|
Name |
Accession |
Description |
Interval |
E-value |
| vWA_midasin |
cd01460 |
VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are ... |
4754-5022 |
2.02e-121 |
|
VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are unified by their common archetectural organization that is based upon a conserved ATPase domain. The AAA domain of midasin contains six tandem AAA protomers. The AAA domains in midasin is followed by a D/E rich domain that is following by a VWA domain. The members of this subgroup have a conserved MIDAS motif. The function of this domain is not exactly known although it has been speculated to play a crucial role in midasin function.
:
Pssm-ID: 238737 Cd Length: 266 Bit Score: 385.17 E-value: 2.02e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4754 LAMGLCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFKKDKIWLRRTKMSKRQYQIMISVDDSKSMSESRSVQ 4833
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4834 LAYETLALISKALTQLEVGDISISSFGERVRLLHPFGQPFTAESGASVLQQFTFAQQKTYVKNLIETSLGLFENAKHTSg 4913
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4914 pGKDDLWQLQLVISDGICEDH-DKLRSLVRSALEQRIMIIFIVVDNKPEKDSILNMTNITYtiDDGKYGiQMKPYLETFP 4992
Cdd:cd01460 160 -SSGSLWQLLLIISDGRGEFSeGAQKVRLREAREQNVFVVFIIIDNPDNKQSILDIKVVSF--KNDKSG-VITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|
gi 1954487186 4993 FQYFMIVRDVASLPEALSDALRQYFSFVAS 5022
Cdd:cd01460 236 FPYYVIVRDLNQLPSVLSDALRQWFELVNS 265
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
711-816 |
1.52e-43 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 407722 Cd Length: 104 Bit Score: 155.05 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 711 DLLQIVKQYIYGIASGDERCyDDVAEFYMSAKKLAnEHKLVDGANQRPHFSMRTLARALTYVVQICPTYGLRRSLYEGFC 790
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLV-RDIVKFYLEAKKLA-EKSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90 100
....*....|....*....|....*.
gi 1954487186 791 MTFLTQLDKESEKLMHDLIHKTILRN 816
Cdd:pfam17865 79 MSFLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1172-1320 |
1.33e-29 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
:
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 116.62 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1172 PVLLVGDTGCGKTTVCQMLAE-TYGRELHIVNCHQNTETGDLLGGQRPVRGqdedmdkpkqLFEWHDGPLVQSMKDGHLF 1250
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNIDPG----------GASWVDGPLVRAAREGEIA 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1954487186 1251 LLDEISLADDSVLERLNSVLEPSRLLVlaEKGGkhvEELYGAPE-FKFLATMNPgGDYGKKELSPALRNRF 1320
Cdd:pfam07728 71 VLDEINRANPDVLNSLLSLLDERRLLL--PDGG---ELVKAAPDgFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
879-1015 |
5.47e-25 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
:
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 103.53 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 879 PVLIQGPTSAGKTSMVEYMAKKT-GHRFVRINNHEHTDLQEYLGTYVSNNEGKlVFQEGVLVEALRNGYWIVLDELNLAP 957
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1954487186 958 SDVLEALNRLLDDNRELLIPETQEVVKPHPHFMLFATQNPagLYGGRKALSRAFRNRF 1015
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1654-1752 |
7.59e-25 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 465540 Cd Length: 106 Bit Score: 101.99 E-value: 7.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1654 DLLFICSHLFSeFEPAVLAKMIEFNNQMYQETMVRCSFGRKGSPWEFNLRDVFRWLELMR--------QNNTVDPAEYLD 1725
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSsllptllsPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*..
