NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16263319|ref|NP_436112|]
View 

CyaI3 adenylate/guanylate cyclase [Sinorhizobium meliloti 1021]

Graphical summary

show options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
115-290 6.68e-53

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


:

Pssm-ID: 143636  Cd Length: 177  Bit Score: 184.32  E-value: 6.68e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  115 QLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVAGAIARFEGHVAKYMGDGVLAYFGYPRAHEDEAERAVRAGLAAID 194
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  195 AVRKL--QPPHGETLEARVGIATGLVVVGELigeGAAREE-TVIGETPNLAARLQSVAEPGAVVVASATRQLIGGL-FDL 270
Cdd:cd07302   81 ALAELnaEREGGPPLRLRIGIHTGPVVAGVV---GSERPEyTVIGDTVNLAARLESLAKPGQILVSEATYELLGDAgFEF 157
                        170       180
                 ....*....|....*....|
gi 16263319  271 AELGFHPLKGFAASIPAWRV 290
Cdd:cd07302  158 EELGEVELKGKSGPVRVYRL 177
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
32-85 3.46e-15

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  Cd Length: 56  Bit Score: 72.27  E-value: 3.46e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16263319   32 DIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAI 85
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
COG3903 COG3903
Predicted ATPase [General function prediction only]
753-1157 8.79e-117

Predicted ATPase [General function prediction only]


:

Pssm-ID: 226418  Cd Length: 414  Bit Score: 370.59  E-value: 8.79e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  753 LEGLPDDAARLRKELELQVALSVALMTAKGWAAP-EVGRANARARNLCERLGDKSRLFPVLYGDWVFHVVRAELEAGRKA 831
Cdd:COG3903    3 GEALVRDLLTALRLVTLTGAGGVGKTTLALQAAHaASEYADGVAFVDLAPITDPALVFPTLAGALGLHVQPGDSAVDTLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  832 GEELLRRAQEEREVSAEIVGNRIAGTGAFLRGEIANAREYLERSLALYDPQQHRALAFLFAQD---PRVAGLSVLSLTLF 908
Cdd:COG3903   83 RRIGDRRALLVLDNCEHLLDACAALIVALLGACPRLAILATSREAILVAGEVHRRVPSLSLFDeaiELFVCRAVLVALSF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  909 ALGYPEQAQARSNEALAD--ARELSHSNTLGFALLYGCILSQLRGDWREARDRAgSLITLARAQGSPHFLGAGKILQGWT 986
Cdd:COG3903  163 WLTDDNAAAVAEICRRLDgiPLAIELAAARVRSLSPDEIAAGLRDRFRLLTGGA-RLAVLRQQTLRASLDWSYALLTGWE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  987 LGQTGELPAASTKVQEGLASWQMTGARFLVPYFLSLLARVETQSAGAKRALDLLTDALQRARETGERWFEAELHRLTGEL 1066
Cdd:COG3903  242 RALFGRLAVFVGGFDLGLALAVAAGADVDVPRYLVLLALTLLVDKSLVVALDLLGRARYRLLETGRRYALAELHRSGEAD 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319 1067 MLQLPAFDRAEGEARLQHAVELARGQGADLWELRAATSLARLRIGQNR-FGDVHHLLAPLCGKFAEGFATTDLQSAQRLL 1145
Cdd:COG3903  322 AVLARHRDHYEAAAAEQSAPSAARGQGALLQAEREADNLLRAAFGWSReNGDVAHALALASSLFPLWFNTGDLQEALRWL 401
                        410
                 ....*....|..
gi 16263319 1146 REAAGFDGAIKS 1157
Cdd:COG3903  402 DSALADHGAIHL 413
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the ...
310-498 2.02e-12

AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.


:

Pssm-ID: 257559  Cd Length: 156  Bit Score: 66.33  E-value: 2.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    310 PLVGREHDIGLLLKRWEAVKKGKGRVVLLAGEPGIGKSRLVRALRRRLEGEPHTTVSHYCSPYhqtsPLYPVIRLLERAa 389
Cdd:pfam13191    1 RLVGREEELERLLDALERVRSGRPGLVLLTGPSGVGKTSLLRELLERLARKGGGVLSGKCDEL----PYAALRQLLREL- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    390 gfaaedppevklskLEALLTQSIEEVADAApllaallsvpaddryQPLELSPHRQKKRMLEVLVDQLIGLAARQ-PILAV 468
Cdd:pfam13191   76 --------------LRQLLDELLPELELLP---------------PVPGLPPDDLRNRLEDLLRRLLRRLAARErPLVLV 126
                          170       180       190
                   ....*....|....*....|....*....|
gi 16263319    469 YEDVHWADPTSLELLDLVVDRVQDSPVLVL 498
Cdd:pfam13191  127 LDDLQWADEASLALLLALARLLERLPLLLV 156
CyaA COG2114
Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction ...
72-299 6.09e-42

Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction mechanisms]


:

Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 154.62  E-value: 6.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319   72 VASVGHRRKLLAAIAALREVAEQPSGAAGFGATPVINPEAER-RQLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVA 150
Cdd:COG2114    2 AAVLNLLAKEAKVAAAGLRSDLVLRLYLARVVGRLLARGGAGdRRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  151 GAIARFEGHVAKYMGDGVLAYFGYPRAHEDEAERAVRAGLAAIDAVRKLQpphGETLEARVGIATGLVVVGELIGegaar 230
Cdd:COG2114   82 EVVARHGGRVVKFIGDGFLAVFGRPSPLEDAVACALDLQLALRNPLARLR---RESLRVRIGIHTGEVVVGNTGG----- 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  231 eETVIGETPNLAARLQSVAEPGAVVVASATRQLIGGLFDLAE-LGFHPLKGFAASIPAWRVLGESSAESR 299
Cdd:COG2114  154 -YTVVGSAVNQAARLESLAKPGQVLLSEATYDLVRDLVDLFSgLGSHRLKGLARPVRVYQLCHRSLRRNL 222
COG3899 COG3899
Predicted ATPase [General function prediction only]
310-754 2.12e-108

Predicted ATPase [General function prediction only]


:

Pssm-ID: 226415 [Multi-domain]  Cd Length: 849  Bit Score: 361.72  E-value: 2.12e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  310 PLVGREHDIGLLLKRWEAVKKGKGRVVLLAGEPGIGKSRLVRALRRRLEGEPHTTVSHYCSPYHQTSPLYPVIRLLERAA 389
Cdd:COG3899    1 PLYGRETELAQLLAAFDRVSKGRGEVVLVAGESGIGKSALVNEVHKPITQQRGYFIKGKFDQFERNIPLSPLVQAFRDLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  390 GFAAEDPPEVKLSKLEALLTQSIEEVADAAPLLAALLSVPaDDRYQPLELSPHRQKKRMLEVLVDQLIGLAARQ-PILAV 468
Cdd:COG3899   81 GQLLSESDTRILSWRARLLAALGENGQVIIDVIPELELII-GKRPPALELSPTAAQNRFNLAFLRFIQVFTAEEhPLVIV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  469 YEDVHWADPTSLELLDLVVDRVQ-----DSPVLVLITFRTEFLPPWTRYPHVTVLTLSRLSRRQGAEMVDRLTGR-RALP 542
Cdd:COG3899  160 LEDLHWADSASLKLLQLLMDRIAigayrDNEVLLLHPLRPTLGEILKSATNITTITLAPLSRADTNQLVAATLGCtKLLP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  543 TEVLDQIVAKTDGVPLFVEELTRAILETSLLKAEGDHYALARPLSAISIPATLH---ESLLARLDRL-APAREVMQVAAA 618
Cdd:COG3899  240 APLLELIFEKTKGNPFFIEEFLKALYEEGLLVFNFDTGAWQCSIASLGILATTDavvEFLAARLQKLpGTTREVLKAAAC 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  619 IGREFSHELLVTAAP-LQASEVEEALEDLIASGLVF-----RHGTPPQL-TYSFKHALVRDAAYATLVRTKRQRLHAAIA 691
Cdd:COG3899  320 IGNRFDLDTLAALAEdSPALEAAALLDALQEGLILPlsetyRFGSNVDIaTYKFLHDRVQQAAYNLIPESQRQYLHLRIG 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16263319  692 TAIEQRFPEMVQTQPELLAQHYAEAG----RLEPAVN----YWLRAGQAEIARSATTEAISHLTRGLELLE 754
Cdd:COG3899  400 QLLEQNIPEAGQEEEIFDIVNQLNAGvgliTLEEAVDelaeLNLLAGRKAKLRSAYSAAISYLERGLSLLL 470
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
32-90 2.34e-11

