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Conserved domains on  [gi|755512962|ref|XP_011247895|]
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guanylate binding protein 8 isoform X5 [Mus musculus]

Protein Classification

guanylate-binding family protein( domain architecture ID 12033579)

guanylate-binding family protein such as guanylate-binding protein 1 (GBP1), which is induced by interferon and hydrolyzes GTP to GMP in 2 consecutive cleavage reactions, is a large GTPase of the dynamin superfamily involved in the regulation of membrane, cytoskeleton, and cell cycle progression dynamics

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 282-576 2.09e-154

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: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 445.58  E-value: 2.09e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  282 EGIKVTGNGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKE 361
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  362 AMAVFMEHSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKI 439
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  440 EHDYWQVPRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKR 519
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755512962  520 NKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 576
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 16-280 9.86e-143

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: 460516  Cd Length: 260  Bit Score: 414.08  E-value: 9.86e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   16 NEHLSVNHEAIEILEKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTELirakSSPNPDGIKNSTEFVSFFPDFV 175
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  176 WTVRDFMLELKLNGEDITSDEYLENALKLIPGYNPRVQASNSARECIRCFFPNRKsCFVFDRPTHDRELLQKLETISEDQ 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRK-CFLFDRPGLKKALNPQFEGLREDE 235

                         250       260
                  ....*....|....*....|....*
gi 755512962  256 LDLKFREETNAFVSYIFNYAKIKTL 280
Cdd:pfam02263 236 LDPEFQQQLREFCSYILSHSLVKTL 260
 
Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 282-576 2.09e-154

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: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 445.58  E-value: 2.09e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  282 EGIKVTGNGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKE 361
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  362 AMAVFMEHSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKI 439
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  440 EHDYWQVPRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKR 519
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755512962  520 NKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 576
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 288-576 4.57e-143

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) 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. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 416.21  E-value: 4.57e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 288 GNGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFM 367
Cdd:cd16269    1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 368 EHSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQ 445
Cdd:cd16269   81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 446 VPRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIE 525
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755512962 526 QLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 576
Cdd:cd16269  241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 16-280 9.86e-143

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: 460516  Cd Length: 260  Bit Score: 414.08  E-value: 9.86e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   16 NEHLSVNHEAIEILEKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTELirakSSPNPDGIKNSTEFVSFFPDFV 175
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  176 WTVRDFMLELKLNGEDITSDEYLENALKLIPGYNPRVQASNSARECIRCFFPNRKsCFVFDRPTHDRELLQKLETISEDQ 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRK-CFLFDRPGLKKALNPQFEGLREDE 235

                         250       260
                  ....*....|....*....|....*
gi 755512962  256 LDLKFREETNAFVSYIFNYAKIKTL 280
Cdd:pfam02263 236 LDPEFQQQLREFCSYILSHSLVKTL 260
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 30-272 4.08e-70

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  Cd Length: 224  Bit Score: 226.05  E-value: 4.08e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  30 EKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCMPHP--TKPEHTLVLLDTEGLGDVEKGDP 107
Cdd:cd01851    1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 108 KNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTElirakSSPNPDGIKNsteFVSFFPDFVWTVRDFMLELKL 187
Cdd:cd01851   81 ENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 188 NGEDITSDEYlenalKLIPGYnprvqasNSARECIRCFFPNRKsCFVFDRPTHDRELLQKleTISEDQLDLKFREETNAF 267
Cdd:cd01851  153 EGLDVTEKSE-----TLIEEL-------NKIWSSIRKPFTPIT-CFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKAL 217


                 ....*
gi 755512962 268 VSYIF 272
Cdd:cd01851  218 RQRFF 222
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 486-586 2.83e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.89  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 486 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENiEQLRRKLEQEREQLIKdhnmmvEKKLKEQKALLEEGFKKKA 565
Cdd:PRK09510  77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALK------QKQAEEAAAKAAAAAKAKA 149

                         90       100
                 ....*....|....*....|.
gi 755512962 566 EEMDGEIQQLKHNIEDMKKKQ 586
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKK 170
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 454-586 2.22e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.07  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 454 REVFQSFLQSQAIiESSILQADTALTAGQKAIAEERTKKEAAEKEqdllRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQ 533
Cdd:COG1579    3 PEDLRALLDLQEL-DSELDRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELEIEEVEARIKK 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755512962 534 EREQLikdhnMMVeKKLKEQKALLEE--GFKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:COG1579   78 YEEQL-----GNV-RNNKEYEALQKEieSLKRRISDLEDEILELMERIEELEEEL 126
YeeP COG3596
Predicted GTPase [General function prediction only];
1-108 3.91e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 45.91  E-value: 3.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   1 MTQPQMAPICLVENHNEHLSVNHEAI-EILE--KISQPVVVVAIVGLYRTGKSYLMNRLAGQN-----HGFPlgstvqsQ 72
Cdd:COG3596    1 MSTEVSSLTERLEALKRLPQVLRELLaEALErlLVELPPPVIALVGKTGAGKSSLINALFGAEvaevgVGRP-------C 73

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755512962  73 TKGIwmWCMPHPTKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:COG3596   74 TREI--QRYRLESDGLPGLVLLDTPGLGEVNERDRE 107
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 442-586 2.77e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  442 DYWQVPRKGVKAREVFQSFLQSQAIIESSI----LQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQE 517
Cdd:TIGR02794  23 LYHSVKPEPGGGAEIIQAVLVDPGAVAQQAnriqQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEK 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755512962  518 KrnKENIEQLRRKLEQEREQLIKdhnmMVEKKLKEQKALLEEGFKKKAEEM---DGEIQQLKHNIEDMKKKQ 586
Cdd:TIGR02794 103 A--AKQAEQAAKQAEEKQKQAEE----AKAKQAAEAKAKAEAEAERKAKEEaakQAEEEAKAKAAAEAKKKA 168
 
Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 282-576 2.09e-154

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: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 445.58  E-value: 2.09e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  282 EGIKVTGNGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKE 361
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  362 AMAVFMEHSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKI 439
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  440 EHDYWQVPRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKR 519
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755512962  520 NKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 576
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 288-576 4.57e-143