gi 1954487186 1726 IIYMQRMRTQEDRKHIAQLFETVFGVK 1752
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
272-386 |
4.32e-21 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 465540 Cd Length: 106 Bit Score: 91.21 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 272 ELEQVIRQKFQHIQDFAPHAMELFQTVVGIYEDPNFSSLSSssMGRFLSTRDLMKWCHRVDLLmgekledSNLGMDLTLR 351
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSG--SPREFNLRDLLRWCRRLSSL-------LPTLLSPTVR 71
|
90 100 110
....*....|....*....|....*....|....*
gi 1954487186 352 QDLFNEANDCFCGMISDYNIWMTVLQTIGRPLQIS 386
Cdd:pfam17867 72 EEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1027-1121 |
1.37e-17 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 465540 Cd Length: 106 Bit Score: 81.19 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1027 ELETILSKRCAIAPSYCKKLVKVYQDLMAHRQSTRIFEQKHG--FITLRDLFRWAGR---------DPQGYQELAENGYM 1095
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCRRlssllptllSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 1954487186 1096 LLAERCRREEEKKVVKQVLEQVMKVK 1121
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1503-1642 |
1.40e-17 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 82.34 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1503 PILLEGSPGVGKTSLVSALAAA-SGHHLVRINLSEQTDLMDLFGSDLPVEGGnsgeFAWRDAPFLQAMKRGDWVLLDELN 1581
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNIDPGG----ASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954487186 1582 LASQSVLEGLNSCLDHRgavYIPELDREFFCHAE---FRVFGAQNPLQQGGgrKGLPKSFVNRF 1642
Cdd:pfam07728 77 RANPDVLNSLLSLLDER---RLLLPDGGELVKAApdgFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
117-248 |
6.36e-16 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 77.33 E-value: 6.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 117 PTLLEGVTGAGKTCLVEELAWRTgRGAGLVKIHLGDQTDPKVLLGTYVSTstPGSFRWQAGVLTTAVLEGRWVLIEDIDL 196
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL-SNRPVFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEINR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1954487186 197 APAEVLSVLLPLLETGHLFIPSRGEKIKAKA-GFHLFGTrSFVPSRSGKGVSA 248
Cdd:pfam07728 78 ANPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIAT-MNPLDRGLNELSP 129
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
461-697 |
7.10e-10 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 60.00 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 461 PVLLVGETGTGKTTVVQHLADMIH-QNLIVVNLSQQSDSSDLLGGFKPVDGKvlaiplndeferlfektfsvkknvkfld 539
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDPGG---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 540 mvrkmfvhqkwtsfvallkqsvkmsqqkfeaeqnvenkkvsgpqlrnawkmfakhveefevqqvqsqnkfvFSFMEGSLV 619
Cdd:pfam07728 53 -----------------------------------------------------------------------ASWVDGPLV 61
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954487186 620 KAVRNGDWILLDEINLATTETLECLSGLLQDvnGSLLLTEKGDVEPIQRhPNFRLFACMNPAtDVGKRDLPPGLRNRF 697
Cdd:pfam07728 62 RAAREGEIAVLDEINRANPDVLNSLLSLLDE--RRLLLPDGGELVKAAP-DGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1971-2061 |
1.65e-07 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 53.45 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1971 DTIAGKFEWIDGLLINALEKGHWLLIDNANLCNPSVLDRLNPLFENdgvlmvNERGLVDGTVKVIKPHPNFRMFMTVDPQ 2050
Cdd:pfam07728 47 NIDPGGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPL 120
|
90
....*....|....
gi 1954487186 2051 NG---ELSRAMRNR 2061
Cdd:pfam07728 121 DRglnELSPALRSR 134
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4108-4681 |
1.74e-07 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
:
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 58.10 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4108 EGEEGDADGKQSGTGIGEGEGAKDVSHEIEDEEQvLGTQNEERSDEKQDTKEEKNGMDMDNDFEGNLEDMEQDQDEEDES 4187
Cdd:COG5271 297 QAADPESDDDADDSTLAALEGAAEDTEIATADEL-AAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4188 DSSDDEDNEPDEQIGDVDDMDPDAVDDKMWGEEGEDNLNESDKTVEDQGQQQDKQEESDIVAKEEEEGAQDDKKENKPDK 4267
Cdd:COG5271 376 SEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4268 NQQ----------KDSADKDENGDDKEEGEQGEDEGQEGDEKDEGEEGAEEDEDDVQNR---PGEQLDT-EIPEAETLEL 4333
Cdd:COG5271 456 EEEaeaeldteedTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETsadDGADTDAaADPEDSDEDA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4334 PEDmnmEGDDGEDKEGDDGEDKEGDENEETGMDDPMDMDETPAEEQNEEGEAfhdvlDDLNEGEQGEQEDEEMADASAQM 4413
Cdd:COG5271 536 LED---ETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADA-----DETEESADESEEAEASEDEAAEE 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4414 DTEQNEQegdqengeeeseekgeeegkeEVADATGDQEDSKNGAQIEQDEDEDIESTAQNREQPNSDAAADNQF---GVQ 4490
Cdd:COG5271 608 EEADDDE---------------------ADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEAsadESE 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4491 GQSGKQSKSSAGKKEGEDDTADMAEGEDEAEKKENKGKSSSGSNEANEEDNEESAEGAEDEPkrEEANPQRSLGDAlekw 4570
Cdd:COG5271 667 EEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADAEEADTEADGTAEEA--EEAAEEAESADE---- 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4571 rrrlanlndelnneeeenEKTEDKDTEDAQVKEDDAFEYVKNDEDAHDmqamgNAQADQVQDLKTAAMDEDQQD---ENQ 4647
Cdd:COG5271 741 ------------------EAASLPDEADAEEEAEEAEEAEEDDADGLE-----EALEEEKADAEEAATDEEAEAaaeEKE 797
|
570 580 590
....*....|....*....|....*....|....