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 [Multi-domain]  Cd Length: 68  Bit Score: 61.54  E-value: 2.34e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319      32 DIGAWLRDQGLGQYEGTFRQNDID-PEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALRE 90
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
115-290 6.68e-53

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636  Cd Length: 177  Bit Score: 184.32  E-value: 6.68e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  115 QLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVAGAIARFEGHVAKYMGDGVLAYFGYPRAHEDEAERAVRAGLAAID 194
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  195 AVRKL--QPPHGETLEARVGIATGLVVVGELigeGAAREE-TVIGETPNLAARLQSVAEPGAVVVASATRQLIGGL-FDL 270
Cdd:cd07302   81 ALAELnaEREGGPPLRLRIGIHTGPVVAGVV---GSERPEyTVIGDTVNLAARLESLAKPGQILVSEATYELLGDAgFEF 157
                        170       180
                 ....*....|....*....|
gi 16263319  271 AELGFHPLKGFAASIPAWRV 290
Cdd:cd07302  158 EELGEVELKGKSGPVRVYRL 177
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
32-85 3.46e-15

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  Cd Length: 56  Bit Score: 72.27  E-value: 3.46e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16263319   32 DIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAI 85
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
COG3903 COG3903
Predicted ATPase [General function prediction only]
753-1157 8.79e-117

Predicted ATPase [General function prediction only]


Pssm-ID: 226418  Cd Length: 414  Bit Score: 370.59  E-value: 8.79e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  753 LEGLPDDAARLRKELELQVALSVALMTAKGWAAP-EVGRANARARNLCERLGDKSRLFPVLYGDWVFHVVRAELEAGRKA 831
Cdd:COG3903    3 GEALVRDLLTALRLVTLTGAGGVGKTTLALQAAHaASEYADGVAFVDLAPITDPALVFPTLAGALGLHVQPGDSAVDTLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  832 GEELLRRAQEEREVSAEIVGNRIAGTGAFLRGEIANAREYLERSLALYDPQQHRALAFLFAQD---PRVAGLSVLSLTLF 908
Cdd:COG3903   83 RRIGDRRALLVLDNCEHLLDACAALIVALLGACPRLAILATSREAILVAGEVHRRVPSLSLFDeaiELFVCRAVLVALSF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  909 ALGYPEQAQARSNEALAD--ARELSHSNTLGFALLYGCILSQLRGDWREARDRAgSLITLARAQGSPHFLGAGKILQGWT 986
Cdd:COG3903  163 WLTDDNAAAVAEICRRLDgiPLAIELAAARVRSLSPDEIAAGLRDRFRLLTGGA-RLAVLRQQTLRASLDWSYALLTGWE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  987 LGQTGELPAASTKVQEGLASWQMTGARFLVPYFLSLLARVETQSAGAKRALDLLTDALQRARETGERWFEAELHRLTGEL 1066
Cdd:COG3903  242 RALFGRLAVFVGGFDLGLALAVAAGADVDVPRYLVLLALTLLVDKSLVVALDLLGRARYRLLETGRRYALAELHRSGEAD 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319 1067 MLQLPAFDRAEGEARLQHAVELARGQGADLWELRAATSLARLRIGQNR-FGDVHHLLAPLCGKFAEGFATTDLQSAQRLL 1145
Cdd:COG3903  322 AVLARHRDHYEAAAAEQSAPSAARGQGALLQAEREADNLLRAAFGWSReNGDVAHALALASSLFPLWFNTGDLQEALRWL 401
                        410
                 ....*....|..
gi 16263319 1146 REAAGFDGAIKS 1157
Cdd:COG3903  402 DSALADHGAIHL 413
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
110-280 9.11e-29

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 249682  Cd Length: 184  Bit Score: 115.42  E-value: 9.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    110 EAER-RQLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVAGAIARFEGHVAKYMGDGVLAYFGYPRAHEDEAERAVRA 188
Cdd:pfam00211    2 YAQSyDNVTILFADIVGFTALSSAHSPEEVVRLLNDLYTRFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHAQTIAEM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    189 GLAAIDAVRKLQPPHGETLEARVGIATGLVVVGeLIGEGAAReETVIGETPNLAARLQSVAEPGAVVVASATRQLI--GG 266
Cdd:pfam00211   82 ALDMLEAIKSVNIPSFEGLRVRVGIHTGPVVAG-VIGAKRPR-YDVWGDTVNLASRMESTGVPGKIHVSEETYRLLktRE 159
                          170
                   ....*....|....
gi 16263319    267 LFDLAELGFHPLKG 280
Cdd:pfam00211  160 GFEFTERGEVEVKG 173
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
31-89 1.33e-15

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: 249940  Cd Length: 64  Bit Score: 73.43  E-value: 1.33e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16263319     31 MDIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:pfam00536    6 EDVGEWLESIGLGQYADNFRAGYIDGDALLLLTEEDLEKLGVTLPGHRKKILSSIQGLK 64
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the ...
310-498 2.02e-12

AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.


Pssm-ID: 257559  Cd Length: 156  Bit Score: 66.33  E-value: 2.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    310 PLVGREHDIGLLLKRWEAVKKGKGRVVLLAGEPGIGKSRLVRALRRRLEGEPHTTVSHYCSPYhqtsPLYPVIRLLERAa 389
Cdd:pfam13191    1 RLVGREEELERLLDALERVRSGRPGLVLLTGPSGVGKTSLLRELLERLARKGGGVLSGKCDEL----PYAALRQLLREL- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    390 gfaaedppevklskLEALLTQSIEEVADAApllaallsvpaddryQPLELSPHRQKKRMLEVLVDQLIGLAARQ-PILAV 468
Cdd:pfam13191   76 --------------LRQLLDELLPELELLP---------------PVPGLPPDDLRNRLEDLLRRLLRRLAARErPLVLV 126
                          170       180       190
                   ....*....|....*....|....*....|
gi 16263319    469 YEDVHWADPTSLELLDLVVDRVQDSPVLVL 498
Cdd:pfam13191  127 LDDLQWADEASLALLLALARLLERLPLLLV 156
CyaA COG2114
Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction ...
72-299 6.09e-42

Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction mechanisms]


Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 154.62  E-value: 6.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319   72 VASVGHRRKLLAAIAALREVAEQPSGAAGFGATPVINPEAER-RQLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVA 150
Cdd:COG2114    2 AAVLNLLAKEAKVAAAGLRSDLVLRLYLARVVGRLLARGGAGdRRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  151 GAIARFEGHVAKYMGDGVLAYFGYPRAHEDEAERAVRAGLAAIDAVRKLQpphGETLEARVGIATGLVVVGELIGegaar 230
Cdd:COG2114   82 EVVARHGGRVVKFIGDGFLAVFGRPSPLEDAVACALDLQLALRNPLARLR---RESLRVRIGIHTGEVVVGNTGG----- 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  231 eETVIGETPNLAARLQSVAEPGAVVVASATRQLIGGLFDLAE-LGFHPLKGFAASIPAWRVLGESSAESR 299
Cdd:COG2114  154 -YTVVGSAVNQAARLESLAKPGQVLLSEATYDLVRDLVDLFSgLGSHRLKGLARPVRVYQLCHRSLRRNL 222
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
112-1108 1.24e-164

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein [Cellular processes, Toxin production and resistance].