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) 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. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 416.21  E-value: 4.57e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 288 GNGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFM 367
Cdd:cd16269    1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 368 EHSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQ 445
Cdd:cd16269   81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 446 VPRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIE 525
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755512962 526 QLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 576
Cdd:cd16269  241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 16-280 9.86e-143

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: 460516  Cd Length: 260  Bit Score: 414.08  E-value: 9.86e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   16 NEHLSVNHEAIEILEKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTELirakSSPNPDGIKNSTEFVSFFPDFV 175
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  176 WTVRDFMLELKLNGEDITSDEYLENALKLIPGYNPRVQASNSARECIRCFFPNRKsCFVFDRPTHDRELLQKLETISEDQ 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRK-CFLFDRPGLKKALNPQFEGLREDE 235

                         250       260
                  ....*....|....*....|....*
gi 755512962  256 LDLKFREETNAFVSYIFNYAKIKTL 280
Cdd:pfam02263 236 LDPEFQQQLREFCSYILSHSLVKTL 260
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 30-272 4.08e-70

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  Cd Length: 224  Bit Score: 226.05  E-value: 4.08e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  30 EKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCMPHP--TKPEHTLVLLDTEGLGDVEKGDP 107
Cdd:cd01851    1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 108 KNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTElirakSSPNPDGIKNsteFVSFFPDFVWTVRDFMLELKL 187
Cdd:cd01851   81 ENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 188 NGEDITSDEYlenalKLIPGYnprvqasNSARECIRCFFPNRKsCFVFDRPTHDRELLQKleTISEDQLDLKFREETNAF 267
Cdd:cd01851  153 EGLDVTEKSE-----TLIEEL-------NKIWSSIRKPFTPIT-CFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKAL 217


                 ....*
gi 755512962 268 VSYIF 272
Cdd:cd01851  218 RQRFF 222
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 40-115 1.51e-08

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: 54.38  E-value: 1.51e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755512962  40 AIVGLYRTGKSYLMNRLAGQNHGFPlgSTVQSQTKGIWMWCMPHPtKPEHTLVLLDTEGLGDVEKGDPKNDLWIFA 115
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEV--SDVPGTTRDPDVYVKELD-KGKVKLVLVDTPGLDEFGGLGREELARLLL 73
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 488-584 1.85e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 54.36  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  488 ERTKKEAAEKEQDL--LRQKQKEQ--QEYMEAQEKRNKENIEQLRRK-----LEQEREQLIKDHN--MMVEKKLKE-QKA 555
Cdd:pfam17380 449 ERVRLEEQERQQQVerLRQQEEERkrKKLELEKEKRDRKRAEEQRRKilekeLEERKQAMIEEERkrKLLEKEMEErQKA 528

                          90       100       110
                  ....*....|....*....|....*....|..
gi 755512962  556 LLEEGFKKKAEE---MDGEIQQLKHNIEDMKK 584
Cdd:pfam17380 529 IYEEERRREAEEerrKQQEMEERRRIQEQMRK 560
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 486-586 2.83e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.89  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 486 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENiEQLRRKLEQEREQLIKdhnmmvEKKLKEQKALLEEGFKKKA 565
Cdd:PRK09510  77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALK------QKQAEEAAAKAAAAAKAKA 149

                         90       100
                 ....*....|....*....|.
gi 755512962 566 EEMDGEIQQLKHNIEDMKKKQ 586
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKK 170
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 310-580 2.10e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 50.99  E-value: 2.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   310 VDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVE-LIGE 388
Cdd:pfam12128  453 LNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqLFPQ 532

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   389 AKVLFLLKNEEASD------KYCQEELdRLSKDLMDNISTFSVPGGHRLY---MDMrEKIEHDYW-----QVPRKGVKAR 454
Cdd:pfam12128  533 AGTLLHFLRKEAPDweqsigKVISPEL-LHRTDLDPEVWDGSVGGELNLYgvkLDL-KRIDVPEWaaseeELRERLDKAE 610

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   455 EVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQE 534
Cdd:pfam12128  611 EALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ 690

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 755512962   535 REQLIKDHNMMVE---KKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIE 580
Cdd:pfam12128  691 LKQLDKKHQAWLEeqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIA 739
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 487-574 5.27e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 46.57  E-value: 5.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  487 EERTKKEAAEKEQDLLRQKQKEQQEYMEaQEKRNKENIEQLRRKLEQEREQLikdhnMMVEKKLKEQKALLEEGFKKKAE 566
Cdd:pfam05672   9 AEEAARILAEKRRQAREQREREEQERLE-KEEEERLRKEELRRRAEEERARR-----EEEARRLEEERRREEEERQRKAE 82


                  ....*...
gi 755512962  567 EMDGEIQQ 574
Cdd:pfam05672  83 EEAEEREQ 90
PTZ00121 PTZ00121
MAEBL; Provisional
 452-585 6.36e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 6.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  452 KAREVFQSFLQSQAIIESSILQAD--------TALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRnkeN 523
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEelkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK---K 1703

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755512962  524 IEQLRRKLEQER---EQLIKDHNmmvEKKLK-EQKALLEEGFKKKAEEM---DGEIQQLKHNIEDMKKK 585
Cdd:PTZ00121 1704 AEELKKKEAEEKkkaEELKKAEE---ENKIKaEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLKKEEEKK 1769
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 484-585 6.36e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.65  E-value: 6.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 484 AIAEE-----RTKKEAAEKEQdlLRQKQKEQQeymeAQEKRNKENIEQLR-RKLEQEREQLIKdhnmmvEKKLKEQKALL 557
Cdd:PRK09510  59 AVVEQynrqqQQQKSAKRAEE--QRKKKEQQQ----AEELQQKQAAEQERlKQLEKERLAAQE------QKKQAEEAAKQ 126

                         90       100
                 ....*....|....*....|....*...
gi 755512962 558 EEGFKKKAEEmdgeiqQLKHNIEDMKKK 585
Cdd:PRK09510 127 AALKQKQAEE------AAAKAAAAAKAK 148
PTZ00121 PTZ00121
MAEBL; Provisional
 451-586 1.25e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  451 VKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKEniEQLRRK 530
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA--EALKKE 1697

