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Conserved domains on  [gi|568936338|ref|XP_006535344|]
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guanylate binding protein 8 isoform X1 [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 ...
206-493 1.19e-148

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: 397124 [Multi-domain]  Cd Length: 297  Bit Score: 427.47  E-value: 1.19e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  206 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 285
Cdd:pfam02841   8 PRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKEAIAVFMK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  286 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 363
Cdd:pfam02841  88 RSFKDENQEFQKELVELLEKKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKLEAKYNQV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  364 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 443
Cdd:pfam02841 168 PRKGVKAEEVLQEFLKSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQ 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 568936338  444 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 493
Cdd:pfam02841 248 LIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
16-207 7.44e-110

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member pfam02263:

Pssm-ID: 453896  Cd Length: 260  Bit Score: 327.41  E-value: 7.44e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   16 NEHLSVNHEAIEILEKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTELirakSSPNPDGIKNSTEFVSFFPDFV 175
Cdd:pfam02263  81 TEGLGDVEQSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156
                         170       180       190
                  ....*....|....*....|....*....|..
gi 568936338  176 WTVRDFMLELKLNGEDITSDEYLENALKLIPG 207
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQG 188
 
Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
206-493 1.19e-148

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: 397124 [Multi-domain]  Cd Length: 297  Bit Score: 427.47  E-value: 1.19e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  206 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 285
Cdd:pfam02841   8 PRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKEAIAVFMK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  286 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 363
Cdd:pfam02841  88 RSFKDENQEFQKELVELLEKKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKLEAKYNQV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  364 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 443
Cdd:pfam02841 168 PRKGVKAEEVLQEFLKSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQ 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 568936338  444 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 493
Cdd:pfam02841 248 LIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
206-493 8.74e-141

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: 407.35  E-value: 8.74e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 206 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 285
Cdd:cd16269    2 RRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFMK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 286 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 363
Cdd:cd16269   82 RSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 364 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 443
Cdd:cd16269  162 PRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQ 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568936338 444 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 493
Cdd:cd16269  242 LKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
16-207 7.44e-110

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: 426686  Cd Length: 260  Bit Score: 327.41  E-value: 7.44e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   16 NEHLSVNHEAIEILEKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTELirakSSPNPDGIKNSTEFVSFFPDFV 175
Cdd:pfam02263  81 TEGLGDVEQSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156
                         170       180       190
                  ....*....|....*....|....*....|..
gi 568936338  176 WTVRDFMLELKLNGEDITSDEYLENALKLIPG 207
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQG 188
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
30-217 1.26e-59

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: 196.39  E-value: 1.26e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  30 EKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCMPHP--TKPEHTLVLLDTEGLGDVEKGDP 107
Cdd:cd01851    1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 108 KNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTElirakSSPNPDGIKNsteFVSFFPDFVWTVRDFMLELKL 187
Cdd:cd01851   81 ENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPL 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568936338 188 NGEDITS-----DEYLENALKLIPGLGILVTTYVD 217
Cdd:cd01851  153 EGLDVTEksetlIEELNKIWSSIRKPFTPITCFVL 187
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
403-503 3.56e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.50  E-value: 3.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 403 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENiEQLRRKLEQEREQLIKdhnmmvEKKLKEQKALLEEGFKKKA 482
Cdd:PRK09510  77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALK------QKQAEEAAAKAAAAAKAKA 149
                         90       100
                 ....*....|....*....|.
gi 568936338 483 EEMDGEIQQLKHNIEDMKKKQ 503
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKK 170
TolA COG3064
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
369-491 2.82e-05

Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225606 [Multi-domain]  Cd Length: 387  Bit Score: 46.48  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 369 KAREVFQSFLQSQAIIESSILQADTaltagQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKL 448
Cdd:COG3064   84 KEEQVAEELKPKQAAEQERLKQLEK-----ERLKAQEQQKQAEEAEKQAQLEQKQQEEQARKAAAEQKKKAEAAKAKAAA 158
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568936338 449 EQEREQLIKDhnmmvEKKLKEQKALLEEGFKKKAEEMDGEIQQ 491
Cdd:COG3064  159 EAAKLKAAAE-----AKKKAEEAAKAAEEAKAKAEAAAAKKKA 196
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
359-503 3.69e-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: 42.91  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  359 DYWQVPRKGVKAREVFQSFLQSQAIIESSI----LQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQE 434
Cdd:TIGR02794  23 LYHSVKPEPGGGAEIIQAVLVDPGAVAQQAnriqQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEK 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936338  435 KrnKENIEQLRRKLEQEREQLIKdhnmMVEKKLKEQKALLEEGFKKKAEEM---DGEIQQLKHNIEDMKKKQ 503
Cdd:TIGR02794 103 A--AKQAEQAAKQAEEKQKQAEE----AKAKQAAEAKAKAEAEAERKAKEEaakQAEEEAKAKAAAEAKKKA 168
YeeP COG3596
Predicted GTPase [General function prediction only];
23-108 7.91e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 226124 [Multi-domain]  Cd Length: 296  Bit Score: 38.23  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  23 HEAIEILEKISQPVVVVAIVGLYRTGKSYLMNRLAGQNhGFP---LGSTVQSQTKGIwmwcmphPTKPEHTLVLLDTEGL 99
Cdd:COG3596   26 LEQLRMLQLTEKEPVNVLLMGATGAGKSSLINALFQGE-VKEvskVGVGTDITTRLR-------LSYDGENLVLWDTPGL 97

                 ....*....
gi 568936338 100 GDVEKGDPK 108
Cdd:COG3596   98 GDGKDKDAE 106
 
Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
206-493 1.19e-148

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: 397124 [Multi-domain]  Cd Length: 297  Bit Score: 427.47  E-value: 1.19e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  206 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 285
Cdd:pfam02841   8 PRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKEAIAVFMK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  286 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 363
Cdd:pfam02841  88 RSFKDENQEFQKELVELLEKKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKLEAKYNQV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  364 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 443
Cdd:pfam02841 168 PRKGVKAEEVLQEFLKSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQ 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 568936338  444 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 493
Cdd:pfam02841 248 LIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
206-493 8.74e-141

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: 407.35  E-value: 8.74e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 206 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 285
Cdd:cd16269    2 RRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFMK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 286 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 363
Cdd:cd16269   82 RSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 364 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 443
Cdd:cd16269  162 PRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQ 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568936338 444 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 493
Cdd:cd16269  242 LKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
16-207 7.44e-110