gi 1954487186 4648 VSGEMNVDQPEDIETMPLPRDTLDMSGSTDQQGA 4681
Cdd:COG5271 798 KVADEDQDTDEDALLDEAEADEEEDLDGEDEETA 831
|
|
| COG2842 super family |
cl34499 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
413-502 |
5.78e-03 |
|
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];
The actual alignment was detected with superfamily member COG2842:
Pssm-ID: 442090 [Multi-domain] Cd Length: 254 Bit Score: 41.86 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 413 VNLSSIAASGKQKKKASLIKREKQRPFATTGHALRLMEKIAVTIHLNEPVLLVGETGTGKTTVVQHLADMiHQNLIVVNL 492
Cdd:COG2842 4 KTQAAVAKEIGNEKLEAKIARWEAPSFVETKNVRRFAEALDEARALPGIGVVYGESGVGKTTAAREYANR-NPNVIYVTA 82
|
90
....*....|
gi 1954487186 493 SQQSDSSDLL 502
Cdd:COG2842 83 SPSWTSKELL 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| vWA_midasin |
cd01460 |
VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are ... |
4754-5022 |
2.02e-121 |
|
VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are unified by their common archetectural organization that is based upon a conserved ATPase domain. The AAA domain of midasin contains six tandem AAA protomers. The AAA domains in midasin is followed by a D/E rich domain that is following by a VWA domain. The members of this subgroup have a conserved MIDAS motif. The function of this domain is not exactly known although it has been speculated to play a crucial role in midasin function.
Pssm-ID: 238737 Cd Length: 266 Bit Score: 385.17 E-value: 2.02e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4754 LAMGLCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFKKDKIWLRRTKMSKRQYQIMISVDDSKSMSESRSVQ 4833
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4834 LAYETLALISKALTQLEVGDISISSFGERVRLLHPFGQPFTAESGASVLQQFTFAQQKTYVKNLIETSLGLFENAKHTSg 4913
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4914 pGKDDLWQLQLVISDGICEDH-DKLRSLVRSALEQRIMIIFIVVDNKPEKDSILNMTNITYtiDDGKYGiQMKPYLETFP 4992
Cdd:cd01460 160 -SSGSLWQLLLIISDGRGEFSeGAQKVRLREAREQNVFVVFIIIDNPDNKQSILDIKVVSF--KNDKSG-VITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|
gi 1954487186 4993 FQYFMIVRDVASLPEALSDALRQYFSFVAS 5022
Cdd:cd01460 236 FPYYVIVRDLNQLPSVLSDALRQWFELVNS 265
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
711-816 |
1.52e-43 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 407722 Cd Length: 104 Bit Score: 155.05 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 711 DLLQIVKQYIYGIASGDERCyDDVAEFYMSAKKLAnEHKLVDGANQRPHFSMRTLARALTYVVQICPTYGLRRSLYEGFC 790
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLV-RDIVKFYLEAKKLA-EKSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90 100
....*....|....*....|....*.
