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Conserved domains on  [gi|91064876|ref|NP_705792|]
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guanylate-binding protein 5 [Mus musculus]

Protein Classification

guanylate-binding family protein( domain architecture ID 12033579)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 18-281 1.66e-137

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


:

Pssm-ID: 460516  Cd Length: 260  Bit Score: 400.21  E-value: 1.66e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876    18 EGHLVTNQEALKILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKEKGFSVGSTVQSHTKGIWMWCVPHPQKPDHTLVLLD 97
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876    98 TEGLGDVEKDDKKNDTQIFALAILLSSTFVYNTMNKIDQGAIDLLHNVTELTDLLRTRNSSDSNQTEGegpadMSFFPDL 177
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTELSSPRYGRVADSADF-----VSFFPDF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   178 VWTLRDFFLDLQANGHAITSDEYLENSLKLKQGSDERTQTFNLPRLCIQKFFPVKKCFVFDAPALGSKL-SQLPTLSNEE 256
Cdd:pfam02263 156 VWTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALnPQFEGLREDE 235

                         250       260
                  ....*....|....*....|....*
gi 91064876   257 LNSDFVQDLSEFCSHIFTQSKTKTL 281
Cdd:pfam02263 236 LDPEFQQQLREFCSYILSHSLVKTL 260
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 283-561 3.51e-134

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


:

Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 393.19  E-value: 3.51e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   283 GGIQVNGPRLESLVLTYVDAINSGALPSIENTVVTLARRENSAAVQKAIGHYDQLMSEKVQLPTETLQELLDLHRTCERE 362
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   363 AIEIFRKHSFKDEGEFFQKELESLLSAKQDEICKKNADASAALCSTLLGSIFKPLEQEVAQEFYHKPGGHKLFLQRMEQL 442
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   443 KANYRQQPGKGTQAEEVLQTYLNAKETVSRTILQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQ 522
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 91064876   523 HQEQLRQ----IALEKARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:pfam02841 241 YQEHVKQliekMEAEREQLLAEQERMLEHKLQEQEELLKEGFK 283
 
Name Accession Description Interval E-value
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 18-281 1.66e-137

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


Pssm-ID: 460516  Cd Length: 260  Bit Score: 400.21  E-value: 1.66e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876    18 EGHLVTNQEALKILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKEKGFSVGSTVQSHTKGIWMWCVPHPQKPDHTLVLLD 97
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876    98 TEGLGDVEKDDKKNDTQIFALAILLSSTFVYNTMNKIDQGAIDLLHNVTELTDLLRTRNSSDSNQTEGegpadMSFFPDL 177
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTELSSPRYGRVADSADF-----VSFFPDF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   178 VWTLRDFFLDLQANGHAITSDEYLENSLKLKQGSDERTQTFNLPRLCIQKFFPVKKCFVFDAPALGSKL-SQLPTLSNEE 256
Cdd:pfam02263 156 VWTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALnPQFEGLREDE 235

                         250       260
                  ....*....|....*....|....*
gi 91064876   257 LNSDFVQDLSEFCSHIFTQSKTKTL 281
Cdd:pfam02263 236 LDPEFQQQLREFCSYILSHSLVKTL 260
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 283-561 3.51e-134

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


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 393.19  E-value: 3.51e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   283 GGIQVNGPRLESLVLTYVDAINSGALPSIENTVVTLARRENSAAVQKAIGHYDQLMSEKVQLPTETLQELLDLHRTCERE 362
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   363 AIEIFRKHSFKDEGEFFQKELESLLSAKQDEICKKNADASAALCSTLLGSIFKPLEQEVAQEFYHKPGGHKLFLQRMEQL 442
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   443 KANYRQQPGKGTQAEEVLQTYLNAKETVSRTILQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQ 522
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 91064876   523 HQEQLRQ----IALEKARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:pfam02841 241 YQEHVKQliekMEAEREQLLAEQERMLEHKLQEQEELLKEGFK 283
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 289-557 1.10e-114

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: 343.02  E-value: 1.10e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 289 GPRLESLVLTYVDAINSGALPSIENTVVTLARRENSAAVQKAIGHYDQLMSEKVQLPTETLQELLDLHRTCEREAIEIFR 368
Cdd:cd16269   1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 369 KHSFKDEGEFFQKELESLLSAKQDEICKKNADASAALCSTLLGSIFKPLEQEVAQEFYHKPGGHKLFLQRMEQLKANYRQ 448
Cdd:cd16269  81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISQGSYSVPGGYQLYLEDREKLVEKYRQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 449 QPGKGTQAEEVLQTYLNAKETVSRTILQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQLR 528
Cdd:cd16269 161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240

                       250       260       270
                ....*....|....*....|....*....|...
gi 91064876 529 QIAL----EKARVAQEQQWILKQRAQEEADRIK 557
Cdd:cd16269 241 QLKEkmeeERENLLKEQERALESKLKEQEALLE 273
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 32-274 6.12e-70

