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Conserved domains on  [gi|1806732386|ref|XP_032239740|]
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kazrin isoform X2 [Nematostella vectensis]

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 ...
 659-730 8.11e-44

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: 152.21  E-value: 8.11e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806732386 659 DPVVWTNDKVMRWCRSIDLQEYADNLRDSGVHGAMMVINETFGPDEMANCLAIHPSKNIIRRHLTSEMTALI 730
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 ...
 495-564 1.25e-39

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: 140.28  E-value: 1.25e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 495 MACWKANMVLAWLEVECHMPMYAQMCYENVKSGRVLLDLSDAELESGLGISNVMHRRKLRLAIEEYRDPS 564
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 ...
 573-637 1.47e-34

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


:

Pssm-ID: 188966  Cd Length: 65  Bit Score: 125.98  E-value: 1.47e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806732386 573 KIDHFWVARTWIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMEKHLHISKKFHQTSILNGVDLLR 637
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 16-312 2.13e-07

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


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 54.69  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   16 TGSRNSLSTAEAREKLDSLNEKVRSFSL---SVASREESSEGGSARLVRKQDDLIACLSVMRRLMEQAEHESKRLKEEkf 92
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEGLKRelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER-- 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   93 miAAKINNSLNSVNREVEHLKAELQDQDKRLAELasgrERVPHRSEstscsnlpstvfdscENTEDTGPKLGDMTIENqr 172
Cdd:TIGR02169  739 --LEELEEDLSSLEQEIENVKSELKELEARIEEL----EEDLHKLE---------------EALNDLEARLSHSRIPE-- 795

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  173 LRQENEFLSKELDEFKERNTNLTELLERLHCCEHEISRAKETIVCM-------KAERKK----LKSEKMELLSQMKQVYA 241
Cdd:TIGR02169  796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridlkeqIKSIEKeienLNGKKEELEEELEELEA 875

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1806732386  242 ILEDKESELGEF---IKNYQQHMRESEIKIQRLlsekeSWERERKNSLqyLDDMNTQLRTKESQLAVVESELLE 312
Cdd:TIGR02169  876 ALRDLESRLGDLkkeRDELEAQLRELERKIEEL-----EAQIEKKRKR--LSELKAKLEALEEELSEIEDPKGE 942
 
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 ...
 659-730 8.11e-44

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: 152.21  E-value: 8.11e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806732386 659 DPVVWTNDKVMRWCRSIDLQEYADNLRDSGVHGAMMVINETFGPDEMANCLAIHPSKNIIRRHLTSEMTALI 730
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 ...
 495-564 1.25e-39

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: 140.28  E-value: 1.25e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 495 MACWKANMVLAWLEVECHMPMYAQMCYENVKSGRVLLDLSDAELESGLGISNVMHRRKLRLAIEEYRDPS 564
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 ...
 573-637 1.47e-34

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 125.98  E-value: 1.47e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806732386 573 KIDHFWVARTWIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMEKHLHISKKFHQTSILNGVDLLR 637
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 576-637 3.00e-10

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 56.51  E-value: 3.00e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806732386 576 HFWVARTWIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMEKhLHISKKFHQTSILNGVDLLR 637
Cdd:pfam00536   4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 571-637 4.77e-09

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 53.45  E-value: 4.77e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1806732386  571 MSKIDHFWVARtWIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMEKHLHISKKFHQTSILNGVDLLR 637
Cdd:smart00454   1 VSQWSPESVAD-WLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-312 2.13e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.69  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   16 TGSRNSLSTAEAREKLDSLNEKVRSFSL---SVASREESSEGGSARLVRKQDDLIACLSVMRRLMEQAEHESKRLKEEkf 92
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEGLKRelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER-- 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   93 miAAKINNSLNSVNREVEHLKAELQDQDKRLAELasgrERVPHRSEstscsnlpstvfdscENTEDTGPKLGDMTIENqr 172
Cdd:TIGR02169  739 --LEELEEDLSSLEQEIENVKSELKELEARIEEL----EEDLHKLE---------------EALNDLEARLSHSRIPE-- 795

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  173 LRQENEFLSKELDEFKERNTNLTELLERLHCCEHEISRAKETIVCM-------KAERKK----LKSEKMELLSQMKQVYA 241
Cdd:TIGR02169  796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridlkeqIKSIEKeienLNGKKEELEEELEELEA 875