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 524.41  E-value: 1.24e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    112 ERRQLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVAGAIA----RFEGHVAKYMGDGVLAYFGYPRAHEDEAERAVR 187
Cdd:TIGR03903  283 ERRQLTALCCHVGLSTPPEPAEGVEEDDEELDLLLRSWLTRCAdiavRYGAHVGGVLGDTLLFYFGYPSAAERDARRAAR 362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    188 AGL----AAIDAVRKLQPPHGETLEARVGIATGLVVvgeligegAAREETVIGETPNLAARLQSVAEPGAVVVASATRQL 263
Cdd:TIGR03903  363 AALemvrQAGRKGEAAAGEGKWRVEIAAGIHTGLVL--------AQAPHASGGTTPNAAVRMQAQAEPGQILVSEAARKL 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    264 IGGLFDLAELGFHPLKGFAASIPAWRVLGESSAESRFEAFHGASLTPLVGREHDIGLLLKRWEAVKKGKGRVVLLAGEPG 343
Cdd:TIGR03903  435 LRRHADFDPTALEEAAAGAESQPVFELLGERAARTPFTSLDGGTTTPLVGRSRELEALRRRWRDTVAGRGRAILVVGEAG 514
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    344 IGKSRLVRALRRRLEGEPHTTVSHYCSPYHQTSPLYPVIRLLERAAGFAAEDPPEVKLSKLEALLTQSIEEVADAAPLLA 423
Cdd:TIGR03903  515 IGKSRLVHELVEKVRGRPHAFLECRCLPEQENHALFPVLRLVRAHWGLDRNAPPEQALAAIDALLTANGCDLAEARPLLA 594
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    424 ALLSVPAdDRYQPLELSPHRQKKRMLEVLVDQLIGLAARQPILAVYEDVHWADPTSLELLDLVVDRVQDSPVLVLITFRT 503
Cdd:TIGR03903  595 GWLSLPG-GAYPVPEWSPARQKELLFDVLVQLLFSLAQGAPVLLLVEDLHWADSATLEFLAALAEDPATARLCLVLTARP 673
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    504 EFLPPWtRYPHVTVLTLSRLSRRQGAEMVDRLTGRRALPTEVLDQIVAKTDGVPLFVEELTRAILETsLLKAEGDHYALA 583
Cdd:TIGR03903  674 ERLPRW-RMGAALRVQLRRLDRARAEEMVSGLLQPTPLPRAVLDQLVSRTDGVPLFIEELARMLMET-LPGRDGELPSRA 751
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    584 RPlSAISIPATLHESLLARLDRLAPAREVMQVAAAIGREFSHELLVTAAPLQASEVEEALEDLIASGLVFRHGTPPQLTY 663
Cdd:TIGR03903  752 QA-DRLPIPSTLRDSLELRFDRLGPARETAQLAATIGREFDAELLADASPHDEAELDRDLRALADARLVYAQHRVGNPSY 830
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    664 SFKHALVRDAAYATLVRTKRQRLHAAIATAIEQRFPEMVQTQPELLAQHYAEAGRLEPAVNYWLRAGQAEIARSATTEAI 743
Cdd:TIGR03903  831 LFRHALIRDAAYESMLRAMRREVHERVAAALLARFPRVVAARPDLLALHFARADAFAQAVPYGIKAARRALMRSLNDEAI 910
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    744 SHLTRGLELLEGLpDDAARLRKELELQVALSVALMTAKGWAAPEVGRANARARNLCERLGDKSRLFPVLYGDWVFHVVRA 823
Cdd:TIGR03903  911 RYATAVLAWLEVV-DEAERAEDELGLDGTLIHARMARHGWADPQIRERIEQSLELVDLLGDSPLVAPALWTLGTYHHVAG 989
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    824 ELEAGRKAGEELLRRAQEEREVSAEIVGNRIAGTGAFLRGEIANAREYLERSLALYDPQQHRALAFLFAQDPRVAGLSVL 903
Cdd:TIGR03903  990 HRVGVRRIGERLLALARQSGDAGLVVAADTGLGMALWVEGRYAEAREAFDAALALYDARRDAKHAVYLGLDTRAWAQAAR 1069
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    904 SLTLFALGYPEQAQARSNEALADARELSHSNTLGFALLYGCILSQLRGDWREARDRAGSLITLARAQGSPHFLGAGKILQ 983
Cdd:TIGR03903 1070 AFVRWGLGDDDLAAAYARSAVTWATCLDHLPSLGLTMMYLARFLQAQGDRDQARAVADAALELSHRYGLPAVEVYAAVIR 1149
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    984 GWTLgqtGELPAASTKVQeglASWQMtGARFLVPYFLSLLARVETQSAGAKRALDLLTDALQRARETGERWFEAELHRLT 1063
Cdd:TIGR03903 1150 AWAV---RDRAGARADID---ALRQS-GCGLGLTYYASLLAELDAERGRYGAALAIIDECLALAESPDERYYLAELLLKK 1222
                          970       980       990      1000
                   ....*....|....*....|....*....|....*....|....*.
gi 16263319   1064 GELMLQlpAFDRA-EGEARLQHAVELARGQGADLWELRAATSLARL 1108
Cdd:TIGR03903 1223 GRCLRA--AGERAvAAEACLRRAVEVARQQGMKRIERKAAAALREL 1266
COG3899 COG3899
Predicted ATPase [General function prediction only]
310-754 2.12e-108

Predicted ATPase [General function prediction only]


Pssm-ID: 226415 [Multi-domain]  Cd Length: 849  Bit Score: 361.72  E-value: 2.12e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  310 PLVGREHDIGLLLKRWEAVKKGKGRVVLLAGEPGIGKSRLVRALRRRLEGEPHTTVSHYCSPYHQTSPLYPVIRLLERAA 389
Cdd:COG3899    1 PLYGRETELAQLLAAFDRVSKGRGEVVLVAGESGIGKSALVNEVHKPITQQRGYFIKGKFDQFERNIPLSPLVQAFRDLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  390 GFAAEDPPEVKLSKLEALLTQSIEEVADAAPLLAALLSVPaDDRYQPLELSPHRQKKRMLEVLVDQLIGLAARQ-PILAV 468
Cdd:COG3899   81 GQLLSESDTRILSWRARLLAALGENGQVIIDVIPELELII-GKRPPALELSPTAAQNRFNLAFLRFIQVFTAEEhPLVIV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  469 YEDVHWADPTSLELLDLVVDRVQ-----DSPVLVLITFRTEFLPPWTRYPHVTVLTLSRLSRRQGAEMVDRLTGR-RALP 542
Cdd:COG3899  160 LEDLHWADSASLKLLQLLMDRIAigayrDNEVLLLHPLRPTLGEILKSATNITTITLAPLSRADTNQLVAATLGCtKLLP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  543 TEVLDQIVAKTDGVPLFVEELTRAILETSLLKAEGDHYALARPLSAISIPATLH---ESLLARLDRL-APAREVMQVAAA 618
Cdd:COG3899  240 APLLELIFEKTKGNPFFIEEFLKALYEEGLLVFNFDTGAWQCSIASLGILATTDavvEFLAARLQKLpGTTREVLKAAAC 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  619 IGREFSHELLVTAAP-LQASEVEEALEDLIASGLVF-----RHGTPPQL-TYSFKHALVRDAAYATLVRTKRQRLHAAIA 691
Cdd:COG3899  320 IGNRFDLDTLAALAEdSPALEAAALLDALQEGLILPlsetyRFGSNVDIaTYKFLHDRVQQAAYNLIPESQRQYLHLRIG 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16263319  692 TAIEQRFPEMVQTQPELLAQHYAEAG----RLEPAVN----YWLRAGQAEIARSATTEAISHLTRGLELLE 754
Cdd:COG3899  400 QLLEQNIPEAGQEEEIFDIVNQLNAGvgliTLEEAVDelaeLNLLAGRKAKLRSAYSAAISYLERGLSLLL 470
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
80-266 1.47e-22

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485 [Multi-domain]  Cd Length: 194  Bit Score: 97.33  E-value: 1.47e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319      80 KLLAAIAaLREVAEQpsgaAGFGATPVINPEaeRRQLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVAGAIARFEGH 159
Cdd:smart00044    8 RLLDQLL-PASVAEQ----LKRGGSPVPAES--YDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319     160 VAKYMGDGVLAYFGYPRAHE-DEAERAVRAGLAAIDAVRKLQPPHGET-LEARVGIATGLVVVGeLIGEgAAREETVIGE 237
Cdd:smart00044   81 KVKTIGDAYMVASGLPEEALvDHAELIADEALDMVEELKTVLVQHREEgLRVRIGIHTGPVVAG-VVGI-RMPRYCLFGD 158
                           170       180
                    ....*....|....*....|....*....
gi 16263319     238 TPNLAARLQSVAEPGAVVVASATRQLIGG 266
Cdd:smart00044  159 TVNLASRMESAGDPGQIQVSEETYSLLAR 187
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
32-90 2.34e-11

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 [Multi-domain]  Cd Length: 68  Bit Score: 61.54  E-value: 2.34e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319      32 DIGAWLRDQGLGQYEGTFRQNDID-PEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALRE 90
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
115-290 6.68e-53

