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Conserved domains on  [gi|147902627|ref|NP_001090509.1|]
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guanylate binding protein 2, interferon-inducible

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List of domain hits

Name Accession Description Interval E-value
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
46-273 6.64e-60

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


:

Pssm-ID: 206650 [Multi-domain]  Cd Length: 224  Bit Score: 200.63  E-value: 6.64e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  46 GKYRTGKSYLMNKLAGSKTGFPLGSTIQSKTKGIWMWCVPHPHQ--PSQTLVLLDTEGLGDVEKGDSKNDAWIFSLAVLL 123
Cdd:cd01851   14 GSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKDTdgKKHAVLLLDTEGTDGRERGEFENDARLFALATLL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627 124 SSNLVYNSMGTIDNHAMEQLHYVTELSklikvksnpVEEEEKNESGEFKRIFPSFTWCVRDFSLILELNGRTVTEdeylm 203
Cdd:cd01851   94 SSVLIYNMWQTILGDDLDKLMGLLKTA---------LETLGLAGLHNFSKPKPLLLFVVRDFTGPTPLEGLDVTE----- 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627 204 nslklkkGTDKKSQDHNLPRECILHFFHSHKCFVFDRPSSTKNLQRLeDLEERDLERAFVEQTQKFCDYI 273
Cdd:cd01851  160 -------KSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN-DGRLKDLPPEFRKALKALRQRF 221
OmpH super family cl21485
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
460-557 6.22e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


The actual alignment was detected with superfamily member smart00935:

Pssm-ID: 276321  Cd Length: 140  Bit Score: 36.02  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   460 EVLQEFMDNKKA---IEATILQADESLTAKEKEIaesQAQAEEAERQRLVLEEKERS-LQKSMEDQRKSHEQHEKMLIEK 535
Cdd:smart00935   8 KILQESPAGKAAqkqLEKEFKKRQAELEKLEKEL---QKLKEKLQKDAATLSEAAREkKEKELQKKVQEFQRKQQKLQQD 84
                           90       100
                   ....*....|....*....|..
gi 147902627   536 MERDRVNLIAENERVINQKLQE 557
Cdd:smart00935  85 LQKRQQEELQKILDKINKAIKE 106
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
284-581 5.47e-136

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


:

Pssm-ID: 202427 [Multi-domain]  Cd Length: 297  Bit Score: 401.28  E-value: 5.47e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  284 GGLLVTGRMLAHLANLYIETIKSGSVPCMENAVLALSVIENTGAIQDALTKYETCMNNQVpRFPTETLEEFLHMHQESEK 363
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKV-KLPTETLQELLDLHRDCEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  364 EALKVFLKRSFNDENQNFQREFKHLLDGKMKEFSERNERESMERCQIIIEELSDPLDQRISQGEFLKPGGHMLFLEEKMI 443
Cdd:pfam02841  80 EAIAVFMKRSFKDENQEFQKELVELLEKKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  444 IMTVYNTTPYKGLKSLEVLQEFMDNKKAIEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRK 523
Cdd:pfam02841 160 LEAKYNQVPRKGVKAEEVLQEFLNSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQER 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 147902627  524 SHEQHEKMLIEKMERDRVNLIAENERVINQKLQEQNAMLTAGFQGKVNALQREIDDLK 581
Cdd:pfam02841 240 SYQEHVKQLIEKMEAEREKLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
 
Name Accession Description Interval E-value
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
46-273 6.64e-60

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650 [Multi-domain]  Cd Length: 224  Bit Score: 200.63  E-value: 6.64e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  46 GKYRTGKSYLMNKLAGSKTGFPLGSTIQSKTKGIWMWCVPHPHQ--PSQTLVLLDTEGLGDVEKGDSKNDAWIFSLAVLL 123
Cdd:cd01851   14 GSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKDTdgKKHAVLLLDTEGTDGRERGEFENDARLFALATLL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627 124 SSNLVYNSMGTIDNHAMEQLHYVTELSklikvksnpVEEEEKNESGEFKRIFPSFTWCVRDFSLILELNGRTVTEdeylm 203
Cdd:cd01851   94 SSVLIYNMWQTILGDDLDKLMGLLKTA---------LETLGLAGLHNFSKPKPLLLFVVRDFTGPTPLEGLDVTE----- 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627 204 nslklkkGTDKKSQDHNLPRECILHFFHSHKCFVFDRPSSTKNLQRLeDLEERDLERAFVEQTQKFCDYI 273
Cdd:cd01851  160 -------KSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN-DGRLKDLPPEFRKALKALRQRF 221
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
20-282 3.77e-120

Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 111185  Cd Length: 264  Bit Score: 359.39  E-value: 3.77e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   20 NEFVINAEAEEILSQITDPVVVVVIVGKYRTGKSYLMNKLAGSKTGFPLGSTIQSKTKGIWMWCVPHPHQPSQTLVLLDT 99
Cdd:pfam02263   2 HQLELNEEALEILSAITQPVVVVAIVGLYRTGKSYLMNFLAGKLTGFSLGSTVESETKGIWMWCVPHPNKPKHTLVLLDT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  100 EGLGDVEKGDSKNDAWIFSLAVLLSSNLVYNSMGTIDNHAMEQLHYVTELSKLIKVKSNPvEEEEKNESGEFKRIFPSFT 179
Cdd:pfam02263  82 EGLGDVEKSDPKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTELIRAKSSP-RYGRVADSAEFVSFFPDFV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  180 WCVRDFSLILELNGRTVTEDEYLMNSLKLKKGTDKKSQDHNLPRECILHFFHSHKCFVFDRPSSTKNLQ-RLEDLEERDL 258
Cdd:pfam02263 161 WTVRDFSLPLELDGGPITGDEYLENRLKLSQGQHEELQNFNLPRECIRSFFPKRKCFLFDRPGLDVALNpQLEGLREDEL 240
                         250       260
                  ....*....|....*....|....
gi 147902627  259 ERAFVEQTQKFCDYIHRQGIVKTL 282
Cdd:pfam02263 241 DPEFQQQLREFCSYIFSESLVKTL 264
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
460-557 6.22e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922  Cd Length: 140  Bit Score: 36.02  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   460 EVLQEFMDNKKA---IEATILQADESLTAKEKEIaesQAQAEEAERQRLVLEEKERS-LQKSMEDQRKSHEQHEKMLIEK 535
Cdd:smart00935   8 KILQESPAGKAAqkqLEKEFKKRQAELEKLEKEL---QKLKEKLQKDAATLSEAAREkKEKELQKKVQEFQRKQQKLQQD 84
                           90       100
                   ....*....|....*....|..
gi 147902627   536 MERDRVNLIAENERVINQKLQE 557
Cdd:smart00935  85 LQKRQQEELQKILDKINKAIKE 106
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
284-581 5.47e-136

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 202427 [Multi-domain]  Cd Length: 297  Bit Score: 401.28  E-value: 5.47e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  284 GGLLVTGRMLAHLANLYIETIKSGSVPCMENAVLALSVIENTGAIQDALTKYETCMNNQVpRFPTETLEEFLHMHQESEK 363
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKV-KLPTETLQELLDLHRDCEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  364 EALKVFLKRSFNDENQNFQREFKHLLDGKMKEFSERNERESMERCQIIIEELSDPLDQRISQGEFLKPGGHMLFLEEKMI 443
Cdd:pfam02841  80 EAIAVFMKRSFKDENQEFQKELVELLEKKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  444 IMTVYNTTPYKGLKSLEVLQEFMDNKKAIEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRK 523
Cdd:pfam02841 160 LEAKYNQVPRKGVKAEEVLQEFLNSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQER 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 147902627  524 SHEQHEKMLIEKMERDRVNLIAENERVINQKLQEQNAMLTAGFQGKVNALQREIDDLK 581
Cdd:pfam02841 240 SYQEHVKQLIEKMEAEREKLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
RAD50_homologue_ceRAD50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
395-581 1.31e-05