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


Pssm-ID: 206650  Cd Length: 224  Bit Score: 224.89  E-value: 6.12e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876  32 SAITQPVVVVAIVGLYRTGKSYLMNKLAGKEKGFSVGSTVQSHTKGIWMWCVPHPQ--KPDHTLVLLDTEGLGDVEKDDK 109
Cdd:cd01851   1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKDtdGKKHAVLLLDTEGTDGRERGEF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 110 KNDTQIFALAILLSSTFVYNTMNKIDQGAIDLLHNVTELTDLLrtrnssdsnQTEGEGPADMSFFPDLVWTLRDFFLDLQ 189
Cdd:cd01851  81 ENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTALET---------LGLAGLHNFSKPKPLLLFVVRDFTGPTP 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 190 ANGHAITsdeylenslklkQGSDERTQTFNLPRLCIQKFFPVKKCFVFDAPALGSKLSQLpTLSNEELNSDFVQDLSEFC 269
Cdd:cd01851 152 LEGLDVT------------EKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN-DGRLKDLPPEFRKALKALR 218


                ....*
gi 91064876 270 SHIFT 274
Cdd:cd01851 219 QRFFS 223
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 476-560 1.49e-06

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: 50.61  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   476 QTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQLRQIALEKAR--VAQEQQWILKQRAQEEA 553
Cdd:TIGR02794  51 QANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAkqAEEKQKQAEEAKAKQAA 130


                  ....*..
gi 91064876   554 DRIKAEQ 560
Cdd:TIGR02794 131 EAKAKAE 137
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 432-561 1.97e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 432 HKLFLQRMEQLKANYRQQPGKGTQAEEVLQTYLNAKETVSRTILQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQ 511
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 91064876 512 EEQRKAEMERQHQEQLRQIALEKARVAQEQQwiLKQRAQEEADRIKAEQE 561
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEE--ELEELEEELEEAEEELE 354
YeeP COG3596
Predicted GTPase [General function prediction only];
33-110 6.16e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 45.53  E-value: 6.16e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91064876  33 AITQPVVVVAIVGLYRTGKSYLMNKLAGKEKGfSVGStVQSHTKGIWmwCVPHPQKPDHTLVLLDTEGLGDVEKDDKK 110
Cdd:COG3596  34 LVELPPPVIALVGKTGAGKSSLINALFGAEVA-EVGV-GRPCTREIQ--RYRLESDGLPGLVLLDTPGLGEVNERDRE 107
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 476-561 1.85e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876  476 QTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQ-EQLRQIALEKARVAQEQqwilkQRAQEEAD 554
Cdd:PRK09510  71 QKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQaEEAAKQAALKQKQAEEA-----AAKAAAAA 145


                 ....*..
gi 91064876  555 RIKAEQE 561
Cdd:PRK09510 146 KAKAEAE 152
growth_prot_Scy NF041483
polarized growth protein Scy;
466-559 6.45e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.81  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   466 AKETVSRTILQTDQVLTDKEIQSKAEQERAEAA----RLEAQRleAIRIQEEQRKAEMERQHQEQLRQI-----ALEKAR 536
Cdd:NF041483  522 AEETLERTRAEAERLRAEAEEQAEEVRAAAERAarelREETER--AIAARQAEAAEELTRLHTEAEERLtaaeeALADAR 599

                          90       100
                  ....*....|....*....|...
gi 91064876   537 VAQEQqwiLKQRAQEEADRIKAE 559
Cdd:NF041483  600 AEAER---IRREAAEETERLRTE 619
 
Name Accession Description Interval E-value
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 18-281 1.66e-137

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


Pssm-ID: 460516  Cd Length: 260  Bit Score: 400.21  E-value: 1.66e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876    18 EGHLVTNQEALKILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKEKGFSVGSTVQSHTKGIWMWCVPHPQKPDHTLVLLD 97
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876    98 TEGLGDVEKDDKKNDTQIFALAILLSSTFVYNTMNKIDQGAIDLLHNVTELTDLLRTRNSSDSNQTEGegpadMSFFPDL 177
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTELSSPRYGRVADSADF-----VSFFPDF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   178 VWTLRDFFLDLQANGHAITSDEYLENSLKLKQGSDERTQTFNLPRLCIQKFFPVKKCFVFDAPALGSKL-SQLPTLSNEE 256
Cdd:pfam02263 156 VWTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALnPQFEGLREDE 235

                         250       260
                  ....*....|....*....|....*
gi 91064876   257 LNSDFVQDLSEFCSHIFTQSKTKTL 281
Cdd:pfam02263 236 LDPEFQQQLREFCSYILSHSLVKTL 260
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 283-561 3.51e-134