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755512962  531 LEQER--EQLIKDHNMmvEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:PTZ00121 1698 AEEAKkaEELKKKEAE--EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
PRK12704 PRK12704
phosphodiesterase; Provisional
 492-586 1.45e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.85  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 492 KEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMvEKKLKEQKALLE---EGFKKKAEEM 568
Cdd:PRK12704  34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKL-EKRLLQKEENLDrklELLEKREEEL 112

                         90
                 ....*....|....*...
gi 755512962 569 DGEIQQLKHNIEDMKKKQ 586
Cdd:PRK12704 113 EKKEKELEQKQQELEKKE 130
PTZ00121 PTZ00121
MAEBL; Provisional
 483-585 1.80e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  483 KAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEK-RNKENIEQLRRKLEQEReqliKDHNMmveKKLKEQKALLEEgF 561
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAK----KAEEA---KKKAEEAKKADE-A 1475

                          90       100
                  ....*....|....*....|....
gi 755512962  562 KKKAEEMDgEIQQLKHNIEDMKKK 585
Cdd:PTZ00121 1476 KKKAEEAK-KADEAKKKAEEAKKK 1498
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 454-586 2.22e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.07  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 454 REVFQSFLQSQAIiESSILQADTALTAGQKAIAEERTKKEAAEKEqdllRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQ 533
Cdd:COG1579    3 PEDLRALLDLQEL-DSELDRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELEIEEVEARIKK 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755512962 534 EREQLikdhnMMVeKKLKEQKALLEE--GFKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:COG1579   78 YEEQL-----GNV-RNNKEYEALQKEieSLKRRISDLEDEILELMERIEELEEEL 126
PTZ00121 PTZ00121
MAEBL; Provisional
 436-586 2.50e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  436 REKIEHDYWQVPRKGVKAREVFQSFLQSQAII--ESSILQADTALTAGQKAIAEERTKKEAAEKEQdLLRQKQKEQQEYM 513
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK-VEQLKKKEAEEKK 1647

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755512962  514 EAQEKRNKENIEQLRRKLEQEREQlikdhnmmvEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAE---------EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
PTZ00121 PTZ00121
MAEBL; Provisional
 482-581 3.02e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  482 QKAIAEERTKKEAAEKEQ-DLLRQKQKEQQ---EYMEAQEKRNKENIEQLRRKLEQER----------------EQLIKD 541
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKaEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAEEDKkkaeeakkdeeekkkiAHLKKE 1765

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 755512962  542 HNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIED 581
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
YeeP COG3596
Predicted GTPase [General function prediction only];
1-108 3.91e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 45.91  E-value: 3.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   1 MTQPQMAPICLVENHNEHLSVNHEAI-EILE--KISQPVVVVAIVGLYRTGKSYLMNRLAGQN-----HGFPlgstvqsQ 72
Cdd:COG3596    1 MSTEVSSLTERLEALKRLPQVLRELLaEALErlLVELPPPVIALVGKTGAGKSSLINALFGAEvaevgVGRP-------C 73

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755512962  73 TKGIwmWCMPHPTKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:COG3596   74 TREI--QRYRLESDGLPGLVLLDTPGLGEVNERDRE 107
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 464-586 4.67e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 464 QAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEymEAQEKRNKENIEQLRRKLEQEREQLIKDHN 543
Cdd:COG1196  354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ--LEELEEAEEALLERLERLEEELEELEEALA 431

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755512962 544 MMVEKKLKEQKALLEEgfKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:COG1196  432 ELEEEEEEEEEALEEA--AEEEAELEEEEEALLELLAELLEEA 472
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 465-585 7.09e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 465 AIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKE-QQEYMEAQEK---------RNKENIEQLRRKLEQE 534
Cdd:COG3883    5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEElNEEYNELQAElealqaeidKLQAEIAEAEAEIEER 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 535 REQL--------------------------------------IKDHNMMVEKKLKEQKALLEEgFKKKAEEMDGEIQQLK 576
Cdd:COG3883   85 REELgeraralyrsggsvsyldvllgsesfsdfldrlsalskIADADADLLEELKADKAELEA-KKAELEAKLAELEALK 163


                 ....*....
gi 755512962 577 HNIEDMKKK 585
Cdd:COG3883  164 AELEAAKAE 172
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 482-588 1.06e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.50  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  482 QKAIAEERTK---KEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREqliKDHNMMVEKKLKEQKALLE 558
Cdd:pfam17380 486 RKRAEEQRRKileKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERR---KQQEMEERRRIQEQMRKAT 562

                          90       100       110
                  ....*....|....*....|....*....|
gi 755512962  559 EGfKKKAEEMDGEIQQLKHNIEDMKKKQWF 588
Cdd:pfam17380 563 EE-RSRLEAMEREREMMRQIVESEKARAEY 591
PTZ00121 PTZ00121
MAEBL; Provisional
 473-585 1.14e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  473 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYME-----AQEKRNKENIEQLRRKLEQEREQLIKDHNMMVE 547
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaakkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 755512962  548 KKLKEQKALLEEgFKKKAEEMDgEIQQLKHNIEDMKKK 585
Cdd:PTZ00121 1371 KKKEEAKKKADA-AKKKAEEKK-KADEAKKKAEEDKKK 1406
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 476-571 1.17e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 45.07  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 476 TALTAGQKAIAEERTKKEAAEKEQDL--------LRQKQ---KEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNM 544
Cdd:COG0542  411 EELDELERRLEQLEIEKEALKKEQDEasferlaeLRDELaelEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490

                         90       100
                 ....*....|....*....|....*..
gi 755512962 545 mvEKKLKEQKALLEEGFKKKAEEMDGE 571
Cdd:COG0542  491 --EKELAELEEELAELAPLLREEVTEE 515
PTZ00121 PTZ00121
MAEBL; Provisional
 473-585 1.28e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  473 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMM-VEKKLK 551
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkAEEAKK 1614