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636  Cd Length: 177  Bit Score: 184.32  E-value: 6.68e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  115 QLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVAGAIARFEGHVAKYMGDGVLAYFGYPRAHEDEAERAVRAGLAAID 194
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  195 AVRKL--QPPHGETLEARVGIATGLVVVGELigeGAAREE-TVIGETPNLAARLQSVAEPGAVVVASATRQLIGGL-FDL 270
Cdd:cd07302   81 ALAELnaEREGGPPLRLRIGIHTGPVVAGVV---GSERPEyTVIGDTVNLAARLESLAKPGQILVSEATYELLGDAgFEF 157
                        170       180
                 ....*....|....*....|
gi 16263319  271 AELGFHPLKGFAASIPAWRV 290
Cdd:cd07302  158 EELGEVELKGKSGPVRVYRL 177
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
32-85 3.46e-15

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  Cd Length: 56  Bit Score: 72.27  E-value: 3.46e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16263319   32 DIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAI 85
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
COG3903 COG3903
Predicted ATPase [General function prediction only]
753-1157 8.79e-117

Predicted ATPase [General function prediction only]


Pssm-ID: 226418  Cd Length: 414  Bit Score: 370.59  E-value: 8.79e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  753 LEGLPDDAARLRKELELQVALSVALMTAKGWAAP-EVGRANARARNLCERLGDKSRLFPVLYGDWVFHVVRAELEAGRKA 831
Cdd:COG3903    3 GEALVRDLLTALRLVTLTGAGGVGKTTLALQAAHaASEYADGVAFVDLAPITDPALVFPTLAGALGLHVQPGDSAVDTLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  832 GEELLRRAQEEREVSAEIVGNRIAGTGAFLRGEIANAREYLERSLALYDPQQHRALAFLFAQD---PRVAGLSVLSLTLF 908
Cdd:COG3903   83 RRIGDRRALLVLDNCEHLLDACAALIVALLGACPRLAILATSREAILVAGEVHRRVPSLSLFDeaiELFVCRAVLVALSF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  909 ALGYPEQAQARSNEALAD--ARELSHSNTLGFALLYGCILSQLRGDWREARDRAgSLITLARAQGSPHFLGAGKILQGWT 986
Cdd:COG3903  163 WLTDDNAAAVAEICRRLDgiPLAIELAAARVRSLSPDEIAAGLRDRFRLLTGGA-RLAVLRQQTLRASLDWSYALLTGWE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  987 LGQTGELPAASTKVQEGLASWQMTGARFLVPYFLSLLARVETQSAGAKRALDLLTDALQRARETGERWFEAELHRLTGEL 1066
Cdd:COG3903  242 RALFGRLAVFVGGFDLGLALAVAAGADVDVPRYLVLLALTLLVDKSLVVALDLLGRARYRLLETGRRYALAELHRSGEAD 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319 1067 MLQLPAFDRAEGEARLQHAVELARGQGADLWELRAATSLARLRIGQNR-FGDVHHLLAPLCGKFAEGFATTDLQSAQRLL 1145
Cdd:COG3903  322 AVLARHRDHYEAAAAEQSAPSAARGQGALLQAEREADNLLRAAFGWSReNGDVAHALALASSLFPLWFNTGDLQEALRWL 401
                        410
                 ....*....|..
gi 16263319 1146 REAAGFDGAIKS 1157
Cdd:COG3903  402 DSALADHGAIHL 413
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
110-280 9.11e-29

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 249682  Cd Length: 184  Bit Score: 115.42  E-value: 9.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    110 EAER-RQLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVAGAIARFEGHVAKYMGDGVLAYFGYPRAHEDEAERAVRA 188
Cdd:pfam00211    2 YAQSyDNVTILFADIVGFTALSSAHSPEEVVRLLNDLYTRFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHAQTIAEM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    189 GLAAIDAVRKLQPPHGETLEARVGIATGLVVVGeLIGEGAAReETVIGETPNLAARLQSVAEPGAVVVASATRQLI--GG 266
Cdd:pfam00211   82 ALDMLEAIKSVNIPSFEGLRVRVGIHTGPVVAG-VIGAKRPR-YDVWGDTVNLASRMESTGVPGKIHVSEETYRLLktRE 159
                          170
                   ....*....|....
gi 16263319    267 LFDLAELGFHPLKG 280
Cdd:pfam00211  160 GFEFTERGEVEVKG 173
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
115-255 1.12e-25

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637  Cd Length: 133  Bit Score: 104.75  E-value: 1.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  115 QLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVAGAIARFEGHVAKYMGDGVLAYFGyprahEDEAERAVRAGLAAID 194
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16263319  195 AVRKLQPPHGETLEARVGIATGLVVVGeliGEGAAREETVIGETPNLAARLQSVAEPGAVV 255
Cdd:cd07556   76 AVSALNQSEGNPVRVRIGIHTGPVVVG---VIGSRPQYDVWGALVNLASRMESQAKAGQVL 133
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
31-89 1.33e-15

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: 249940  Cd Length: 64  Bit Score: 73.43  E-value: 1.33e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16263319     31 MDIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:pfam00536    6 EDVGEWLESIGLGQYADNFRAGYIDGDALLLLTEEDLEKLGVTLPGHRKKILSSIQGLK 64
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
32-92 3.88e-13

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: 66.57  E-value: 3.88e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16263319   32 DIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIG-VGVASVGHRRKLLAAIAALREVA 92
Cdd:cd09505    9 DVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKdLKIESLGHRNKILRKIEELKMKS 70
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the ...
310-498 2.02e-12

AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.


Pssm-ID: 257559  Cd Length: 156  Bit Score: 66.33  E-value: 2.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    310 PLVGREHDIGLLLKRWEAVKKGKGRVVLLAGEPGIGKSRLVRALRRRLEGEPHTTVSHYCSPYhqtsPLYPVIRLLERAa 389
Cdd:pfam13191    1 RLVGREEELERLLDALERVRSGRPGLVLLTGPSGVGKTSLLRELLERLARKGGGVLSGKCDEL----PYAALRQLLREL- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    390 gfaaedppevklskLEALLTQSIEEVADAApllaallsvpaddryQPLELSPHRQKKRMLEVLVDQLIGLAARQ-PILAV 468
Cdd:pfam13191   76 --------------LRQLLDELLPELELLP---------------PVPGLPPDDLRNRLEDLLRRLLRRLAARErPLVLV 126
                          170       180       190
                   ....*....|....*....|....*....|
gi 16263319    469 YEDVHWADPTSLELLDLVVDRVQDSPVLVL 498
Cdd:pfam13191  127 LDDLQWADEASLALLLALARLLERLPLLLV 156
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
32-85 3.88e-12

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: 63.49  E-value: 3.88e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16263319   32 DIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAI 85
Cdd:cd09533    1 DVADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAV 54
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
32-89 1.08e-10

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 59.15  E-value: 1.08e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16263319   32 DIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:cd09534    5 FVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSLR 62
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
32-89 1.81e-10

SAM domain (Sterile alpha motif);


Pssm-ID: 254328  Cd Length: 66  Bit Score: 58.83  E-value: 1.81e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16263319     32 DIGAWLRDQGLGQYEGTFRQNDID-PEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:pfam07647    8 DVAEWLRSIGLPQYADNFRDQGITgAELLLRLTEEDLKALGITSVGHRRKILKKIQRLK 66
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
29-88 2.57e-09

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 55.50  E-value: 2.57e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319   29 GAMDIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAAL 88
Cdd:cd09507    6 TTEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIKDL 65
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
32-78 4.11e-09

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 54.63  E-value: 4.11e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 16263319   32 DIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHR 78
Cdd:cd09506    9 DVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHR 55
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
33-89 2.80e-08

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188896  Cd Length: 66  Bit Score: 52.26  E-value: 2.80e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16263319   33 IGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:cd09497    7 IFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQ 63
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
41-90 1.70e-07

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.


Pssm-ID: 188919  Cd Length: 65  Bit Score: 49.99  E-value: 1.70e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 16263319   41 GLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALRE 90
Cdd:cd09520   15 GLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKMLLAISELNK 64
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
33-88 3.72e-07

SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design.