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1806732386  242 ILEDKESELGEF---IKNYQQHMRESEIKIQRLlsekeSWERERKNSLqyLDDMNTQLRTKESQLAVVESELLE 312
Cdd:TIGR02169  876 ALRDLESRLGDLkkeRDELEAQLRELERKIEEL-----EAQIEKKRKR--LSELKAKLEALEEELSEIEDPKGE 942
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
660-725 2.21e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 45.72  E-value: 2.21e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1806732386 660 PVVWTNDKVMRWCRSIDLQEYADNLRDSGVHGAMMVINetFGPDEMAnclAIHPSKNIIRRHLTSE 725
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK---RLGITSVGHRRKILKK 61
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 169-321 1.29e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 169 ENQRLRQENEFLSKELDEFKERNTNLTELLERLhccEHEISRAKETIVCMKAERKKLKSEKMELLSQMKQVYAILEDKES 248
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1806732386 249 ELGEFIKNYQQHMRESEIKIqrLLSEKESWERERknSLQYLDDMNTQLRTKESQLAVVESELLEVKQHLTLLR 321
Cdd:COG4942   105 ELAELLRALYRLGRQPPLAL--LLSPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
172-320 3.32e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 172 RLRQENEFLSKELDEFKERNTNLTELLERLHCCEHEISRAKETIVCMKAERKKLKSEKMELLSQMKQVYAILEDKE--SE 249
Cdd:PRK03918  218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyIK 297

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806732386 250 LGEFIKNYQQHMRESEIKIQRLLSEKESWERErknsLQYLDDMNTQLRTKESQLAVVESELLEVKQHLTLL 320
Cdd:PRK03918  298 LSEFYEEYLDELREIEKRLSRLEEEINGIEER----IKELEEKEERLEELKKKLKELEKRLEELEERHELY 364
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 660-695 8.61e-05

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: 41.13  E-value: 8.61e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1806732386  660 PVVWTNDKVMRWCRSIDLQEYADNLRDSGVHGAMMV 695
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLL 36
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 498-563 1.23e-04

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 40.74  E-value: 1.23e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1806732386  498 WKANMVLAWLEvECHMPMYAQMCYENVKSGRVLLDLSDAELESGLGISNVMHRRKLRLAIEEYRDP 563
Cdd:smart00454   4 WSPESVADWLE-SIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKEQ 68
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 20-318 7.79e-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: 43.18  E-value: 7.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   20 NSLSTAEAREKLDSLNEKVRSFSLSVASREESSEGGSAR---LVRKQDDLIACLSVMRRLMEQAEHESKRLKEEkfMIAA 96
Cdd:pfam15921  410 NSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEE--LTAK 487

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   97 KInnSLNSVNREVEHLKAELQDQDKRL----AELASGRERV-------PH--------RSESTSCSNLP----------S 147
Cdd:pfam15921  488 KM--TLESSERTVSDLTASLQEKERAIeatnAEITKLRSRVdlklqelQHlknegdhlRNVQTECEALKlqmaekdkviE 565

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  148 TVFDSCENTEDT----GPKLGDMTIENQRLRQENEFLSKELDEFK----ERNTNLTELLERLHCCEHEisraKETIVCMK 219
Cdd:pfam15921  566 ILRQQIENMTQLvgqhGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdKKDAKIRELEARVSDLELE----KVKLVNAG 641

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  220 AER----KKLKSEKMELLSQMK----QVYAILEDKESeLGEFIKNYQQHMRESEIKIQRLLSEKESWERERKNSLQYLD- 290
Cdd:pfam15921  642 SERlravKDIKQERDQLLNEVKtsrnELNSLSEDYEV-LKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEg 720

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1806732386  291 ----------DMNTQLRTKESQLAVVESELLEVKQHLT 318
Cdd:pfam15921  721 sdghamkvamGMQKQITAKRGQIDALQSKIQFLEEAMT 758
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 498-561 1.17e-03

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: 38.02  E-value: 1.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1806732386 498 WKANMVLAWLEvECHMPMYAQMCYENVKSGRVLLDLSDAELESgLGISNVMHRRKLRLAIEEYR 561
Cdd:pfam00536   3 WSVEDVGEWLE-SIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRLK 64
 
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 ...
 659-730 8.11e-44

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: 152.21  E-value: 8.11e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806732386 659 DPVVWTNDKVMRWCRSIDLQEYADNLRDSGVHGAMMVINETFGPDEMANCLAIHPSKNIIRRHLTSEMTALI 730
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 ...
 495-564 1.25e-39