                          90       100       110
                  ....*....|....*....|....*....|....
gi 755512962  552 EQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKK 585
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
PTZ00121 PTZ00121
MAEBL; Provisional
 480-586 1.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  480 AGQKAIAEERTKK-EAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNmmVEKKLKEQKALLE 558
Cdd:PTZ00121 1311 AEEAKKADEAKKKaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE--AKKKADAAKKKAE 1388

                          90       100
                  ....*....|....*....|....*...
gi 755512962  559 EgfKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:PTZ00121 1389 E--KKKADEAKKKAEEDKKKADELKKAA 1414
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 497-585 1.68e-04

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 41.40  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  497 KEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKleqerEQLIKDHNMMVEKKLKEQKALLEEGFKKKAEE------MDG 570
Cdd:pfam13863   6 REMFLVQLALDAKREEIERLEELLKQREEELEKK-----EQELKEDLIKFDKFLKENDAKRRRALKKAEEEtklkkeKEK 80

                          90
                  ....*....|....*
gi 755512962  571 EIQQLKHNIEDMKKK 585
Cdd:pfam13863  81 EIKKLTAQIEELKSE 95
PRK12704 PRK12704
phosphodiesterase; Provisional
 462-568 2.11e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 462 QSQAIIESSILQADT----ALTAGQKAIAEERTK--KEAAEKEQDLLRQKQKEQQEymEAQEKRNKENIEQLRRKLEQER 535
Cdd:PRK12704  39 EAKRILEEAKKEAEAikkeALLEAKEEIHKLRNEfeKELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKKE 116

                         90       100       110
                 ....*....|....*....|....*....|...
gi 755512962 536 EQLIKDhnmmvEKKLKEQKALLEEGFKKKAEEM 568
Cdd:PRK12704 117 KELEQK-----QQELEKKEEELEELIEEQLQEL 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 448-582 2.23e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 448 RKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQL 527
Cdd:COG1196  645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755512962 528 RRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDM 582
Cdd:COG1196  725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 442-586 2.77e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  442 DYWQVPRKGVKAREVFQSFLQSQAIIESSI----LQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQE 517
Cdd:TIGR02794  23 LYHSVKPEPGGGAEIIQAVLVDPGAVAQQAnriqQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEK 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755512962  518 KrnKENIEQLRRKLEQEREQLIKdhnmMVEKKLKEQKALLEEGFKKKAEEM---DGEIQQLKHNIEDMKKKQ 586
Cdd:TIGR02794 103 A--AKQAEQAAKQAEEKQKQAEE----AKAKQAAEAKAKAEAEAERKAKEEaakQAEEEAKAKAAAEAKKKA 168
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 477-559 3.58e-04

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 41.24  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  477 ALTAGQKAIAE-----ERTKKEAA---EKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEK 548
Cdd:TIGR01144  23 AIETRQKKIADglasaERAKKEAAlaqKKAQVILKEAKDEAQEIIENANKRGSEILEEAKAEAREEREKIKAQARAEIEA 102

                          90
                  ....*....|..
gi 755512962  549 KLKE-QKALLEE 559
Cdd:TIGR01144 103 EKEQaREELRKQ 114
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 487-569 3.98e-04

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 41.85  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 487 EERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKK-LKEQKALLEEGFKKKA 565
Cdd:COG1390   12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKElLEAKEELIEEVFEEAL 91


                 ....
gi 755512962 566 EEMD 569
Cdd:COG1390   92 EKLK 95
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 457-574 4.25e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 4.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 457 FQSFLQSQAIIeSSILQADTALTAGQKA-IAEERTKKEAAEKEQDLLRQKQKE---QQEYMEAQEKRNKENIEQLRRKLE 532
Cdd:COG3883  114 FSDFLDRLSAL-SKIADADADLLEELKAdKAELEAKKAELEAKLAELEALKAEleaAKAELEAQQAEQEALLAQLSAEEA 192

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755512962 533 QEREQLikdHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQ 574
Cdd:COG3883  193 AAEAQL---AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 482-567 5.23e-04

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 41.21  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  482 QKAIAEERTKKEAAEKEQDllRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLK-EQKALLEEG 560
Cdd:pfam11600  43 EEAKAEKERAKEEARRKKE--EEKELKEKERREKKEKDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKeEEKRLKEEE 120


                  ....*..
gi 755512962  561 FKKKAEE 567
Cdd:pfam11600 121 KRIKAEK 127
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 468-585 5.34e-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: 43.12  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   468 ESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQK---QKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNM 544
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 755512962   545 MVEKK-----LKEQKALLE---EGFKKKAEEMDGEIQQLKHNIEDMKKK 585
Cdd:TIGR02168  332 LDELAeelaeLEEKLEELKeelESLEAELEELEAELEELESRLEELEEQ 380
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 494-586 5.43e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.49  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 494 AAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLikdhnmmvekKLKEQKALLEEGFKKKAEEMDGEIQ 573
Cdd:PRK09510  59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERL----------KQLEKERLAAQEQKKQAEEAAKQAA 128

                         90
                 ....*....|...
gi 755512962 574 QLKHNIEDMKKKQ 586
Cdd:PRK09510 129 LKQKQAEEAAAKA 141
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 468-584 5.54e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 42.82  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  468 ESSILQADTALTAGQKAIAEERTKKEA--------AEKEQDLLRQKQKEQQEY-MEAQEKRNKENIE--------QLRRK 530
Cdd:pfam09731 286 NSLIAHAHREIDQLSKKLAELKKREEKhieralekQKEELDKLAEELSARLEEvRAADEAQLRLEFErereeireSYEEK 365

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755512962  531 LEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKK-----AEEMDGEIQQL---KHNIEDMKK 584
Cdd:pfam09731 366 LRTELERQAEAHEEHLKDVLVEQEIELQREFLQDikekvEEERAGRLLKLnelLANLKGLEK 427
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
464-586 5.87e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 41.73  E-value: 5.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 464 QAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEY-MEAQEKRNkeniEQLRRKLEQEREQLikdh 542
Cdd:COG1842   25 EKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKaRLALEKGR----EDLAREALERKAEL---- 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 755512962 543 nmmvEKKLKEQKALLEEgFKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:COG1842   97 ----EAQAEALEAQLAQ-LEEQVEKLKEALRQLESKLEELKAKK 135
PTZ00121 PTZ00121
MAEBL; Provisional
 473-585 6.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  473 QADTALTAGQKAIAEERtKKEAAEKEQDLLRQKQKEQQEYMEAQEK--RNKENIEQLRRKLEQEREQLIKDHNMMVEKKL 550
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEK-KKEEAKKKADAAKKKAEEKKKADEAKKKaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKA 1433