Pssm-ID: 188953  Cd Length: 67  Bit Score: 49.09  E-value: 3.72e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16263319   33 IGAWLRDQGLGQYEGTFRQNDIDP-EVLRHLTAEDLIGVGVASVGHRRKLLAAIAAL 88
Cdd:cd09554    6 VGEWLRAIKMERYEDSFLQAGFTTfQLVSQISTEDLLRMGVTLAGHQKKILSSIQAM 62
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
32-91 3.91e-07

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 49.22  E-value: 3.91e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16263319   32 DIGAWLRDQGLGQYEGTFRQNDIDP-EVLRHLTAEDLIGVGVASVGHRRKLLAAIAALREV 91
Cdd:cd09498    9 DLLEWLSLLGLPQYHKVLVENGYDSiDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLKDL 69
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
36-89 4.37e-07

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: 48.84  E-value: 4.37e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16263319   36 WLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:cd09566   10 WLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
33-88 7.93e-06

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 44.91  E-value: 7.93e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16263319   33 IGAWLRDQGLGQYEGTFRQNDID--PEVLRhLTAEDLIGVGVASVGHRRKLLAAIAAL 88
Cdd:cd09488    5 VGEWLESIKMGRYKENFTAAGYTslDAVAQ-MTAEDLTRLGVTLVGHQKKILNSIQAL 61
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
29-88 1.06e-05

SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK-delta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. In particular DGK-delta is involved in the regulation of clathrin-dependent endocytosis. The SAM domain of DGK-delta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-eta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it inhibits the translocation of the protein to the plasma membrane from the cytoplasm. The SAM domain also can bind Zn at multiple (not conserved) sites driving the formation of highly ordered large sheets of polymers, thus suggesting that Zn may play important role in the function of DCK-delta.


Pssm-ID: 188974  Cd Length: 65  Bit Score: 44.56  E-value: 1.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319   29 GAMDIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAAL 88
Cdd:cd09575    6 GTEEVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
36-90 1.51e-05

SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188926  Cd Length: 63  Bit Score: 44.36  E-value: 1.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16263319   36 WLRDQGLGQYEGTFRQNDIDP-EVLRHLTAEDLIGVGVASVGHRRKLLAAIAALRE 90
Cdd:cd09527    8 WLRTLQLEQYAEKFVDNGYDDlEVCKQIGDPDLDAIGVMNPAHRKRILEAVRRLKE 63
SAM_HD cd09508
SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily ...
32-91 1.72e-05

SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily proteins is a putative protein-protein interaction domain. Proteins of this group, additionally to the SAM domain, contain a HD hydrolase domain. Human SAM-HD1 is a nuclear protein involved in innate immune response and may act as a negative regulator of the cell-intrinsic antiviral response. Mutations in this gene lead to Aicardi-Goutieres syndrome (symptoms include cerebral atrophy, leukoencephalopathy, hepatosplenomegaly, and increased production of alpha-interferon).


Pssm-ID: 188907  Cd Length: 70  Bit Score: 44.23  E-value: 1.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16263319   32 DIGAWLRDQGLGQYE--GTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALREV 91
Cdd:cd09508    9 DVCQFLRGNGFGEPEllEIFRENEITGAHLPDLTESRLEKLGVSSLGERLKLLKCLQKLSQI 70
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
27-86 3.33e-05

SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. SAM is a widespread domain in signaling proteins. In many cases it mediates homo-dimerization/oligomerization.


Pssm-ID: 188918  Cd Length: 64  Bit Score: 43.25  E-value: 3.33e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319   27 GEGAMDIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIA 86
Cdd:cd09519    1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIA 60
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
26-89 4.42e-05

SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 subfamily is a protein-protein interaction domain. In addition to the SAM domain, proteins of this group have ankyrin repeats and a ADP- ribosyltransferase (poly-(ADP-ribose) synthase) domain. Tankyrases can polymerize through their SAM domains forming homoligomers and these complexes are disrupted by autoribosylation. Tankyrases apparently act as master scaffolding proteins and thus may interact simultaneously with multiple proteins, in particular with TRF1, NuMA, IRAP and Grb14 (ankyrin repeats are involved in these interactions). Tankyrases participate in a variety of cell signaling pathways as effector molecules. Their functions are different depending on the intracellular location: at telomeres they play a role in the regulation of telomere length via control of telomerase access to telomeres, at centrosomes they promote spindle assembly/disassembly, in Golgi vesicles they participate in the regulation of vesicle trafficking and Golgi dynamics. Tankyrase 1 may be of interest as new potential target for telomerase-directed cancer therapy.


Pssm-ID: 188923  Cd Length: 66  Bit Score: 42.70  E-value: 4.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16263319   26 DGEGAMDIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:cd09524    1 VNGTDFSISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLI 64
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
33-86 5.79e-05

SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 subfamily is a protein-protein interaction domain. Ship2 proteins are lipid phosphatases (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2) containing an N-terminal SH2 domain, a central phosphatase domain and a C-terminal SAM domain. Ship2 is involved in a number of PI3K signaling pathways. For example, it plays a role in regulation of the actin cytoskeleton remodeling, in insulin signaling pathways, and in EphA2 receptor endocytosis. SAM domain of Ship2 can interact with SAM domain of other proteins in these pathways, thus participating in signal transduction. In particular, SAM of Ship2 is known to form heterodimers with SAM domain of Eph-A2 receptor tyrosine kinase during receptor endocytosis as well as with SAM domain of PI3K effector protein Arap3 in the actin cytoskeleton signaling network. Since Ship2 plays a role in negatively regulating insulin signaling, it has been suggested that inhibition of its expression or function may contribute in treating type 2 diabetes and obesity-induced insulin resistance.


Pssm-ID: 188890  Cd Length: 63  Bit Score: 42.51  E-value: 5.79e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16263319   33 IGAWLRDQGLGQYEGTFRQNDIDP-EVLRHLTAEDLIGVGVASVGHRRKLLAAIA 86
Cdd:cd09491    8 VSEWLMNLGLQQYEEGLMHNGWDSlEFLSDITEEDLEEAGVTNPAHKRRLLDSLQ 62
SAM_DGK-eta cd09576
SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily ...
29-88 8.78e-05

SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases. The SAM domain is located at the C-terminus of two out of three isoforms of DGK-eta protein. DGK-eta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DCK-eta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-delta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it is responsible for sustained endosomal localization of the protein and resulted in negative regulation of DCK-eta catalytic activity.


Pssm-ID: 188975  Cd Length: 65  Bit Score: 41.88  E-value: 8.78e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319   29 GAMDIGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAAL 88
Cdd:cd09576    6 GTDEVAAWLDLLSLGEYKEIFIRHDIRGSELLHLERRDLKDLGIPKVGHMKRILQGIKEL 65
SAM_EPH-B6 cd09555
SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
35-90 9.02e-05

SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B6 receptors and appears to mediate cell-cell initiated signal transduction. Receptors of this type are highly expressed in embryo and adult nervous system, in thymus and also in T-cells. They are involved in regulation of cell adhesion and migration. (EPH-B6 receptor is unusual; it fails to show catalytic activity due to alteration in kinase domain). EPH-B6 may be considered as a biomarker in some types of tumors; EPH-B6 activates MAP kinase signaling in lung adenocarcinoma, suppresses metastasis formation in non-small cell lung cancer, and slows invasiveness in some breast cancer cell lines.


Pssm-ID: 188954  Cd Length: 69  Bit Score: 41.84  E-value: 9.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16263319   35 AWLRDQGLGQYEGTFRQNDIDP-EVLRHLTAEDLIGVGVASVGHRRKLLAAIAALRE 90
Cdd:cd09555   11 AWLSAIGLECYQDNFSKFGLCTfSDVAQLSLEDLPALGITLAGHQKKLLHHIQLLQQ 67
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
33-88 1.23e-04

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188898  Cd Length: 67  Bit Score: 41.51  E-value: 1.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16263319   33 IGAWLRDQGLGQYEGTFRQNDIDPevLRHLTA-----EDLIGVGVASVGHRRKLLAAIAAL 88
Cdd:cd09499    5 VGQWLESIGLPQYESKLLLNGFDD--VDFLGSgvmedQDLKEIGITDEQHRQIILQAARSL 63
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
37-95 1.59e-04

SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.


Pssm-ID: 188916  Cd Length: 66  Bit Score: 41.17  E-value: 1.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16263319   37 LRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVaSVGHRRKLLAAIAALREVAEQP 95
Cdd:cd09517    9 LTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKL-PLGPRRKLLNAIAKRKQALENP 66
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
33-89 1.91e-04

SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A5 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A5 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A5 gene is almost exclusively expressed in the nervous system. Murine EPH-A5 receptors participate in axon guidance during embryogenesis and play a role in the adult synaptic plasticity, particularly in neuron-target interactions in multiple neural circuits. Additionally EPH-A5 receptors and its ligand ephrin A5 regulate dopaminergic axon outgrowth and influence the formation of the midbrain dopaminergic pathways. EphA5 gene expression was found decreased in a few different breast cancer cell lines, thus it might be a potential molecular marker for breast cancer carcinogenesis and progression.