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: 140.28  E-value: 1.25e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 495 MACWKANMVLAWLEVECHMPMYAQMCYENVKSGRVLLDLSDAELESGLGISNVMHRRKLRLAIEEYRDPS 564
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 ...
 573-637 1.47e-34

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 125.98  E-value: 1.47e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806732386 573 KIDHFWVARTWIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMEKHLHISKKFHQTSILNGVDLLR 637
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 659-730 6.79e-23

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: 92.90  E-value: 6.79e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806732386 659 DPVVWTNDKVMRWCRSIDLQEYADNLRDSGVHGAMMVINETFGPDEMANCLAIHPSKNIIRRHLTSEMTALI 730
Cdd:cd09569     1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 667-728 2.89e-20

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: 84.90  E-value: 2.89e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806732386 667 KVMRWCRSIDLQEYADNLRDSGVHGAMMVINETFGPDEMANCLAIHPSKNIIRRHLTSEMTA 728
Cdd:cd09496     1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 503-559 6.14e-20

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


Pssm-ID: 188893  Cd Length: 58  Bit Score: 83.81  E-value: 6.14e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1806732386 503 VLAWLEVECHMPMYAQMCYENVKSGRVLLDLSDAELESGLGISNVMHRRKLRLAIEE 559
Cdd:cd09494     2 VCAWLEDFGLMPMYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 578-637 2.43e-16

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: 73.72  E-value: 2.43e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 578 WVARTWIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMEKHLHISKKFHQTSILNGVDLLR 637
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 ...
 659-730 2.88e-16

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: 73.89  E-value: 2.88e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1806732386 659 DPVVWTNDKVMRWCRSIDLQEYADNLRDSGVHGAMMVINETFGPDEMANCLAIhPSKNIIRRH-LTSEMTALI 730
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQI-PTQNTQARQiLEREFNNLL 72
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 ...
 496-559 7.83e-15

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: 69.90  E-value: 7.83e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806732386 496 ACWKANMVLAWLEVECHMPM-YAQMCYENVKSGRVLLDLSDAELESGLGISNVMHRRKLRLAIEE 559
Cdd:cd09562     2 ALWNGPTVVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 66
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 573-637 9.06e-14

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: 66.56  E-value: 9.06e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806732386 573 KIDHFWVARtWIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMEkHLHISKKFHQTSILNGVDLLR 637
Cdd:cd09566     1 KLDTHWVLR-WLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
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 ...
 574-637 1.03e-11

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: 60.95  E-value: 1.03e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1806732386 574 IDHFWVARTWIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMEKHLHISKKFHQTSILNGVDLLR 637
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLK 64
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 498-558 2.98e-11

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: 59.55  E-value: 2.98e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806732386 498 WKANMVLAWLEvECHMPMYAQMCYENVKSGRVLLDLSDAELESGLGISNVMHRRKLRLAIE 558
Cdd:cd09563     4 WSTEQVCDWLA-ELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 576-637 3.00e-10

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 56.51  E-value: 3.00e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806732386 576 HFWVARTWIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMEKhLHISKKFHQTSILNGVDLLR 637
Cdd:pfam00536   4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 571-637 4.77e-09

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 53.45  E-value: 4.77e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1806732386  571 MSKIDHFWVARtWIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMEKHLHISKKFHQTSILNGVDLLR 637
Cdd:smart00454   1 VSQWSPESVAD-WLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-312 2.13e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.69  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   16 TGSRNSLSTAEAREKLDSLNEKVRSFSL---SVASREESSEGGSARLVRKQDDLIACLSVMRRLMEQAEHESKRLKEEkf 92
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEGLKRelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER-- 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   93 miAAKINNSLNSVNREVEHLKAELQDQDKRLAELasgrERVPHRSEstscsnlpstvfdscENTEDTGPKLGDMTIENqr 172
Cdd:TIGR02169  739 --LEELEEDLSSLEQEIENVKSELKELEARIEEL----EEDLHKLE---------------EALNDLEARLSHSRIPE-- 795

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  173 LRQENEFLSKELDEFKERNTNLTELLERLHCCEHEISRAKETIVCM-------KAERKK----LKSEKMELLSQMKQVYA 241
Cdd:TIGR02169  796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridlkeqIKSIEKeienLNGKKEELEEELEELEA 875