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755512962  551 KEQKALLEEgfKKKAEEMDGEIQQlKHNIEDMKKK 585
Cdd:PTZ00121 1434 DEAKKKAEE--AKKADEAKKKAEE-AKKAEEAKKK 1465
PTZ00121 PTZ00121
MAEBL; Provisional
 483-585 6.80e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  483 KAIAEERTKK-EAAEKEQDLLRQKQKEQQEYMEAQEKRN---KENIEQLRRKLEQERE-QLIKDHNMMVEKKLKEQKALL 557
Cdd:PTZ00121 1335 KKKAEEAKKAaEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAA 1414

                          90       100
                  ....*....|....*....|....*...
gi 755512962  558 EEgfKKKAEEMDGEIQQLKhNIEDMKKK 585
Cdd:PTZ00121 1415 AA--KKKADEAKKKAEEKK-KADEAKKK 1439
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 482-566 8.37e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 41.75  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  482 QKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKEN-------IEQLRRKLEQEREQLIKDHNmmvEKKLKEQK 554
Cdd:TIGR02794  96 QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEaeaerkaKEEAAKQAEEEAKAKAAAEA---KKKAEEAK 172

                          90
                  ....*....|..
gi 755512962  555 ALLEEGFKKKAE 566
Cdd:TIGR02794 173 KKAEAEAKAKAE 184
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 453-586 9.76e-04

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 42.34  E-value: 9.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  453 AREVFQsfLQSQAII---ESSILQADTAltagqkaiaeertkKEAAEKEQDLLR-QKQKEQQEYMEAQEKRNK--ENIEQ 526
Cdd:pfam10168 530 PQECLQ--LLSRATQvfrEEYLKKHDLA--------------REEIQKRVKLLKlQKEQQLQELQSLEEERKSlsERAEK 593

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755512962  527 LRRKLE--QEREQLI--KDHNMMveKKLKEQKALL---EEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:pfam10168 594 LAEKYEeiKDKQEKLmrRCKKVL--QRLNSQLPVLsdaEREMKKELETINEQLKHLANAIKQAKKKM 658
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
 488-580 1.04e-03

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 41.44  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  488 ERTKKEAAEKEQDLLRQKQKEQQEYME--AQEKRNKEniEQLRRK-----LEQEREQLikdhnMMVEKK---LKEQKALL 557
Cdd:pfam15991   5 KMSEQMWRALKRHIMRERERKKQEQEAkmEEERLRRE--REEREKedrmtLEETKEQI-----LKLEKKladLKEEKHQL 77

                          90       100
                  ....*....|....*....|...
gi 755512962  558 EEGFKKKAEEMDGEIQQLKHNIE 580
Cdd:pfam15991  78 FLQLKKVLHEDETRKRQLKEQSE 100
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 482-586 1.08e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 482 QKAIAEERTKKEAAEKE--QDLLRQKQKEQQEYMEAQEKRNKENIEQlrrklEQEREQLIKDHNMMVEKKLKEQKALLEE 559
Cdd:PRK09510  85 EQQQAEELQQKQAAEQErlKQLEKERLAAQEQKKQAEEAAKQAALKQ-----KQAEEAAAKAAAAAKAKAEAEAKRAAAA 159

                         90       100
                 ....*....|....*....|....*..
gi 755512962 560 gfKKKAEEmdgEIQqlKHNIEDMKKKQ 586
Cdd:PRK09510 160 --AKKAAA---EAK--KKAEAEAAKKA 179
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 374-586 1.21e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  374 ENQqFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNistfsvpgghrlyMDMREKIEhdywqvprKGVKA 453
Cdd:pfam17380 267 ENE-FLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE-------------VERRRKLE--------EAEKA 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  454 RevfQSFLQSQAIIessilQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQ---------KEQQEYMEAQEK--RNKE 522
Cdd:pfam17380 325 R---QAEMDRQAAI-----YAEQERMAMERERELERIRQEERKRELERIRQEEiameisrmrELERLQMERQQKneRVRQ 396

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755512962  523 NIEQLRRK--LEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLKhnIEDMKKKQ 586
Cdd:pfam17380 397 ELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR--LEEQERQQ 460
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 473-574 1.25e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.53  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  473 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQ---EYMEAQEKRNKENIeQLRRKLEQEREQLIKDHNMMVEKK 549
Cdd:pfam05262 221 ELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKnlpKPADTSSPKEDKQV-AENQKREIEKAQIEIKKNDEEALK 299

                          90       100
                  ....*....|....*....|....*
gi 755512962  550 LKEQKAlleEGFKKKAEEMDGEIQQ 574
Cdd:pfam05262 300 AKDHKA---FDLKQESKASEKEAED 321
PTZ00121 PTZ00121
MAEBL; Provisional
 480-584 1.29e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  480 AGQKAIAEErTKKEAAEKEQ-DLLRQKQKEQQEYMEAQEK-RNKENIEQLRRKLEQEREQlikdhnmmVEKKLKEQKALL 557
Cdd:PTZ00121 1414 AAAKKKADE-AKKKAEEKKKaDEAKKKAEEAKKADEAKKKaEEAKKAEEAKKKAEEAKKA--------DEAKKKAEEAKK 1484

                          90       100
                  ....*....|....*....|....*..
gi 755512962  558 EEGFKKKAEEMDGEIQQLKHNIEDMKK 584
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKADEAKKAAEAKKK 1511
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 489-586 1.33e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   489 RTKKEAAEKEQDLLRQKQK--------------EQQEYMEAQEKRNKENIEQLRRKLEQ------EREQLIKDHNMMVEK 548
Cdd:TIGR02169  204 RREREKAERYQALLKEKREyegyellkekealeRQKEAIERQLASLEEELEKLTEEISElekrleEIEQLLEELNKKIKD 283