Pssm-ID: 188945  Cd Length: 66  Bit Score: 41.07  E-value: 1.91e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16263319   33 IGAWLRDQGLGQYEGTFRQNDIDP-EVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:cd09546    6 VGEWLEAIKMGRYTEIFMENGYSSmDAVAQVTLEDLRRLGVTLVGHQKKIMNSIQEMR 63
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
33-89 2.07e-04

SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B3 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B3 receptor protein kinase performs kinase-dependent and kinase-independent functions. It is known to be involved in thymus morphogenesis, in regulation of cell adhesion and migration. Also EphB3 controls cell positioning and ordered migration in the intestinal epithelium and plays a role in the regulation of adult retinal ganglion cell axon plasticity after optic nerve injury. In some experimental models overexpression of EphB3 enhances cell/cell contacts and suppresses colon tumor growth.


Pssm-ID: 188952  Cd Length: 69  Bit Score: 40.79  E-value: 2.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16263319   33 IGAWLRDQGLGQYEGTFRQNDIDP-EVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:cd09553    9 VGDWLDAIKMGRYKENFVSAGFASfDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMR 66
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
41-88 2.37e-04

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


Pssm-ID: 188920  Cd Length: 64  Bit Score: 40.73  E-value: 2.37e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 16263319   41 GLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAAL 88
Cdd:cd09521   16 ELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPGDQKKILDAIKEV 63
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
33-97 3.58e-04

SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A4 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of EPH-A4 receptors can form homodimers. EPH-A4 receptors bind ligands such as erphirin A1, A4, A5. They are known to interact with a number of different proteins, including meltrin beta metalloprotease, Cdk5, and EFS2alpha, however SAM domain doesn't participate in these interactions. EPH-A4 receptors are involved in regulation of corticospinal tract formation, in pathway controlling voluntary movements, in formation of motor neurons, and in axon guidance (SAM domain is not required for axon guidance or for EPH-A4 kinase signaling). In Xenopus embryos EPH-A4 induces loss of cell adhesion, ventro-lateral protrusions, and severely expanded posterior structures. Mutations in SAM domain conserved tyrosine (Y928F) enhance the ability of EPH-A4 to induce these phenotypes, thus supporting the idea that the SAM domain may negatively regulate some aspects of EPH-A4 activity. EphA4 gene was found overexpressed in a number of different cancers including human gastric cancer, colorectal cancer, and pancreatic ductal adenocarcinoma. It is likely to be a promising molecular target for the cancer therapy.


Pssm-ID: 188944  Cd Length: 71  Bit Score: 40.32  E-value: 3.58e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16263319   33 IGAWLRDQGLGQYEGTFRQND-IDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALREVAEQPSG 97
Cdd:cd09545    6 VDDWLQAIKMERYKDNFTAAGyTTLEAVVHMNQDDLARIGISAIAHQNKILSSVQGMRSQMQQMQG 71
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
32-89 3.91e-04

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.


Pssm-ID: 188914  Cd Length: 70  Bit Score: 39.93  E-value: 3.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16263319   32 DIGAWLRDQGLGQYEGTFR-QNDIDPEVLRHLTAEDL--IGVGVASVGHRRKLLAAIAALR 89
Cdd:cd09515    8 DVAKWLKKEGFSKYVDLLCnKHRIDGKVLLSLTEEDLrsPPLEIKVLGDIKRLWLAIRKLQ 68
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
33-89 4.15e-04

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188948  Cd Length: 70  Bit Score: 39.85  E-value: 4.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16263319   33 IGAWLRDQGLGQYEGTFRQNDIDP-EVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:cd09549   10 VGEWLEALDLCRYKDNFAAAGYGSlEAVARMTAQDVLSLGITSLEHQELLLAGIQALR 67
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
34-89 4.64e-04

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: 39.70  E-value: 4.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16263319   34 GAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIG-VGVASVGHRRKLLAAIAALR 89
Cdd:cd09567    9 REWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKhLGVSKKFHQASLLRGIELLR 65
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 ...
36-91 5.22e-04

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: 39.76  E-value: 5.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16263319   36 WLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIG-VGVASVGHRRKLLAAIAALREV 91
Cdd:cd09565   10 WLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRThLKMVDSFHRTSLQYGILCLKRL 66
SAM_MLTK cd09529
SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a ...
41-88 5.98e-04

SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a protein-protein interaction domain. Besides SAM domain, these proteins have N-terminal protein tyrosine kinase domain and leucine-zipper motif. Proteins of this group act as mitogen-activated protein triple kinase in a number of MAPK cascades. They can be activated by autophosphorylation in response to stress signals. MLTK-alpha is known to phosphorylate histone H3. In mammals, MLTKs participate in the activation of the JNK/SAPK, p38, ERK5 pathways, the transcriptional factor NF-kB, in the regulation of the cell cycle checkpoint, and in the induction of apoptosis in a hepatoma cell line. Some members of this subfamily are proto-oncogenes, thus MLTK-alpha is involved in neoplasmic cell transformation and/or skin cancer development in athymic nude mice. Based on in vivo coprecipitation experiments in mammalian cells, it has been demonstrated that MLTK proteins might form homodimers/oligomers via their SAM domains.


Pssm-ID: 188928  Cd Length: 71  Bit Score: 39.41  E-value: 5.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 16263319   41 GLGQYEGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAAL 88
Cdd:cd09529   23 ELSQYADLFKENHITGKRLLLLTEEDLRDMGIGSKGHIIHLKSAIEKL 70
SAM_VTS1_fungal cd09556
SAM domain of VTS1 RNA-binding proteins; SAM (sterile alpha motif) domain of VTS1 subfamily ...
32-90 7.32e-04

SAM domain of VTS1 RNA-binding proteins; SAM (sterile alpha motif) domain of VTS1 subfamily proteins is RNA binding domain located in the C-terminal region. SAM interacts with stem-loop structures of mRNA. Proteins of this subfamily participate in regulation of transcript stability and degradation, and also may be involved in vacuolar protein transport regulation. VTS1 protein of S.cerevisiae induces mRNA degradation via the major deadenylation-dependent mRNA decay pathway; VTS1 recruits CCR4/POP2/NOT deadenylase complex to target mRNA. The recruitment is the initial step resulting in poly(A) tail removal transcripts. Potentially SAM domain may be responsible not only for RNA binding but also for deadenylase binding.


Pssm-ID: 188955  Cd Length: 69  Bit Score: 39.21  E-value: 7.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16263319   32 DIGAWLRDQGLGQYEGTFrqNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALRE 90
Cdd:cd09556    8 DIPAWLRSLRLHKYTDNL--KDLSWKELIELDDEDLEDKGVSALGARRKLLKAFEIVRE 64
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
36-94 8.05e-04

SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B2 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B2 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of this subfamily form homodimers/oligomers (in head-to-head/tail-to-tail orientation); apparently such clustering is necessary for signaling. EPH-B2 receptor is involved in regulation of synaptic function; it is needed for normal vestibular function, proper formation of anterior commissure, control of cell positioning, and ordered migration in the intestinal epithelium. EPH-B2 plays a tumor suppressor role in colorectal cancer. It was found to be downregulated in gastric cancer and thus may be a negative biomarker for it.


Pssm-ID: 188951  Cd Length: 71  Bit Score: 39.22  E-value: 8.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319   36 WLRDQGLGQYEGTFRQNDIDP-EVLRHLTAEDLIGVGVASVGHRRKLLAAIAALREVAEQ 94
Cdd:cd09552   12 WLDAIKMGQYKESFANAGFTSfDVVSQMTMEDILRVGVTLAGHQKKILNSIQVMRAQMNQ 71
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
31-89 9.72e-04

SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation).