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 46.96  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   395 EFSERNERESMErCQIIIEELSDPLDQRISQGEFLKPgghmlFLEEKMIIMTVYNTTPYKGLKSLEVLQEFMDNK----K 470
Cdd:TIGR00606  885 QFEEQLVELSTE-VQSLIREIKDAKEQDSPLETFLEK-----DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymK 958
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   471 AIEATILQA-DESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRksheQHEKMLIEKME-RDRVNLIAENE 548
Cdd:TIGR00606  959 DIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK----IQERWLQDNLTlRKRENELKEVE 1034
                          170       180       190
                   ....*....|....*....|....*....|...
gi 147902627   549 RVINQKLQEQNAMLTAGFQGKVNALQREIDDLK 581
Cdd:TIGR00606 1035 EELKQHLKEMGQMQVLQMKQEHQKLEENIDLIK 1067
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
500-589 6.91e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 44.73  E-value: 6.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  500 AERQRLvleEKERSLQKSMED---QRKSHEQHEKMLIEKMERDRVNLIaENERVINQKLQEQNAMLTAGFQGKVNALQRE 576
Cdd:PTZ00266  435 AERARI---EKENAHRKALEMkilEKKRIERLEREERERLERERMERI-ERERLERERLERERLERDRLERDRLDRLERE 510
                          90
                  ....*....|...
gi 147902627  577 IDDLKGRNRAAKS 589
Cdd:PTZ00266  511 RVDRLERDRLEKA 523
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
356-587 1.50e-04

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.55  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  356 HMHQESEKEALKvfLKRSFNDENQNFQREFKHLLDGKMKEFSERNE--RESMERCQIIIEELSDPLDQRIS-----QGEF 428
Cdd:COG1196   725 LAALEEELEQLQ--SRLEELEEELEELEEELEELQERLEELEEELEslEEALAKLKEEIEELEEKRQALQEeleelEEEL 802
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  429 LKPGGHMLFLEEKMIIMTVYNTTPYKGLKSL--------EVLQEFMDNKKAIEATILQADESLTAKEKEIAESQAQAEEA 500
Cdd:COG1196   803 EEAERRLDALERELESLEQRRERLEQEIEELeeeieeleEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKEL 882
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  501 ERQRLVLEEKERSLQKSMEDQRkshEQHEKMLIEKMERDRVNLIAENE-RVINQKLQEQN-AMLTAGFQGKVNALQREID 578
Cdd:COG1196   883 EEEKEELEEELRELESELAELK---EEIEKLRERLEELEAKLERLEVElPELEEELEEEYeDTLETELEREIERLEEEIE 959

                  ....*....
gi 147902627  579 DLKGRNRAA 587
Cdd:COG1196   960 ALGPVNLRA 968
 
Name Accession Description Interval E-value
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
46-273 6.64e-60

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650 [Multi-domain]  Cd Length: 224  Bit Score: 200.63  E-value: 6.64e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  46 GKYRTGKSYLMNKLAGSKTGFPLGSTIQSKTKGIWMWCVPHPHQ--PSQTLVLLDTEGLGDVEKGDSKNDAWIFSLAVLL 123
Cdd:cd01851   14 GSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKDTdgKKHAVLLLDTEGTDGRERGEFENDARLFALATLL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627 124 SSNLVYNSMGTIDNHAMEQLHYVTELSklikvksnpVEEEEKNESGEFKRIFPSFTWCVRDFSLILELNGRTVTEdeylm 203
Cdd:cd01851   94 SSVLIYNMWQTILGDDLDKLMGLLKTA---------LETLGLAGLHNFSKPKPLLLFVVRDFTGPTPLEGLDVTE----- 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627 204 nslklkkGTDKKSQDHNLPRECILHFFHSHKCFVFDRPSSTKNLQRLeDLEERDLERAFVEQTQKFCDYI 273
Cdd:cd01851  160 -------KSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN-DGRLKDLPPEFRKALKALRQRF 221
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
20-282 3.77e-120

Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 111185  Cd Length: 264  Bit Score: 359.39  E-value: 3.77e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   20 NEFVINAEAEEILSQITDPVVVVVIVGKYRTGKSYLMNKLAGSKTGFPLGSTIQSKTKGIWMWCVPHPHQPSQTLVLLDT 99
Cdd:pfam02263   2 HQLELNEEALEILSAITQPVVVVAIVGLYRTGKSYLMNFLAGKLTGFSLGSTVESETKGIWMWCVPHPNKPKHTLVLLDT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  100 EGLGDVEKGDSKNDAWIFSLAVLLSSNLVYNSMGTIDNHAMEQLHYVTELSKLIKVKSNPvEEEEKNESGEFKRIFPSFT 179
Cdd:pfam02263  82 EGLGDVEKSDPKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTELIRAKSSP-RYGRVADSAEFVSFFPDFV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  180 WCVRDFSLILELNGRTVTEDEYLMNSLKLKKGTDKKSQDHNLPRECILHFFHSHKCFVFDRPSSTKNLQ-RLEDLEERDL 258
Cdd:pfam02263 161 WTVRDFSLPLELDGGPITGDEYLENRLKLSQGQHEELQNFNLPRECIRSFFPKRKCFLFDRPGLDVALNpQLEGLREDEL 240
                         250       260
                  ....*....|....*....|....
gi 147902627  259 ERAFVEQTQKFCDYIHRQGIVKTL 282
Cdd:pfam02263 241 DPEFQQQLREFCSYIFSESLVKTL 264
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
46-117 6.15e-06

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 45.14  E-value: 6.15e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 147902627  46 GKYRTGKSYLMNKLAGSKtgFPLGSTIQSKTKGIWMWCVPHpHQPSQTLVLLDTEGLGDVEKGDSKNDAWIF 117
Cdd:cd00882    4 GRGGVGKSSLLNALLGGE--VGEVSDVPGTTRDPDVYVKEL-DKGKVKLVLVDTPGLDEFGGLGREELARLL 72
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
460-557 6.22e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922  Cd Length: 140  Bit Score: 36.02  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   460 EVLQEFMDNKKA---IEATILQADESLTAKEKEIaesQAQAEEAERQRLVLEEKERS-LQKSMEDQRKSHEQHEKMLIEK 535
Cdd:smart00935   8 KILQESPAGKAAqkqLEKEFKKRQAELEKLEKEL---QKLKEKLQKDAATLSEAAREkKEKELQKKVQEFQRKQQKLQQD 84
                           90       100
                   ....*....|....*....|..
gi 147902627   536 MERDRVNLIAENERVINQKLQE 557
Cdd:smart00935  85 LQKRQQEELQKILDKINKAIKE 106
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
284-581 5.47e-136

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 202427 [Multi-domain]  Cd Length: 297  Bit Score: 401.28  E-value: 5.47e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  284 GGLLVTGRMLAHLANLYIETIKSGSVPCMENAVLALSVIENTGAIQDALTKYETCMNNQVpRFPTETLEEFLHMHQESEK 363
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKV-KLPTETLQELLDLHRDCEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  364 EALKVFLKRSFNDENQNFQREFKHLLDGKMKEFSERNERESMERCQIIIEELSDPLDQRISQGEFLKPGGHMLFLEEKMI 443
Cdd:pfam02841  80 EAIAVFMKRSFKDENQEFQKELVELLEKKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  444 IMTVYNTTPYKGLKSLEVLQEFMDNKKAIEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRK 523
Cdd:pfam02841 160 LEAKYNQVPRKGVKAEEVLQEFLNSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQER 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 147902627  524 SHEQHEKMLIEKMERDRVNLIAENERVINQKLQEQNAMLTAGFQGKVNALQREIDDLK 581
Cdd:pfam02841 240 SYQEHVKQLIEKMEAEREKLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
RAD50_homologue_ceRAD50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
395-581 1.31e-05

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 46.96  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   395 EFSERNERESMErCQIIIEELSDPLDQRISQGEFLKPgghmlFLEEKMIIMTVYNTTPYKGLKSLEVLQEFMDNK----K 470
Cdd:TIGR00606  885 QFEEQLVELSTE-VQSLIREIKDAKEQDSPLETFLEK-----DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymK 958
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   471 AIEATILQA-DESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRksheQHEKMLIEKME-RDRVNLIAENE 548
Cdd:TIGR00606  959 DIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK----IQERWLQDNLTlRKRENELKEVE 1034
                          170       180       190
                   ....*....|....*....|....*....|...
gi 147902627   549 RVINQKLQEQNAMLTAGFQGKVNALQREIDDLK 581
Cdd:TIGR00606 1035 EELKQHLKEMGQMQVLQMKQEHQKLEENIDLIK 1067
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
500-589 6.91e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 44.73  E-value: 6.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  500 AERQRLvleEKERSLQKSMED---QRKSHEQHEKMLIEKMERDRVNLIaENERVINQKLQEQNAMLTAGFQGKVNALQRE 576
Cdd:PTZ00266  435 AERARI---EKENAHRKALEMkilEKKRIERLEREERERLERERMERI-ERERLERERLERERLERDRLERDRLDRLERE 510
                          90
                  ....*....|...
gi 147902627  577 IDDLKGRNRAAKS 589
Cdd:PTZ00266  511 RVDRLERDRLEKA 523
hypothetical_protein TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
470-585 1.01e-04