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 755512962   549 KLKEQKAlleeGFKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:TIGR02169  284 LGEEEQL----RVKEKIGELEAEIASLERSIAEKEREL 317
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 486-564 1.34e-03

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 39.25  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  486 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRN---KENIEQLRRKLEQEREQLIKDHNMMVEkKLKEQKALLEEGFK 562
Cdd:pfam00836  54 AEERRKSLEAQKLKQLAEKREKEEEALQKADEENNnfsKMAEEKLKQKMEAYKENREAQIAALKE-KLKEKEKHVEEVRK 132


                  ..
gi 755512962  563 KK 564
Cdd:pfam00836 133 NK 134
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 487-586 1.42e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 39.65  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  487 EERTKKEAAEKEQDLLRQ----KQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKeqkalLEEGFK 562
Cdd:pfam15346  25 EEELEKRKDEIEAEVERRveeaRKIMEKQVLEELEREREAELEEERRKEEEERKKREELERILEENNRK-----IEEAQR 99

                          90       100
                  ....*....|....*....|....*..
gi 755512962  563 KKAEE---MDGEIQQLKHNIEDMKKKQ 586
Cdd:pfam15346 100 KEAEErlaMLEEQRRMKEERQRREKEE 126
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 482-586 1.42e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  482 QKAIAEERTKKEA----------AEKEQDLLRQKQKEQQEYMEAQEKRNKENIE--QLRRKLEQEREQLIKDHNMMVEKK 549
Cdd:pfam13868  88 KRQEEYEEKLQEReqmdeiveriQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEwkELEKEEEREEDERILEYLKEKAER 167

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 755512962  550 LKEQKALLEEgfkkKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:pfam13868 168 EEEREAEREE----IEEEKEREIARLRAQQEKAQDEK 200
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 466-586 1.65e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 466 IIESSILQAdtaLTAGQKAIAEERTKKEAAEKEQDLLRQKQkEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMM 545
Cdd:PRK00409 521 LIASLEELE---RELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 755512962 546 VEKKLKEQKAlleegfkKKAEEMdgeIQQLKHNIEDMKKKQ 586
Cdd:PRK00409 597 QKGGYASVKA-------HELIEA---RKRLNKANEKKEKKK 627
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 477-575 1.71e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.39  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 477 ALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEymEAQEKRnKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKAL 556
Cdd:COG0711   28 ALDERQEKIADGLAEAERAKEEAEAALAEYEEKLA--EARAEA-AEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAE 104

                         90
                 ....*....|....*....
gi 755512962 557 LEEGFKKKAEEMDGEIQQL 575
Cdd:COG0711  105 IEQERAKALAELRAEVADL 123
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 456-559 1.77e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 456 VFQSFLQSQAiieSSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKEnIEQLRRKLEQER 535
Cdd:COG4942   10 LLALAAAAQA---DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAEL 85

                         90       100
                 ....*....|....*....|....
gi 755512962 536 EQLIKDHNMMvEKKLKEQKALLEE 559
Cdd:COG4942   86 AELEKEIAEL-RAELEAQKEELAE 108
PTZ00121 PTZ00121
MAEBL; Provisional
 486-585 1.92e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  486 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKA 565
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA 1324

                          90       100
                  ....*....|....*....|
gi 755512962  566 EEMDGEIQQLKHNIEDMKKK 585
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKA 1344
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 482-567 1.95e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.09  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  482 QKAIAEERTKKEAAE---KEQDLLRQKQKEQQEYMEAQEKRNKENIEQL----RRKLEQEREQLIKdhnMMVEKKLKEQK 554
Cdd:pfam15709 413 QLQAAQERARQQQEEfrrKLQELQRKKQQEEAERAEAEKQRQKELEMQLaeeqKRLMEMAEEERLE---YQRQKQEAEEK 489

                          90
                  ....*....|....
gi 755512962  555 ALLE-EGFKKKAEE 567
Cdd:pfam15709 490 ARLEaEERRQKEEE 503
PTZ00121 PTZ00121
MAEBL; Provisional
 473-585 2.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  473 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRN--KENIEQLRRKLEQEREQLIKDHNMMVEKKL 550
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAaaKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755512962  551 KEQKALLEEgfKKKAEEMDGEIQQlKHNIEDMKKK 585
Cdd:PTZ00121 1447 DEAKKKAEE--AKKAEEAKKKAEE-AKKADEAKKK 1478
DUF4175 pfam13779
Domain of unknown function (DUF4175);
473-575 2.19e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 41.13  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  473 QADTALTAGQKAIAE--ERTkkeAAEKE-QDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKD--HNMMve 547
Cdd:pfam13779 486 DAERRLRAAQERLSEalERG---ASDEEiAKLMQELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTQQdlQRML-- 560

                          90       100
                  ....*....|....*....|....*...
gi 755512962  548 KKLKEqkaLLEEGFKKKAEEMDGEIQQL 575
Cdd:pfam13779 561 DRIEE---LARSGRRAEAQQMLSQLQQM 585
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 488-586 2.23e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  488 ERTKKEAAEKEQDLL---RQKQ--KEQQEYMEAQEKRNKENIEQLR-RKLEQEREqlIKDhnmmVEKKLKEQKALLE-EG 560
Cdd:TIGR04523 485 EQKQKELKSKEKELKklnEEKKelEEKVKDLTKKISSLKEKIEKLEsEKKEKESK--ISD----LEDELNKDDFELKkEN 558

                          90       100
                  ....*....|....*....|....*.
gi 755512962  561 FKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQ 584
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 472-585 2.53e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  472 LQADTALTAGQKAIAEERTKKEAAEKEQD-LLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNmmvEKKL 550
Cdd:pfam13868 231 ARQRQELQQAREEQIELKERRLAEEAEREeEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEERE---EQRA 307

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755512962  551 KEQKALLEEGFKKKAEEmdgeiQQLKHNIEDMKKK 585
Cdd:pfam13868 308 AEREEELEEGERLREEE-----AERRERIEEERQK 337
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 468-586 2.59e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 468 ESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEyMEAQEKRNKENIEQLRRKLE--QEREQLIKDHNMM 545
Cdd:COG1196  221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEeaQAEEYELLAELAR 299

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 755512962 546 VEKKLKEQKALLEEgFKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:COG1196  300 LEQDIARLEERRRE-LEERLEELEEELAELEEELEELEEEL 339
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
 483-598 2.96e-03

Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.