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


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 393.19  E-value: 3.51e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   283 GGIQVNGPRLESLVLTYVDAINSGALPSIENTVVTLARRENSAAVQKAIGHYDQLMSEKVQLPTETLQELLDLHRTCERE 362
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   363 AIEIFRKHSFKDEGEFFQKELESLLSAKQDEICKKNADASAALCSTLLGSIFKPLEQEVAQEFYHKPGGHKLFLQRMEQL 442
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   443 KANYRQQPGKGTQAEEVLQTYLNAKETVSRTILQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQ 522
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 91064876   523 HQEQLRQ----IALEKARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:pfam02841 241 YQEHVKQliekMEAEREQLLAEQERMLEHKLQEQEELLKEGFK 283
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 289-557 1.10e-114

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: 343.02  E-value: 1.10e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 289 GPRLESLVLTYVDAINSGALPSIENTVVTLARRENSAAVQKAIGHYDQLMSEKVQLPTETLQELLDLHRTCEREAIEIFR 368
Cdd:cd16269   1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 369 KHSFKDEGEFFQKELESLLSAKQDEICKKNADASAALCSTLLGSIFKPLEQEVAQEFYHKPGGHKLFLQRMEQLKANYRQ 448
Cdd:cd16269  81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISQGSYSVPGGYQLYLEDREKLVEKYRQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 449 QPGKGTQAEEVLQTYLNAKETVSRTILQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQLR 528
Cdd:cd16269 161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240

                       250       260       270
                ....*....|....*....|....*....|...
gi 91064876 529 QIAL----EKARVAQEQQWILKQRAQEEADRIK 557
Cdd:cd16269 241 QLKEkmeeERENLLKEQERALESKLKEQEALLE 273
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 32-274 6.12e-70

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


Pssm-ID: 206650  Cd Length: 224  Bit Score: 224.89  E-value: 6.12e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876  32 SAITQPVVVVAIVGLYRTGKSYLMNKLAGKEKGFSVGSTVQSHTKGIWMWCVPHPQ--KPDHTLVLLDTEGLGDVEKDDK 109
Cdd:cd01851   1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKDtdGKKHAVLLLDTEGTDGRERGEF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 110 KNDTQIFALAILLSSTFVYNTMNKIDQGAIDLLHNVTELTDLLrtrnssdsnQTEGEGPADMSFFPDLVWTLRDFFLDLQ 189
Cdd:cd01851  81 ENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTALET---------LGLAGLHNFSKPKPLLLFVVRDFTGPTP 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 190 ANGHAITsdeylenslklkQGSDERTQTFNLPRLCIQKFFPVKKCFVFDAPALGSKLSQLpTLSNEELNSDFVQDLSEFC 269
Cdd:cd01851 152 LEGLDVT------------EKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN-DGRLKDLPPEFRKALKALR 218


                ....*
gi 91064876 270 SHIFT 274
Cdd:cd01851 219 QRFFS 223
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 42-125 1.25e-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: 1.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876  42 AIVGLYRTGKSYLMNKLAGKEkgFSVGSTVQSHTKGIWMWCVPHpQKPDHTLVLLDTEGLGDVEKDDKKNDTQIFA---- 117
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGE--VGEVSDVPGTTRDPDVYVKEL-DKGKVKLVLVDTPGLDEFGGLGREELARLLLrgad 77


                ....*...
gi 91064876 118 LAILLSST 125
Cdd:cd00882  78 LILLVVDS 85
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 475-561 1.12e-07

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 54.57  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   475 LQTDQVLTDKEIQSKAEQE---RAEAARLEAQRLEairiQEEQRKAEMERQHQEQLrQIALEKARVAQEQ-----QWILK 546
Cdd:pfam15709 363 LQQEQLERAEKMREELELEqqrRFEEIRLRKQRLE----EERQRQEEEERKQRLQL-QAAQERARQQQEEfrrklQELQR 437

                          90
                  ....*....|....*
gi 91064876   547 QRAQEEADRIKAEQE 561
Cdd:pfam15709 438 KKQQEEAERAEAEKQ 452
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 476-560 1.49e-06

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: 50.61  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   476 QTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQLRQIALEKAR--VAQEQQWILKQRAQEEA 553
Cdd:TIGR02794  51 QANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAkqAEEKQKQAEEAKAKQAA 130


                  ....*..
gi 91064876   554 DRIKAEQ 560
Cdd:TIGR02794 131 EAKAKAE 137
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 432-561 1.97e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 432 HKLFLQRMEQLKANYRQQPGKGTQAEEVLQTYLNAKETVSRTILQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQ 511
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 91064876 512 EEQRKAEMERQHQEQLRQIALEKARVAQEQQwiLKQRAQEEADRIKAEQE 561
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEE--ELEELEEELEEAEEELE 354
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 484-561 1.08e-05

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 45.80  E-value: 1.08e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91064876   484 KEIQSKAEQERAEAARlEAQRLEAIRIQEEQRKAEMERQHQEQLRQIALEKARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:pfam05672  46 EELRRRAEEERARREE-EARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQERE 122
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 448-561 1.12e-05

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: 47.92  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   448 QQPGKGTQAEEvlqtylNAKETVSRTILQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQ-EQ 526
Cdd:TIGR02794  50 QQANRIQQQKK------PAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQaEE 123