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 42.30  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  470 KAIEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDqrksheqhekmlIEKMERDRVNLIAENER 549
Cdd:TIGR04211  69 PELQQELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELER------------IKQISANAIELDEENRE 136
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 147902627  550 vinqkLQEQNAMLTAgfqgKVNALQREIDDLKGRNR 585
Cdd:TIGR04211 137 -----LREELAELKQ----ENEALEAENERLQENEQ 163
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
356-587 1.50e-04

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.55  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  356 HMHQESEKEALKvfLKRSFNDENQNFQREFKHLLDGKMKEFSERNE--RESMERCQIIIEELSDPLDQRIS-----QGEF 428
Cdd:COG1196   725 LAALEEELEQLQ--SRLEELEEELEELEEELEELQERLEELEEELEslEEALAKLKEEIEELEEKRQALQEeleelEEEL 802
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  429 LKPGGHMLFLEEKMIIMTVYNTTPYKGLKSL--------EVLQEFMDNKKAIEATILQADESLTAKEKEIAESQAQAEEA 500
Cdd:COG1196   803 EEAERRLDALERELESLEQRRERLEQEIEELeeeieeleEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKEL 882
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  501 ERQRLVLEEKERSLQKSMEDQRkshEQHEKMLIEKMERDRVNLIAENE-RVINQKLQEQN-AMLTAGFQGKVNALQREID 578
Cdd:COG1196   883 EEEKEELEEELRELESELAELK---EEIEKLRERLEELEAKLERLEVElPELEEELEEEYeDTLETELEREIERLEEEIE 959

                  ....*....
gi 147902627  579 DLKGRNRAA 587
Cdd:COG1196   960 ALGPVNLRA 968
DUF3523 pfam12037
Domain of unknown function (DUF3523); This presumed domain is functionally uncharacterized. ...
454-560 3.38e-04

Domain of unknown function (DUF3523); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 257 to 277 amino acids in length. This domain is found associated with pfam00004. This domain has a conserved LER sequence motif.


Pssm-ID: 256812 [Multi-domain]  Cd Length: 272  Bit Score: 41.30  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  454 KGLKSLEVLQEFMDNKKAIEATILQADESLTAKEKEIAESQAQAEEA--ERQRLVLEEKERSLQKSMEDQRKSHEQHEKM 531
Cdd:pfam12037  32 RGAKALRELESSPHAKKAFELSKLQEKTRQAELEAKIKEYEAQQAQAklERARVESEERRKTLQEQTQQERQRAQYKDEL 111
                          90       100
                  ....*....|....*....|....*....
gi 147902627  532 LIEKMERDRVNLIAENERviNQKLQEQNA 560
Cdd:pfam12037 112 ARKRYQKELEQQRRQNEE--LLKMQEESV 138
COG1322 COG1322
Predicted nuclease of restriction endonuclease-like fold, RmuC family [General function ...
459-581 4.64e-04

Predicted nuclease of restriction endonuclease-like fold, RmuC family [General function prediction only]