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1806732386  242 ILEDKESELGEF---IKNYQQHMRESEIKIQRLlsekeSWERERKNSLqyLDDMNTQLRTKESQLAVVESELLE 312
Cdd:TIGR02169  876 ALRDLESRLGDLkkeRDELEAQLRELERKIEEL-----EAQIEKKRKR--LSELKAKLEALEEELSEIEDPKGE 942
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 25-310 2.30e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.69  E-value: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   25 AEAREKLDSLNEKVRSFS----LSVASREESSEGGSARLVRKQDDLiaclsvmRRLMEQAEHESKRLKEEkfmiaakinn 100
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGeeeqLRVKEKIGELEAEIASLERSIAEK-------ERELEDAEERLAKLEAE---------- 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  101 sLNSVNREVEHLKAELQDQDKRLAELasgrervphrsestscsnlpSTVFDSCENTEDTgpklgdmtienqrLRQENEFL 180
Cdd:TIGR02169  331 -IDKLLAEIEELEREIEEERKRRDKL--------------------TEEYAELKEELED-------------LRAELEEV 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  181 SKEL----DEFKERNTNLTELLERLHCCEHEISRaketivcmKAERKKLKSEKmelLSQMKQVYAILEDKESELGEFIKN 256
Cdd:TIGR02169  377 DKEFaetrDELKDYREKLEKLKREINELKRELDR--------LQEELQRLSEE---LADLNAAIAGIEAKINELEEEKED 445

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1806732386  257 YQQHMRESEIKIQRLLSEKESWERERKNSLQYLDDMNTQLRTKESQLAVVESEL 310
Cdd:TIGR02169  446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 26-316 4.36e-07

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 53.90  E-value: 4.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   26 EAREKLDSLNEKVRSFSLSVASREESSEGGSARLvRKQDDLIACLSVMRRLMEQAEHESKRLKEEkfmiAAKINNSlnSV 105
Cdd:TIGR00606  748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEE-ESAKVCLTDVTIMERFQMELKDVERKIAQQ----AAKLQGS--DL 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  106 NREVEHLKAELQDQDKRLAELASGRErvphrsESTSCSnlpstvfdscentEDTGPKLGDMTIENQRLRQENEFLSKELD 185
Cdd:TIGR00606  821 DRTVQQVNQEKQEKQHELDTVVSKIE------LNRKLI-------------QDQQEQIQHLKSKTNELKSEKLQIGTNLQ 881

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  186 EFKERNTNLTELLERLHCCEHEISRAKETIVCMKAERKKLKSEKMELLSQMKQVYAILEDKESELGEFIKNYQQHMRESE 265
Cdd:TIGR00606  882 RRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIE 961

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1806732386  266 IKIQrllsekeswererknslqylDDMNTQLRTKESQLAVVESELLEVKQH 316
Cdd:TIGR00606  962 NKIQ--------------------DGKDDYLKQKETELNTVNAQLEECEKH 992
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
660-725 2.21e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 45.72  E-value: 2.21e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1806732386 660 PVVWTNDKVMRWCRSIDLQEYADNLRDSGVHGAMMVINetFGPDEMAnclAIHPSKNIIRRHLTSE 725
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK---RLGITSVGHRRKILKK 61
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 582-634 4.83e-06

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 44.54  E-value: 4.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1806732386 582 TWIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMEKHLhISKKFHQTSILNGVD 634
Cdd:cd09487     4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELG-ITSPGHRKKILRAIQ 55
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 169-321 1.29e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 169 ENQRLRQENEFLSKELDEFKERNTNLTELLERLhccEHEISRAKETIVCMKAERKKLKSEKMELLSQMKQVYAILEDKES 248
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1806732386 249 ELGEFIKNYQQHMRESEIKIqrLLSEKESWERERknSLQYLDDMNTQLRTKESQLAVVESELLEVKQHLTLLR 321
Cdd:COG4942   105 ELAELLRALYRLGRQPPLAL--LLSPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
172-320 3.32e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 172 RLRQENEFLSKELDEFKERNTNLTELLERLHCCEHEISRAKETIVCMKAERKKLKSEKMELLSQMKQVYAILEDKE--SE 249
Cdd:PRK03918  218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyIK 297

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806732386 250 LGEFIKNYQQHMRESEIKIQRLLSEKESWERErknsLQYLDDMNTQLRTKESQLAVVESELLEVKQHLTLL 320
Cdd:PRK03918  298 LSEFYEEYLDELREIEKRLSRLEEEINGIEER----IKELEEKEERLEELKKKLKELEKRLEELEERHELY 364
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
175-341 6.98e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 6.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 175 QENEFLSKELDEFKERNTNLTELLERLHCCEHEISRAKETIVCMKAERKKLKSEKM--ELLSQMKQVYAILEDKESELgE 252
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERL-E 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 253 FIKNYQQHMRESEIKIQRLLSEKESWERERKNSLQY--------LDDMNTQLRTKESQLAVVESELLEVKQHLTLLRLNA 324
Cdd:COG4717   150 ELEERLEELRELEEELEELEAELAELQEELEELLEQlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                         170
                  ....*....|....*..
gi 1806732386 325 PSRESNSSQAADSNLIR 341
Cdd:COG4717   230 EQLENELEAAALEERLK 246
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 660-695 8.61e-05

