEE 653
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 ...
 668-733 3.97e-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: 3.97e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161077381  668 LGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLRIV 733
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 ...
 667-731 3.16e-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: 3.16e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077381  667 QLGHTWVaTEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEkFLGVTRKFHQASIVHGIHVLR 731
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 ...
 590-653 2.79e-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: 2.79e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077381  590 DRWRATQVLAWLEVALGMPQ-YSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIEE 653
Cdd:cd09562     2 ALWNGPTVVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 667-731 6.16e-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: 6.16e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077381   667 QLGHTWVATEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKfLGVTRKFHQASIVHGIHVLR 731
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 ...
 591-652 1.91e-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: 1.91e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077381  591 RWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIE 652
Cdd:cd09563     3 EWSTEQVCDWLA-ELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
754-824 4.54e-10

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 56.51  E-value: 4.54e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077381   754 PIVWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEpsFSGDTMAtALGIppSKNIIRRHLNTEFDALI 824
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGI--TSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 676-731 2.35e-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: 2.35e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 161077381    676 EWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKFLGVTRKFHQASIVHGIHVLR 731
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 590-652 4.81e-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: 4.81e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077381   590 DRWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAgLGLAHPMHRKKLRLAIE 652
Cdd:pfam00536    1 DGWSVEDVGEWLE-SIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQ 61
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
217-331 5.62e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.06  E-value: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  217 ASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF---IRNYQERVRETET 293
Cdd:COG4372    92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELeeqLESLQEELAALEQ 171

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 161077381  294 TNAKISGDRDRERF-QLLKQARDEAERSLALAQQLSARD 331
Cdd:COG4372   172 ELQALSEAEAEQALdELLKEANRNAEKEEELAEAEKLIE 210
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 672-727 7.91e-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: 7.91e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161077381  672 WVAtEWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKfLGVTRKFHQASIVHGI 727
Cdd:cd09487     1 DVA-EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAI 54
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 590-652 8.99e-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: 8.99e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161077381    590 DRWRATQVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAGLGLAHPMHRKKLRLAIE 652
Cdd:smart00454    2 SQWSPESVADWLE-SIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQ 63
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 596-653 2.35e-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: 2.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 161077381  596 QVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAgLGLAHPMHRKKLRLAIEE 653
Cdd:cd09487     1 DVAEWLE-SLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAIQR 56
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 215-331 2.98e-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: 2.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   215 AVASGEGSAAKERIER------LESELRSVKNQL--LTMRLERKKLRTDKSD-LLGQVKqlcASLQEKEQELRDFIRNYQ 285
Cdd:pfam19220  210 RLRALEGQLAAEQAEReraeaqLEEAVEAHRAERasLRMKLEALTARAAATEqLLAEAR---NQLRDRDEAIRAAERRLK 286

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 161077381   286 ERVRETETTNAKISG-----DRDRERFQLLKQARDEA-ERSLALAQQLSARD 331
Cdd:pfam19220  287 EASIERDTLERRLAGleadlERRTQQFQEMQRARAELeERAEMLTKALAAKD 338
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 223-330 4.84e-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: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  223 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETEttnakisgDR 302
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE--------EL 384

                          90       100
                  ....*....|....*....|....*...
gi 161077381  303 DRERFQLLKQARDEAERSLALAQQLSAR 330
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEAL 412
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
223-389 9.21e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 9.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  223 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKS--DLLGQVKQLCASLQEKEQELRDF------IRNYQERVRETETT 294
Cdd:COG4717    92 ELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELeerleeLRELEEELEELEAE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  295 NAKISGDRDRERFQLLKQARDEAERSL----ALAQQLSARDLQLQRLQEQLQEARRQLTGCLSDQESLHSFAPLTPPSAA 370
Cdd:COG4717   172 LAELQEELEELLEQLSLATEEELQDLAeeleELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251