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 91064876   527 LRQIALEKARVAQEQQwiLKQRAQEEADRiKAEQE 561
Cdd:TIGR02794 124 AKAKQAAEAKAKAEAE--AERKAKEEAAK-QAEEE 155
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 437-561 2.11e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 437 QRMEQLKANYRQQpgkGTQAEEVLQTYLNAKETVSRtiLQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRK 516
Cdd:COG1196 281 LELEEAQAEEYEL---LAELARLEQDIARLEERRRE--LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 91064876 517 AEMERQHQEQlRQIALEKARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:COG1196 356 AEAELAEAEE-ALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
468-561 2.12e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 47.17  E-value: 2.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 468 ETVSRTILQTDQVLTDKEIQSKAEQERAEAarlEAQrlEAIRIQEEQRKAEMERQHQ--EQLRQIALEKARVAQ-EQQWI 544
Cdd:COG2268 233 EIETARIAEAEAELAKKKAEERREAETARA---EAE--AAYEIAEANAEREVQRQLEiaEREREIELQEKEAEReEAELE 307

                        90
                ....*....|....*..
gi 91064876 545 LKQRAQEEADRIKAEQE 561
Cdd:COG2268 308 ADVRKPAEAEKQAAEAE 324
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
483-559 3.03e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.79  E-value: 3.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 483 DKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQ--EQLRQIALEKARVAQEQQWILK-------------- 546
Cdd:COG2268 243 EAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEiaEREREIELQEKEAEREEAELEAdvrkpaeaekqaae 322

                        90
                ....*....|...
gi 91064876 547 QRAQEEADRIKAE 559
Cdd:COG2268 323 AEAEAEAEAIRAK 335
YeeP COG3596
Predicted GTPase [General function prediction only];
33-110 6.16e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 45.53  E-value: 6.16e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91064876  33 AITQPVVVVAIVGLYRTGKSYLMNKLAGKEKGfSVGStVQSHTKGIWmwCVPHPQKPDHTLVLLDTEGLGDVEKDDKK 110
Cdd:COG3596  34 LVELPPPVIALVGKTGAGKSSLINALFGAEVA-EVGV-GRPCTREIQ--RYRLESDGLPGLVLLDTPGLGEVNERDRE 107
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 436-561 9.31e-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: 45.50  E-value: 9.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   436 LQRMEQLKANYRQQPGKGTQAEEVLQTYLNAKETVSRTILQTDQVLTdkeiQSKAEQEraEAARLEAQRLEAIRIQEEQR 515
Cdd:pfam17380 377 MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQE--EARQREVRRLEEERAREMER 450

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 91064876   516 --KAEMERQHQ-EQLRQIALEKARVAQEQQWILKQRAQ-EEADRIKAEQE 561
Cdd:pfam17380 451 vrLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRaEEQRRKILEKE 500
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 441-582 9.31e-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: 45.50  E-value: 9.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   441 QLKANYRQQPGKGTQAEEvlQTYLNAKETVSRTILQTDQvLTDKEIQSKAEQERAEAARLEAQRL------EAIRIQEEQ 514
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQ--ERLRQEKEEKAREVERRRK-LEEAEKARQAEMDRQAAIYAEQERMamererELERIRQEE 357

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91064876   515 RKAEMERQHQEqlrQIALEKARVAQEQQwiLKQRAQEEADRIKAEQEAQLRALQQQLQHMREMNHHRR 582
Cdd:pfam17380 358 RKRELERIRQE---EIAMEISRMRELER--LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKV 420
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 481-561 1.40e-04

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 42.34  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   481 LTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQ-HQEQLRQIALEKARVAQEQQWILKQRAQEEADRIKAE 559
Cdd:pfam05672  16 LAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERArREEEARRLEEERRREEEERQRKAEEEAEEREQREQEE 95


                  ..
gi 91064876   560 QE 561
Cdd:pfam05672  96 QE 97
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
 486-561 1.45e-04

Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 41.27  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   486 IQSKAEQERAEAARLEAQRLEAIRIQE--EQRKAEMERQHQEQLRQIALE-----KARVAQEQQWIlKQRAQEEADRIKA 558
Cdd:pfam16999   7 LSELAEREAALDQQIEAARKEAEREVEaaEAEAARILREAEAKAKALQAEyrqelAAETARIREEA-RARAEAEAQAVRT 85


                  ...
gi 91064876   559 EQE 561
Cdd:pfam16999  86 RAE 88
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 476-561 1.85e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876  476 QTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQ-EQLRQIALEKARVAQEQqwilkQRAQEEAD 554
Cdd:PRK09510  71 QKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQaEEAAKQAALKQKQAEEA-----AAKAAAAA 145


                 ....*..
gi 91064876  555 RIKAEQE 561
Cdd:PRK09510 146 KAKAEAE 152
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
497-561 2.20e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.87  E-value: 2.20e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91064876 497 AARLEAQRLEAIRIQEEQRKAEMERQHQEQLRQIALEKARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:COG3064   1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAE 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 437-561 3.67e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 3.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 437 QRMEQLKANYRQQPGKGTQAEEVLQTYLNAKETVSRTILQTDQVLTDKEIQSKAEQERAEAARLEAQRLEairiQEEQRK 516
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE----EELAEL 328

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 91064876 517 AEMERQHQEQLRQIALEKARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 485-559 4.31e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.87  E-value: 4.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91064876  485 EIQSKAEQERAEAARLEAQRLEAIRIQ---EEQRKAEMERQHQ-EQLRQIALEKARVAQEQQwilKQRAQEEADRIKAE 559
Cdd:PRK09510  91 ELQQKQAAEQERLKQLEKERLAAQEQKkqaEEAAKQAALKQKQaEEAAAKAAAAAKAKAEAE---AKRAAAAAKKAAAE 166
PTZ00121 PTZ00121
MAEBL; Provisional
 438-582 5.50e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   438 RMEQLKANYRQQPGKGTQAEEVLQTYLNAKETVSRTILQTDQVltdKEIQSKAEQERAEAARL-EAQRLEAIRIQEEQRK 516
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA---EELKKKEAEEKKKAEELkKAEEENKIKAEEAKKE 1738

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91064876   517 AEMERQHQEQLRQIALEKARVAQeqqwiLKQRAQEEADRIKAEQEAQLRALQQQLQHMREMNHHRR 582
Cdd:PTZ00121 1739 AEEDKKKAEEAKKDEEEKKKIAH-----LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
PTZ00121 PTZ00121
MAEBL; Provisional
 361-560 6.20e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   361 REAIEIFRKHSFKDEGEFFQKELESLLSAKQDEICKKNADASAALCSTLLGSIFKPLEQEVAQEFYHKPGGHKLflQRME 440
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL--KKAE 1629

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   441 QLKANYRQQPGKgtQAEEVLQTYLNAKETVSRTILQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEME 520
Cdd:PTZ00121 1630 EEKKKVEQLKKK--EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 91064876   521 RQHQEQLRQIAlEKARVAQEQQWILKQRA--QEEADRIKAEQ 560
Cdd:PTZ00121 1708 KKKEAEEKKKA-EELKKAEEENKIKAEEAkkEAEEDKKKAEE 1748
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 493-559 6.46e-04

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


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.54  E-value: 6.46e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91064876 493 ERAEAARLEAQRLEAiRIQEEQRKAEMERQhqeQLRQIALEKARVAQEQqwiLKQRAQEEADRIKAE 559
Cdd:COG0711  41 AEAERAKEEAEAALA-EYEEKLAEARAEAA---EIIAEARKEAEAIAEE---AKAEAEAEAERIIAQ 100
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
485-561 6.61e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 42.72  E-value: 6.61e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91064876 485 EIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQLRQIALEKARVAQEQQWI--LKQRAQEEAdRIKAEQE 561
Cdd:COG3064  63 EAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAeeAKRKAEEEA-KRKAEEE 140
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 455-561 8.27e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 8.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 455 QAEEVLQTYLNAKETVSRTILQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERqHQEQLRQIALEK 534
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-LEEELEELEEAL 430

                        90       100
                ....*....|....*....|....*..
gi 91064876 535 ARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEE 457
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
 490-559 8.52e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 40.81  E-value: 8.52e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   490 AEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQLRQIALEKarvaqEQQWILKQRAQEEADRIKAE 559
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEEL-----EELKHLLEERKEALEKLRAE 65
PTZ00121 PTZ00121
MAEBL; Provisional
 455-561 9.33e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   455 QAEEVLQTYLNAKEtvsrtiLQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQLRQIALEK 534
Cdd:PTZ00121 1593 RIEEVMKLYEEEKK------MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666

                          90       100
                  ....*....|....*....|....*..
gi 91064876   535 ARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 491-561 1.14e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 1.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91064876  491 EQERAEAARLEAQRleaiRIQEEQRKAE-MERQHQEQLRQIALEKARVAQEQQwilkQRAQEEADRIKAEQE 561
Cdd:PRK09510  68 QQQQKSAKRAEEQR----KKKEQQQAEElQQKQAAEQERLKQLEKERLAAQEQ----KKQAEEAAKQAALKQ 131
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 472-561 1.32e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 472 RTILQTDQVLTDKEIQSKAEQERAEAARLEAQ-----------RLEAIRIQEEQRKAEMERQHQEQLRQIALEKARVAQE 540
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEaelaeaeeallEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405

                        90       100
                ....*....|....*....|.
gi 91064876 541 QQwiLKQRAQEEADRIKAEQE 561
Cdd:COG1196 406 EE--AEEALLERLERLEEELE 424
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 483-560 1.43e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 1.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91064876   483 DKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQLRQIALEKARVAQEQQWILK-QRAQEEADRIKAEQ 560
Cdd:pfam13868  42 ERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEiVERIQEEDQAEAEE 120
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 465-556 1.60e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.48  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   465 NAKETVSRTILQTDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHqEQLRQIALEKARVAQEQqwi 544
Cdd:PRK11448  142 NLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQL-EQLQEKAAETSQERKQK--- 217

                          90
                  ....*....|..
gi 91064876   545 LKQRAQEEADRI 556
Cdd:PRK11448  218 RKEITDQAAKRL 229
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
476-561 1.99e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.01  E-value: 1.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 476 QTDQVLTDKEIQ-SKAEQERAEaARLEAQR-LEAIRIQEEQRKAEMERQHQEQLRQIALEKARVAQEQQWILKQRA-QEE 552
Cdd:COG2268 204 AEAEAERETEIAiAQANREAEE-AELEQEReIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREvQRQ 282


                ....*....
gi 91064876 553 ADRIKAEQE 561
Cdd:COG2268 283 LEIAERERE 291
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 490-561 2.21e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.67  E-value: 2.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91064876   490 AEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQLRQIALEKA-RVAQEQQWILKQRA-QEEADRIKAEQE 561
Cdd:pfam13868 191 AQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQElQQAREEQIELKERRlAEEAEREEEEFE 264
PTZ00121 PTZ00121
MAEBL; Provisional
 440-561 2.22e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   440 EQLKANYRQQPGKGTQAEEVLQTYLNAK-ETVSRTILQTDQVLTDKEIQSKAEQERAEAA-----RLEAQRLEAIRIQEE 513
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAKKAEE 1617

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 91064876   514 QR-KAEMERQHQEQLRQIALEKARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:PTZ00121 1618 AKiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 483-536 2.36e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 40.88  E-value: 2.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 91064876   483 DKEIQSKAEQERAEAARLEAQRLEAIRIqEEQRKAEMERQHQEQLRQIALEKAR 536
Cdd:PTZ00266  472 ERERMERIERERLERERLERERLERDRL-ERDRLDRLERERVDRLERDRLEKAR 524
PTZ00121 PTZ00121
MAEBL; Provisional
 485-558 2.40e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91064876   485 EIQSKAEQERAEAArlEAQRLEAIRIQEEQRKAEMERQHQEQLRqiaLEKARVAQEQQWILKQRAQEEADRIKA 558
Cdd:PTZ00121 1112 EEARKAEEAKKKAE--DARKAEEARKAEDARKAEEARKAEDAKR---VEIARKAEDARKAEEARKAEDAKKAEA 1180
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 440-561 2.57e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 2.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 440 EQLKANYRQqpGKGTQAEEVL------QTYLNAKETVSRTILQTDQVLTD-KEIQSKAEQERAEAARLEAQrLEAIRIQE 512
Cdd:COG3883  90 ERARALYRS--GGSVSYLDVLlgsesfSDFLDRLSALSKIADADADLLEElKADKAELEAKKAELEAKLAE-LEALKAEL 166

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 91064876 513 EQRKAEMERQHQEQLRQIALEKARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 455-561 2.69e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 455 QAEEVLQTYLNAKETVSRTILQTDQVLTDKEiQSKAEQERAEAARLEAQ----RLEAIRIQEEQRKAEMERQHQEQLRQI 530
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEE-ALLERLERLEEELEELEealaELEEEEEEEEEALEEAAEEEAELEEEE 458

                        90       100       110
                ....*....|....*....|....*....|.
gi 91064876 531 ALEKARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEA 489
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 493-559 2.85e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.19  E-value: 2.85e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91064876 493 ERAEAARLEAQRLEAiRIQEEQRKAEMERQhqeQLRQIALEKARVAQEQqwiLKQRAQEEADRIKAE 559
Cdd:cd06503  40 EEAEKAKEEAEELLA-EYEEKLAEARAEAQ---EIIEEARKEAEKIKEE---ILAEAKEEAERILEQ 99
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 483-561 3.06e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   483 DKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQlrQIALEKARVAQEQQWILKQRAQEEADRIK--AEQ 560
Cdd:pfam15709 397 EEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQ--QEEAERAEAEKQRQKELEMQLAEEQKRLMemAEE 474


                  .
gi 91064876   561 E 561
Cdd:pfam15709 475 E 475
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 481-561 3.08e-03

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.48  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   481 LTDKEIQSKAEQERAEAARLEAQRLEAIRIQ---EEQRKAEMERQHQEQLRQIALEKARVAQEQqwilkQRAQEEADRIK 557
Cdd:pfam05672   6 TTDAEEAARILAEKRRQAREQREREEQERLEkeeEERLRKEELRRRAEEERARREEEARRLEEE-----RRREEEERQRK 80


                  ....
gi 91064876   558 AEQE 561
Cdd:pfam05672  81 AEEE 84
PRK13665 PRK13665
hypothetical protein; Provisional
 475-520 3.56e-03

hypothetical protein; Provisional


Pssm-ID: 237462  Cd Length: 316  Bit Score: 39.87  E-value: 3.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 91064876  475 LQTDQVLTDKEI-QSKAEQERAEAARLEaQRLEAiRIQEEQRK---AEME 520
Cdd:PRK13665 234 LQTDQAEADKRIaQAKAEERRAMAVALE-QEMKA-KVQEMRAKvveAEAE 281
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 437-561 3.66e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876 437 QRMEQLKANYRQQPGKGTQAEEVLQTYLNAKETVSRTILQTDQVLTDKEIQ-SKAEQERAEAARLEAQRLEAIRIQEEQR 515
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEElEELAEELLEALRAAAELAAQLEELEEAE 409

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 91064876 516 KAEMERQHQEQLRQIALEKARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
PTZ00121 PTZ00121
MAEBL; Provisional
 485-584 3.77e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   485 EIQSKAEQ-ERAEAARleaqRLEAIRIQEEQRKAEMERQHQ-----EQLRQIalEKARVAQEQQWILKQRAQEEADriKA 558
Cdd:PTZ00121 1167 EEARKAEDaKKAEAAR----KAEEVRKAEELRKAEDARKAEaarkaEEERKA--EEARKAEDAKKAEAVKKAEEAK--KD 1238

                          90       100
                  ....*....|....*....|....*.
gi 91064876   559 EQEAQLRALQQQLQHMREMNHHRRHH 584
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAH 1264
PTZ00121 PTZ00121
MAEBL; Provisional
 360-560 3.90e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   360 EREAIEIFRKHSFKDEGEFFQKELESllSAKQDEICKKNADASAAlcstllGSIFKPLEQEVAQEFYHKPGGHKlflQRM 439
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKKA------EEAKKKAEEAKKADEAKKKAEEA---KKA 1485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   440 EQLKANYRQQPGKGTQAEEVLQTYLNAKETVSRTILQTDQVLTDKEIQSKAEQER-AEAARL--EAQRLEAIRIQEEQRK 516
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkAEEKKKadELKKAEELKKAEEKKK 1565

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91064876   517 AEMERQHQ----------EQLRQIalEKARV-------AQEQQWILKQRAQEEADRIKAEQ 560
Cdd:PTZ00121 1566 AEEAKKAEedknmalrkaEEAKKA--EEARIeevmklyEEEKKMKAEEAKKAEEAKIKAEE 1624
PRK11281 PRK11281
mechanosensitive channel MscK;
301-558 4.07e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.28  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   301 DAINSGALPSIENTVV------TLARRENSAAVQKAIghyDQLMSEKVQLPTETLQ---ELLDLHRTCEREAIEIFRKHS 371
Cdd:PRK11281   46 DALNKQKLLEAEDKLVqqdleqTLALLDKIDRQKEET---EQLKQQLAQAPAKLRQaqaELEALKDDNDEETRETLSTLS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   372 fkdegeffQKELESLLSAKQDEICKKNADASAAlCSTLLGSIFKPleqEVAQ-EFYHKpgghklfLQRMEQLkanyRQQP 450
Cdd:PRK11281  123 --------LRQLESRLAQTLDQLQNAQNDLAEY-NSQLVSLQTQP---ERAQaALYAN-------SQRLQQI----RNLL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   451 GKGTQAEEVL-----------QTYLNAKETVSRTILQTDQVLTDkeiqskAEQERAEAARLEAQRLeairiqeeqrkaem 519
Cdd:PRK11281  180 KGGKVGGKALrpsqrvllqaeQALLNAQNDLQRKSLEGNTQLQD------LLQKQRDYLTARIQRL-------------- 239

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 91064876   520 erQHQEQLRQIALEKARVAQEQQWILKQRAQEEADRIKA 558
Cdd:PRK11281  240 --EHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQA 276
fliD PRK08724
flagellar filament capping protein FliD;
477-542 4.07e-03

flagellar filament capping protein FliD;


Pssm-ID: 236335 [Multi-domain]  Cd Length: 673  Bit Score: 40.24  E-value: 4.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876  477 TDQVLTDKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRK----AEMERQHQEQLRQIALEKARVAQEQQ 542
Cdd:PRK08724 355 TDSYVTPKEAQAEIEQKLAQEKAQLDAAVEKGELTPEQAKqiarAKLEPEERERLEKIDKAQAALKQAQS 424
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 484-582 4.49e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 39.63  E-value: 4.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   484 KEIQSKAEQERAEAARLEAQRLEaiRIQEEQRKAEMERQHQEQLRQIALEKARVAQEQQWILKQRAQEEADRIKAEQEAQ 563
Cdd:pfam15558  87 KQVIEKESRWREQAEDQENQRQE--KLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKERE 164

                          90
                  ....*....|....*....
gi 91064876   564 LRALQQQLQHMREMNHHRR 582
Cdd:pfam15558 165 EQKKVQENNLSELLNHQAR 183
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 437-561 4.57e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.79  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876  437 QRMEQLKANYRQQPGKGTQAEEVLQTYLNAKETVSRtilQTDQVLTDKEIQSKAEQER-----------------AEAAR 499
Cdd:PRK09510  70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ---LEKERLAAQEQKKQAEEAAkqaalkqkqaeeaaakaAAAAK 146