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: 41.13  E-value: 8.61e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1806732386  660 PVVWTNDKVMRWCRSIDLQEYADNLRDSGVHGAMMV 695
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLL 36
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 182-317 1.02e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.53  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 182 KELDEFKERNTNLTELLERLhccEHEISRAKETIVCMKAERKKLKSEKMELLSQMKQVYAILEDKESELGEfIKNYqqhm 261
Cdd:COG1579    17 SELDRLEHRLKELPAELAEL---EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNN---- 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1806732386 262 REseikIQRLLSEKESWERERKNSLQYLDDMNTQLRTKESQLAVVESELLEVKQHL 317
Cdd:COG1579    89 KE----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 498-563 1.23e-04

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 40.74  E-value: 1.23e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1806732386  498 WKANMVLAWLEvECHMPMYAQMCYENVKSGRVLLDLSDAELESGLGISNVMHRRKLRLAIEEYRDP 563
Cdd:smart00454   4 WSPESVADWLE-SIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKEQ 68
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 59-337 2.40e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  59 LVRKQDDLIACLSVMRRLMEQAEHESKRLKEEKFMIAAKIN---NSLNSVNREVEHLKAELQDQDKRLAELASGRERvph 135
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEelrLELEELELELEEAQAEEYELLAELARLEQDIAR--- 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 136 rsestscsnlpstvfdscentedtgpklgdmtiENQRLRQENEFLSKELDEFKERNTNLTELLERLHCCEHEISRAKETI 215
Cdd:COG1196   307 ---------------------------------LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 216 VCMKAERKKLKSEKMELLSQM----------KQVYAILEDKESELGEFIKNYQQHMRESEIKIQRLLSEKESWERERKNS 285
Cdd:COG1196   354 EEAEAELAEAEEALLEAEAELaeaeeeleelAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1806732386 286 LQYLDDMNTQLRTKESQLAVVESELLEVKQHLTLLRLNAPSRESNSSQAADS 337
Cdd:COG1196   434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 25-265 2.83e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  25 AEAREKLDSLNEKVrsfslsvasreESSEGGSARLVRKQDDLIACLSVMRRLMEQAEHESKRLKEEkfmiAAKINNSLNS 104
Cdd:COG4942    23 AEAEAELEQLQQEI-----------AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----LAALEAELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 105 VNREVEHLKAELQDQDKRLAELAsgreRVPHRSESTScsnlPSTVFDSCENTEDTGPKLGDMTIENQRLRQENEFLSKEL 184
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAELL----RALYRLGRQP----PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 185 DEFKERNTNLTELLERLHCCEHEISRAKETIVCMKAERKKLKSEKMELLSQMKQVYAILEDKESELGEFIKNYQQHMRES 264
Cdd:COG4942   160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239


                  .
gi 1806732386 265 E 265
Cdd:COG4942   240 A 240
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 503-559 3.87e-04

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 39.14  E-value: 3.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1806732386 503 VLAWLEvECHMPMYAQMCYENVKSGRVLLDLSDAELESgLGISNVMHRRKLRLAIEE 559
Cdd:cd09487     2 VAEWLE-SLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAIQR 56
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 20-318 7.79e-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: 43.18  E-value: 7.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   20 NSLSTAEAREKLDSLNEKVRSFSLSVASREESSEGGSAR---LVRKQDDLIACLSVMRRLMEQAEHESKRLKEEkfMIAA 96
Cdd:pfam15921  410 NSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEE--LTAK 487

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   97 KInnSLNSVNREVEHLKAELQDQDKRL----AELASGRERV-------PH--------RSESTSCSNLP----------S 147
Cdd:pfam15921  488 KM--TLESSERTVSDLTASLQEKERAIeatnAEITKLRSRVdlklqelQHlknegdhlRNVQTECEALKlqmaekdkviE 565

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  148 TVFDSCENTEDT----GPKLGDMTIENQRLRQENEFLSKELDEFK----ERNTNLTELLERLHCCEHEisraKETIVCMK 219
Cdd:pfam15921  566 ILRQQIENMTQLvgqhGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdKKDAKIRELEARVSDLELE----KVKLVNAG 641