gi 1954487186 791 MTFLTQLDKESEKLMHDLIHKTILRN 816
Cdd:pfam17865 79 MSFLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1172-1320 |
1.33e-29 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 116.62 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1172 PVLLVGDTGCGKTTVCQMLAE-TYGRELHIVNCHQNTETGDLLGGQRPVRGqdedmdkpkqLFEWHDGPLVQSMKDGHLF 1250
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNIDPG----------GASWVDGPLVRAAREGEIA 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1954487186 1251 LLDEISLADDSVLERLNSVLEPSRLLVlaEKGGkhvEELYGAPE-FKFLATMNPgGDYGKKELSPALRNRF 1320
Cdd:pfam07728 71 VLDEINRANPDVLNSLLSLLDERRLLL--PDGG---ELVKAAPDgFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
879-1015 |
5.47e-25 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 103.53 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 879 PVLIQGPTSAGKTSMVEYMAKKT-GHRFVRINNHEHTDLQEYLGTYVSNNEGKlVFQEGVLVEALRNGYWIVLDELNLAP 957
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1954487186 958 SDVLEALNRLLDDNRELLIPETQEVVKPHPHFMLFATQNPagLYGGRKALSRAFRNRF 1015
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1654-1752 |
7.59e-25 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 101.99 E-value: 7.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1654 DLLFICSHLFSeFEPAVLAKMIEFNNQMYQETMVRCSFGRKGSPWEFNLRDVFRWLELMR--------QNNTVDPAEYLD 1725
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSsllptllsPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*..
gi 1954487186 1726 IIYMQRMRTQEDRKHIAQLFETVFGVK 1752
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
272-386 |
4.32e-21 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 91.21 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 272 ELEQVIRQKFQHIQDFAPHAMELFQTVVGIYEDPNFSSLSSssMGRFLSTRDLMKWCHRVDLLmgekledSNLGMDLTLR 351
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSG--SPREFNLRDLLRWCRRLSSL-------LPTLLSPTVR 71
|
90 100 110
....*....|....*....|....*....|....*
gi 1954487186 352 QDLFNEANDCFCGMISDYNIWMTVLQTIGRPLQIS 386
Cdd:pfam17867 72 EEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1027-1121 |
1.37e-17 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 81.19 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1027 ELETILSKRCAIAPSYCKKLVKVYQDLMAHRQSTRIFEQKHG--FITLRDLFRWAGR---------DPQGYQELAENGYM 1095
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCRRlssllptllSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 1954487186 1096 LLAERCRREEEKKVVKQVLEQVMKVK 1121
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1503-1642 |
1.40e-17 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 82.34 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1503 PILLEGSPGVGKTSLVSALAAA-SGHHLVRINLSEQTDLMDLFGSDLPVEGGnsgeFAWRDAPFLQAMKRGDWVLLDELN 1581
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNIDPGG----ASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954487186 1582 LASQSVLEGLNSCLDHRgavYIPELDREFFCHAE---FRVFGAQNPLQQGGgrKGLPKSFVNRF 1642
Cdd:pfam07728 77 RANPDVLNSLLSLLDER---RLLLPDGGELVKAApdgFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
117-248 |
6.36e-16 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 77.33 E-value: 6.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 117 PTLLEGVTGAGKTCLVEELAWRTgRGAGLVKIHLGDQTDPKVLLGTYVSTstPGSFRWQAGVLTTAVLEGRWVLIEDIDL 196
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL-SNRPVFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEINR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1954487186 197 APAEVLSVLLPLLETGHLFIPSRGEKIKAKA-GFHLFGTrSFVPSRSGKGVSA 248
Cdd:pfam07728 78 ANPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIAT-MNPLDRGLNELSP 129
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1491-1642 |
3.52e-13 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 73.66 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1491 AMRVVRAMQLRKPILLEGSPGVGKTSLVSALAAASGHHLVRINLSEqtDLM--DLFGSDLPVEggNSGEFAWRDAPFLQA 1568
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTP--DLLpsDILGTYIYDQ--QTGEFEFRPGPLFAN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1569 MkrgdwVLLDELNLAS---QSV-LEglnsCLDHRgAVYIP----ELDREFFchaefrVFGAQNPLQQGGGRKgLPKSFVN 1640
Cdd:COG0714 97 V-----LLADEINRAPpktQSAlLE----AMEER-QVTIPggtyKLPEPFL------VIATQNPIEQEGTYP-LPEAQLD 159
|
..