Pssm-ID: 224241 [Multi-domain]  Cd Length: 448  Bit Score: 41.61  E-value: 4.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627 459 LEVLQEFMDNKKAIEATILQADESLTAKEKeiAESQAQAEEAERQRLVLEEKERSLQKSMEDQRKSHEQHEKMLIEKMER 538
Cdd:COG1322   69 LELIQELNELKARLQQQLLQSREQLQLLIE--SLAQLSSEFQELANEIFEELNRRLAELNQQNLKQLLKPLREVLEKFRE 146
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 147902627 539 DRVNLIAENERvinqKLQEQNAMLTAGfQGKVNALQREIDDLK 581
Cdd:COG1322  147 QLEQRIHESAE----ERSTLLEEIDRL-LGEIQQLAQEAGNLT 184
Chromosome_partition_protein_Smc TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
462-590 4.82e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 4.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   462 LQEFMDNKKAIEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMED--QRKSH-EQHEKMLIEKMER 538
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaNEISRlEQQKQILRERLAN 313
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   539 DRVNLIAENERVIN--QKLQEQNAMLT------AGFQGKVNALQREIDDLKGRNRAAKSG 590
Cdd:TIGR02168  314 LERQLEELEAQLEEleSKLDELAEELAeleeklEELKEELESLEAELEELEAELEELESR 373
chromosome_segregation_protein_related_ptotein TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
402-583 5.86e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 5.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   402 RESMERCQIIIEELSDPLDQRisQGEFLKpgghmlfLEEkmiimtvynttpYKGLKslEVLQEF-----MDNKKAIEATI 476
Cdd:TIGR02169  183 EENIERLDLIIDEKRQQLERL--RREREK-------AER------------YQALL--KEKREYegyelLKEKEALERQK 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   477 LQADESLTAKEKEIAESQAQ----AEEAERQRLVLEEKERSLQKSMED-----QRKSHEQHEKmlIEKMERDrvnlIAEN 547
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEiselEKRLEEIEQLLEELNKKIKDLGEEeqlrvKEKIGELEAE--IASLERS----IAEK 313
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 147902627   548 ERVInQKLQEQNAMLTAgfqgKVNALQREIDDLKGR 583
Cdd:TIGR02169  314 EREL-EDAEERLAKLEA----EIDKLLAEIEELERE 344
Chromosome_partition_protein_Smc TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
457-589 6.07e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 6.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   457 KSLEVLQEFMDNKKA----IEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRKSHEQHEKML 532
Cdd:TIGR02168  281 EEIEELQKELYALANeisrLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 147902627   533 iEKMERDRVNLiaenerviNQKLQEQNAMLTAgFQGKVNALQREIDDLKGRNRAAKS 589
Cdd:TIGR02168  361 -EELEAELEEL--------ESRLEELEEQLET-LRSKVAQLELQIASLNNEIERLEA 407
Chromosome_partition_protein_Smc TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
457-582 7.08e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 7.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   457 KSLEVLQEfmdNKKAIEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMED---QRKSHEQHEKMLI 533
Cdd:TIGR02168  838 RRLEDLEE---QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEElseELRELESKRSELR 914
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147902627   534 EKME--RDRVNLIAENERVINQKLQEQNAMLTAGFQ--------------GKVNALQREIDDLKG 582
Cdd:TIGR02168  915 RELEelREKLAQLELRLEGLEVRIDNLQERLSEEYSltleeaealenkieDDEEEARRRLKRLEN 979
Nuclease_SbcCD_subunit_C TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
395-578 8.29e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 8.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   395 EFSERNERESMERCQIIIEELsdPLDQ--RISQGEFLKPG---GHMLFLEEKMIIMTVY-NTTPYKGLKSLEVLQEFMDN 468
Cdd:TIGR00618  153 EFAQFLKAKSKEKKELLMNLF--PLDQytQLALMEFAKKKslhGKAELLTLRSQLLTLCtPCMPDTYHERKQVLEKELKH 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   469 KKAIEATILQADESLTaKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRKSHEQHEKMLIEKMERDRVNLIAENE 548
Cdd:TIGR00618  231 LREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQA 309
                          170       180       190
                   ....*....|....*....|....*....|
gi 147902627   549 RVINQKLQEQNAMLTAGFQGKVNALQREID 578
Cdd:TIGR00618  310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSS 339
RNase_Y TIGR03319
ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from ...
460-583 1.01e-03

ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from Bacillus subtilis, YmdA, has been shown to be involved in turnover of yitJ riboswitch. [Transcription, Degradation of RNA]