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: 426686  Cd Length: 260  Bit Score: 327.41  E-value: 7.44e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   16 NEHLSVNHEAIEILEKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTELirakSSPNPDGIKNSTEFVSFFPDFV 175
Cdd:pfam02263  81 TEGLGDVEQSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156
                         170       180       190
                  ....*....|....*....|....*....|..
gi 568936338  176 WTVRDFMLELKLNGEDITSDEYLENALKLIPG 207
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQG 188
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
30-217 1.26e-59

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: 196.39  E-value: 1.26e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  30 EKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCMPHP--TKPEHTLVLLDTEGLGDVEKGDP 107
Cdd:cd01851    1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 108 KNDLWIFALSVLLSSTFIYNSMNTISHDSLEKLHYVTELTElirakSSPNPDGIKNsteFVSFFPDFVWTVRDFMLELKL 187
Cdd:cd01851   81 ENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPL 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568936338 188 NGEDITS-----DEYLENALKLIPGLGILVTTYVD 217
Cdd:cd01851  153 EGLDVTEksetlIEELNKIWSSIRKPFTPITCFVL 187
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
40-115 1.16e-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: 1.16e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936338  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 ...
405-501 1.60e-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: 53.97  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  405 ERTKKEAAEKEQDL--LRQKQKEQ--QEYMEAQEKRNKENIEQLRRK-----LEQEREQLIKDHN--MMVEKKLKE-QKA 472
Cdd:pfam17380 449 ERVRLEEQERQQQVerLRQQEEERkrKKLELEKEKRDRKRAEEQRRKilekeLEERKQAMIEEERkrKLLEKEMEErQKA 528
                          90       100       110
                  ....*....|....*....|....*....|..
gi 568936338  473 LLEEGFKKKAEE---MDGEIQQLKHNIEDMKK 501
Cdd:pfam17380 529 IYEEERRREAEEerrKQQEMEERRRIQEQMRK 560
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
403-503 3.56e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.50  E-value: 3.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 403 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENiEQLRRKLEQEREQLIKdhnmmvEKKLKEQKALLEEGFKKKA 482
Cdd:PRK09510  77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALK------QKQAEEAAAKAAAAAKAKA 149
                         90       100
                 ....*....|....*....|.
gi 568936338 483 EEMDGEIQQLKHNIEDMKKKQ 503
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKK 170
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
227-497 2.43e-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: 50.61  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   227 VDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVE-LIGE 305
Cdd:pfam12128  453 LNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqLFPQ 532
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   306 AKVLFLLKNEEASD------KYCQEELdRLSKDLMDNISTFSVPGGHRLY---MDMrEKIEHDYW-----QVPRKGVKAR 371
Cdd:pfam12128  533 AGTLLHFLRKEAPDweqsigKVISPEL-LHRTDLDPEVWDGSVGGELNLYgvkLDL-KRIDVPEWaaseeELRERLDKAE 610
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   372 EVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQE 451
Cdd:pfam12128  611 EALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ 690
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 568936338   452 REQLIKDHNMMVE---KKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIE 497
Cdd:pfam12128  691 LKQLDKKHQAWLEeqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIA 739
PTZ00121 PTZ00121
MAEBL; Provisional
369-502 4.25e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 4.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  369 KAREVFQSFLQSQAIIESSILQAD--------TALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRnkeN 440
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEelkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK---K 1703
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936338  441 IEQLRRKLEQER---EQLIKDHNmmvEKKLK-EQKALLEEGFKKKAEEM---DGEIQQLKHNIEDMKKK 502
Cdd:PTZ00121 1704 AEELKKKEAEEKkkaEELKKAEE---ENKIKaEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLKKEEEKK 1769
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ...
404-491 8.34e-06

MAP7 (E-MAP-115) family; The organisation 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-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 428577 [Multi-domain]  Cd Length: 153  Bit Score: 45.78  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  404 EERTKKEAAEKEQDLLRQKQKEQQEYMEaQEKRNKENIEQLRRKLEQEREQLikdhnMMVEKKLKEQKALLEEGFKKKAE 483
Cdd:pfam05672   9 AEEAARILAEKRRQAREQREREEQERLE-KEEEERLRREELRRRAEEERARR-----EEEARRLEEERKREEEERQRKAE 82

                  ....*...
gi 568936338  484 EMDGEIQQ 491
Cdd:pfam05672  83 EEAEEKEQ 90
PTZ00121 PTZ00121
MAEBL; Provisional
368-503 9.25e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 9.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  368 VKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKEniEQLRRK 447
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA--EALKKE 1697
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568936338  448 LEQER--EQLIKDHNMmvEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 503
Cdd:PTZ00121 1698 AEEAKkaEELKKKEAE--EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
401-484 1.01e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.88  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 401 AIAEE-----RTKKEAAEKEQdlLRQKQKEQQeymeAQEKRNKENIEQLR-RKLEQEREQLIKdhnmmvEKKLKEQKALL 474
Cdd:PRK09510  59 AVVEQynrqqQQQKSAKRAEE--QRKKKEQQQ----AEELQQKQAAEQERlKQLEKERLAAQE------QKKQAEEAAKQ 126
                         90
                 ....*....|
gi 568936338 475 EEGFKKKAEE 484
Cdd:PRK09510 127 AALKQKQAEE 136
PTZ00121 PTZ00121
MAEBL; Provisional
400-502 1.31e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  400 KAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEK-RNKENIEQLRRKLEQEReqliKDHNMmveKKLKEQKALLEEgF 478
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAK----KAEEA---KKKAEEAKKADE-A 1475
                          90       100
                  ....*....|....*....|....
gi 568936338  479 KKKAEEMDgEIQQLKHNIEDMKKK 502
Cdd:PTZ00121 1476 KKKAEEAK-KADEAKKKAEEAKKK 1498
PRK12704 PRK12704
phosphodiesterase; Provisional
409-503 1.46e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 409 KEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMvEKKLKEQKALLE---EGFKKKAEEM 485
Cdd:PRK12704  34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKL-EKRLLQKEENLDrklELLEKREEEL 112
                         90
                 ....*....|....*...
gi 568936338 486 DGEIQQLKHNIEDMKKKQ 503
Cdd:PRK12704 113 EKKEKELEQKQQELEKKE 130
PTZ00121 PTZ00121
MAEBL; Provisional
353-503 1.76e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  353 REKIEHDYWQVPRKGVKAREVFQSFLQSQAII--ESSILQADTALTAGQKAIAEERTKKEAAEKEQdLLRQKQKEQQEYM 430
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK-VEQLKKKEAEEKK 1647
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936338  431 EAQEKRNKENIEQLRRKLEQEREQlikdhnmmvEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 503
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAE---------EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
PTZ00121 PTZ00121
MAEBL; Provisional
399-498 2.12e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  399 QKAIAEERTKKEAAEKEQ-DLLRQKQKEQQ---EYMEAQEKRNKENIEQLRRKLEQER----------------EQLIKD 458
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKaEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAEEDKkkaeeakkdeeekkkiAHLKKE 1765
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568936338  459 HNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIED 498
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
414-502 2.18e-05