gi 1954487186 1641 RF 1642
Cdd:COG0714 160 RF 161
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
851-1035 |
5.19e-13 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 72.89 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 851 EEDTRYILTQSIEVKLYNLArvIMSRKfPVLIQGPTSAGKTSMVEYMAKKTGHRFVRINNHEHTDLQEYLGTYVSN-NEG 929
Cdd:COG0714 8 AEIGKVYVGQEELIELVLIA--LLAGG-HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDqQTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 930 KLVFQEGVLveaLRNgywIVL-DELNLAP----SDVLEALnrlldDNRELLIPEtqEVVK-PHPhFMLFATQNPAGLYGG 1003
Cdd:COG0714 85 EFEFRPGPL---FAN---VLLaDEINRAPpktqSALLEAM-----EERQVTIPG--GTYKlPEP-FLVIATQNPIEQEGT 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1954487186 1004 RkALSRAFRNRFL-ELHFD--DiPEDELEtILSKR 1035
Cdd:COG0714 151 Y-PLPEAQLDRFLlKLYIGypD-AEEERE-ILRRH 182
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1172-1339 |
1.14e-10 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 65.96 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1172 PVLLVGDTGCGKTTVCQMLAETYGRELHIVNCHQNTETGDLLGgqrpvrgqDEDMDKPKQLFEWHDGPLVQSmkdghLFL 1251
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILG--------TYIYDQQTGEFEFRPGPLFAN-----VLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1252 LDEISLADDSVlerlnsvlePSRLL-VLAEK----GGKHVEelygAPE-FKFLATMNPGGDYGKKELSPALRNRFT-EIW 1324
Cdd:COG0714 100 ADEINRAPPKT---------QSALLeAMEERqvtiPGGTYK----LPEpFLVIATQNPIEQEGTYPLPEAQLDRFLlKLY 166
|
170
....*....|....*..
gi 1954487186 1325 V--PsvtDRDDLINIID 1339
Cdd:COG0714 167 IgyP---DAEEEREILR 180
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
461-697 |
7.10e-10 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 60.00 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 461 PVLLVGETGTGKTTVVQHLADMIH-QNLIVVNLSQQSDSSDLLGGFKPVDGKvlaiplndeferlfektfsvkknvkfld 539
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDPGG---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 540 mvrkmfvhqkwtsfvallkqsvkmsqqkfeaeqnvenkkvsgpqlrnawkmfakhveefevqqvqsqnkfvFSFMEGSLV 619
Cdd:pfam07728 53 -----------------------------------------------------------------------ASWVDGPLV 61
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954487186 620 KAVRNGDWILLDEINLATTETLECLSGLLQDvnGSLLLTEKGDVEPIQRhPNFRLFACMNPAtDVGKRDLPPGLRNRF 697
Cdd:pfam07728 62 RAAREGEIAVLDEINRANPDVLNSLLSLLDE--RRLLLPDGGELVKAAP-DGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1171-1320 |
5.95e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.77 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1171 EPVLLVGDTGCGKTTVCQMLAETYGRELH---IVNCHQNTETGDLLGGQRPVRG---QDEDMDKPKQLFEwhdgpLVQSM 1244
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGgviYIDGEDILEEVLDQLLLIIVGGkkaSGSGELRLRLALA-----LARKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1954487186 1245 KDGhLFLLDEISLADDSVLERLNSVLEPSRLLVLAEKGGKhveelygapeFKFLATMNPGGDYGKKELSPALRNRF 1320
Cdd:smart00382 78 KPD-VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKN----------LTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1971-2061 |
1.65e-07 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 53.45 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1971 DTIAGKFEWIDGLLINALEKGHWLLIDNANLCNPSVLDRLNPLFENdgvlmvNERGLVDGTVKVIKPHPNFRMFMTVDPQ 2050
Cdd:pfam07728 47 NIDPGGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPL 120
|
90
....*....|....