Pssm-ID: 464893 [Multi-domain]  Cd Length: 1048  Bit Score: 40.70  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   483 KAIAEERTKKEaaEKEQDL---------LRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQ 553
Cdd:pfam15818  239 KKINEEITHIQ--EEKQDIiisfqhmqqLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHE 316

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 755512962   554 KALleEGFKKKAEEMDGEIQQLKHNIEDMKKKQwFHFRYYYKRSC 598
Cdd:pfam15818  317 KAL--GTWKKHVEELNGEINEIKNELSSLKETH-IKLQEHYNKLC 358
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 447-563 3.04e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 447 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLR---QKQKEQQEYMEAQEKRNKEN 523
Cdd:COG4942  131 FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERaalEALKAERQKLLARLEKELAE 210

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 755512962 524 IEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKK 563
Cdd:COG4942  211 LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
PTZ00121 PTZ00121
MAEBL; Provisional
 480-586 3.09e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  480 AGQKAIAEERTKKEAAEKEQDLLR-QKQKEQQEYMEAQEKRNKENI---EQLR-----RKLEQEREQLiKDHNMMV---- 546
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELkkaEELKkaeekKKAEEAKKAE-EDKNMALrkae 1584

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 755512962  547 ------EKKLKEQKALLEEGFKKKAEEMDGEiQQLKHNIEDMKKKQ 586
Cdd:PTZ00121 1585 eakkaeEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAE 1629
PTZ00121 PTZ00121
MAEBL; Provisional
 452-585 3.14e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  452 KAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKK---EAAEKEQDLLRQKQKEQQEYMEAQEKRNKE--NIEQ 526
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAdeaEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkKADE 1395

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755512962  527 LRRKLEQER---EQLIKDHNmmVEKKLKEQKALLEEgfKKKAEEMDGEIQQlKHNIEDMKKK 585
Cdd:PTZ00121 1396 AKKKAEEDKkkaDELKKAAA--AKKKADEAKKKAEE--KKKADEAKKKAEE-AKKADEAKKK 1452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 467-586 3.21e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 467 IESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEymEAQEKRNKENIEQLRRK-LEQEREQLIKDHNMM 545
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA--ELARLEQDIARLEERRReLEERLEELEEELAEL 328

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 755512962 546 VEKKLKEQKALLEEgfKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:COG1196  329 EEELEELEEELEEL--EEELEEAEEELEEAEAELAEAEEAL 367
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 475-574 3.33e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.58  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  475 DTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLeQEREQLIKDhnmmvekkLKEQ- 553
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPEL-TEKESSLID--------LKEHa 505

                          90       100
                  ....*....|....*....|...
gi 755512962  554 KALLEEGFKK--KAEEMDGEIQQ 574
Cdd:pfam10174 506 SSLASSGLKKdsKLKSLEIAVEQ 528
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 314-586 3.36e-03

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: 40.72  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   314 VTTLAQRENSVAVQRAADHYSEQMVQRLSlptdtlqELLDVHAACE------KEAMAVFMEHSFKDENQQFLKKLVELIG 387
Cdd:TIGR00618  412 IDTRTSAFRDLQGQLAHAKKQQELQQRYA-------ELCAAAITCTaqceklEKIHLQESAQSLKEREQQLQTKEQIHLQ 484

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   388 EAKVlfllKNEEASDKYCQEELDRLSKD----LMDNISTFSVPGGHRLYMdmrEKIEHDYWQVPRKGVKAREVFQSFLQS 463
Cdd:TIGR00618  485 ETRK----KAVVLARLLELQEEPCPLCGscihPNPARQDIDNPGPLTRRM---QRGEQTYAQLETSEEDVYHQLTSERKQ 557

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962   464 QAIIES---SILQADTALTAGQKAIAEE-------------------RTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNK 521
Cdd:TIGR00618  558 RASLKEqmqEIQQSFSILTQCDNRSKEDipnlqnitvrlqdlteklsEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC 637

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755512962   522 ENIEQLRR-KLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:TIGR00618  638 SQELALKLtALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQ 703
fliH PRK06669
flagellar assembly protein H; Validated
 446-585 3.51e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 39.61  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 446 VPRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQ-KAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKE-- 522
Cdd:PRK06669  12 INKEKLKTHEIQKYRFKVLSIKEKERLREEEEEQVEQlREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEas 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755512962 523 -NIEQLRRKLEQEreqlIKDHNMMVEKKLKEQKAL-----LEEGFKKKAEEMDGEIQQLKHNIEDMKKK 585
Cdd:PRK06669  92 sIIEKLQMQIERE----QEEWEEELERLIEEAKAEgyeegYEKGREEGLEEVRELIEQLNKIIEKLIKK 156
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 491-586 3.88e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 39.30  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  491 KKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ-LRRKLEQE---REQLIKDH---------NMMVEKKLKE-QKAL 556
Cdd:pfam13904  64 KQRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQEwLQRKARQQtkkREESHKQKaaesaskslAKPERKVSQEeAKEV 143

                          90       100       110
                  ....*....|....*....|....*....|
gi 755512962  557 LEEGFKKKAEEmdgEIQQLKHNIEDMKKKQ 586
Cdd:pfam13904 144 LQEWERKKLEQ---QQRKREEEQREQLKKE 170
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 491-584 3.99e-03

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.55  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  491 KKEAAEKEQDLLRQKQKEQQEYMEAQEKRnKENIEQLRRKLEQEREQL---IKDH---------NMMVEKKLKEQKALLE 558
Cdd:pfam13863   4 KKREMFLVQLALDAKREEIERLEELLKQR-EEELEKKEQELKEDLIKFdkfLKENdakrrralkKAEEETKLKKEKEKEI 82