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


Pssm-ID: 433535 [Multi-domain]  Cd Length: 119  Bit Score: 43.72  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  414 KEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKleqerEQLIKDHNMMVEKKLKEQKALLEEGFKKKAEE------MDG 487
Cdd:pfam13863   6 REMFLVQLALDAKREEIQRLEELLKQREEELEKK-----EQELKEDLVKFDKFLKENDAKRRRALKKAEEEtklkkeKEK 80
                          90
                  ....*....|....*
gi 568936338  488 EIQQLKHNIEDMKKK 502
Cdd:pfam13863  81 EIKKLTAQLEELKSE 95
TolA COG3064
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
369-491 2.82e-05

Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225606 [Multi-domain]  Cd Length: 387  Bit Score: 46.48  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 369 KAREVFQSFLQSQAIIESSILQADTaltagQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKL 448
Cdd:COG3064   84 KEEQVAEELKPKQAAEQERLKQLEK-----ERLKAQEQQKQAEEAEKQAQLEQKQQEEQARKAAAEQKKKAEAAKAKAAA 158
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568936338 449 EQEREQLIKDhnmmvEKKLKEQKALLEEGFKKKAEEMDGEIQQ 491
Cdd:COG3064  159 EAAKLKAAAE-----AKKKAEEAAKAAEEAKAKAEAAAAKKKA 196
PTZ00121 PTZ00121
MAEBL; Provisional
390-502 8.18e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 8.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  390 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYME-----AQEKRNKENIEQLRRKLEQEREQLIKDHNMMVE 464
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaakkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568936338  465 KKLKEQKALLEEgFKKKAEEMDgEIQQLKHNIEDMKKK 502
Cdd:PTZ00121 1371 KKKEEAKKKADA-AKKKAEEKK-KADEAKKKAEEDKKK 1406
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
399-505 8.81e-05

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: 45.11  E-value: 8.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  399 QKAIAEERTK---KEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREqliKDHNMMVEKKLKEQKALLE 475
Cdd:pfam17380 486 RKRAEEQRRKileKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERR---KQQEMEERRRIQEQMRKAT 562
                          90       100       110
                  ....*....|....*....|....*....|
gi 568936338  476 EGfKKKAEEMDGEIQQLKHNIEDMKKKQWF 505
Cdd:pfam17380 563 EE-RSRLEAMEREREMMRQIVESEKARAEY 591
TolA COG3064
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
404-484 9.13e-05

Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225606 [Multi-domain]  Cd Length: 387  Bit Score: 44.94  E-value: 9.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 404 EERTKKEAAEKEQdlLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKdhnmmvEKKLKEQKALLEEGFKKKAE 483
Cdd:COG3064   79 QQRKKKEEQVAEE--LKPKQAAEQERLKQLEKERLKAQEQQKQAEEAEKQAQLE------QKQQEEQARKAAAEQKKKAE 150

                 .
gi 568936338 484 E 484
Cdd:COG3064  151 A 151
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
384-503 9.16e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 45.48  E-value: 9.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  384 IESSILQADTALTAGQKAIAE-ERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRK-LEQEREQLIKDHNM 461
Cdd:COG1196   279 LREELEELQEELLELKEEIEElEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEEREtLLEELEQLLAELEE 358
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568936338  462 MV---EKKLKEQKALLEEGFKKKAEEMD----------GEIQQLKHNIEDMKKKQ 503
Cdd:COG1196   359 AKeelEEKLSALLEELEELFEALREELAeleaelaeirNELEELKREIESLEERL 413
PTZ00121 PTZ00121
MAEBL; Provisional
390-502 9.38e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 9.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  390 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMM-VEKKLK 468
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkAEEAKK 1614
                          90       100       110
                  ....*....|....*....|....*....|....
gi 568936338  469 EQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKK 502
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
209-486 1.38e-04

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


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 44.33  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 209 GILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQraadhySEQMVQRLSLPTDTLQELLDVHAACEKEAMAVfmEHSF 288
Cdd:COG4942   11 RMLGTILLASLLSAAVLAAAFSAAADDKQLKQIQKE------IAALEKKIREQQDQRAKLEKQLKSLETEIASL--EAQL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 289 KdENQQFLKKLveligEAKVLFLLKNEEASDKYCQEELDRLSKDL-MDNISTFSVPGGHRLYmdmrekiEHDywqvPRKG 367
Cdd:COG4942   83 I-ETADDLKKL-----RKQIADLNARLNALEVQEREQRRRLAEQLaALQRSGRNPPPALLVS-------PED----AQRS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 368 VKAREVFQSFLQSqaiiessILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRK 447
Cdd:COG4942  146 VRLAIYYGALNPA-------RAERIDALKATLKQLAAVRAEIAAEQAELTTLLSEQRAQQAKLAQLLEERKKTLAQLNSE 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568936338 448 LEQER---EQLIKDhnmmvEKKLKEQKALLEEGFKKKAEEMD 486
Cdd:COG4942  219 LSADQkklEELRAN-----ESRLKNEIASAEAAAAKAREAAA 255
PRK12704 PRK12704
phosphodiesterase; Provisional
379-485 2.21e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 379 QSQAIIESSILQADT----ALTAGQKAIAEERTK--KEAAEKEQDLLRQKQKEQQEymEAQEKRNKENIEQLRRKLEQER 452
Cdd:PRK12704  39 EAKRILEEAKKEAEAikkeALLEAKEEIHKLRNEfeKELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKKE 116
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568936338 453 EQLIKDhnmmvEKKLKEQKALLEEGFKKKAEEM 485
Cdd:PRK12704 117 KELEQK-----QQELEKKEEELEELIEEQLQEL 144
TolA COG3064
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
378-502 2.25e-04

Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225606 [Multi-domain]  Cd Length: 387  Bit Score: 43.40  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 378 LQSQaiiESSILQADTALTAGQKAIAEERTKKEAAEKEQdlLRQKQKEQQEymeAQEKRnKENIEQLRRKLEQEREQLIK 457
Cdd:COG3064   67 IQSQ---QSSAKKGEQQRKKKEEQVAEELKPKQAAEQER--LKQLEKERLK---AQEQQ-KQAEEAEKQAQLEQKQQEEQ 137
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568936338 458 DHNMMVEKKLKEQKAL---LEEGFKKKA-EEMDGEIQQLKHNIEDMKKK 502
Cdd:COG3064  138 ARKAAAEQKKKAEAAKakaAAEAAKLKAaAEAKKKAEEAAKAAEEAKAK 186
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
384-502 3.55e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.55  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  384 IESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQK---QKEQQEYMEAQEKRNKENIEQLRRKLEQEREQL----- 455
Cdd:COG1196   763 LEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEEleeAERRLDALERELESLEQRRERLEQEIEELEEEIeelee 842
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568936338  456 ----IKDHNMMVEKKLKEQKALLEE-------------GFKKKAEEMDGEIQQLKHNIEDMKKK 502
Cdd:COG1196   843 kldeLEEELEELEKELEELKEELEEleaekeeledelkELEEEKEELEEELRELESELAELKEE 906
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
359-503 3.69e-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: 42.91  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  359 DYWQVPRKGVKAREVFQSFLQSQAIIESSI----LQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQE 434
Cdd:TIGR02794  23 LYHSVKPEPGGGAEIIQAVLVDPGAVAQQAnriqQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEK 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936338  435 KrnKENIEQLRRKLEQEREQLIKdhnmMVEKKLKEQKALLEEGFKKKAEEM---DGEIQQLKHNIEDMKKKQ 503
Cdd:TIGR02794 103 A--AKQAEQAAKQAEEKQKQAEE----AKAKQAAEAKAKAEAEAERKAKEEaakQAEEEAKAKAAAEAKKKA 168
PTZ00121 PTZ00121
MAEBL; Provisional
390-502 4.36e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  390 QADTALTAGQKAIAEERtKKEAAEKEQDLLRQKQKEQQEYMEAQEK--RNKENIEQLRRKLEQEREQLIKDHNMMVEKKL 467
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEK-KKEEAKKKADAAKKKAEEKKKADEAKKKaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKA 1433
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568936338  468 KEQKALLEEgfKKKAEEMDGEIQQlKHNIEDMKKK 502
Cdd:PTZ00121 1434 DEAKKKAEE--AKKADEAKKKAEE-AKKAEEAKKK 1465
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
399-484 4.99e-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: 40.83  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  399 QKAIAEERTKKEAAEKEQDllRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLK-EQKALLEEG 477
Cdd:pfam11600  43 EEAKAEKERAKEEARRKKE--EEKELKEKERREKKEKDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKeEEKRLKEEE 120

                  ....*..
gi 568936338  478 FKKKAEE 484
Cdd:pfam11600 121 KRIKAEK 127
PTZ00121 PTZ00121
MAEBL; Provisional
400-502 5.04e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 5.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  400 KAIAEERTKK-EAAEKEQDLLRQKQKEQQEYMEAQEKRN---KENIEQLRRKLEQERE-QLIKDHNMMVEKKLKEQKALL 474
Cdd:PTZ00121 1335 KKKAEEAKKAaEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAA 1414
                          90       100
                  ....*....|....*....|....*...
gi 568936338  475 EEgfKKKAEEMDGEIQQLKhNIEDMKKK 502
Cdd:PTZ00121 1415 AA--KKKADEAKKKAEEKK-KADEAKKK 1439
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
394-476 5.08e-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: 40.46  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  394 ALTAGQKAIAE-----ERTKKEAA---EKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEK 465
Cdd:TIGR01144  23 AIETRQKKIADglasaERAKKEAAlaqKKAQVILKEAKDEAQEIIENANKRGSEILEEAKAEAREEREKIKAQARAEIEA 102
                          90
                  ....*....|..
gi 568936338  466 KLKE-QKALLEE 476
Cdd:TIGR01144 103 EKEQaREELRKQ 114
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
385-502 5.76e-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: 42.74  E-value: 5.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   385 ESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQK---QKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNM 461
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 568936338   462 MVEKK-----LKEQKALLE---EGFKKKAEEMDGEIQQLKHNIEDMKKK 502
Cdd:TIGR02168  332 LDELAeelaeLEEKLEELKeelESLEAELEELEAELEELESRLEELEEQ 380
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
400-523 6.40e-04

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: 434960 [Multi-domain]  Cd Length: 1050  Bit Score: 42.57  E-value: 6.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   400 KAIAEERTKKEAAEKE--------QDLLRQKQKEQQEyMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQK 471
Cdd:pfam15818  239 KKINEEITHIQEEKQDiiisfqhmQQLLQQQTQANTE-MEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEK 317
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568936338   472 ALleEGFKKKAEEMDGEIQQLKHNIEDMKKKQwFHFRYYYKRSCFIYFFSHF 523
Cdd:pfam15818  318 AL--GTWKKHVEELNGEINEIKNELSSLKETH-IKLQEHYNKLCNQKKLEED 366
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
411-503 6.78e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.10  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 411 AAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLikdhnmmvekKLKEQKALLEEGFKKKAEEMDGEIQ 490
Cdd:PRK09510  59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERL----------KQLEKERLAAQEQKKQAEEAAKQAA 128
                         90
                 ....*....|...
gi 568936338 491 QLKHNIEDMKKKQ 503
Cdd:PRK09510 129 LKQKQAEEAAAKA 141
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
409-503 7.85e-04

