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Conserved domains on  [gi|1039772804|ref|XP_017176629|]
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guanylate binding protein 8 isoform X2 [Mus musculus]

Protein Classification

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 ...
 129-416 4.12e-146

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: 418.23  E-value: 4.12e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 129 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 208
Cdd:pfam02841   8 PRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKEAIAVFMK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 209 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 286
Cdd:pfam02841  88 RSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKLEAKYNQV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 287 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 366
Cdd:pfam02841 168 PRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQ 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039772804 367 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 416
Cdd:pfam02841 248 LIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP super family cl46410
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 1-130 1.02e-66

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.


The actual alignment was detected with superfamily member pfam02263:

Pssm-ID: 460516  Cd Length: 260  Bit Score: 214.16  E-value: 1.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804   1 MWCMPHPTKPEHTLVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTELirakSSPN 80
Cdd:pfam02263  63 MWCVPHPNKPKHTLVLLDTEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPR 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039772804  81 PDGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDEYLENALKLIPG 130
Cdd:pfam02263 139 YGRVADSADFVSFFPDFVWTVRDFSLPLEADGGPITGDEYLENRLKLSQG 188
 
Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 129-416 4.12e-146

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: 418.23  E-value: 4.12e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 129 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 208
Cdd:pfam02841   8 PRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKEAIAVFMK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 209 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 286
Cdd:pfam02841  88 RSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKLEAKYNQV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 287 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 366
Cdd:pfam02841 168 PRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQ 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039772804 367 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 416
Cdd:pfam02841 248 LIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 129-416 1.66e-138

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: 398.87  E-value: 1.66e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 129 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 208
Cdd:cd16269     2 RRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFMK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 209 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 286
Cdd:cd16269    82 RSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 287 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 366
Cdd:cd16269   162 PRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQ 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039772804 367 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 416
Cdd:cd16269   242 LKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 1-130 1.02e-66

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: 214.16  E-value: 1.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804   1 MWCMPHPTKPEHTLVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTELirakSSPN 80
Cdd:pfam02263  63 MWCVPHPNKPKHTLVLLDTEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPR 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039772804  81 PDGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDEYLENALKLIPG 130
Cdd:pfam02263 139 YGRVADSADFVSFFPDFVWTVRDFSLPLEADGGPITGDEYLENRLKLSQG 188
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 1-140 7.46e-31

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: 118.58  E-value: 7.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804   1 MWCMPHP--TKPEHTLVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTElirakSS 78
Cdd:cd01851    49 MWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ET 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039772804  79 PNPDGIKNsteFVSFFPDFVWTVRDFMLELKLNGEDITS-----DEYLENALKLIPGLGILVTTYVD 140
Cdd:cd01851   124 LGLAGLHN---FSKPKPLLLFVVRDFTGPTPLEGLDVTEksetlIEELNKIWSSIRKPFTPITCFVL 187
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 326-426 8.59e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.96  E-value: 8.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 326 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENiEQLRRKLEQEREQLIKdhnmmvEKKLKEQKALLEEGFKKKA 405
Cdd:PRK09510   77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALK------QKQAEEAAAKAAAAAKAKA 149

                          90       100
                  ....*....|....*....|.
gi 1039772804 406 EEMDGEIQQLKHNIEDMKKKQ 426
Cdd:PRK09510  150 EAEAKRAAAAAKKAAAEAKKK 170
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 304-426 7.96e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 7.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 304 QAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEymEAQEKRNKENIEQLRRKLEQEREQLIKDHN 383
Cdd:COG1196   354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ--LEELEEAEEALLERLERLEEELEELEEALA 431

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039772804 384 MMVEKKLKEQKALLEEgfKKKAEEMDGEIQQLKHNIEDMKKKQ 426
Cdd:COG1196   432 ELEEEEEEEEEALEEA--AEEEAELEEEEEALLELLAELLEEA 472
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 282-426 1.03e-03

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: 40.98  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 282 DYWQVPRKGVKAREVFQSFLQSQAIIESSI----LQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQE 357
Cdd:TIGR02794  23 LYHSVKPEPGGGAEIIQAVLVDPGAVAQQAnriqQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEK 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039772804 358 KrnKENIEQLRRKLEQEREQLIKdhnmMVEKKLKEQKALLEEGFKKKAEEM---DGEIQQLKHNIEDMKKKQ 426
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 ...
 129-416 4.12e-146

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: 418.23  E-value: 4.12e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 129 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 208
Cdd:pfam02841   8 PRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKEAIAVFMK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 209 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 286
Cdd:pfam02841  88 RSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKLEAKYNQV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 287 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 366
Cdd:pfam02841 168 PRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQ 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039772804 367 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 416
Cdd:pfam02841 248 LIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 129-416 1.66e-138