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  220 AER----KKLKSEKMELLSQMK----QVYAILEDKESeLGEFIKNYQQHMRESEIKIQRLLSEKESWERERKNSLQYLD- 290
Cdd:pfam15921  642 SERlravKDIKQERDQLLNEVKtsrnELNSLSEDYEV-LKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEg 720

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1806732386  291 ----------DMNTQLRTKESQLAVVESELLEVKQHLT 318
Cdd:pfam15921  721 sdghamkvamGMQKQITAKRGQIDALQSKIQFLEEAMT 758
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 70-357 1.02e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  70 LSVMRRLMEQAEHESKRLKEEkfmiAAKINNSLNSVNREVEHLKAELQDQDKRLAELasgRERVPHRSEstscsnlpstv 149
Cdd:COG3883    25 LSELQAELEAAQAELDALQAE----LEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERRE----------- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 150 fdscentedtgpKLGDMTIENQRLRQENEFLSKELDefkerNTNLTELLERLHCCEHEISRAKETIVCMKAERKKLKSEK 229
Cdd:COG3883    87 ------------ELGERARALYRSGGSVSYLDVLLG-----SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 230 MEL---LSQMKQVYAILEDKESELGEFIKNYQQHMRESEIKIQRLLSEKESWERERKNSLQYLDDMNTQLRTKESQLAVV 306
Cdd:COG3883   150 AELeakLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1806732386 307 ESELLEVKQHLTLLRLNAPSRESNSSQAADSNLIRNNLNTSSGSSRFSRAI 357
Cdd:COG3883   230 AAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAAS 280
COG5022 COG5022
Myosin heavy chain [General function prediction only];
19-438 1.17e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.76  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   19 RNSLSTAEAREKLDSLNEKVRSFSLSVASREesseggSARLVRKQDDLIACLSVMRRLMEQAEHESKRLKEEKFMIAAKI 98
Cdd:COG5022    800 QPLLSLLGSRKEYRSYLACIIKLQKTIKREK------KLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   99 nnslnsvnrevehlKAELQDQDKRLAELASGRERVPHRSESTSCsnLPSTVFdscENTEDTGPklgDMTIENQRLRQENE 178
Cdd:COG5022    874 --------------AQRVELAERQLQELKIDVKSISSLKLVNLE--LESEII---ELKKSLSS---DLIENLEFKTELIA 931

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  179 FLSK-----ELDEFKERNTNLTELLERLHCCEHEISRAKETIVCMKAERKKLKSEKMELLSQMKQVYAILEDKESELGEF 253
Cdd:COG5022    932 RLKKllnniDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGAL 1011

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  254 IKNYQQHmRESEIKIQRLLSE-----KESWERERKNSLQ----YLDDMNTQLRTKESQLAV-VESELLEVKQHLTLLRLN 323
Cdd:COG5022   1012 QESTKQL-KELPVEVAELQSAskiisSESTELSILKPLQklkgLLLLENNQLQARYKALKLrRENSLLDDKQLYQLESTE 1090

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  324 APSRESNSS--QAADSNL-----IRNNLNTSSGSSRFSRAIQADVEKLLHSREKYEEMVPSPYSTTERL----SASPVPT 392
Cdd:COG5022   1091 NLLKTINVKdlEVTNRNLvkpanVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLfweaNLEALPS 1170

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1806732386  393 PPGSDTQSESSQIdQLATLSPEEREVFEYVTPVLNNVEEKKSRKKD 438
Cdd:COG5022   1171 PPPFAALSEKRLY-QSALYDEKSKLSSSEVNDLKNELIALFSKIFS 1215
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 498-561 1.17e-03

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: 38.02  E-value: 1.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1806732386 498 WKANMVLAWLEvECHMPMYAQMCYENVKSGRVLLDLSDAELESgLGISNVMHRRKLRLAIEEYR 561
Cdd:pfam00536   3 WSVEDVGEWLE-SIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRLK 64
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 498-555 1.41e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 38.08  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806732386 498 WKANMVLAWLEVECHMPMYAQMCYENVKSGRVLLDLSDAE---LESGLGISNVMHRRKLRL 555
Cdd:cd09504     5 WTVEDTVEWLVNSVELPQYVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 75-455 1.55e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.34  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386   75 RLMEQAEHESKRLKEEKFMIAAKINNSLNSVNREVEHLKAELQDQdkrlaELASGRERVPHRSESTscsnlpsTVFDSCE 154
Cdd:PTZ00108   999 YLLGKLERELARLSNKVRFIKHVINGELVITNAKKKDLVKELKKL-----GYVRFKDIIKKKSEKI-------TAEEEEG 1066

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  155 NTEDTGPKLGDMTIENQRLRQENEFLSKELdefkernTNLT-ELLERLhccEHEISRAketivcmKAERKKLKS---EKM 230
Cdd:PTZ00108  1067 AEEDDEADDEDDEEELGAAVSYDYLLSMPI-------WSLTkEKVEKL---NAELEKK-------EKELEKLKNttpKDM 1129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  231 ------ELLSQMKQVYAILEDKESELGEFIKNYQQHMRESEIKIQRLLSEKESwERERKNSLQYLDDMNTQLRTKESQLA 304
Cdd:PTZ00108  1130 wledldKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKK-KSSADKSKKASVVGNSKRVDSDEKRK 1208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  305 VVESELLEVKQHLTLLRLNAPSRESNSSQAADSNLIRNNLNTSSGSSRFSRAIQADVEKLLHSREKYEEMVPSPYSTTER 384
Cdd:PTZ00108  1209 LDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPP 1288

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806732386  385 LSASPVPTPPGSDTQSESSQIDQlATLSPEEREVFEYVTPVLNNVEEKKSRKKDKRGSLSRLFSKGRNRKS 455
Cdd:PTZ00108  1289 SKRPDGESNGGSKPSSPTKKKVK-KRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRK 1358
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
583-637 1.56e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 37.63  E-value: 1.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1806732386 583 WIRDLGLSQYGPAFESQMIDG-RLLNVLTRKDMeKHLHISKKFHQTSILNGVDLLR 637
Cdd:pfam07647  12 WLRSIGLEQYTDNFRDQGITGaELLLRLTLEDL-KRLGITSVGHRRKILKKIQELK 66
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 583-633 2.39e-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: 2.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1806732386 583 WIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMeKHLHISKKFHQTSILNGV 633
Cdd:cd09533     5 WLSSLGLPQYEDQFIENGITGDVLVALDHEDL-KEMGITSVGHRLTILKAV 54
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 78-314 2.62e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  78 EQAEHESKRLKEEKFMIAAKI---NNSLNSVNREVEHLKAELQDQDKRLAELasgrervphrseSTSCSNLPSTVFDSCE 154
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIkdlTNQDSVKELIIKNLDNTRESLETQLKVL------------SRSINKIKQNLEQKQK 489

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 155 NTEDTGPKLGDMTIENQRLRQENEFLSKELDEFKERNTNLTELLERLhccEHEISRAKETIVCMKAERKK--LKSEKMEL 232
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK---ESKISDLEDELNKDDFELKKenLEKEIDEK 566

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 233 ---LSQMKQVYAILEDKESELGEFIKNYQQH-------MRESEIKIQRLLSEKESWERERKNSLQYLDDMNTQLRTKESQ 302
Cdd:TIGR04523 567 nkeIEELKQTQKSLKKKQEEKQELIDQKEKEkkdlikeIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646

                         250
                  ....*....|..
gi 1806732386 303 LAVVESELLEVK 314
Cdd:TIGR04523 647 VKQIKETIKEIR 658
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 582-637 3.92e-03

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


Pssm-ID: 188904  Cd Length: 72  Bit Score: 36.53  E-value: 3.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1806732386 582 TWIRDLGLSQYGPAFESQMIDGRLLNVLTRKDMEKHLHISKKFHQTSILNGVDLLR 637
Cdd:cd09505    12 TWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELK 67
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 24-375 3.95e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.86  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  24 TAEAREKLDSLNEK-------VRSFSLSVASREESSEGGSARLVRKQDDLIACLSVMRRLMEQAEHESK-------RLKE 89
Cdd:pfam05483 330 TEEKEAQMEELNKAkaahsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnkevELEE 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  90 EKFMIAAKinNSLNSVNREVEHLKAELQDQDKRLAELASGRERVPHRSE------STSCSNLPSTVFDSCENTEDTGPKL 163
Cdd:pfam05483 410 LKKILAED--EKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltaiKTSEEHYLKEVEDLKTELEKEKLKN 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 164 GDMT-------IENQRLRQENEFLSKELDEFKERNTNLTELLERLHcceHEISRAKETIVCMkaeRKKLKSEKMELLSQM 236
Cdd:pfam05483 488 IELTahcdkllLENKELTQEASDMTLELKKHQEDIINCKKQEERML---KQIENLEEKEMNL---RDELESVREEFIQKG 561

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 237 KQVYAILEDKEselgEFIKNYQQHMRESEIKIQRLLSEKESWERERKNSLQYLDDM--------------NTQLRTKESQ 302
Cdd:pfam05483 562 DEVKCKLDKSE----ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELhqenkalkkkgsaeNKQLNAYEIK 637

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1806732386 303 LAVVESELLEVKQHLTLLrLNAPSRESNSSQAADSNLIRnnlNTSSGSSRFSRAIQADVEKLLHSREKYEEMV 375
Cdd:pfam05483 638 VNKLELELASAKQKFEEI-IDNYQKEIEDKKISEEKLLE---EVEKAKAIADEAVKLQKEIDKRCQHKIAEMV 706
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 166-319 4.91e-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: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 166 MTIENQRLRQENE----FLSKELDEFKERNTNLTELLERLHCCEHEISRA-KETIVCMKAERK------KLKSEKMELLS 234
Cdd:pfam05557  21 MELEHKRARIELEkkasALKRQLDRESDRNQELQKRIRLLEKREAEAEEAlREQAELNRLKKKylealnKKLNEKESQLA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 235 QMKQVYAILEDKESElgefiknYQQHMRESEIKIQRLLSEKESWER---ERKNSLQYLDDMNTQLRTKESQLAVVESELL 311
Cdd:pfam05557 101 DAREVISCLKNELSE-------LRRQIQRAELELQSTNSELEELQErldLLKAKASEAEQLRQNLEKQQSSLAEAEQRIK 173


                  ....*...
gi 1806732386 312 EVKQHLTL 319
Cdd:pfam05557 174 ELEFEIQS 181
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 23-412 5.02e-03

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


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 40.51  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386  23 STAEAREKLDSLNEKVRSFSLSVASREESSEGGSARLVRKQddliACLSVMRRLMEQAEHESKRLKEEKFMIAAKINNSL 102
Cdd:pfam07111 332 SVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVER----MSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVV 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 103 NSVNREVEHLKAELQDQDKRLAELASGRERVPH--------RSESTSCSNLPSTVFDSCENTEDTGPKLGDMTIENQRLR 174
Cdd:pfam07111 408 NAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYavrkvhtiKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLR 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 175 QENEFLSKEL---------------DEFKERNTNLTELLERLhccEHEISRAKETIVCMKAERKKLKSEKMEL------- 232
Cdd:pfam07111 488 EERNRLDAELqlsahliqqevgrarEQGEAERQQLSEVAQQL---EQELQRAQESLASVGQQLEVARQGQQESteeaasl 564

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 233 ---LSQMKQVYAiledkeSELGEFIKNYQQHMRESEIKIQRLLSEKESWERERKNSLQYLDDMNTQLRTKESQLAVVESE 309
Cdd:pfam07111 565 rqeLTQQQEIYG------QALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDE 638

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 310 LLEVKQHLTLLRLNAPSResnssqaaDSNLIrnnLNTSSGSSRFSRAIQADVEKLLHSREKYEEMVPSPYSTTERLSASP 389
Cdd:pfam07111 639 ARKEEGQRLARRVQELER--------DKNLM---LATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPIP 707

                         410       420
                  ....*....|....*....|....
gi 1806732386 390 VPTPPGSDTQ-SESSQIDQLATLS 412
Cdd:pfam07111 708 AAVPTRESIKgSLTVLLDNLQGLS 731
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 581-637 8.64e-03

SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK (connector enhancer of kinase suppressor of ras (Ksr)) subfamily is a protein-protein interaction domain. CNK proteins are multidomain scaffold proteins containing a few protein-protein interaction domains and are required for connecting Rho and Ras signaling pathways. In Drosophila, the SAM domain of CNK is known to interact with the SAM domain of the aveugle protein, forming a heterodimer. Mutation of the SAM domain in human CNK1 abolishes the ability to cooperate with the Ras effector, supporting the idea that this interaction is necessary for proper Ras signal transduction.


Pssm-ID: 188910  Cd Length: 69  Bit Score: 35.73  E-value: 8.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806732386 581 RTWIR--DLGLSQYGPAFESQMIDG-RLLNvLTRKDMEkHLHISKKFHQTSILNGVDLLR 637
Cdd:cd09511    10 TDWLKglDDCLQQYIYTFEREKVTGeQLLN-LSPQDLE-NLGVTKIGHQELILEAVELLC 67
 
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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