Pssm-ID: 188934  Cd Length: 65  Bit Score: 38.69  E-value: 9.72e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319   31 MDIGAWLRDQGLGQY-EGTFRQNDIDPEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:cd09535    6 EQVAEWLLSAGFDDSvCEKFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEIKSLR 65
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
36-89 1.04e-03

SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B1 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH- B1 receptors. In human vascular endothelial cells it appears to mediate cell-cell initiated signal transduction via the binding of the adaptor protein GRB10 (growth factor) through its SH2 domain to a conserved tyrosine that is phosphorylated. EPH-B1 receptors play a role in neurogenesis, in particular in regulation of proliferation and migration of neural progenitors in the hippocampus and in corneal neovascularization; they are involved in converting the crossed retinal projection to ipsilateral retinal projection. They may be potential targets in angiogenesis-related disorders.


Pssm-ID: 188950  Cd Length: 68  Bit Score: 38.87  E-value: 1.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16263319   36 WLRDQGLGQYEGTFRQNDIDP-EVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:cd09551   12 WLSAIKMSQYRDNFLSSGFTSlQLVAQMTSEDLLRIGVTLAGHQKKILNSIQSMR 66
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
35-89 2.43e-03

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: 37.51  E-value: 2.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16263319   35 AWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDL-IGVGVASVGHRRKLLAAIAALR 89
Cdd:cd09495    5 RWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLlVHLKVTSQLHHLSLKCGIHVLH 60
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
33-89 2.87e-03

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.


Pssm-ID: 188946  Cd Length: 64  Bit Score: 37.17  E-value: 2.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16263319   33 IGAWLRDQGLGQYEGTFRQNDIDP-EVLRHLTAEDLIGVGVASVGHRRKLLAAIAALR 89
Cdd:cd09547    6 VSDWLDSIKMGQYKNNFMAAGFTTlDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLR 63
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
33-85 4.68e-03

SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell.


Pssm-ID: 188941  Cd Length: 63  Bit Score: 36.52  E-value: 4.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16263319   33 IGAWLRDQGLGQYEGTFRQNDIDP-EVLRHLTAEDLIGVGVASVGHRRKLLAAI 85
Cdd:cd09542    7 VSEWLESIRMKRYILHFRSAGLDTmECVLELTAEDLTQMGITLPGHQKRILCSI 60
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
33-87 7.94e-03

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: 36.05  E-value: 7.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16263319   33 IGAWLRDQGLGQYEGTFRQNDIDPEVLRHLTAEDLIGV-GVASVGHRRKLLAAIAA 87
Cdd:cd09563    9 VCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKElGIKHPLHRKKLQLALQA 64
CyaA COG2114
Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction ...
72-299 6.09e-42

Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction mechanisms]


Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 154.62  E-value: 6.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319   72 VASVGHRRKLLAAIAALREVAEQPSGAAGFGATPVINPEAER-RQLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVA 150
Cdd:COG2114    2 AAVLNLLAKEAKVAAAGLRSDLVLRLYLARVVGRLLARGGAGdRRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  151 GAIARFEGHVAKYMGDGVLAYFGYPRAHEDEAERAVRAGLAAIDAVRKLQpphGETLEARVGIATGLVVVGELIGegaar 230
Cdd:COG2114   82 EVVARHGGRVVKFIGDGFLAVFGRPSPLEDAVACALDLQLALRNPLARLR---RESLRVRIGIHTGEVVVGNTGG----- 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  231 eETVIGETPNLAARLQSVAEPGAVVVASATRQLIGGLFDLAE-LGFHPLKGFAASIPAWRVLGESSAESR 299
Cdd:COG2114  154 -YTVVGSAVNQAARLESLAKPGQVLLSEATYDLVRDLVDLFSgLGSHRLKGLARPVRVYQLCHRSLRRNL 222
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
112-1108 1.24e-164

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein [Cellular processes, Toxin production and resistance].


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 524.41  E-value: 1.24e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    112 ERRQLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVAGAIA----RFEGHVAKYMGDGVLAYFGYPRAHEDEAERAVR 187
Cdd:TIGR03903  283 ERRQLTALCCHVGLSTPPEPAEGVEEDDEELDLLLRSWLTRCAdiavRYGAHVGGVLGDTLLFYFGYPSAAERDARRAAR 362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    188 AGL----AAIDAVRKLQPPHGETLEARVGIATGLVVvgeligegAAREETVIGETPNLAARLQSVAEPGAVVVASATRQL 263
Cdd:TIGR03903  363 AALemvrQAGRKGEAAAGEGKWRVEIAAGIHTGLVL--------AQAPHASGGTTPNAAVRMQAQAEPGQILVSEAARKL 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    264 IGGLFDLAELGFHPLKGFAASIPAWRVLGESSAESRFEAFHGASLTPLVGREHDIGLLLKRWEAVKKGKGRVVLLAGEPG 343
Cdd:TIGR03903  435 LRRHADFDPTALEEAAAGAESQPVFELLGERAARTPFTSLDGGTTTPLVGRSRELEALRRRWRDTVAGRGRAILVVGEAG 514
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    344 IGKSRLVRALRRRLEGEPHTTVSHYCSPYHQTSPLYPVIRLLERAAGFAAEDPPEVKLSKLEALLTQSIEEVADAAPLLA 423
Cdd:TIGR03903  515 IGKSRLVHELVEKVRGRPHAFLECRCLPEQENHALFPVLRLVRAHWGLDRNAPPEQALAAIDALLTANGCDLAEARPLLA 594
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    424 ALLSVPAdDRYQPLELSPHRQKKRMLEVLVDQLIGLAARQPILAVYEDVHWADPTSLELLDLVVDRVQDSPVLVLITFRT 503
Cdd:TIGR03903  595 GWLSLPG-GAYPVPEWSPARQKELLFDVLVQLLFSLAQGAPVLLLVEDLHWADSATLEFLAALAEDPATARLCLVLTARP 673
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    504 EFLPPWtRYPHVTVLTLSRLSRRQGAEMVDRLTGRRALPTEVLDQIVAKTDGVPLFVEELTRAILETsLLKAEGDHYALA 583
Cdd:TIGR03903  674 ERLPRW-RMGAALRVQLRRLDRARAEEMVSGLLQPTPLPRAVLDQLVSRTDGVPLFIEELARMLMET-LPGRDGELPSRA 751
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    584 RPlSAISIPATLHESLLARLDRLAPAREVMQVAAAIGREFSHELLVTAAPLQASEVEEALEDLIASGLVFRHGTPPQLTY 663
Cdd:TIGR03903  752 QA-DRLPIPSTLRDSLELRFDRLGPARETAQLAATIGREFDAELLADASPHDEAELDRDLRALADARLVYAQHRVGNPSY 830
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    664 SFKHALVRDAAYATLVRTKRQRLHAAIATAIEQRFPEMVQTQPELLAQHYAEAGRLEPAVNYWLRAGQAEIARSATTEAI 743
Cdd:TIGR03903  831 LFRHALIRDAAYESMLRAMRREVHERVAAALLARFPRVVAARPDLLALHFARADAFAQAVPYGIKAARRALMRSLNDEAI 910
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    744 SHLTRGLELLEGLpDDAARLRKELELQVALSVALMTAKGWAAPEVGRANARARNLCERLGDKSRLFPVLYGDWVFHVVRA 823
Cdd:TIGR03903  911 RYATAVLAWLEVV-DEAERAEDELGLDGTLIHARMARHGWADPQIRERIEQSLELVDLLGDSPLVAPALWTLGTYHHVAG 989
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    824 ELEAGRKAGEELLRRAQEEREVSAEIVGNRIAGTGAFLRGEIANAREYLERSLALYDPQQHRALAFLFAQDPRVAGLSVL 903
Cdd:TIGR03903  990 HRVGVRRIGERLLALARQSGDAGLVVAADTGLGMALWVEGRYAEAREAFDAALALYDARRDAKHAVYLGLDTRAWAQAAR 1069
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    904 SLTLFALGYPEQAQARSNEALADARELSHSNTLGFALLYGCILSQLRGDWREARDRAGSLITLARAQGSPHFLGAGKILQ 983
Cdd:TIGR03903 1070 AFVRWGLGDDDLAAAYARSAVTWATCLDHLPSLGLTMMYLARFLQAQGDRDQARAVADAALELSHRYGLPAVEVYAAVIR 1149
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319    984 GWTLgqtGELPAASTKVQeglASWQMtGARFLVPYFLSLLARVETQSAGAKRALDLLTDALQRARETGERWFEAELHRLT 1063
Cdd:TIGR03903 1150 AWAV---RDRAGARADID---ALRQS-GCGLGLTYYASLLAELDAERGRYGAALAIIDECLALAESPDERYYLAELLLKK 1222
                          970       980       990      1000
                   ....*....|....*....|....*....|....*....|....*.
gi 16263319   1064 GELMLQlpAFDRA-EGEARLQHAVELARGQGADLWELRAATSLARL 1108
Cdd:TIGR03903 1223 GRCLRA--AGERAvAAEACLRRAVEVARQQGMKRIERKAAAALREL 1266
COG3899 COG3899
Predicted ATPase [General function prediction only]
310-754 2.12e-108