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: 398.87  E-value: 1.66e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 129 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 208
Cdd:cd16269     2 RRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFMK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 209 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 286
Cdd:cd16269    82 RSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 287 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 366
Cdd:cd16269   162 PRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQ 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039772804 367 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 416
Cdd:cd16269   242 LKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 1-130 1.02e-66

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: 214.16  E-value: 1.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804   1 MWCMPHPTKPEHTLVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTELirakSSPN 80
Cdd:pfam02263  63 MWCVPHPNKPKHTLVLLDTEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPR 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039772804  81 PDGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDEYLENALKLIPG 130
Cdd:pfam02263 139 YGRVADSADFVSFFPDFVWTVRDFSLPLEADGGPITGDEYLENRLKLSQG 188
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 1-140 7.46e-31

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: 118.58  E-value: 7.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804   1 MWCMPHP--TKPEHTLVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTElirakSS 78
Cdd:cd01851    49 MWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ET 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039772804  79 PNPDGIKNsteFVSFFPDFVWTVRDFMLELKLNGEDITS-----DEYLENALKLIPGLGILVTTYVD 140
Cdd:cd01851   124 LGLAGLHN---FSKPKPLLLFVVRDFTGPTPLEGLDVTEksetlIEELNKIWSSIRKPFTPITCFVL 187
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 328-424 3.48e-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: 52.82  E-value: 3.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 328 ERTKKEAAEKEQDL--LRQKQKEQ--QEYMEAQEKRNKENIEQLRRK-----LEQEREQLIKDHN--MMVEKKLKE-QKA 395
Cdd:pfam17380 449 ERVRLEEQERQQQVerLRQQEEERkrKKLELEKEKRDRKRAEEQRRKilekeLEERKQAMIEEERkrKLLEKEMEErQKA 528

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039772804 396 LLEEGFKKKAEE---MDGEIQQLKHNIEDMKK 424
Cdd:pfam17380 529 IYEEERRREAEEerrKQQEMEERRRIQEQMRK 560
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 326-426 8.59e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.96  E-value: 8.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 326 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENiEQLRRKLEQEREQLIKdhnmmvEKKLKEQKALLEEGFKKKA 405
Cdd:PRK09510   77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALK------QKQAEEAAAKAAAAAKAKA 149

                          90       100
                  ....*....|....*....|.
gi 1039772804 406 EEMDGEIQQLKHNIEDMKKKQ 426
Cdd:PRK09510  150 EAEAKRAAAAAKKAAAEAKKK 170
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 150-420 6.09e-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: 48.68  E-value: 6.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  150 VDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVE-LIGE 228
Cdd:pfam12128  453 LNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqLFPQ 532

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  229 AKVLFLLKNEEASD------KYCQEELdRLSKDLMDNISTFSVPGGHRLY---MDMrEKIEHDYW-----QVPRKGVKAR 294
Cdd:pfam12128  533 AGTLLHFLRKEAPDweqsigKVISPEL-LHRTDLDPEVWDGSVGGELNLYgvkLDL-KRIDVPEWaaseeELRERLDKAE 610

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  295 EVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQE 374
Cdd:pfam12128  611 EALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ 690

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1039772804  375 REQLIKDHNMMVE---KKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIE 420
Cdd:pfam12128  691 LKQLDKKHQAWLEeqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIA 739
PRK12704 PRK12704
phosphodiesterase; Provisional
 332-426 1.67e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 332 KEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMvEKKLKEQKALLE---EGFKKKAEEM 408
Cdd:PRK12704   34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKL-EKRLLQKEENLDrklELLEKREEEL 112

                          90
                  ....*....|....*...
gi 1039772804 409 DGEIQQLKHNIEDMKKKQ 426
Cdd:PRK12704  113 EKKEKELEQKQQELEKKE 130
PTZ00121 PTZ00121
MAEBL; Provisional
 292-425 1.83e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  292 KAREVFQSFLQSQAIIESSILQAD--------TALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRnkeN 363
Cdd:PTZ00121  1627 KAEEEKKKVEQLKKKEAEEKKKAEelkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK---K 1703

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039772804  364 IEQLRRKLEQER---EQLIKDHNmmvEKKLK-EQKALLEEGFKKKAEEM---DGEIQQLKHNIEDMKKK 425
Cdd:PTZ00121  1704 AEELKKKEAEEKkkaEELKKAEE---ENKIKaEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLKKEEEKK 1769
PTZ00121 PTZ00121
MAEBL; Provisional
 291-426 2.50e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  291 VKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKEniEQLRRK 370
Cdd:PTZ00121  1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA--EALKKE 1697

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039772804  371 LEQER--EQLIKDHNMmvEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 426
Cdd:PTZ00121  1698 AEEAKkaEELKKKEAE--EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 324-407 2.67e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.34  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 324 AIAEE-----RTKKEAAEKEQdlLRQKQKEQQeymeAQEKRNKENIEQLR-RKLEQEREQLIKdhnmmvEKKLKEQKALL 397
Cdd:PRK09510   59 AVVEQynrqqQQQKSAKRAEE--QRKKKEQQQ----AEELQQKQAAEQERlKQLEKERLAAQE------QKKQAEEAAKQ 126

                          90
                  ....*....|
gi 1039772804 398 EEGFKKKAEE 407
Cdd:PRK09510  127 AALKQKQAEE 136
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 327-414 3.28e-05

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: 43.88  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 327 EERTKKEAAEKEQDLLRQKQKEQQEYMEaQEKRNKENIEQLRRKLEQEREQLikdhnMMVEKKLKEQKALLEEGFKKKAE 406
Cdd:pfam05672   9 AEEAARILAEKRRQAREQREREEQERLE-KEEEERLRKEELRRRAEEERARR-----EEEARRLEEERRREEEERQRKAE 82


                  ....*...
gi 1039772804 407 EMDGEIQQ 414
Cdd:pfam05672  83 EEAEEREQ 90
PTZ00121 PTZ00121
MAEBL; Provisional
 323-425 4.76e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 4.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  323 KAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEK-RNKENIEQLRRKLEQEReqliKDHNMmveKKLKEQKALLEEgF 401
Cdd:PTZ00121  1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAK----KAEEA---KKKAEEAKKADE-A 1475

                           90       100
                   ....*....|....*....|....
gi 1039772804  402 KKKAEEMDgEIQQLKHNIEDMKKK 425
Cdd:PTZ00121  1476 KKKAEEAK-KADEAKKKAEEAKKK 1498
PTZ00121 PTZ00121
MAEBL; Provisional
 276-426 5.32e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 5.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  276 REKIEHDYWQVPRKGVKAREVFQSFLQSQAII--ESSILQADTALTAGQKAIAEERTKKEAAEKEQdLLRQKQKEQQEYM 353
Cdd:PTZ00121  1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK-VEQLKKKEAEEKK 1647

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039772804  354 EAQEKRNKENIEQLRRKLEQEREQlikdhnmmvEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 426
Cdd:PTZ00121  1648 KAEELKKAEEENKIKAAEEAKKAE---------EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
PTZ00121 PTZ00121
MAEBL; Provisional
 322-421 6.32e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 6.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  322 QKAIAEERTKKEAAEKEQ-DLLRQKQKEQQ---EYMEAQEKRNKENIEQLRRKLEQER----------------EQLIKD 381
Cdd:PTZ00121  1686 DEKKAAEALKKEAEEAKKaEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAEEDKkkaeeakkdeeekkkiAHLKKE 1765

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1039772804  382 HNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIED 421
Cdd:PTZ00121  1766 EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 304-426 7.96e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 7.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 304 QAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEymEAQEKRNKENIEQLRRKLEQEREQLIKDHN 383
Cdd:COG1196   354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ--LEELEEAEEALLERLERLEEELEELEEALA 431

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039772804 384 MMVEKKLKEQKALLEEgfKKKAEEMDGEIQQLKHNIEDMKKKQ 426
Cdd:COG1196   432 ELEEEEEEEEEALEEA--AEEEAELEEEEEALLELLAELLEEA 472
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 307-426 1.14e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.37  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 307 IESSILQADTALTAGQKAIAEERTKKEAAEKEqdllRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLikdhnMMV 386
Cdd:COG1579    15 LDSELDRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-----GNV 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039772804 387 eKKLKEQKALLEE--GFKKKAEEMDGEIQQLKHNIEDMKKKQ 426
Cdd:COG1579    86 -RNNKEYEALQKEieSLKRRISDLEDEILELMERIEELEEEL 126
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 316-411 1.25e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 44.69  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 316 TALTAGQKAIAEERTKKEAAEKEQDL--------LRQKQ---KEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNM 384
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKEQDEasferlaeLRDELaelEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490

                          90       100
                  ....*....|....*....|....*..
gi 1039772804 385 mvEKKLKEQKALLEEGFKKKAEEMDGE 411
Cdd:COG0542   491 --EKELAELEEELAELAPLLREEVTEE 515
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 322-428 1.52e-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: 44.34  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 322 QKAIAEERTK---KEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREqliKDHNMMVEKKLKEQKALLE 398
Cdd:pfam17380 486 RKRAEEQRRKileKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERR---KQQEMEERRRIQEQMRKAT 562

                          90       100       110
                  ....*....|....*....|....*....|
gi 1039772804 399 EGfKKKAEEMDGEIQQLKHNIEDMKKKQWF 428
Cdd:pfam17380 563 EE-RSRLEAMEREREMMRQIVESEKARAEY 591
PTZ00121 PTZ00121
MAEBL; Provisional
 313-425 2.12e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  313 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMM-VEKKLK 391
Cdd:PTZ00121  1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkAEEAKK 1614

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1039772804  392 EQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKK 425
Cdd:PTZ00121  1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
PTZ00121 PTZ00121
MAEBL; Provisional
 313-425 2.25e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  313 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYME-----AQEKRNKENIEQLRRKLEQEREQLIKDHNMMVE 387
Cdd:PTZ00121  1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaakkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1039772804  388 KKLKEQKALLEEgFKKKAEEMDgEIQQLKHNIEDMKKK 425
Cdd:PTZ00121  1371 KKKEEAKKKADA-AKKKAEEKK-KADEAKKKAEEDKKK 1406
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 305-425 2.41e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 305 AIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQK----------QKEQQEYMEAQEKRNKENIEQLRRKLEQE 374
Cdd:COG3883     5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAEleelneeyneLQAELEALQAEIDKLQAEIAEAEAEIEER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 375 REQL--------------------------------------IKDHNMMVEKKLKEQKALLEEgFKKKAEEMDGEIQQLK 416
Cdd:COG3883    85 REELgeraralyrsggsvsyldvllgsesfsdfldrlsalskIADADADLLEELKADKAELEA-KKAELEAKLAELEALK 163


                  ....*....
gi 1039772804 417 HNIEDMKKK 425
Cdd:COG3883   164 AELEAAKAE 172
PRK12704 PRK12704
phosphodiesterase; Provisional
 302-408 2.79e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 302 QSQAIIESSILQADT----ALTAGQKAIAEERTK--KEAAEKEQDLLRQKQKEQQEymEAQEKRNKENIEQLRRKLEQER 375
Cdd:PRK12704   39 EAKRILEEAKKEAEAikkeALLEAKEEIHKLRNEfeKELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKKE 116

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1039772804 376 EQLIKDhnmmvEKKLKEQKALLEEGFKKKAEEM 408
Cdd:PRK12704  117 KELEQK-----QQELEKKEEELEELIEEQLQEL 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 288-422 3.05e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 288 RKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQL 367
Cdd:COG1196   645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039772804 368 RRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDM 422
Cdd:COG1196   725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 282-426 1.03e-03

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: 40.98  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 282 DYWQVPRKGVKAREVFQSFLQSQAIIESSI----LQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQE 357
Cdd:TIGR02794  23 LYHSVKPEPGGGAEIIQAVLVDPGAVAQQAnriqQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEK 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039772804 358 KrnKENIEQLRRKLEQEREQLIKdhnmMVEKKLKEQKALLEEGFKKKAEEM---DGEIQQLKHNIEDMKKKQ 426
Cdd:TIGR02794 103 A--AKQAEQAAKQAEEKQKQAEE----AKAKQAAEAKAKAEAEAERKAKEEaakQAEEEAKAKAAAEAKKKA 168
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 293-426 1.05e-03

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: 41.57  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 293 AREVFQsfLQSQAII---ESSILQADTAltagqkaiaeertkKEAAEKEQDLLR-QKQKEQQEYMEAQEKRNK--ENIEQ 366
Cdd:pfam10168 530 PQECLQ--LLSRATQvfrEEYLKKHDLA--------------REEIQKRVKLLKlQKEQQLQELQSLEEERKSlsERAEK 593

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039772804 367 LRRKLE--QEREQLI--KDHNMMveKKLKEQKALL---EEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 426
Cdd:pfam10168 594 LAEKYEeiKDKQEKLmrRCKKVL--QRLNSQLPVLsdaEREMKKELETINEQLKHLANAIKQAKKKM 658
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 297-414 1.05e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 297 FQSFLQSQAIIeSSILQADTALTAGQKA-IAEERTKKEAAEKEQDLLRQKQKE---QQEYMEAQEKRNKENIEQLRRKLE 372
Cdd:COG3883   114 FSDFLDRLSAL-SKIADADADLLEELKAdKAELEAKKAELEAKLAELEALKAEleaAKAELEAQQAEQEALLAQLSAEEA 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039772804 373 QEREQLikdHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQ 414
Cdd:COG3883   193 AAEAQL---AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 308-425 1.15e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  308 ESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQK---QKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNM 384
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1039772804  385 MVEKK-----LKEQKALLE---EGFKKKAEEMDGEIQQLKHNIEDMKKK 425
Cdd:TIGR02168  332 LDELAeelaeLEEKLEELKeelESLEAELEELEAELEELESRLEELEEQ 380
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 334-426 1.17e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 334 AAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLikdhnmmvekKLKEQKALLEEGFKKKAEEMDGEIQ 413
Cdd:PRK09510   59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERL----------KQLEKERLAAQEQKKQAEEAAKQAA 128

                          90
                  ....*....|...
gi 1039772804 414 QLKHNIEDMKKKQ 426
Cdd:PRK09510  129 LKQKQAEEAAAKA 141
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 327-409 1.21e-03

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: 39.93  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 327 EERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKK-LKEQKALLEEGFKKKA 405
Cdd:COG1390    12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKElLEAKEELIEEVFEEAL 91


                  ....
gi 1039772804 406 EEMD 409
Cdd:COG1390    92 EKLK 95
PTZ00121 PTZ00121
MAEBL; Provisional
 313-425 1.26e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  313 QADTALTAGQKAIAEERtKKEAAEKEQDLLRQKQKEQQEYMEAQEK--RNKENIEQLRRKLEQEREQLIKDHNMMVEKKL 390
Cdd:PTZ00121  1355 AADEAEAAEEKAEAAEK-KKEEAKKKADAAKKKAEEKKKADEAKKKaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKA 1433

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1039772804  391 KEQKALLEEgfKKKAEEMDGEIQQlKHNIEDMKKK 425
Cdd:PTZ00121  1434 DEAKKKAEE--AKKADEAKKKAEE-AKKAEEAKKK 1465
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 317-399 1.35e-03

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: 38.92  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 317 ALTAGQKAIAE-----ERTKKEAA---EKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEK 388
Cdd:TIGR01144  23 AIETRQKKIADglasaERAKKEAAlaqKKAQVILKEAKDEAQEIIENANKRGSEILEEAKAEAREEREKIKAQARAEIEA 102

                          90
                  ....*....|..
gi 1039772804 389 KLKE-QKALLEE 399
Cdd:TIGR01144 103 EKEQaREELRKQ 114
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 337-425 1.44e-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: 38.32  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 337 KEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKleqerEQLIKDHNMMVEKKLKEQKALLEEGFKKKAEE------MDG 410
Cdd:pfam13863   6 REMFLVQLALDAKREEIERLEELLKQREEELEKK-----EQELKEDLIKFDKFLKENDAKRRRALKKAEEEtklkkeKEK 80

                          90
                  ....*....|....*
gi 1039772804 411 EIQQLKHNIEDMKKK 425
Cdd:pfam13863  81 EIKKLTAQIEELKSE 95
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
 328-420 1.44e-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: 40.29  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 328 ERTKKEAAEKEQDLLRQKQKEQQEYME--AQEKRNKEniEQLRRK-----LEQEREQLikdhnMMVEKK---LKEQKALL 397
Cdd:pfam15991   5 KMSEQMWRALKRHIMRERERKKQEQEAkmEEERLRRE--REEREKedrmtLEETKEQI-----LKLEKKladLKEEKHQL 77

                          90       100
                  ....*....|....*....|...
gi 1039772804 398 EEGFKKKAEEMDGEIQQLKHNIE 420
Cdd:pfam15991  78 FLQLKKVLHEDETRKRQLKEQSE 100
PTZ00121 PTZ00121
MAEBL; Provisional
 323-425 1.55e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  323 KAIAEERTKK-EAAEKEQDLLRQKQKEQQEYMEAQEKRN---KENIEQLRRKLEQERE-QLIKDHNMMVEKKLKEQKALL 397
Cdd:PTZ00121  1335 KKKAEEAKKAaEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAA 1414

                           90       100
                   ....*....|....*....|....*...
gi 1039772804  398 EEgfKKKAEEMDGEIQQLKhNIEDMKKK 425
Cdd:PTZ00121  1415 AA--KKKADEAKKKAEEKK-KADEAKKK 1439
DUF4175 pfam13779
Domain of unknown function (DUF4175);
313-415 1.60e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 41.13  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 313 QADTALTAGQKAIAE--ERTkkeAAEKE-QDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKD--HNMMve 387
Cdd:pfam13779 486 DAERRLRAAQERLSEalERG---ASDEEiAKLMQELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTQQdlQRML-- 560

                          90       100
                  ....*....|....*....|....*...
gi 1039772804 388 KKLKEqkaLLEEGFKKKAEEMDGEIQQL 415
Cdd:pfam13779 561 DRIEE---LARSGRRAEAQQMLSQLQQM 585
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 308-424 1.71e-03

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: 40.90  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 308 ESSILQADTALTAGQKAIAEERTKKEA--------AEKEQDLLRQKQKEQQEY-MEAQEKRNKENIE--------QLRRK 370
Cdd:pfam09731 286 NSLIAHAHREIDQLSKKLAELKKREEKhieralekQKEELDKLAEELSARLEEvRAADEAQLRLEFErereeireSYEEK 365

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039772804 371 LEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKK-----AEEMDGEIQQL---KHNIEDMKK 424
Cdd:pfam09731 366 LRTELERQAEAHEEHLKDVLVEQEIELQREFLQDikekvEEERAGRLLKLnelLANLKGLEK 427
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 306-426 1.97e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 306 IIESSILQAdtaLTAGQKAIAEERTKKEAAEKEQDLLRQKQkEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMM 385
Cdd:PRK00409  521 LIASLEELE---RELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039772804 386 VEKKLKEQKAlleegfkKKAEEMdgeIQQLKHNIEDMKKKQ 426
Cdd:PRK00409  597 QKGGYASVKA-------HELIEA---RKRLNKANEKKEKKK 627
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 313-414 2.22e-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: 40.37  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 313 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQ---EYMEAQEKRNKENIeQLRRKLEQEREQLIKDHNMMVEKK 389
Cdd:pfam05262 221 ELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKnlpKPADTSSPKEDKQV-AENQKREIEKAQIEIKKNDEEALK 299

                          90       100
                  ....*....|....*....|....*
gi 1039772804 390 LKEQKAlleEGFKKKAEEMDGEIQQ 414
Cdd:pfam05262 300 AKDHKA---FDLKQESKASEKEAED 321
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 296-399 2.34e-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: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 296 VFQSFLQSQAiieSSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKEnIEQLRRKLEQER 375
Cdd:COG4942    10 LLALAAAAQA---DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAEL 85

                          90       100
                  ....*....|....*....|....
gi 1039772804 376 EQLIKDHNMMvEKKLKEQKALLEE 399
Cdd:COG4942    86 AELEKEIAEL-RAELEAQKEELAE 108
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 322-406 2.39e-03

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: 39.83  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 322 QKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKEN-------IEQLRRKLEQEREQLIKDHNmmvEKKLKEQK 394
Cdd:TIGR02794  96 QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEaeaerkaKEEAAKQAEEEAKAKAAAEA---KKKAEEAK 172

                          90
                  ....*....|..
gi 1039772804 395 ALLEEGFKKKAE 406
Cdd:TIGR02794 173 KKAEAEAKAKAE 184
PTZ00121 PTZ00121
MAEBL; Provisional
 326-425 2.71e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  326 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKA 405
Cdd:PTZ00121  1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA 1324

                           90       100
                   ....*....|....*....|
gi 1039772804  406 EEMDGEIQQLKHNIEDMKKK 425
Cdd:PTZ00121  1325 EEAKKKADAAKKKAEEAKKA 1344
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 276-426 2.72e-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: 40.11  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 276 REKIEHDYWQVPRKGVKAREVFQSFLQSQAIIESsilQAdtALTAGQKAIAEERTKK----EAAEKEQDLLRQKQKE--- 348
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDR---QA--AIYAEQERMAMEREREleriRQEERKRELERIRQEEiam 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 349 --------QQEYMEAQEK--RNKENIEQLRRK--LEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 416
Cdd:pfam17380 373 eisrmrelERLQMERQQKneRVRQELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR 452

                         170
                  ....*....|
gi 1039772804 417 HniEDMKKKQ 426
Cdd:pfam17380 453 L--EEQERQQ 460
PTZ00121 PTZ00121
MAEBL; Provisional
 320-424 2.83e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  320 AGQKAIAEErTKKEAAEKEQ-DLLRQKQKEQQEYMEAQEK-RNKENIEQLRRKLEQEREQlikdhnmmVEKKLKEQKALL 397
Cdd:PTZ00121  1414 AAAKKKADE-AKKKAEEKKKaDEAKKKAEEAKKADEAKKKaEEAKKAEEAKKKAEEAKKA--------DEAKKKAEEAKK 1484

                           90       100
                   ....*....|....*....|....*..
gi 1039772804  398 EEGFKKKAEEMDGEIQQLKHNIEDMKK 424
Cdd:PTZ00121  1485 ADEAKKKAEEAKKKADEAKKAAEAKKK 1511
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
304-426 3.14e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.04  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 304 QAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEY-MEAQEKRNkeniEQLRRKLEQEREQLikdh 382
Cdd:COG1842    25 EKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKaRLALEKGR----EDLAREALERKAEL---- 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039772804 383 nmmvEKKLKEQKALLEEgFKKKAEEMDGEIQQLKHNIEDMKKKQ 426
Cdd:COG1842    97 ----EAQAEALEAQLAQ-LEEQVEKLKEALRQLESKLEELKAKK 135
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 287-403 3.57e-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: 39.36  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 287 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLR---QKQKEQQEYMEAQEKRNKEN 363
Cdd:COG4942   131 FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERaalEALKAERQKLLARLEKELAE 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039772804 364 IEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKK 403
Cdd:COG4942   211 LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 329-426 3.60e-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: 40.05  E-value: 3.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  329 RTKKEAAEKEQDLLRQKQK--------------EQQEYMEAQEKRNKENIEQLRRKLEQ------EREQLIKDHNMMVEK 388
Cdd:TIGR02169  204 RREREKAERYQALLKEKREyegyellkekealeRQKEAIERQLASLEEELEKLTEEISElekrleEIEQLLEELNKKIKD 283

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1039772804  389 KLKEQKAlleeGFKKKAEEMDGEIQQLKHNIEDMKKKQ 426
Cdd:TIGR02169  284 LGEEEQL----RVKEKIGELEAEIASLERSIAEKEREL 317
PTZ00121 PTZ00121
MAEBL; Provisional
 313-425 3.88e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  313 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRN--KENIEQLRRKLEQEREQLIKDHNMMVEKKL 390
Cdd:PTZ00121  1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAaaKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1039772804  391 KEQKALLEEgfKKKAEEMDGEIQQlKHNIEDMKKK 425
Cdd:PTZ00121  1447 DEAKKKAEE--AKKAEEAKKKAEE-AKKADEAKKK 1478
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 322-426 3.94e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.40  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 322 QKAIAEERTKKEAAEKE--QDLLRQKQKEQQEYMEAQEKRNKENIEQlrrklEQEREQLIKDHNMMVEKKLKEQKAlLEE 399
Cdd:PRK09510   85 EQQQAEELQQKQAAEQErlKQLEKERLAAQEQKKQAEEAAKQAALKQ-----KQAEEAAAKAAAAAKAKAEAEAKR-AAA 158

                          90       100
                  ....*....|....*....|....*..
gi 1039772804 400 GFKKKAEEMDgeiqqlKHNIEDMKKKQ 426
Cdd:PRK09510  159 AAKKAAAEAK------KKAEAEAAKKA 179
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 326-404 3.98e-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: 37.33  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 326 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRN---KENIEQLRRKLEQEREQLIKDHNMMVEkKLKEQKALLEEGFK 402
Cdd:pfam00836  54 AEERRKSLEAQKLKQLAEKREKEEEALQKADEENNnfsKMAEEKLKQKMEAYKENREAQIAALKE-KLKEKEKHVEEVRK 132


                  ..
gi 1039772804 403 KK 404
Cdd:pfam00836 133 NK 134
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-426 4.37e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 308 ESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEyMEAQEKRNKENIEQLRRKLE--QEREQLIKDHNMM 385
Cdd:COG1196   221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEeaQAEEYELLAELAR 299

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039772804 386 VEKKLKEQKALLEEgFKKKAEEMDGEIQQLKHNIEDMKKKQ 426
Cdd:COG1196   300 LEQDIARLEERRRE-LEERLEELEEELAELEEELEELEEEL 339
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 322-407 4.46e-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: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 322 QKAIAEERTKKEAAEKEQDllRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLK-EQKALLEEG 400
Cdd:pfam11600  43 EEAKAEKERAKEEARRKKE--EEKELKEKERREKKEKDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKeEEKRLKEEE 120


                  ....*..
gi 1039772804 401 FKKKAEE 407
Cdd:pfam11600 121 KRIKAEK 127
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
 323-438 4.78e-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: 39.54  E-value: 4.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  323 KAIAEERTKKEaaEKEQDL---------LRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQ 393
Cdd:pfam15818  239 KKINEEITHIQ--EEKQDIiisfqhmqqLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHE 316