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 425860 [Multi-domain]  Cd Length: 247  Bit Score: 41.08  E-value: 7.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  409 KEAAEKEQDLLRQKQKE--------QQEYMEAQEK------------RNKENIEQLRRKLEQEREQLIKDHNM-MVEKKL 467
Cdd:pfam00769   1 REEAEREKQELEERLKQyeeetrkaQEELEESEETaelleeklrvaeEEAELLEQKAQEAEEEKERLEESAEMeAEEKEQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568936338  468 KEQK--------ALLEEGFKKKAEEMDgeiqQLKHNIEDMKKKQ 503
Cdd:pfam00769  81 LERElreaqeevARLEEESERKEEEAE----RLQEELEEAREEE 120
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
385-501 7.92e-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: 42.05  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  385 ESSILQADTALTAGQKAIAEERTKKEA--------AEKEQDLLRQKQKEQQEY-MEAQEKRNKENIE--------QLRRK 447
Cdd:pfam09731 286 NSLIAHAHREIDQLSKKLAELKKREEKhieralekQKEELDKLAEELSARLEEvRAADEAQLRLEFErereeireSYEEK 365
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936338  448 LEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKK-----AEEMDGEIQQL---KHNIEDMKK 501
Cdd:pfam09731 366 LRTELERQAEAHEEHLKDVLVEQEIELQREFLQDikekvEEERAGRLLKLnelLANLKGLEK 427
PTZ00121 PTZ00121
MAEBL; Provisional
397-501 9.48e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 9.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  397 AGQKAIAEErTKKEAAEKEQ-DLLRQKQKEQQEYMEAQEK-RNKENIEQLRRKLEQEREQlikdhnmmVEKKLKEQKALL 474
Cdd:PTZ00121 1414 AAAKKKADE-AKKKAEEKKKaDEAKKKAEEAKKADEAKKKaEEAKKAEEAKKKAEEAKKA--------DEAKKKAEEAKK 1484
                          90       100
                  ....*....|....*....|....*..
gi 568936338  475 EEGFKKKAEEMDGEIQQLKHNIEDMKK 501
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKADEAKKAAEAKKK 1511
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
399-483 1.04e-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: 41.37  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  399 QKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKEN-------IEQLRRKLEQEREQLIKDHNmmvEKKLKEQK 471
Cdd:TIGR02794  96 QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEaeaerkaKEEAAKQAEEEAKAKAAAEA---KKKAEEAK 172
                          90
                  ....*....|..
gi 568936338  472 ALLEEGFKKKAE 483
Cdd:TIGR02794 173 KKAEAEAKAKAE 184
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
290-503 1.12e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.62  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  290 DENQQFLKKLVELIGEAKVLFLLKNEEASDKycQEELDRLSKDLMD---NIstfsvpgghRLYMDMREKIEHDYWQVPRK 366
Cdd:COG1196   256 EELQEELEEAEKEIEELKSELEELREELEEL--QEELLELKEEIEElegEI---------SLLRERLEELENELEELEER 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  367 GVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRR 446
Cdd:COG1196   325 LEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKR 404
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568936338  447 KLEQEREQLIKDHNMM--VEKKLKEQKALLEEgFKKKAEEMDGEIQQLKHNIEDMKKKQ 503
Cdd:COG1196   405 EIESLEERLERLSERLedLKEELKELEAELEE-LQTELEELNEELEELEEQLEELRDRL 462
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion];
399-502 1.12e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion];


Pssm-ID: 223783 [Multi-domain]  Cd Length: 161  Bit Score: 39.59  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 399 QKAIAEERTKKEAAEKEQDLLRQKQKEQQEymEAQEKRnKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGF 478
Cdd:COG0711   39 QAKIADDLAEAERLKEEAQALLAEYEQELE--EAREQA-SEIIEQAKKEAEQIAEEIKAEAEEELERIKEAAEAEIEAEK 115
                         90       100
                 ....*....|....*....|....*
gi 568936338 479 KKKAEEMDGEIQQLKHNI-EDMKKK 502
Cdd:COG0711  116 ERALEELRAEVAELAVAIaEKLLGK 140
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
291-503 1.13e-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: 41.65  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  291 ENQqFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNistfsvpgghrlyMDMREKIEhdywqvprKGVKA 370
Cdd:pfam17380 267 ENE-FLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE-------------VERRRKLE--------EAEKA 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  371 RevfQSFLQSQAIIessilQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQ---------KEQQEYMEAQEK--RNKE 439
Cdd:pfam17380 325 R---QAEMDRQAAI-----YAEQERMAMERERELERIRQEERKRELERIRQEEiameisrmrELERLQMERQQKneRVRQ 396
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936338  440 NIEQLRRK--LEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLKhnIEDMKKKQ 503
Cdd:pfam17380 397 ELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR--LEEQERQQ 460
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
273-503 1.14e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 41.67  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 273 AACEKEAMAVFMEHSFKDENQQFLKKLVELIGEAKVLFllknEEASDKYCQEELDRLSkDLMDNIStfSVPGGHRLYMDM 352
Cdd:COG0419  512 ELEEELIELLELEEALKEELEEKLEKLENLLEELEELK----EKLQLQQLKEELRQLE-DRLQELK--ELLEELRLLRTR 584
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 353 REKIEhdywqvprkgvKAREVFQSFLQSQAIIESSILQADTALTAGQkaIAEERTKKEAAEKEQDLLRQKQKEQQEYMEA 432
Cdd:COG0419  585 KEELE-----------ELRERLKELKKKLKELEERLSQLEELLQSLE--LSEAENELEEAEEELESELEKLNLQAELEEL 651
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 433 ------QEKRNKENIEQLRRKLEQEREQLIKDHNMM-----VEKKLKEQKALLEEgFKKKAEEMDGEIQQLKHNIEDMKK 501
Cdd:COG0419  652 lqaaleELEEKVEELEAEIRRELQRIENEEQLEEKLeeleqLEEELEQLREELEE-LLKKLGEIEQLIEELESRKAELEE 730

                 ..
gi 568936338 502 KQ 503
Cdd:COG0419  731 LK 732
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
390-491 1.22e-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: 41.53  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  390 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQ---EYMEAQEKRNKENIeQLRRKLEQEREQLIKDHNMMVEKK 466
Cdd:pfam05262 221 ELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKnlpKPADTSSPKEDKQV-AENQKREIEKAQIEIKKNDEEALK 299
                          90       100
                  ....*....|....*....|....*
gi 568936338  467 LKEQKAlleEGFKKKAEEMDGEIQQ 491
Cdd:pfam05262 300 AKDHKA---FDLKQESKASEKEAED 321
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
406-503 1.39e-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: 41.59  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   406 RTKKEAAEKEQDLLRQKQK--------------EQQEYMEAQEKRNKENIEQLRRKLEQ------EREQLIKDHNMMVEK 465
Cdd:TIGR02169  204 RREREKAERYQALLKEKREyegyellkekealeRQKEAIERQLASLEEELEKLTEEISElekrleEIEQLLEELNKKIKD 283
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568936338   466 KLKEQKAlleeGFKKKAEEMDGEIQQLKHNIEDMKKKQ 503
Cdd:TIGR02169  284 LGEEEQL----RVKEKIGELEAEIASLERSIAEKEREL 317
PTZ00121 PTZ00121
MAEBL; Provisional
403-502 1.44e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  403 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKA 482
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA 1324
                          90       100
                  ....*....|....*....|
gi 568936338  483 EEMDGEIQQLKHNIEDMKKK 502
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKA 1344
PTZ00121 PTZ00121
MAEBL; Provisional
390-502 1.49e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  390 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRN--KENIEQLRRKLEQEREQLIKDHNMMVEKKL 467
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAaaKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568936338  468 KEQKALLEEgfKKKAEEMDGEIQQlKHNIEDMKKK 502
Cdd:PTZ00121 1447 DEAKKKAEE--AKKAEEAKKKAEE-AKKADEAKKK 1478
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
383-503 1.54e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 383 IIESSILQAdtaLTAGQKAIAEERTKKEAAEKEQDLLRQKQkEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMM 462
Cdd:PRK00409 521 LIASLEELE---RELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568936338 463 VEKKLKEQKAlleegfkKKAEEMdgeIQQLKHNIEDMKKKQ 503
Cdd:PRK00409 597 QKGGYASVKA-------HELIEA---RKRLNKANEKKEKKK 627
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
399-503 1.55e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 399 QKAIAEERTKKEAAEKE--QDLLRQKQKEQQEYMEAQEKRNKENIEQlrrklEQEREQLIKDHNMMVEKKLKEQKALLEE 476
Cdd:PRK09510  85 EQQQAEELQQKQAAEQErlKQLEKERLAAQEQKKQAEEAAKQAALKQ-----KQAEEAAAKAAAAAKAKAEAEAKRAAAA 159
                         90       100
                 ....*....|....*....|....*..
gi 568936338 477 gfKKKAEEmdgEIQqlKHNIEDMKKKQ 503
Cdd:PRK09510 160 --AKKAAA---EAK--KKAEAEAAKKA 179
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
365-503 1.58e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 41.28  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 365 RKGVKAREVFQSFLQSQAIIESSILQADTALTAGQ---KAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQeKRNKENI 441
Cdd:COG0419  253 ELKARLLEIESLELEALKIREEELRELERLLEELEekiERLEELEREIEELEEELEGLRALLEELEELLEKL-KSLEERL 331
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936338 442 EQLRRKLE--QEREQLIKDHNMMVEKKLKEQKALLE---EGFKKKAEEMDGEIQQLKHNIEDMKKKQ 503
Cdd:COG0419  332 EKLEEKLEklESELEELAEEKNELAKLLEERLKELEerlEELEKELEKALERLKQLEEAIQELKEEL 398
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
379-472 1.97e-03

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


Pssm-ID: 224755 [Multi-domain]  Cd Length: 225  Bit Score: 39.99  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 379 QSQAIIESSILQADTALTAGQKAIAeertkKEAAEKEQDLLRQKQKEQQEYMEA--QEKRNKENIEQLRRKLEQEREQLI 456
Cdd:COG1842   63 EAQARAEKLEEKAELALQAGNEDLA-----REALEEKQSLEDLAKALEAELQQAeeQVEKLKKQLAALEQKIAELRAKKE 137
                         90
                 ....*....|....*.
gi 568936338 457 kdhnmMVEKKLKEQKA 472
Cdd:COG1842  138 -----ALKARKAAAKA 148
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
404-503 2.02e-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: 38.88  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  404 EERTKKEAAEKEQDLLRQ----KQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKeqkalLEEGFK 479
Cdd:pfam15346  25 EEELEKRKDEIEAEVERRveeaRKIMEKQVLEELEREREAELEEERRKEEEERKKREELERILEENNRK-----IEEAQR 99
                          90       100
                  ....*....|....*....|....*..
gi 568936338  480 KKAEE---MDGEIQQLKHNIEDMKKKQ 503
Cdd:pfam15346 100 KEAEErlaMLEEQRRMKEERQRREKEE 126
PTZ00121 PTZ00121
MAEBL; Provisional
397-503 2.21e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  397 AGQKAIAEERTKKEAAEKEQDLLR-QKQKEQQEYMEAQEKRNKENI---EQLR-----RKLEQEREQLiKDHNMMV---- 463
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELkkaEELKkaeekKKAEEAKKAE-EDKNMALrkae 1584
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568936338  464 ------EKKLKEQKALLEEGFKKKAEEMDGEiQQLKHNIEDMKKKQ 503
Cdd:PTZ00121 1585 eakkaeEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAE 1629
PTZ00121 PTZ00121
MAEBL; Provisional
369-502 2.24e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  369 KAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKK---EAAEKEQDLLRQKQKEQQEYMEAQEKRNKE--NIEQ 443
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAdeaEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkKADE 1395
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936338  444 LRRKLEQER---EQLIKDHNmmVEKKLKEQKALLEEgfKKKAEEMDGEIQQlKHNIEDMKKK 502
Cdd:PTZ00121 1396 AKKKAEEDKkkaDELKKAAA--AKKKADEAKKKAEE--KKKADEAKKKAEE-AKKADEAKKK 1452
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
370-503 2.31e-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 tumor cells.


Pssm-ID: 431106  Cd Length: 713  Bit Score: 40.80  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  370 AREVFQsfLQSQAII---ESSILQADTAltagqkaiaeertkKEAAEKEQDLLR-QKQKEQQEYMEAQEKRNK--ENIEQ 443
Cdd:pfam10168 530 PQECLQ--LLSRATQvfrEEYLKKHDLA--------------REEIQKRVKLLKlQKEQQLQELQSLEEERKSlsERAEK 593
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936338  444 LRRKLE--QEREQLI--KDHNMMveKKLKEQKALL---EEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 503
Cdd:pfam10168 594 LAEKYEeiKDKQEKLmrRCKKVL--QRLNSQLPVLsdaEREMKKELETINEQLKHLANAIKQAKKKM 658
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
405-503 2.45e-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: 40.77  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  405 ERTKKEAAEKEQDLL---RQKQ--KEQQEYMEAQEKRNKENIEQLR-RKLEQEREqlIKDhnmmVEKKLKEQKALLE-EG 477
Cdd:TIGR04523 485 EQKQKELKSKEKELKklnEEKKelEEKVKDLTKKISSLKEKIEKLEsEKKEKESK--ISD----LEDELNKDDFELKkEN 558
                          90       100
                  ....*....|....*....|....*.
gi 568936338  478 FKKKAEEMDGEIQQLKHNIEDMKKKQ 503
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQ 584
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
399-503 2.48e-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: 433539 [Multi-domain]  Cd Length: 341  Bit Score: 40.28  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  399 QKAIAEERTKKEA----------AEKEQDLLRQKQKEQQEYMEAQEKRNKENIE--QLRRKLEQEREQLIKDHNMMVEKK 466
Cdd:pfam13868  88 KRQEEYEEKLQEReqmdeiveriQEEDQAEAEEKLEKQRQLREEIDEFNEEQAKwkELEKEEEKEEDLRILEYLKEKAER 167
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568936338  467 LKEQKALLEEgfkkKAEEMDGEIQQLKHNIEDMKKKQ 503
Cdd:pfam13868 168 EEEREAERRE----IKEEKEREIARLRAQQEKAQDEK 200
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
405-497 2.55e-03