Predicted ATPase [General function prediction only]


Pssm-ID: 226415 [Multi-domain]  Cd Length: 849  Bit Score: 361.72  E-value: 2.12e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  310 PLVGREHDIGLLLKRWEAVKKGKGRVVLLAGEPGIGKSRLVRALRRRLEGEPHTTVSHYCSPYHQTSPLYPVIRLLERAA 389
Cdd:COG3899    1 PLYGRETELAQLLAAFDRVSKGRGEVVLVAGESGIGKSALVNEVHKPITQQRGYFIKGKFDQFERNIPLSPLVQAFRDLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  390 GFAAEDPPEVKLSKLEALLTQSIEEVADAAPLLAALLSVPaDDRYQPLELSPHRQKKRMLEVLVDQLIGLAARQ-PILAV 468
Cdd:COG3899   81 GQLLSESDTRILSWRARLLAALGENGQVIIDVIPELELII-GKRPPALELSPTAAQNRFNLAFLRFIQVFTAEEhPLVIV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  469 YEDVHWADPTSLELLDLVVDRVQ-----DSPVLVLITFRTEFLPPWTRYPHVTVLTLSRLSRRQGAEMVDRLTGR-RALP 542
Cdd:COG3899  160 LEDLHWADSASLKLLQLLMDRIAigayrDNEVLLLHPLRPTLGEILKSATNITTITLAPLSRADTNQLVAATLGCtKLLP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  543 TEVLDQIVAKTDGVPLFVEELTRAILETSLLKAEGDHYALARPLSAISIPATLH---ESLLARLDRL-APAREVMQVAAA 618
Cdd:COG3899  240 APLLELIFEKTKGNPFFIEEFLKALYEEGLLVFNFDTGAWQCSIASLGILATTDavvEFLAARLQKLpGTTREVLKAAAC 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  619 IGREFSHELLVTAAP-LQASEVEEALEDLIASGLVF-----RHGTPPQL-TYSFKHALVRDAAYATLVRTKRQRLHAAIA 691
Cdd:COG3899  320 IGNRFDLDTLAALAEdSPALEAAALLDALQEGLILPlsetyRFGSNVDIaTYKFLHDRVQQAAYNLIPESQRQYLHLRIG 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16263319  692 TAIEQRFPEMVQTQPELLAQHYAEAG----RLEPAVN----YWLRAGQAEIARSATTEAISHLTRGLELLE 754
Cdd:COG3899  400 QLLEQNIPEAGQEEEIFDIVNQLNAGvgliTLEEAVDelaeLNLLAGRKAKLRSAYSAAISYLERGLSLLL 470
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
80-266 1.47e-22

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485 [Multi-domain]  Cd Length: 194  Bit Score: 97.33  E-value: 1.47e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319      80 KLLAAIAaLREVAEQpsgaAGFGATPVINPEaeRRQLTVMFVDLVESTRLSSRLDPEEMGELLRGYQRAVAGAIARFEGH 159
Cdd:smart00044    8 RLLDQLL-PASVAEQ----LKRGGSPVPAES--YDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319     160 VAKYMGDGVLAYFGYPRAHE-DEAERAVRAGLAAIDAVRKLQPPHGET-LEARVGIATGLVVVGeLIGEgAAREETVIGE 237
Cdd:smart00044   81 KVKTIGDAYMVASGLPEEALvDHAELIADEALDMVEELKTVLVQHREEgLRVRIGIHTGPVVAG-VVGI-RMPRYCLFGD 158
                           170       180
                    ....*....|....*....|....*....
gi 16263319     238 TPNLAARLQSVAEPGAVVVASATRQLIGG 266
Cdd:smart00044  159 TVNLASRMESAGDPGQIQVSEETYSLLAR 187
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
32-90 2.34e-11

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 [Multi-domain]  Cd Length: 68  Bit Score: 61.54  E-value: 2.34e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319      32 DIGAWLRDQGLGQYEGTFRQNDID-PEVLRHLTAEDLIGVGVASVGHRRKLLAAIAALRE 90
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
MalT COG2909
ATP-dependent transcriptional regulator [Transcription]
449-1109 1.01e-04

ATP-dependent transcriptional regulator [Transcription]


Pssm-ID: 225461 [Multi-domain]  Cd Length: 894  Bit Score: 45.08  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  449 LEVLVDQLIGLAAR--QPILAVYEDVHWA-DPTSLELLDLVVDRVQDSPVLVLITfrtEFLPPWtrypHVTVLTLS---- 521
Cdd:COG2909  113 LESLLSSLLNELASyeGPLYLVLDDYHLIsDPALHEALRFLLKHAPENLTLVVTS---RSRPQL----GLARLRLRdell 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  522 -------RLSRRQGAEMVDRlTGRRALPTEVLDQIVAKTDGVPlfveeltrAILETSLLKAEGDHYA--LARPLSAISip 592
Cdd:COG2909  186 eigseelRFDTEEAAAFLND-RGSLPLDAADLKALYDRTEGWA--------AALQLIALALRNNTSAeqSLRGLSGAA-- 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  593 ATLHESLLAR-LDRLAPAREVMQVAAAIGREFSHELLVtaAPLQASEVEEALEDLIASGLvfrhgtppqltysFKHALVR 671
Cdd:COG2909  255 SHLSDYLVEEvLDRLPPELRDFLLQTSVLSRFNDELCN--ALTGEENGQAMLEELERRGL-------------FLQRLDD 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  672 DaayatlvrTKRQRLHAAIATAIEQRF-PEMVQTQPELL---AQHYAEAGRLEPAVNYWLRAGQAEIARS------ATTE 741
Cdd:COG2909  320 E--------GQWFRYHHLFAEFLRQRLqRELAARLKELHraaAEWFAEHGLPSEAIDHALAAGDPEMAADlleqleWQLF 391
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  742 AISHLTRGLELLEGLPDDAARLRKELELQVALSVALMTAKGWAAPEVGRANAR-ARNLCERLGDKSRLFPVLYGdwVFHV 820
Cdd:COG2909  392 NGSELSLLLAWLKALPAELLASTPRLVLLQAWLLASQHRLAEAETLIARLEHFlKAPMHSRQGDLLAEFQALRA--QVAL 469
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  821 VRAELEAGRKAGEELLRRAQEEREVSaEIVGNRIAGTGAFLRGEIANAREYLERslALYDPQQHRALAFLfaqdprVAGL 900
Cdd:COG2909  470 NRGDPEEAEDLARLALVQLPEAAYRS-RIVALSVLGEAAHIRGELTQALALMQQ--AEQMARQHDVYHLA------LWSL 540
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  901 SVLSLTLFALGYPEQAQARSNEALADARELSHSNTLGFALlygCILSQLRGDW---------------------REARDR 959
Cdd:COG2909  541 LQQSEILEAQGQVARAEQEKAFNLIREQHLEQKPRHEFLV---RIRAQLLRAWlrldlaeaearlgievgsvytPQPLLS 617
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319  960 AGSLITLARAQ-GSPHFLGAGKILQGWTLGQTG-----ELPAASTKVQegLASWQMTG---------------------- 1011
Cdd:COG2909  618 RLALSMLAELEfLRGDLDKALAQLDELERLLLNgqyhvDYLAAAYKVK--LILWLAQGdkelaaewllksgdpdkanahf 695
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16263319 1012 ----ARFLVPYFLSLLARVETQSAGAKRALDLLTDALQRARETGE-RWFEAELHRLTGELMLQLPAFDRA--------EG 1078
Cdd:COG2909  696 pqlqWRLIAREQILLGILLEAELALDELASRLTEDLNRNLRLLGLlYEGEAVKGQLALDLLDALQLRERTgflrhfaiEG 775
                        730       740       750
                 ....*....|....*....|....*....|...
gi 16263319 1079 EARLQH--AVELARGQGADLWELRAATSLARLR 1109
Cdd:COG2909  776 EARMAEqlRQLILLGELPELERHRLQRILREIL 808
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH