|
Name |
Accession |
Description |
Interval |
E-value |
| pilM |
TIGR01175 |
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV ... |
8-353 |
2.62e-161 |
|
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV fimbria in Pseudomonas aeruginosa responsible for twitching motility, and for a similar pilus-like structure in Synechocystis. It is also found in species such as Deinococcus described as having natural transformation (for which a type IV pilus-like structure is proposed) but not fimbria.
Pssm-ID: 273484 [Multi-domain] Cd Length: 348 Bit Score: 455.01 E-value: 2.62e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 8 KANTLLGIDISSTSVKLLELSRSGGRYKVEAYAVEPLPPNAVVEKNIVELEGVGQALSRVLVKAKTNLKSAVVAVAGSAV 87
Cdd:TIGR01175 1 KKSLLVGIDIGSTSVKVAQLKRSGDRYKLEHYAVEPLPAGIFTEGHIVEYQAVAEALKELLSELGINTKKAATAVPGSAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 88 ITKTIEMEAGLSEDELENQLKIEADQYIPYPLEEVAIDFEVQGLSARNPE-RVDVLLAACRKENVEVREAALALAGLTAK 166
Cdd:TIGR01175 81 ITKVIPVPAGLDERELEFAVYIEASHYIPYPIEEVSLDFEKLGLKANNPEsTVQVLLAATRKEVVDSRLHALKLAGLEPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 167 VVDVEAYALERSYALLSSQLGADTDQLT-VAVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGL 245
Cdd:TIGR01175 161 VVDVESFALLRAWRLLGEQLASRTYRLTdAALVDIGATSSTLNLLHPGRMLFTREVPFGTRQLTSELSRAYGLNPEEAGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 246 AKKQGGLPDDYDSEVLRPFKDAVVQQVSRSLQFFFAAGQFNDVDYIVLAGGTASIQDLDRLIQQKIGTPTLVANPFADMA 325
Cdd:TIGR01175 241 AKQQGGLPLLYDPEVLRRFKGELVDEIRRSLQFFTAQSGTNSLDGLVLAGGGATLSGLDAAIYQRLGLPTEVANPFALMA 320
|
330 340
....*....|....*....|....*...
gi 15600237 326 LNGKVNAGALASDAPALMIACGLALRSF 353
Cdd:TIGR01175 321 LDAKVDAGRLAVDAPALMTALGLALRGF 348
|
|
| PilM_2 |
pfam11104 |
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ... |
14-353 |
1.07e-157 |
|
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for competency and pilus biogenesis. It binds to PilN and ATP.
Pssm-ID: 431656 [Multi-domain] Cd Length: 340 Bit Score: 445.58 E-value: 1.07e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 14 GIDISSTSVKLLELSRSGGRYKVEAYAVEPLPPNAVVEKNIVELEGVGQALSRVLVKAKTNLKSAVVAVAGSAVITKTIE 93
Cdd:pfam11104 1 GIDISSSAIKLVELSKKKGGYRLERYAIEPLPKGAVVDGNIENIDAVSEALRRAVKKSGTRLKNVAIAVPGSAVITKKII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 94 MEAGLSEDELENQLKIEADQYIPYPLEEVAIDFEVQGLSARNPERVDVLLAACRKENVEVREAALALAGLTAKVVDVEAY 173
Cdd:pfam11104 81 LPAGLSEEELEAQVEIEANQYIPFPLDEVSLDFEVLGPNAANPDDVDVLLAAARKEKVEDRVDLLEAAGLKPKVVDVESY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 174 ALERSYALLSSQLGADTDQLTVAVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGLAKKQGGLP 253
Cdd:pfam11104 161 ALERAFERIVSQLPNDGKDKCVAIVDIGANMTTLSVLRNGEIIYTREQAFGGAQLTQEIVRRYGMSYEEAEIAKRNGDLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 254 DDYDSEVLRPFKDAVVQQVSRSLQFFFAAGQFNDVDYIVLAGGTASIQDLDRLIQQKIGTPTLVANPFADMALNGKVNAG 333
Cdd:pfam11104 241 EDYESEVLEPFVEALAQQISRALQFFFTSTPYNKVDYIVLAGGCANIPGLAELVTERLGFSTTVANPFRGMELSPRVRQK 320
|
330 340
....*....|....*....|
gi 15600237 334 ALASDAPALMIACGLALRSF 353
Cdd:pfam11104 321 QLLRDAPSYMVACGLALRSF 340
|
|
| PilM |
COG4972 |
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures]; |
9-352 |
6.75e-103 |
|
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
Pssm-ID: 443997 [Multi-domain] Cd Length: 294 Bit Score: 304.47 E-value: 6.75e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 9 ANTLLGIDISSTSVKLLELSRSGGRYKVEAYAVEPLPPNAVVEKNIVELEGVGQALSRVLVKAKTNLKSAVVAVAGSAVI 88
Cdd:COG4972 1 KKPLVGIDIGSSSIKLVELSKSGGGYRLERYAEEPLPEGAVVDGNIVDPEAVAEALKELLKRLKIKTKRVAIAVPGSSVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 89 TKTIEMEAgLSEDELENQLKIEADQYIPYPLEEVAIDFEVQGLSARNPERVDVLLAACRKENVEVREAALALAGLTAKVV 168
Cdd:COG4972 81 TRKITLPA-LSEKELEEAIEFEAEQYIPFPLEEVVLDFQVLGPSEEGPEKVEVLLVAARKEVVEDYVELLEAAGLKPVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 169 DVEAYALERSYALlssqLGADTDQLTVAVVDIGATMTTLSVLHNGRTIYTREQLFGgrqlteeiqrryglsveeaglakk 248
Cdd:COG4972 160 DVEPFALLRALEL----LPPSGPDETVALVDIGASSTTLSVLSNGKPIFTREIPFG------------------------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 249 qgglpddydsevlrpfkdaVVQQVSRSLQFFFAAGQFNDVDYIVLAGGTASIQDLDRLIQQKIGTPTLVANPFADMALNg 328
Cdd:COG4972 212 -------------------LAQEIRRSLQFYRSQSGGNEVDRILLAGGGAKLPGLAEYLEERLGIPVEVLNPFAGMALS- 271
|
330 340
....*....|....*....|....
gi 15600237 329 kVNAGALASDAPALMIACGLALRS 352
Cdd:COG4972 272 -VDEEALAEDAPSFAVALGLALRG 294
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
13-350 |
1.92e-86 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 264.14 E-value: 1.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 13 LGIDISSTSVKLLELSRSGGRYKVEAYAVEPLPPNAVVEKNIVELEGVGQALSRVLVKAKTNLKSAVVAVAGSAVITKTI 92
Cdd:cd24049 1 LGIDIGSSSIKAVELKRSGGGLVLVAFAIIPLPEGAIVDGEIADPEALAEALKKLLKENKIKGKKVVVALPGSDVIVRTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 93 EMeAGLSEDELENQLKIEADQYIPYPLEEVAIDFEVQGLSARNPERVDVLLAACRKENVEVREAALALAGLTAKVVDVEA 172
Cdd:cd24049 81 KL-PKMPEKELEEAIRFEAEQYLPFPLEEVVLDYQILGEVEEGGEKLEVLVVAAPKEIVESYLELLKEAGLKPVAIDVES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 173 YALERSYallsSQLGADTDQLTVAVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGLAKKQGGL 252
Cdd:cd24049 160 FALARAL----EYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRSIPVGGNDITEAIAKALGLSFEEAEELKREYGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 253 PDDYD-------SEVLRPFKDAVVQQVSRSLQFFFAAGQFNDVDYIVLAGGTASIQDLDRLIQQKIGTPTLVANPFADMA 325
Cdd:cd24049 236 LLEGEegelkkvAEALRPVLERLVSEIRRSLDYYRSQNGGEPIDKIYLTGGGSLLPGLDEYLSERLGIPVEILNPFSNIE 315
|
330 340
....*....|....*....|....*
gi 15600237 326 LNgKVNAGALASDAPALMIACGLAL 350
Cdd:cd24049 316 SK-KSDDEELKEDAPLFAVAIGLAL 339
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
196-321 |
1.06e-09 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 58.30 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 196 AVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGLAKKQGglpdDYDSE---VLRPFKDAVVQQV 272
Cdd:PRK15080 138 AVVDIGGGTTGISILKDGKVVYSADEPTGGTHMSLVLAGAYGISFEEAEQYKRDP----KHHKEifpVVKPVVEKMASIV 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15600237 273 SRSLQFFfaagqfnDVDYIVLAGGTASIQDLDRLIQQKIGTPTLV-ANPF 321
Cdd:PRK15080 214 ARHIEGQ-------DVEDIYLVGGTCCLPGFEEVFEKQTGLPVHKpQHPL 256
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| pilM |
TIGR01175 |
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV ... |
8-353 |
2.62e-161 |
|
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV fimbria in Pseudomonas aeruginosa responsible for twitching motility, and for a similar pilus-like structure in Synechocystis. It is also found in species such as Deinococcus described as having natural transformation (for which a type IV pilus-like structure is proposed) but not fimbria.
Pssm-ID: 273484 [Multi-domain] Cd Length: 348 Bit Score: 455.01 E-value: 2.62e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 8 KANTLLGIDISSTSVKLLELSRSGGRYKVEAYAVEPLPPNAVVEKNIVELEGVGQALSRVLVKAKTNLKSAVVAVAGSAV 87
Cdd:TIGR01175 1 KKSLLVGIDIGSTSVKVAQLKRSGDRYKLEHYAVEPLPAGIFTEGHIVEYQAVAEALKELLSELGINTKKAATAVPGSAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 88 ITKTIEMEAGLSEDELENQLKIEADQYIPYPLEEVAIDFEVQGLSARNPE-RVDVLLAACRKENVEVREAALALAGLTAK 166
Cdd:TIGR01175 81 ITKVIPVPAGLDERELEFAVYIEASHYIPYPIEEVSLDFEKLGLKANNPEsTVQVLLAATRKEVVDSRLHALKLAGLEPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 167 VVDVEAYALERSYALLSSQLGADTDQLT-VAVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGL 245
Cdd:TIGR01175 161 VVDVESFALLRAWRLLGEQLASRTYRLTdAALVDIGATSSTLNLLHPGRMLFTREVPFGTRQLTSELSRAYGLNPEEAGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 246 AKKQGGLPDDYDSEVLRPFKDAVVQQVSRSLQFFFAAGQFNDVDYIVLAGGTASIQDLDRLIQQKIGTPTLVANPFADMA 325
Cdd:TIGR01175 241 AKQQGGLPLLYDPEVLRRFKGELVDEIRRSLQFFTAQSGTNSLDGLVLAGGGATLSGLDAAIYQRLGLPTEVANPFALMA 320
|
330 340
....*....|....*....|....*...
gi 15600237 326 LNGKVNAGALASDAPALMIACGLALRSF 353
Cdd:TIGR01175 321 LDAKVDAGRLAVDAPALMTALGLALRGF 348
|
|
| PilM_2 |
pfam11104 |
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ... |
14-353 |
1.07e-157 |
|
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for competency and pilus biogenesis. It binds to PilN and ATP.
Pssm-ID: 431656 [Multi-domain] Cd Length: 340 Bit Score: 445.58 E-value: 1.07e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 14 GIDISSTSVKLLELSRSGGRYKVEAYAVEPLPPNAVVEKNIVELEGVGQALSRVLVKAKTNLKSAVVAVAGSAVITKTIE 93
Cdd:pfam11104 1 GIDISSSAIKLVELSKKKGGYRLERYAIEPLPKGAVVDGNIENIDAVSEALRRAVKKSGTRLKNVAIAVPGSAVITKKII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 94 MEAGLSEDELENQLKIEADQYIPYPLEEVAIDFEVQGLSARNPERVDVLLAACRKENVEVREAALALAGLTAKVVDVEAY 173
Cdd:pfam11104 81 LPAGLSEEELEAQVEIEANQYIPFPLDEVSLDFEVLGPNAANPDDVDVLLAAARKEKVEDRVDLLEAAGLKPKVVDVESY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 174 ALERSYALLSSQLGADTDQLTVAVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGLAKKQGGLP 253
Cdd:pfam11104 161 ALERAFERIVSQLPNDGKDKCVAIVDIGANMTTLSVLRNGEIIYTREQAFGGAQLTQEIVRRYGMSYEEAEIAKRNGDLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 254 DDYDSEVLRPFKDAVVQQVSRSLQFFFAAGQFNDVDYIVLAGGTASIQDLDRLIQQKIGTPTLVANPFADMALNGKVNAG 333
Cdd:pfam11104 241 EDYESEVLEPFVEALAQQISRALQFFFTSTPYNKVDYIVLAGGCANIPGLAELVTERLGFSTTVANPFRGMELSPRVRQK 320
|
330 340
....*....|....*....|
gi 15600237 334 ALASDAPALMIACGLALRSF 353
Cdd:pfam11104 321 QLLRDAPSYMVACGLALRSF 340
|
|
| PilM |
COG4972 |
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures]; |
9-352 |
6.75e-103 |
|
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
Pssm-ID: 443997 [Multi-domain] Cd Length: 294 Bit Score: 304.47 E-value: 6.75e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 9 ANTLLGIDISSTSVKLLELSRSGGRYKVEAYAVEPLPPNAVVEKNIVELEGVGQALSRVLVKAKTNLKSAVVAVAGSAVI 88
Cdd:COG4972 1 KKPLVGIDIGSSSIKLVELSKSGGGYRLERYAEEPLPEGAVVDGNIVDPEAVAEALKELLKRLKIKTKRVAIAVPGSSVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 89 TKTIEMEAgLSEDELENQLKIEADQYIPYPLEEVAIDFEVQGLSARNPERVDVLLAACRKENVEVREAALALAGLTAKVV 168
Cdd:COG4972 81 TRKITLPA-LSEKELEEAIEFEAEQYIPFPLEEVVLDFQVLGPSEEGPEKVEVLLVAARKEVVEDYVELLEAAGLKPVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 169 DVEAYALERSYALlssqLGADTDQLTVAVVDIGATMTTLSVLHNGRTIYTREQLFGgrqlteeiqrryglsveeaglakk 248
Cdd:COG4972 160 DVEPFALLRALEL----LPPSGPDETVALVDIGASSTTLSVLSNGKPIFTREIPFG------------------------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 249 qgglpddydsevlrpfkdaVVQQVSRSLQFFFAAGQFNDVDYIVLAGGTASIQDLDRLIQQKIGTPTLVANPFADMALNg 328
Cdd:COG4972 212 -------------------LAQEIRRSLQFYRSQSGGNEVDRILLAGGGAKLPGLAEYLEERLGIPVEVLNPFAGMALS- 271
|
330 340
....*....|....*....|....
gi 15600237 329 kVNAGALASDAPALMIACGLALRS 352
Cdd:COG4972 272 -VDEEALAEDAPSFAVALGLALRG 294
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
13-350 |
1.92e-86 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 264.14 E-value: 1.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 13 LGIDISSTSVKLLELSRSGGRYKVEAYAVEPLPPNAVVEKNIVELEGVGQALSRVLVKAKTNLKSAVVAVAGSAVITKTI 92
Cdd:cd24049 1 LGIDIGSSSIKAVELKRSGGGLVLVAFAIIPLPEGAIVDGEIADPEALAEALKKLLKENKIKGKKVVVALPGSDVIVRTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 93 EMeAGLSEDELENQLKIEADQYIPYPLEEVAIDFEVQGLSARNPERVDVLLAACRKENVEVREAALALAGLTAKVVDVEA 172
Cdd:cd24049 81 KL-PKMPEKELEEAIRFEAEQYLPFPLEEVVLDYQILGEVEEGGEKLEVLVVAAPKEIVESYLELLKEAGLKPVAIDVES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 173 YALERSYallsSQLGADTDQLTVAVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGLAKKQGGL 252
Cdd:cd24049 160 FALARAL----EYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRSIPVGGNDITEAIAKALGLSFEEAEELKREYGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 253 PDDYD-------SEVLRPFKDAVVQQVSRSLQFFFAAGQFNDVDYIVLAGGTASIQDLDRLIQQKIGTPTLVANPFADMA 325
Cdd:cd24049 236 LLEGEegelkkvAEALRPVLERLVSEIRRSLDYYRSQNGGEPIDKIYLTGGGSLLPGLDEYLSERLGIPVEILNPFSNIE 315
|
330 340
....*....|....*....|....*
gi 15600237 326 LNgKVNAGALASDAPALMIACGLAL 350
Cdd:cd24049 316 SK-KSDDEELKEDAPLFAVAIGLAL 339
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
13-320 |
4.69e-15 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 74.25 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 13 LGIDISSTSVKLLELSRSGGRYKVEAYAVEPLPPNAVVEKNIVELEGVGQALSRVLvkaktnlksavvavagsavitkti 92
Cdd:cd24004 1 FALDIGTRSIKGLVLEEDDENIEVLAFSSEEHPERAMGDGQIHDISKVAESIKELL------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 93 emeaglseDELENQLKIEadqyipypLEEVAIDFevqglsarnPERVDVLLAACRKENVEVreaalalagltaKVVDVEa 172
Cdd:cd24004 57 --------KELEEKLGSK--------LKDVVIAI---------AKVVESLLNVLEKAGLEP------------VGLTLE- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 173 yalerSYALLSSQLGADTDQLTVAVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGLAKKQ--- 249
Cdd:cd24004 99 -----PFAAANLLIPYDMRDLNIALVDIGAGTTDIALIRNGGIEAYRMVPLGGDDFTKAIAEGFLISFEEAEKIKRTygi 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 250 GGLPDDYD-----------SEVLRPFKDAVVQQVSRSLQFFFaaGQFNDVDYIVLAGGTASIQDLDRLIQQKIGTPTLVA 318
Cdd:cd24004 174 FLLIEAKDqlgftinkkevYDIIKPVLEELASGIANAIEEYN--GKFKLPDAVYLVGGGSKLPGLNEALAEKLGLPVERI 251
|
..
gi 15600237 319 NP 320
Cdd:cd24004 252 AP 253
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
196-320 |
2.61e-14 |
|
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.
Pssm-ID: 464177 [Multi-domain] Cd Length: 167 Bit Score: 70.05 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 196 AVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGLAKKQGG--LPDDYD---------------- 257
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGsaLASLADedevpgvggrepreis 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600237 258 ----SEVLRPFKDAVVQQVSRSLQFFFAAGQFN-----DVDYIVLAGGTASIQDLDRLIQQKIGTPTLVANP 320
Cdd:pfam14450 81 rkelAEIIEARVEEILELVRAELEDREVLPGEYvrlevDVHGIVLTGGGSALPGLVELAERALGLPVRIGSP 152
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
196-321 |
4.31e-10 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 59.20 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 196 AVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGLAKKQGG-----LPddydseVLRPFKDAVVQ 270
Cdd:cd24047 114 AVVDIGGGTTGIAVLKDGKVVYTADEPTGGTHLSLVLAGNYGISFEEAEIIKRDPArhkelLP------VVRPVIEKMAS 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15600237 271 QVSRSLQFFfaagqfnDVDYIVLAGGTASIQDLDRLIQQKIGTPTLVA-NPF 321
Cdd:cd24047 188 IVKRHIKGY-------KVKDLYLVGGTCCLPGIEEVFEKETGLPVYKPsNPL 232
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
196-321 |
1.06e-09 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 58.30 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 196 AVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGLAKKQGglpdDYDSE---VLRPFKDAVVQQV 272
Cdd:PRK15080 138 AVVDIGGGTTGISILKDGKVVYSADEPTGGTHMSLVLAGAYGISFEEAEQYKRDP----KHHKEifpVVKPVVEKMASIV 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15600237 273 SRSLQFFfaagqfnDVDYIVLAGGTASIQDLDRLIQQKIGTPTLV-ANPF 321
Cdd:PRK15080 214 ARHIEGQ-------DVEDIYLVGGTCCLPGFEEVFEKQTGLPVHKpQHPL 256
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
168-350 |
4.84e-09 |
|
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 57.16 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 168 VDVEAYALErSYAllSSQ--LGADTDQLTVAVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGL 245
Cdd:cd24048 174 LEVDDIVLS-PLA--SAEavLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAIGLNTPFEEAER 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 246 AKKQGG--LPDDYDSEVL-----------RPFKDAVVQQV--SRSLQFFFAAGQ-FNDVDY-------IVLAGGTASIQD 302
Cdd:cd24048 251 LKIKYGsaLSEEADEDEIieipgvggrepREVSRRELAEIieARVEEILELVKKeLKESGYedllpggIVLTGGGSQLPG 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600237 303 LDRLIQQKIGTPTLVANPFADMALNGKVNAGALASdapalmiACGLAL 350
Cdd:cd24048 331 LVELAEEVFGMPVRIGRPKNIGGLPEEVNDPAYAT-------AVGLLL 371
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
168-320 |
5.22e-08 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 53.98 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 168 VDVEAYALErSYALLSSQLGADTDQLTVAVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGLAK 247
Cdd:COG0849 176 LEVEDLVLS-PLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDIAIGLRTPLEEAERLK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 248 KQGG--LPDDYDSEV---LRPFKDAVVQQVSRS---------LQ--FFFAAGQFNDVDY-------IVLAGGTASIQDLD 304
Cdd:COG0849 255 IKYGsaLASLADEDEtieVPGIGGRPPREISRKelaeiiearVEeiFELVRKELKRSGYeeklpagVVLTGGGSQLPGLV 334
|
170
....*....|....*.
gi 15600237 305 RLIQQKIGTPTLVANP 320
Cdd:COG0849 335 ELAEEILGLPVRIGRP 350
|
|
| ASKHA_NBD_actin-like |
cd10169 |
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ... |
197-308 |
8.00e-05 |
|
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ubiquitous in eukaryotes, and the major component of the actin cytoskeleton; monomeric globular protein (G-actin) reversibly polymerizes to form filaments (F-actin). Each actin protomer binds one molecule of ATP and either calcium or magnesium ions. F-actin filaments form with the consequent hydrolysis of ATP. Some actin-related proteins (Arps) have roles in cytoskeletal functions, such as actin polymerization (Arp2/3) and dynein motor activity (Arp1). Both conventional actin and specific Arps have been implicated in chromatin remodeling and/or transcription regulation. The actin/ARP family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466810 [Multi-domain] Cd Length: 258 Bit Score: 43.63 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 197 VVDIGATMTTLSVLHNGRTI-YTREQL-FGGRQLTEEIQRRyglsveeagLAKKQGGLPDDYDSEVLRPFKDA---VVQQ 271
Cdd:cd10169 99 VVDSGEGVTHIVPVYEGYVLpHAVRRLdIGGRDLTDYLAKL---------LREKGYSFSTSAEREIVRDIKEKlcgLHEL 169
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15600237 272 VSRSLQFFfaagqfnDVDY-------IVLAGGTASIQDL-DRLIQ 308
Cdd:cd10169 170 IYDSIMKC-------DIDLrkelysnIVLSGGTTLFPGFaERLQK 207
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
220-350 |
1.33e-04 |
|
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466811 [Multi-domain] Cd Length: 329 Bit Score: 43.25 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 220 EQLFGGRQLTEEIQRRYGLSVEEAGLAKKQGGLPDdydsEVLRPFKDAVVQQVSRSLQFFFAAGQFNDVDYIVLAGGTAS 299
Cdd:cd10170 218 KRFSGGEEDERLVPSLLGGGLPELGLEKGTLLLTE----EEIRDLFDPVIDKILELIEEQLEAKSGTPPDAVVLVGGFSR 293
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15600237 300 IQDLDRLIQQKIGTPTLVANPFadmalngkvnagalaSDAPALMIACGLAL 350
Cdd:cd10170 294 SPYLRERLRERFGSAGIIIVLR---------------SDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
197-318 |
1.54e-04 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 43.23 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 197 VVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEI----QRRYGLSVEE--AGLAKKQGG--LPDDYD----------- 257
Cdd:cd10225 147 VVDIGGGTTEIAVISLGGIVTSRSVRVAGDEMDEAIinyvRRKYNLLIGErtAERIKIEIGsaYPLDEElsmevrgrdlv 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 258 --------------SEVLRPFKDAVVQQVSRSLQFF---FAAgqfnDV--DYIVLAGGTASIQDLDRLIQQKIGTPTLVA 318
Cdd:cd10225 227 tglprtieitseevREALEEPVNAIVEAVRSTLERTppeLAA----DIvdRGIVLTGGGALLRGLDELLREETGLPVHVA 302
|
|
| ASKHA_NBD_ParM_R1-like |
cd24022 |
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ... |
195-300 |
2.44e-04 |
|
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.
Pssm-ID: 466872 [Multi-domain] Cd Length: 324 Bit Score: 42.64 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 195 VAVVDIGATMTTLSVLHNGRTIYTREQL---FGGRQLTEE----IQRRYGLS------VEEA---GLAKKQGGLPDDYdS 258
Cdd:cd24022 176 VAVIDIGGTTTDIAVVSGGLSIDHARSGtieLGVLDVRDAlkdaLKKRFGLSsisdaeLDRAlrtGKFRLNGGKEVDV-S 254
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15600237 259 EVLRPFKDAVVQQVSRSLQFFFaaGQFNDVDYIVLAGGTASI 300
Cdd:cd24022 255 DLVNEAIAEVAERILNEIKRRL--GDASDLDRVIFVGGGAEL 294
|
|
| Actin |
pfam00022 |
Actin; |
197-291 |
4.25e-03 |
|
Actin;
Pssm-ID: 394979 [Multi-domain] Cd Length: 407 Bit Score: 38.82 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 197 VVDIGATMTTLSVLHNGRTIY--TREQLFGGRQLTEEIQR-----------RYGLSVEEAGLAKKQGGLPDDYD------ 257
Cdd:pfam00022 145 VVDSGAGVTSVVPVHDGYVLQkaIRRSDLGGDFLTDYLREllrsrnieitpRYLIKSKKPGDPAPAVTKRELPDttysyk 224
|
90 100 110
....*....|....*....|....*....|....*....
gi 15600237 258 ----SEVLRPFKDAVVqQVSRSLQFFF-AAGQFNDVDYI 291
Cdd:pfam00022 225 tyqeRRVLEEIKESVC-YVSDDPFGDEtTSSSIPTRVYE 262
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
197-319 |
5.43e-03 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 38.14 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 197 VVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEI----QRRYGLSVEEA---------GLAKKQG------------- 250
Cdd:COG1077 155 VVDIGGGTTEVAVISLGGIVVSRSIRVAGDELDEAIiqyvRKKYNLLIGERtaeeikieiGSAYPLEeeltmevrgrdlv 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600237 251 -GLP-----DDYD-SEVLRPFKDAVVQQVSRSLQ---FFFAAgqfnD-VDY-IVLAGGTASIQDLDRLIQQKIGTPTLVA 318
Cdd:COG1077 235 tGLPktitiTSEEiREALEEPLNAIVEAIKSVLEktpPELAA----DiVDRgIVLTGGGALLRGLDKLLSEETGLPVHVA 310
|
.
gi 15600237 319 N 319
Cdd:COG1077 311 E 311
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
291-319 |
6.96e-03 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 37.76 E-value: 6.96e-03
10 20
....*....|....*....|....*....
gi 15600237 291 IVLAGGTASIQDLDRLIQQKIGTPTLVAN 319
Cdd:PRK13927 280 IVLTGGGALLRGLDKLLSEETGLPVHVAE 308
|
|
| |