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91064876  500 LEAQRlEAIRIQEEQRKAEMERQHQEQLRQIALEKARVAQEQQWILKQRAQEEADRiKAEQE 561
Cdd:PRK09510 147 AKAEA-EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKK-KAEAE 206
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 484-561 4.77e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 4.77e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91064876 484 KEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQLRQIALEKARVAQeqqwiLKQRAQEEADRIKAEQE 561
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE-----LRLELEELELELEEAQA 288
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 486-561 5.65e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.13  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   486 IQSKAEQERAEAARLEAQRLEAIRIQEEQR-KAEMERQHQEQLRQIALEK----ARVAQEQQWILKQRAQEEADRIKAEQ 560
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDERILEYLKeKAEREEEREAEREEIEEEKereiARLRAQQEKAQDEKAERDELRAKLYQ 212


                  .
gi 91064876   561 E 561
Cdd:pfam13868 213 E 213
PLN02316 PLN02316
synthase/transferase
 512-561 6.07e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 39.85  E-value: 6.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 91064876   512 EEQRKaEMERQHQEQLrqialEKARVAQEQQWILKQRAQEEADRIKAEQE 561
Cdd:PLN02316  252 EEKRR-ELEKLAKEEA-----ERERQAEEQRRREEEKAAMEADRAQAKAE 295
PTZ00121 PTZ00121
MAEBL; Provisional
 361-560 6.07e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   361 REAIEIFRKHSFKDEGEFFQKELESllSAKQDEICKKNADASAALCSTLLGSIFKPLEQEVAQEFYHKPGGHKLfLQRME 440
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEE--AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA-KKAEE 1520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   441 QLKANYRQQPGKGTQAEEvlqtyLNAKETVSRTilqtDQVLTDKEIQSKAEQERAEAAR-LEAQRLEAIRIQEEQRKAEM 519
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADE-----AKKAEEKKKA----DELKKAEELKKAEEKKKAEEAKkAEEDKNMALRKAEEAKKAEE 1591

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 91064876   520 ERQHQ-----EQLRQIALEKARVAQEQQWILKQRAQEEADRIKAEQ 560
Cdd:PTZ00121 1592 ARIEEvmklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
growth_prot_Scy NF041483
polarized growth protein Scy;
466-559 6.45e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.81  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   466 AKETVSRTILQTDQVLTDKEIQSKAEQERAEAA----RLEAQRleAIRIQEEQRKAEMERQHQEQLRQI-----ALEKAR 536
Cdd:NF041483  522 AEETLERTRAEAERLRAEAEEQAEEVRAAAERAarelREETER--AIAARQAEAAEELTRLHTEAEERLtaaeeALADAR 599

                          90       100
                  ....*....|....*....|...
gi 91064876   537 VAQEQqwiLKQRAQEEADRIKAE 559
Cdd:NF041483  600 AEAER---IRREAAEETERLRTE 619
PRK12757 PRK12757
cell division protein FtsN; Provisional
 436-559 6.50e-03

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 38.87  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876  436 LQRMEQLKANYRQQPgkgTQAEEVlqTYLNAKETVSRTILQTDQvltdKEIQSKAEQERAEAARLEAQRLEAIRIQEEQR 515
Cdd:PRK12757  85 RQLLEQMQADMRQQP---TQLSEV--PYNEQTPQVPRSTVQIQQ----QAQQQQPPATTAQPQPVTPPRQTTAPVQPQTP 155

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 91064876  516 KAEMERQH--QEQLRQIALEKARVAQEQQWILkQ----RAQEEADRIKAE 559
Cdd:PRK12757 156 APVRTQPAapVTQAVEAPKVEAEKEKEQRWMV-QcgsfKGTEQAESVRAQ 204
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 483-559 9.23e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.75  E-value: 9.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91064876   483 DKEIQSKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQLRQIALEKARVAQEQQwILKQRAQEEADRIKAE 559
Cdd:pfam13868 259 EEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGE-RLREEEAERRERIEEE 334
Caldesmon pfam02029
Caldesmon;
465-561 9.93e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 38.70  E-value: 9.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91064876   465 NAKETVSRTILQTDQVLTDKEIQSKAEQEraEAARLEA-QRLEAIRiqeeQRKAEMERQHQEQLRQ----IALEKARVAQ 539
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEE--AEVFLEAeQKLEELR----RRRQEKESEEFEKLRQkqqeAELELEELKK 284

                          90       100
                  ....*....|....*....|..
gi 91064876   540 EQQWILKQRAQEEADRIKAEQE 561
Cdd:pfam02029 285 KREERRKLLEEEEQRRKQEEAE 306
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 488-561 9.97e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 9.97e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91064876 488 SKAEQERAEAARLEAQRLEAIRIQEEQRKAEMERQHQEQLRQIA-LEKARVAQEQQW-ILKQRAQEEADRIKAEQE 561
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAaLEALKAERQKLLaRLEKELAELAAELAELQQ 220
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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