                          90       100
                  ....*....|....*....|....*.
gi 755512962  559 EGFKKKAEEMDGEIQQLKHNIEDMKK 584
Cdd:pfam13863  83 KKLTAQIEELKSEISKLEEKLEEYKP 108
PRK12704 PRK12704
phosphodiesterase; Provisional
 491-568 4.26e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 4.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 491 KKEAAEKEQDLLRQKQKE---QQEYMEAQEKRNKENIEQLRRKLE--------QEREQLIKDhnmmVEKKLKEQKALL-- 557
Cdd:PRK12704 101 KLELLEKREEELEKKEKEleqKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEK----VEEEARHEAAVLik 176

                         90
                 ....*....|....*...
gi 755512962 558 -------EEGfKKKAEEM 568
Cdd:PRK12704 177 eieeeakEEA-DKKAKEI 193
PTZ00121 PTZ00121
MAEBL; Provisional
 473-584 4.69e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  473 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQ-KEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLK 551
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602

                          90       100       110
                  ....*....|....*....|....*....|...
gi 755512962  552 EQKALLEEGFKKkAEEMDGEIQQLKHNIEDMKK 584
Cdd:PTZ00121 1603 EEKKMKAEEAKK-AEEAKIKAEELKKAEEEKKK 1634
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 462-539 4.76e-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: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 37.68  E-value: 4.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  462 QSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKE-QDLLRQKQKEQQEYMEAQEKRNKENIEQLRR----KLEQERE 536
Cdd:pfam00430  30 KRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEaQEIIENAKKRAEKLKEEIVAAAEAEAERIIEqaaaEIEQEKD 109


                  ...
gi 755512962  537 QLI 539
Cdd:pfam00430 110 RAL 112
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 463-586 5.66e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.51  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  463 SQAIIESSILQADTALTAGQKAIAeeRTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENiEQLRRKLEQEREQLikdh 542
Cdd:pfam04012  23 PEKMLEQAIRDMQSELVKARQALA--QTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN-EELAREALAEKKSL---- 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 755512962  543 nmmvEKKLKEQKALLEEgFKKKAEEMDGEIQQLKHNIEDMKKKQ 586
Cdd:pfam04012  96 ----EKQAEALETQLAQ-QRSAVEQLRKQLAALETKIQQLKAKK 134
RHD3_GTPase pfam05879
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of ...
 47-118 6.11e-03

Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of several eukaryotic root hair defective 3 (RHD3) like GTP-binding proteins, including RHD3 from Arabidopsis and Sey1 from yeast, which are involved in homotypic membrane fusion of the endoplasmic reticulum. This domain binds GTP and forms dimers with other molecule for membrane tethering.


Pssm-ID: 461768  Cd Length: 243  Bit Score: 38.59  E-value: 6.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755512962   47 TGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLDTEGLGDVEKG---DPKNDLWIFALSV 118
Cdd:pfam05879   6 TGKSTLLNHLFGTNFSVMDASGRQQTTKGIWLAKCKGIGNMEPNILVMDVEGTDGRERGedqDFERKSALFALAT 80
Utp11 pfam03998
Utp11 protein; This protein is found to be part of a large ribonucleoprotein complex ...
 487-564 6.26e-03

Utp11 protein; This protein is found to be part of a large ribonucleoprotein complex containing the U3 snoRNA. Depletion of the Utp proteins impedes production of the 18S rRNA, indicating that they are part of the active pre-rRNA processing complex. This large RNP complex has been termed the small subunit (SSU) processome.


Pssm-ID: 461122 [Multi-domain]  Cd Length: 241  Bit Score: 38.76  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  487 EERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQ--EREQLIKDhnmmVEKKLKEQKALLEEGFKKK 564
Cdd:pfam03998 146 YFDTDPELLDRRENRLKKEQLESNSLTAATLKKLDKKKEKLYKELKArlEREKELKK----AEQKLELQRALMKKGAKKK 221
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 468-585 6.50e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 38.26  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  468 ESSILQADTALTAGQKA--IAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNkeniEQLRRKLEQEREQlIKDHNMM 545
Cdd:pfam06785  66 EKSFLEEKEAKLTELDAegFKILEETLEELQSEEERLEEELSQKEEELRRLTEEN----QQLQIQLQQISQD-FAEFRLE 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 755512962  546 VEKKLKEQKALLEEgFKKKAEEMDGEIQQLKHNIEDMKKK 585
Cdd:pfam06785 141 SEEQLAEKQLLINE-YQQTIEEQRSVLEKRQDQIENLESK 179
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 448-563 6.93e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 37.75  E-value: 6.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  448 RKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTK----KEAAEKEQDLLRQK-QKEQQEYMEAQEKRNKE 522
Cdd:pfam11600  16 QRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKkeeeKELKEKERREKKEKdEKEKAEKLRLKEEKRKE 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 755512962  523 NIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKK 563
Cdd:pfam11600  96 KQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITRFLQK 136
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 482-585 7.09e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.02  E-value: 7.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962 482 QKAIAE-ERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRR---KLEQEREQlikdhnmmveKKLKEQKALL 557
Cdd:PRK09510  94 QKQAAEqERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAaaaKAKAEAEA----------KRAAAAAKKA 163

                         90       100
                 ....*....|....*....|....*...
gi 755512962 558 EEGFKKKAEEmdgeiQQLKHNIEDMKKK 585
Cdd:PRK09510 164 AAEAKKKAEA-----EAAKKAAAEAKKK 186
PTZ00121 PTZ00121
MAEBL; Provisional
 482-584 9.33e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 9.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512962  482 QKAIAEERTKKEAAEKEQDLLRQK-----QKEQQEYMEAQEKR----NKENIEQLRRKLEQEREQLIKDHNMMVEKKLKE 552
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKaeeakKEAEEDKKKAEEAKkdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787

                          90       100       110
                  ....*....|....*....|....*....|..
gi 755512962  553 QKalleegfKKKAEEMDGEIQQLKHNIEDMKK 584
Cdd:PTZ00121 1788 ED-------EKRRMEVDKKIKDIFDNFANIIE 1812
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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