Pssm-ID: 188306 [Multi-domain]  Cd Length: 514  Bit Score: 40.68  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  460 EVLQEFMDNKKAIEATILQADESLTAKEKEIAESQAQAEEAERQRlvLEEKERSLQKSMEDQRksheqheKMLIEKMERD 539
Cdd:TIGR03319  90 ETLDRKMESLDKKEENLEKKEKELSNKEKNLDEKEEELEELIAEQ--REELERISGLTQEEAK-------EILLEEVEEE 160
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 147902627  540 rvnliAENERVINQKLQEQNAMLTAGFQGK---VNALQR-------EI---------DDLKGR 583
Cdd:TIGR03319 161 -----ARHEAAKLIKEIEEEAKEEADKKAKeilATAIQRyagdhvaETtvsvvnlpnDEMKGR 218
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
395-581 1.54e-03

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.08  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  395 EFSERNERESMERCQIIIEELSDPLD----QRISQGEFLKPGGHMLFLEEKMIimtvynttpykglksLEVLQEFMDNKK 470
Cdd:COG1196   178 ERKLERTEENLERLEDLLEELEKQLEklerQAEKAERYQELKAELRELELALL---------------LAKLKELRKELE 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  471 AIEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRKSHEQHEKMLIEKMER-----DRVNLIA 545
Cdd:COG1196   243 ELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERleeleNELEELE 322
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 147902627  546 ENERVINQKLQEQNAMLTAgFQGKVNALQREIDDLK 581
Cdd:COG1196   323 ERLEELKEKIEALKEELEE-RETLLEELEQLLAELE 357
Chromosome_partition_protein_Smc TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
457-588 1.86e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   457 KSLEVLQEFMDNKKAIEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRKS----HEQHEKML 532
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRledlEEQIEELS 851
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147902627   533 ---------IEKMERDRVNLIAENERVINQKLQEQNAMLTAGFQgkVNALQREIDDLKGRNRAAK 588
Cdd:TIGR02168  852 edieslaaeIEELEELIEELESELEALLNERASLEEALALLRSE--LEELSEELRELESKRSELR 914
chromosome_segregation_protein_related_ptotein TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
472-581 2.28e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   472 IEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRKSHEQHEKMLIEKMERdrvnliaenERVI 551
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE---------LEDL 369
                           90       100       110
                   ....*....|....*....|....*....|
gi 147902627   552 NQKLQEQNAMLTAGFQgKVNALQREIDDLK 581
Cdd:TIGR02169  370 RAELEEVDKEFAETRD-ELKDYREKLEKLK 398
DUF2968 pfam11180
Protein of unknown function (DUF2968); This family of proteins has no known function.
466-591 3.43e-03

Protein of unknown function (DUF2968); This family of proteins has no known function.


Pssm-ID: 256337 [Multi-domain]  Cd Length: 192  Bit Score: 37.79  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  466 MDNKKAIEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQksmEDQRKSHEQHEKMLIEKME--RDRVNL 543
Cdd:pfam11180  83 AARAEAIYRDFARQTAQLADVEIRRAQLEAQKAQLERQIAASEARAERLQ---ADLQLAQAQEQQVAARQQQarQEAVAL 159
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 147902627  544 IAEnerviNQKLQEQnamltagfqgkVNALQREIDDLKGRNRAAKSGP 591
Cdd:pfam11180 160 EAQ-----RQAAQAQ-----------LRKLQRQIRQLQAQQNEPIPHL 191
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit ...
442-558 3.50e-03

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 109486 [Multi-domain]  Cd Length: 132  Bit Score: 36.85  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  442 MIIMTVYNTTPYKglksleVLQEFMDN-KKAIEATILQADESLTAKEKEIAESQAQAEEAERQ-RLVLEEKERSLQKSME 519
Cdd:pfam00430  10 LILVGLLIYFGYK------PLGKILDErKEKIANNIKEAEERLKQAAALLAEAEQQLAQARAEaSEIINNAKKEAQKLKE 83
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 147902627  520 DQRKSHEQHEKMLIEKMERDrvnLIAENERVINQkLQEQ 558
Cdd:pfam00430  84 EILAEAQKDAERLLESARAE---IEQEKEQALAE-LRQQ 118
Chromosome_partition_protein_Smc TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
470-589 3.61e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627   470 KAIEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRKSHEQHEKMlIEKMERDRVNLIAEnER 549
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER-IAQLSKELTELEAE-IE 764
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 147902627   550 VINQKLQEQNAMLTAGFQgKVNALQREIDDLKGRNRAAKS 589
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEA-EIEELEAQIEQLKEELKALRE 803
Hemolysin_secretion_protein_D_plasmid TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
460-589 4.08e-03

type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 130902 [Multi-domain]  Cd Length: 423  Bit Score: 38.45  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  460 EVLQEFMDNKKAIEATILQadesltaKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRKSHEQHEKML--IEKME 537
Cdd:TIGR01843 137 SRKSTLRAQLELILAQIKQ-------LEAELAGLQAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLELEreRAEAQ 209
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 147902627  538 RDRVNLIAENE------RVINQKLQEQNAMLTAGFQGKVNALQREIDDLKGRNRAAKS 589
Cdd:TIGR01843 210 GELGRLEAELEvlkrqiDELQLERQQIEQTFREEVLEELTEAQARLAELRERLNKARD 267
PTZ00121 PTZ00121
MAEBL; Provisional
457-578 4.44e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  457 KSLEVLQEFMDNKKAIEATILQADESLTAKE--KEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRKSHEQHEKmliE 534
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK---D 1752
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 147902627  535 KMERDRV-NLIAENERVINQKLQEQNAMLTAGFQGKVNALQREID 578
Cdd:PTZ00121 1753 EEEKKKIaHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
RNase_Y TIGR03319
ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from ...
476-557 7.40e-03

ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from Bacillus subtilis, YmdA, has been shown to be involved in turnover of yitJ riboswitch. [Transcription, Degradation of RNA]


Pssm-ID: 188306 [Multi-domain]  Cd Length: 514  Bit Score: 37.60  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  476 ILQADESLTaKEKEIAESQAQAEEAERQRL--VLEEKERSLQKSMEDQRK---SHEQHEKMLIEKmERDRVNLIAENERV 550
Cdd:TIGR03319  53 LLEAKEEVH-KLRAELERELKERRNELQRLerRLLQREETLDRKMESLDKkeeNLEKKEKELSNK-EKNLDEKEEELEEL 130

                  ....*..
gi 147902627  551 INQKLQE 557
Cdd:TIGR03319 131 IAEQREE 137
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
467-589 7.47e-03

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 38.16  E-value: 7.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  467 DNKKAIEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERSLQKSMEDQRKSHEQHEKMLIEKmeRDRVNLIAE 546
Cdd:COG1196   369 ALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEEL--QTELEELNE 446
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 147902627  547 NERVINQKLQEQNAMLTAgFQGKVNALQREIDDLKGRNRAAKS 589
Cdd:COG1196   447 ELEELEEQLEELRDRLKE-LERELAELQEELQRLEKELSSLEA 488
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
483-583 8.40e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 258133 [Multi-domain]  Cd Length: 126  Bit Score: 35.29  E-value: 8.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  483 LTAKEKEIAESQ----AQAEEAERQRLVLEEKERSLQKSMEDQRKSHEQHEKMLIE-KMERDRVNLIAENERVINQKLQE 557
Cdd:pfam13863   2 LLEKRREMYEVQlaldAKREEFERREELFKQREEELEEKEEELQEDLVKFDKFLKEnEAKRERAEKKAEEEKKLRKEKEK 81
                          90       100
                  ....*....|....*....|....*.
gi 147902627  558 QNAMLTAgfqgKVNALQREIDDLKGR 583
Cdd:pfam13863  82 EIKELKA----ELEELKAEIQKLEEK 103
PTZ00121 PTZ00121
MAEBL; Provisional
456-588 8.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 8.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902627  456 LKSLEVLQEFMDNKKAIEATILQADESLTAKEKEIAESQAQAEEAERQRLVLEEKERS--LQKSMEDQRKSHEQHEKMLI 533
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAE 1699
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 147902627  534 EKMERDRVNLIAENERVINQKLQEQNAMLtagfQGKVNALQREIDDLKGRNRAAK 588
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEEN----KIKAEEAKKEAEEDKKKAEEAK 1750
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.13
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • 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.
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