                         170
                  ....*....|....*....
gi 161077381  371 SGMLSQMAAASGMGGGLAG 389
Cdd:COG4717   252 LLIAAALLALLGLGGSLLS 270
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
222-331 1.54e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  222 SAAKERIERLESELRSVKNQLLTMRLE----RKKLRTDKSDLL---GQVKQLCASLQEKEQELRDFIRNYQERVRETETT 294
Cdd:COG4372    34 RKALFELDKLQEELEQLREELEQAREEleqlEEELEQARSELEqleEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 161077381  295 NAKISgDRDRERFQLLKQARDEAERSLALAQQLSARD 331
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 ...
 592-649 1.77e-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: 1.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077381  592 WRATQVLAWLEVALGMPQYSARCAENVKSGKVLLEL---NDVELEAGLGLAHPMHRKKLRL 649
Cdd:cd09504     5 WTVEDTVEWLVNSVELPQYVEAFKENGVDGSALPRLavnNPSFLTSVLGIKDPIHRQKLSL 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 204-326 1.56e-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: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   204 VGGVDTAPEMEAVASGEGSAAKERIERLESELRSVKNQLLTMRLER------KKLRTDKSD------------LLGQVKQ 265
Cdd:TIGR02169  162 IAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKREyegyellkekeaLERQKEA 241

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161077381   266 LCASLQEKEQELRDFIRNYQERVRET-------ETTNAKISGDRDRERFQLLKQARD------EAERSLALAQQ 326
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLeeieqllEELNKKIKDLGEEEQLRVKEKIGEleaeiaSLERSIAEKER 315
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 223-326 1.61e-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: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  223 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQElrdfIRNYQERVRETETTNAKISGDR 302
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD----IARLEERRRELEERLEELEEEL 325

                          90       100
                  ....*....|....*....|....*.
gi 161077381  303 DRERFQL--LKQARDEAERSLALAQQ 326
Cdd:COG1196   326 AELEEELeeLEEELEELEEELEEAEE 351
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 676-730 4.25e-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: 4.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 161077381  676 EWLPDIGLPQYAEPFVQSLVDARMLDTLSKKELEKfLGVTRKFHQASIVHGIHVL 730
Cdd:cd09530    10 EWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPR-MGVTDFEHIKAIARKIREL 63
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
209-327 4.53e-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: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  209 TAPEMEAVASGEGSAAKERIERLESELrsvknqlltmrlerKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERV 288
Cdd:COG2433   396 EAEREKEHEERELTEEEEEIRRLEEQV--------------ERLEAEVEELEAELEEKDERIERLERELSEARSEERREI 461

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 161077381  289 RETETTNAkisgdRDRERFQLLKQARDEAERSLALAQQL 327
Cdd:COG2433   462 RKDREISR-----LDREIERLERELEEERERIEELKRKL 495
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
225-318 5.01e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  225 KERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKIsgdrdR 304
Cdd:COG1340    14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL-----N 88

                          90
                  ....*....|....
gi 161077381  305 ERFQLLKQARDEAE 318
Cdd:COG1340    89 ELREELDELRKELA 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 223-326 5.33e-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: 5.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   223 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQElrdfIRNYQERVRETETTNAKISGDR 302
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ----KQILRERLANLERQLEELEAQL 325

                           90       100
                   ....*....|....*....|....
gi 161077381   303 DRerfqlLKQARDEAERSLALAQQ 326
Cdd:TIGR02168  326 EE-----LESKLDELAEELAELEE 344
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 223-330 5.80e-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: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  223 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKISGDR 302
Cdd:COG1196   327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406

                          90       100
                  ....*....|....*....|....*...
gi 161077381  303 DRERFQLLKQARDEAERSLALAQQLSAR 330
Cdd:COG1196   407 EAEEALLERLERLEEELEELEEALAELE 434
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 210-331 7.06e-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: 7.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   210 APEMEAVASGEGSA--------AKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF- 280
Cdd:pfam05701  107 VEEMEQGIADEASVaakaqlevAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELt 186

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161077381   281 -----IRNYQERVR------ETETTNAKISGDRDRERFQL-LKQARDEAERslaLAQQL-SARD 331
Cdd:pfam05701  187 ieliaTKESLESAHaahleaEEHRIGAALAREQDKLNWEKeLKQAEEELQR---LNQQLlSAKD 247
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
675-731 7.98e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 38.79  E-value: 7.98e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 161077381   675 TEWLPDIGLPQYAEPFVQSLVD-ARMLDTLSKKELEKfLGVTRKFHQASIVHGIHVLR 731
Cdd:pfam07647   10 ADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKR-LGITSVGHRRKILKKIQELK 66
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 225-365 8.52e-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: 8.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   225 KERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELrDFIRNYQERVRETETTNAkISGDRDR 304
Cdd:pfam15921  341 EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL-SLEKEQNKRLWDRDTGNS-ITIDHLR 418

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077381   305 ERfqlLKQARDEAERSLALAQQLSARdlqlqrlqeQLQEARRQLTGCLSDQESLHSFAPLT 365
Cdd:pfam15921  419 RE---LDDRNMEVQRLEALLKAMKSE---------CQGQMERQMAAIQGKNESLEKVSSLT 467
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
225-331 9.97e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 9.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  225 KERIERLES------ELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNY-QERVRETETTNAK 297
Cdd:PRK03918  591 EERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLE 670

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 161077381  298 ISGD--RDRERFQLLKQARDEAERSLA-LAQQLSARD 331
Cdd:PRK03918  671 LSRElaGLRAELEELEKRREEIKKTLEkLKEELEERE 707
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 223-321 1.43e-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: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  223 AAKERIERLESELRSVKN---------QLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETET 293
Cdd:COG1579    70 EVEARIKKYEEQLGNVRNnkeyealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149

                          90       100
                  ....*....|....*....|....*...
gi 161077381  294 TNAKIsgDRDRERfqlLKQARDEAERSL 321
Cdd:COG1579   150 ELAEL--EAELEE---LEAEREELAAKI 172
mukB PRK04863
chromosome partition protein MukB;
206-329 1.58e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  206 GVDTAPEMEAVASgegsAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDL-------------LGQVKQLCASLQE 272
Cdd:PRK04863  549 NLDDEDELEQLQE----ELEARLESLSESVSEARERRMALRQQLEQLQARIQRLaarapawlaaqdaLARLREQSGEEFE 624

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161077381  273 KEQELRDFIRNYQERVRETETTNAKISgdrdRERFQLLKQARD-------EAERSLALAQQLSA 329
Cdd:PRK04863  625 DSQDVTEYMQQLLERERELTVERDELA----ARKQALDEEIERlsqpggsEDPRLNALAERFGG 684
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 226-326 1.82e-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: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  226 ERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDfIRN---YQERVRETETTNAKISgDR 302
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNnkeYEALQKEIESLKRRIS-DL 108

                          90       100
                  ....*....|....*....|....
gi 161077381  303 DRERFQLLKQaRDEAERSLALAQQ 326
Cdd:COG1579   109 EDEILELMER-IEELEEELAELEA 131
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 756-805 1.86e-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: 1.86e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 161077381    756 VWTNQRFIRWVRSIDLGEYADNLKDSGVHGGLVVLEPSfsgDTMATALGI 805
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 ...
 212-318 1.91e-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: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   212 EMEAVASgEGSAAKERIERLESELRSV--KNQLLT---MRLErKKLRTDkSDLLGQVKQLCASLQEKEQELRDFIRNYQE 286
Cdd:pfam01576    6 EMQAKEE-ELQKVKERQQKAESELKELekKHQQLCeekNALQ-EQLQAE-TELCAEAEEMRARLAARKQELEEILHELES 82

                           90       100       110
                   ....*....|....*....|....*....|....
gi 161077381   287 RVRETETTNAKISGDRDR--ERFQLLKQARDEAE 318
Cdd:pfam01576   83 RLEEEEERSQQLQNEKKKmqQHIQDLEEQLDEEE 116
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 226-327 2.62e-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: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   226 ERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDF---IRNYQERVRETETTNAKISGDR 302
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELeeeLEELEAALRDLESRLGDLKKER 891

                           90       100
                   ....*....|....*....|....*..
gi 161077381   303 DRERFQL--LKQARDEAERSLALAQQL 327
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 ...
 596-655 3.23e-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: 3.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  596 QVLAWLEvALGMPQYSARCAENVKSGKVLLELNDVELEAgLGLAHPMHRKKLRLAIEEQR 655
Cdd:cd09533     1 DVADWLS-SLGLPQYEDQFIENGITGDVLVALDHEDLKE-MGITSVGHRLTILKAVYELK 58
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
212-338 3.70e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  212 EMEAVASgEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFirnyQERVRET 291
Cdd:COG4372    39 ELDKLQE-ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL----QEEAEEL 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 161077381  292 ETTNAKISGDRDR--ERFQLLKQARDEAERSLALAQ-QLSARDLQLQRLQ 338
Cdd:COG4372   114 QEELEELQKERQDleQQRKQLEAQIAELQSEIAEREeELKELEEQLESLQ 163
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
221-376 3.87e-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: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  221 GSAAKERIERLESELRSVKNQLLTMRLERKKLRtDKSDLLGQVKQLCASLQEKEQELRDfIRNYQERVRETETTNAKIsg 300
Cdd:COG4913   605 GFDNRAKLAALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERL-- 680

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161077381  301 DRDRERFQLLKQARDEAERSL-ALAQQLSARDLQLQRLQEQLQEARRQLTGCLSDQESLHSFAPLTPPSAASGMLSQ 376
Cdd:COG4913   681 DASSDDLAALEEQLEELEAELeELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 223-330 4.18e-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: 4.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   223 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQElrdfIRNYQERVRETETTNAKISGDR 302
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELEAEI 763

                           90       100
                   ....*....|....*....|....*...
gi 161077381   303 dRERFQLLKQARDEAERSLALAQQLSAR 330
Cdd:TIGR02168  764 -EELEERLEEAEEELAEAEAEIEELEAQ 790
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
214-320 4.93e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  214 EAVASGEGSAAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQvkQLCASLQEKEQELRDFIRNYQERVRETET 293
Cdd:COG4717   420 ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAELRELAEEWAALKL 497

                          90       100
                  ....*....|....*....|....*..
gi 161077381  294 TnakisgdrdrerFQLLKQARDEAERS 320
Cdd:COG4717   498 A------------LELLEEAREEYREE 512
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 226-331 5.64e-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: 5.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   226 ERIERLESELRSVKNQL--LTMRLERKKLRTDKSDLlgQVKQLCASLQEKEqelrdfirnyqervRETETTNAKISGDRD 303
Cdd:pfam15921  461 EKVSSLTAQLESTKEMLrkVVEELTAKKMTLESSER--TVSDLTASLQEKE--------------RAIEATNAEITKLRS 524

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 161077381   304 RE--RFQLLKQARDEAE--RSL-----ALAQQLSARD 331
Cdd:pfam15921  525 RVdlKLQELQHLKNEGDhlRNVqteceALKLQMAEKD 561
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 226-331 5.96e-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: 5.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   226 ERIErLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTN-AKIsgdrdr 304
Cdd:pfam05557    3 ELIE-SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALrEQA------ 75

                           90       100
                   ....*....|....*....|....*....
gi 161077381   305 ERFQLLKQARDEAERSLA--LAQQLSARD 331
Cdd:pfam05557   76 ELNRLKKKYLEALNKKLNekESQLADARE 104
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
210-322 5.98e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  210 APEMEAVAS---GEGSAAKERIERLESELRSVKNQLltMRLERKK----LRTDKSDLLGQVKQLCASLQEKEQELRDFIR 282
Cdd:PRK02224  553 AEEKREAAAeaeEEAEEAREEVAELNSKLAELKERI--ESLERIRtllaAIADAEDEIERLREKREALAELNDERRERLA 630

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 161077381  283 NYQERVRETEttnakisGDRDRERFQLLKQARDEAERSLA 322
Cdd:PRK02224  631 EKRERKRELE-------AEFDEARIEEAREDKERAEEYLE 663
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
228-356 6.01e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  228 IERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKISGDRDRerf 307
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--- 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 161077381  308 qlLKQARDEAERSLALAQQLSARDLQLQRLQEQLQEARRQLTGCLSDQE 356
Cdd:COG4372   103 --LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 223-337 6.06e-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: 6.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381   223 AAKERIERLESELRSVKNQLLTMRLERKKLRTDKSDLLGQVKQLcasLQEKEQELRDFIRN----YQERVRETETTNAKI 298
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL---QQEIEELLKKLEEAelkeLQAELEELEEELEEL 452

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 161077381   299 SGDRD---------RERFQLLKQARDEAERSLalaQQLSARDLQLQRL 337
Cdd:TIGR02168  453 QEELErleealeelREELEEAEQALDAAEREL---AQLQARLDSLERL 497
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
246-326 8.36e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 37.96  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077381  246 RLER-KKLRTDKSD----LLGQVKQLCASLQEKEQELRDFIRNYQERVRETETTNAKISGDRDRERF-QLLKQARDEAER 319
Cdd:COG2882     6 RLQTlLDLAEKEEDeaarELGQAQQALEQAEEQLEQLEQYREEYEQRLQQKLQQGLSAAQLRNYQQFiARLDEAIEQQQQ 85


                  ....*..
gi 161077381  320 SLALAQQ 326
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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