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1039772804  394 KALleEGFKKKAEEMDGEIQQLKHNIEDMKKKQwFHFRYYYKRSC 438
Cdd:pfam15818  317 KAL--GTWKKHVEELNGEINEIKNELSSLKETH-IKLQEHYNKLC 358
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 317-415 5.12e-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: 37.46  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 317 ALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEymEAQEKRnKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKAL 396
Cdd:COG0711    28 ALDERQEKIADGLAEAERAKEEAEAALAEYEEKLA--EARAEA-AEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAE 104

                          90
                  ....*....|....*....
gi 1039772804 397 LEEGFKKKAEEMDGEIQQL 415
Cdd:COG0711   105 IEQERAKALAELRAEVADL 123
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 322-407 5.61e-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: 39.16  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 322 QKAIAEERTKKEAAE---KEQDLLRQKQKEQQEYMEAQEKRNKENIEQL----RRKLEQEREQLIKdhnMMVEKKLKEQK 394
Cdd:pfam15709 413 QLQAAQERARQQQEEfrrKLQELQRKKQQEEAERAEAEKQRQKELEMQLaeeqKRLMEMAEEERLE---YQRQKQEAEEK 489

                          90
                  ....*....|....
gi 1039772804 395 ALLE-EGFKKKAEE 407
Cdd:pfam15709 490 ARLEaEERRQKEEE 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-426 5.81e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 307 IESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEymEAQEKRNKENIEQLRRK-LEQEREQLIKDHNMM 385
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA--ELARLEQDIARLEERRReLEERLEELEEELAEL 328

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039772804 386 VEKKLKEQKALLEEgfKKKAEEMDGEIQQLKHNIEDMKKKQ 426
Cdd:COG1196   329 EEELEELEEELEEL--EEELEEAEEELEEAEAELAEAEEAL 367
PRK12704 PRK12704
phosphodiesterase; Provisional
 331-408 6.04e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 331 KKEAAEKEQDLLRQKQKE---QQEYMEAQEKRNKENIEQLRRKLE--------QEREQLIKDhnmmVEKKLKEQKALL-- 397
Cdd:PRK12704  101 KLELLEKREEELEKKEKEleqKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEK----VEEEARHEAAVLik 176

                          90
                  ....*....|....*...
gi 1039772804 398 -------EEGfKKKAEEM 408
Cdd:PRK12704  177 eieeeakEEA-DKKAKEI 193
PRK11637 PRK11637
AmiB activator; Provisional
 320-425 6.31e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 38.91  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804 320 AGQKAIAE-ERTKKEAAEkEQDLLRQKQKEQQEYMEAQeKRNKENIEQLR--RK---------LEQEREQLIK-DHNmmv 386
Cdd:PRK11637  167 ARQETIAElKQTREELAA-QKAELEEKQSQQKTLLYEQ-QAQQQKLEQARneRKktltglessLQKDQQQLSElRAN--- 241

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1039772804 387 EKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKK 425
Cdd:PRK11637  242 ESRLRDSIARAEREAKARAEREAREAARVRDKQKQAKRK 280
PTZ00121 PTZ00121
MAEBL; Provisional
 313-424 7.51e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 7.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  313 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQ-KEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLK 391
Cdd:PTZ00121  1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1039772804  392 EQKALLEEGFKKkAEEMDGEIQQLKHNIEDMKK 424
Cdd:PTZ00121  1603 EEKKMKAEEAKK-AEEAKIKAEELKKAEEEKKK 1634
PTZ00121 PTZ00121
MAEBL; Provisional
 292-425 7.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 7.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  292 KAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKK---EAAEKEQDLLRQKQKEQQEYMEAQEKRNKE--NIEQ 366
Cdd:PTZ00121  1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAdeaEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkKADE 1395

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039772804  367 LRRKLEQER---EQLIKDHNmmVEKKLKEQKALLEEgfKKKAEEMDGEIQQlKHNIEDMKKK 425
Cdd:PTZ00121  1396 AKKKAEEDKkkaDELKKAAA--AKKKADEAKKKAEE--KKKADEAKKKAEE-AKKADEAKKK 1452
PTZ00121 PTZ00121
MAEBL; Provisional
 320-426 7.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 7.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772804  320 AGQKAIAEERTKKEAAEKEQDLLR-QKQKEQQEYMEAQEKRNKENI---EQLR-----RKLEQEREQLiKDHNMMV---- 386
Cdd:PTZ00121  1506 AEAKKKADEAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELkkaEELKkaeekKKAEEAKKAE-EDKNMALrkae 1584

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1039772804  387 ------EKKLKEQKALLEEGFKKKAEEMDGEiQQLKHNIEDMKKKQ 426
Cdd:PTZ00121  1585 eakkaeEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAE 1629
 
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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