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


Pssm-ID: 406402 [Multi-domain]  Cd Length: 273  Bit Score: 39.91  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  405 ERTKKEAAEKEQDLLRQKQKEQQEYME--AQEKRNKEniEQLRRK-----LEQEREQLikdhnMMVEKK---LKEQKALL 474
Cdd:pfam15991   5 KLSEQMWRALKRHIMRERERKKQEEEAkmEEERLRRE--QEEREKedrmtLEETKEQI-----LKLEEKladLQEEKHQL 77
                          90       100
                  ....*....|....*....|...
gi 568936338  475 EEGFKKKAEEMDGEIQQLKHNIE 497
Cdd:pfam15991  78 FLQLKKVLHEDETRKRQLKEQSE 100
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
399-502 3.28e-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: 433539 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  399 QKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNmmvEKKLKEQKALLEEGF 478
Cdd:pfam13868 242 EEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRREKRLEHRRELEKQIEERE---RQRAAEREEELEEGE 318
                          90       100
                  ....*....|....*....|....
gi 568936338  479 KKKAEEmdgeiQQLKHNIEDMKKK 502
Cdd:pfam13868 319 RLREEE-----AERRERIEEERQK 337
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
369-502 3.38e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 40.13  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 369 KAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKE--AAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRR 446
Cdd:COG0419  509 ELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEklQLQQLKEELRQLEDRLQELKELLEELRLLRTRKEEL 588
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568936338 447 KLEQEREQLIKDHNMMVEKKLKEQKALLEE-GFKKKAEEMDGEIQQLKHNIEDMKKK 502
Cdd:COG0419  589 EELRERLKELKKKLKELEERLSQLEELLQSlELSEAENELEEAEEELESELEKLNLQ 645
PTZ00121 PTZ00121
MAEBL; Provisional
390-501 3.44e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  390 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQ-KEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLK 468
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
                          90       100       110
                  ....*....|....*....|....*....|...
gi 568936338  469 EQKALLEEGFKKkAEEMDGEIQQLKHNIEDMKK 501
Cdd:PTZ00121 1603 EEKKMKAEEAKK-AEEAKIKAEELKKAEEEKKK 1634
PRK12704 PRK12704
phosphodiesterase; Provisional
408-485 4.38e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 408 KKEAAEKEQDLLRQKQKE---QQEYMEAQEKRNKENIEQLRRKLE--------QEREQLIKDhnmmVEKKLKEQKALL-- 474
Cdd:PRK12704 101 KLELLEKREEELEKKEKEleqKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEK----VEEEARHEAAVLik 176
                         90
                 ....*....|....*...
gi 568936338 475 -------EEGfKKKAEEM 485
Cdd:PRK12704 177 eieeeakEEA-DKKAKEI 193
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
392-493 4.53e-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: 39.81  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  392 DTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLeQEREQLIKDhnmmvekkLKEQ- 470
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPEL-TEKESSLID--------LKEHa 505
                          90       100
                  ....*....|....*....|....*
gi 568936338  471 KALLEEGFKK--KAEEMDGEIQQLK 493
Cdd:pfam10174 506 SSLASSGLKKdsKLKSLEIAVEQKK 530
DUF4207 pfam13904
Domain of unknown function (DUF4207); This family is found in eukaryotes; it has several ...
408-503 4.59e-03

Domain of unknown function (DUF4207); This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 433570 [Multi-domain]  Cd Length: 223  Bit Score: 38.54  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  408 KKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ-LRRKLEQE---REQLIKDH---------NMMVEKKLKE-QKAL 473
Cdd:pfam13904  66 KQRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQEwLQRKARQQtkkREESHKQKaaesaskslAKPERKVSQEeAKEV 145
                          90       100       110
                  ....*....|....*....|....*....|
gi 568936338  474 LEEGFKKKAEEmdgEIQQLKHNIEDMKKKQ 503
Cdd:pfam13904 146 LQEWELKKLEQ---QQRKREEEQREQLKKE 172
fliH PRK06669
flagellar assembly protein H; Validated
363-502 4.70e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 38.84  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 363 VPRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQ-KAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKE-- 439
Cdd:PRK06669  12 INKEKLKTHEIQKYRFKVLSIKEKERLREEEEEQVEQlREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEas 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936338 440 -NIEQLRRKLEQEreqlIKDHNMMVEKKLKEQKAL-----LEEGFKKKAEEMDGEIQQLKHNIEDMKKK 502
Cdd:PRK06669  92 sIIEKLQMQIERE----QEEWEEELERLIEEAKAEgyeegYEKGREEGLEEVRELIEQLNKIIEKLIKK 156
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
400-502 4.95e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 39.70  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  400 KAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQlIKDHNMMVEKKLKEQKALLEEG-- 477
Cdd:COG1196   200 KQLEKLERQAEKAERYQELKAELRELELALLLAKLKELRKELEELEEELSRLEEE-LEELQEELEEAEKEIEELKSELee 278
                          90       100
                  ....*....|....*....|....*
gi 568936338  478 FKKKAEEMDGEIQQLKHNIEDMKKK 502
Cdd:COG1196   279 LREELEELQEELLELKEEIEELEGE 303
Utp11 pfam03998
Utp11 protein; This protein is found to be part of a large ribonucleoprotein complex ...
404-481 5.26e-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: 427640  Cd Length: 240  Bit Score: 38.75  E-value: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  404 EERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQ--EREQLIKDhnmmVEKKLKEQKALLEEGFKKK 481
Cdd:pfam03998 145 YFDTDPELLDRRENRLKKDQLESNSLTAATLKKLDKKKEKLYKELKArlEREKELKK----AEQKLELQRALMKKGAKKK 220
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 ...
379-456 5.72e-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: 37.29  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  379 QSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKE-QDLLRQKQKEQQEYMEAQEKRNKENIEQLRR----KLEQERE 453
Cdd:pfam00430  30 KRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEaQEIIENAKKRAEKLKEEIVAAAEAEAERIIEqaaaEIEQEKD 109

                  ...
gi 568936338  454 QLI 456
Cdd:pfam00430 110 RAL 112
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
403-503 6.26e-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: 39.18  E-value: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   403 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRR-KLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKK 481
Cdd:TIGR00618  602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKELLASRQLA 681
                           90       100
                   ....*....|....*....|..
gi 568936338   482 AEEMDGEIQQLKHNIEDMKKKQ 503
Cdd:TIGR00618  682 LQKMQSEKEQLTYWKEMLAQCQ 703
PRK11637 PRK11637
AmiB activator; Provisional
397-502 6.39e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 38.91  E-value: 6.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 397 AGQKAIAE-ERTKKEAAEkEQDLLRQKQKEQQEYMEAQeKRNKENIEQLR--RK---------LEQEREQLIK-DHNmmv 463
Cdd:PRK11637 167 ARQETIAElKQTREELAA-QKAELEEKQSQQKTLLYEQ-QAQQQKLEQARneRKktltglessLQKDQQQLSElRAN--- 241
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568936338 464 EKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKK 502
Cdd:PRK11637 242 ESRLRDSIARAEREAKARAEREAREAARVRDKQKQAKRK 280
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
365-480 6.68e-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: 37.36  E-value: 6.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  365 RKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTK----KEAAEKEQDLLRQK-QKEQQEYMEAQEKRNKE 439
Cdd:pfam11600  16 QRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKkeeeKELKEKERREKKEKdEKEKAEKLRLKEEKRKE 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568936338  440 NIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKK 480
Cdd:pfam11600  96 KQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITRFLQK 136
Caldesmon pfam02029
Caldesmon;
375-497 6.71e-03

Caldesmon;


Pssm-ID: 426572 [Multi-domain]  Cd Length: 490  Bit Score: 39.08  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  375 QSFLQSQAIIESSILQADTALTAGQKAiaeERTKKEAAEKEQ---DLLRQKQKEQQEYMEAQEKRNKEnieqlRRKLEQE 451
Cdd:pfam02029 220 ERTFSQKSLVAEDEEEGAAFLEAEQKL---EELRRRRQEKESqefEKLRQKQQEAELELEELKKKREE-----RRKILEE 291
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568936338  452 REQLIKDhnmmvekklkeqkallEEGFKKKAEEmdGEIQQLKHNIE 497
Cdd:pfam02029 292 EEQRRKQ----------------EEAERKAREE--EEKRRMKEEIE 319
PTZ00121 PTZ00121
MAEBL; Provisional
399-501 6.80e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 6.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  399 QKAIAEERTKKEAAEKEQDLLRQK-----QKEQQEYMEAQEKR----NKENIEQLRRKLEQEREQLIKDHNMMVEKKLKE 469
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKaeeakKEAEEDKKKAEEAKkdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
                          90       100       110
                  ....*....|....*....|....*....|..
gi 568936338  470 QKalleegfKKKAEEMDGEIQQLKHNIEDMKK 501
Cdd:PTZ00121 1788 ED-------EKRRMEVDKKIKDIFDNFANIIE 1812
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
383-502 7.03e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 39.31  E-value: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  383 IIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRN---KENIEQLRRKLEQEREQLIKDH 459
Cdd:COG1196   860 ELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLeelEAKLERLEVELPELEEELEEEY 939
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568936338  460 NMMVEKKLKEQKALLEEGFKK------KAEEmdgEIQQLKHNIEDMKKK 502
Cdd:COG1196   940 EDTLETELEREIERLEEEIEAlgpvnlRAIE---EYEEVEERYEELKSQ 985
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ...
404-491 7.62e-03

MAP7 (E-MAP-115) family; The organisation 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-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 428577 [Multi-domain]  Cd Length: 153  Bit Score: 37.31  E-value: 7.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  404 EERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAE 483
Cdd:pfam05672  40 EERLRREELRRRAEEERARREEEARRLEEERKREEEERQRKAEEEAEEKEQREKEEQERLQKQKEEAEAKAREEAERQRQ 119

                  ....*...
gi 568936338  484 EMDGEIQQ 491
Cdd:pfam05672 120 EREKIMQQ 127
YeeP COG3596
Predicted GTPase [General function prediction only];
23-108 7.91e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 226124 [Multi-domain]  Cd Length: 296  Bit Score: 38.23  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  23 HEAIEILEKISQPVVVVAIVGLYRTGKSYLMNRLAGQNhGFP---LGSTVQSQTKGIwmwcmphPTKPEHTLVLLDTEGL 99
Cdd:COG3596   26 LEQLRMLQLTEKEPVNVLLMGATGAGKSSLINALFQGE-VKEvskVGVGTDITTRLR-------LSYDGENLVLWDTPGL 97

                 ....*....
gi 568936338 100 GDVEKGDPK 108
Cdd:COG3596   98 GDGKDKDAE 106
PTZ00121 PTZ00121
MAEBL; Provisional
374-502 8.49e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  374 FQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQ-----DLLRQKQKEQQEYMEAQEK--RNKENIEQLRR 446
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEekkkaDEAKKKAEEAKKADEAKKKaeEAKKKADAAKK 1336
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568936338  447 KLEQEREqliKDHnmmVEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKK 502
Cdd:PTZ00121 1337 KAEEAKK---AAE---AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
UPF0242 pfam06785
Uncharacterized protein family (UPF0242);
385-502 9.06e-03

Uncharacterized protein family (UPF0242);


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 37.49  E-value: 9.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338  385 ESSILQADTALTAGQKA--IAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNkeniEQLRRKLEQEREQlIKDHNMM 462
Cdd:pfam06785  66 EKSFLEEKEAKLTELDAegFKILEETLEELQSEEERLEEELSQKEEELRRLTEEN----QQLQIQLQQISQD-FAEFRLE 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568936338  463 VEKKLKEQKALLEEgFKKKAEEMDGEIQQLKHNIEDMKKK 502
Cdd:pfam06785 141 SEEQLAEKQLLINE-YQQTIEEQRSVLEKRQDQIENLESK 179
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
399-502 9.38e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.25  E-value: 9.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 399 QKAIAE-ERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRR---KLEQEREQlikdhnmmveKKLKEQKALL 474
Cdd:PRK09510  94 QKQAAEqERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAaaaKAKAEAEA----------KRAAAAAKKA 163
                         90       100
                 ....*....|....*....|....*...
gi 568936338 475 EEGFKKKAEEmdgeiQQLKHNIEDMKKK 502
Cdd:PRK09510 164 AAEAKKKAEA-----EAAKKAAAEAKKK 186
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
385-503 9.80e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 38.59  E-value: 9.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338 385 ESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQ---KEQQEYMEAQEKRNKENIEQLRrKLEQEREQLIKDHNM 461
Cdd:COG0419  473 KELLELYELELEELEEELSREKEEAELREEIEELEKELReleEELIELLELEEALKEELEEKLE-KLENLLEELEELKEK 551
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568936338 462 MVEKKLKEQKALLEEGFKK---------KAEEMDGEIQQLKHNIEDMKKKQ 503
Cdd:COG0419  552 LQLQQLKEELRQLEDRLQElkelleelrLLRTRKEELEELRERLKELKKKL 602
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
401-500 9.95e-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: 38.90  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936338   401 AIAEERTKKEAA--EKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEE-- 476
Cdd:TIGR02169  802 KLEEEVSRIEARlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDle 881
                           90       100
                   ....*....|....*....|....*...
gi 568936338   477 ----GFKKKAEEMDGEIQQLKHNIEDMK 500
Cdd:TIGR02169  882 srlgDLKKERDELEAQLRELERKIEELE 909
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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