gi 1954487186 2051 NG---ELSRAMRNR 2061
Cdd:pfam07728 121 DRglnELSPALRSR 134
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4108-4681 |
1.74e-07 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 58.10 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4108 EGEEGDADGKQSGTGIGEGEGAKDVSHEIEDEEQvLGTQNEERSDEKQDTKEEKNGMDMDNDFEGNLEDMEQDQDEEDES 4187
Cdd:COG5271 297 QAADPESDDDADDSTLAALEGAAEDTEIATADEL-AAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4188 DSSDDEDNEPDEQIGDVDDMDPDAVDDKMWGEEGEDNLNESDKTVEDQGQQQDKQEESDIVAKEEEEGAQDDKKENKPDK 4267
Cdd:COG5271 376 SEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4268 NQQ----------KDSADKDENGDDKEEGEQGEDEGQEGDEKDEGEEGAEEDEDDVQNR---PGEQLDT-EIPEAETLEL 4333
Cdd:COG5271 456 EEEaeaeldteedTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETsadDGADTDAaADPEDSDEDA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4334 PEDmnmEGDDGEDKEGDDGEDKEGDENEETGMDDPMDMDETPAEEQNEEGEAfhdvlDDLNEGEQGEQEDEEMADASAQM 4413
Cdd:COG5271 536 LED---ETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADA-----DETEESADESEEAEASEDEAAEE 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4414 DTEQNEQegdqengeeeseekgeeegkeEVADATGDQEDSKNGAQIEQDEDEDIESTAQNREQPNSDAAADNQF---GVQ 4490
Cdd:COG5271 608 EEADDDE---------------------ADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEAsadESE 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4491 GQSGKQSKSSAGKKEGEDDTADMAEGEDEAEKKENKGKSSSGSNEANEEDNEESAEGAEDEPkrEEANPQRSLGDAlekw 4570
Cdd:COG5271 667 EEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADAEEADTEADGTAEEA--EEAAEEAESADE---- 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4571 rrrlanlndelnneeeenEKTEDKDTEDAQVKEDDAFEYVKNDEDAHDmqamgNAQADQVQDLKTAAMDEDQQD---ENQ 4647
Cdd:COG5271 741 ------------------EAASLPDEADAEEEAEEAEEAEEDDADGLE-----EALEEEKADAEEAATDEEAEAaaeEKE 797
|
570 580 590
....*....|....*....|....*....|....
gi 1954487186 4648 VSGEMNVDQPEDIETMPLPRDTLDMSGSTDQQGA 4681
Cdd:COG5271 798 KVADEDQDTDEDALLDEAEADEEEDLDGEDEETA 831
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1501-1643 |
3.78e-07 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 52.92 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1501 RKPILLEGSPGVGKTSLVSALAAAS---GHHLVRINLSeqtdlmDLFGSDlpVEGGNSGEFAWRDAPFLQAMKRGDWVLL 1577
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFI 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1954487186 1578 DELNLASQSVLEGLNSCLDhrgavyipELDREFFCHAEFRVFGAQNPLQQGGGRKGLPKSFVNRFT 1643
Cdd:cd00009 91 DEIDSLSRGAQNALLRVLE--------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIV 148
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1469-1645 |
2.61e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 53.20 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1469 PRGNLAHTTVKFTLAAPTTSDNAMRVVRAMQLRKPILLEGSPGVGKTSLVSALAAAsghhlVRINLSEQTDLMDLFgsdl 1548
Cdd:PHA02244 87 PAGDISGIDTTKIASNPTFHYETADIAKIVNANIPVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAIMDEF---- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1549 PVEGGNSGEFAWRDAPFLQAMKRGDWVLLDELNLASQSVLEGLNSCLDHRgavYIPELDREFFCHAEFRVFGAQNPLQQG 1628
Cdd:PHA02244 158 ELKGFIDANGKFHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANK---FFDFADERVTAHEDFRVISAGNTLGKG 234
|
170 180
....*....|....*....|..
gi 1954487186 1629 G-----GRKGLPKSFVNRFTQV 1645
Cdd:PHA02244 235 AdhiyvARNKIDGATLDRFAPI 256
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
110-235 |
7.94e-06 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 51.32 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 110 LALSIGAPTLLEGVTGAGKTCLVEELAWRTGRGAGLV--KIHLgdqtDPKVLLGTYVSTSTPGSFRWQAGVLTTAVLegr 187
Cdd:COG0714 26 IALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIqfTPDL----LPSDILGTYIYDQQTGEFEFRPGPLFANVL--- 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1954487186 188 wvLIEDIDLAPAEVLSVLLPLLETGHLFIPsrGEKIKAKAGFHLFGTR 235
Cdd:COG0714 99 --LADEINRAPPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIATQ 142
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
4816-4963 |
8.23e-06 |
|
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 49.38 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4816 IMISVDDSKSMSESRsvqlAYETLALISKALTQLEVGD----ISISSFGERVRLLHPFGQPFTAESGASVLQQFT-FAQQ 4890
Cdd:smart00327 2 VVFLLDGSGSMGGNR----FELAKEFVLKLVEQLDIGPdgdrVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954487186 4891 KTYVKNLIETSLGLFENAKHTSGPGKDdlwQLQLVISDGICEDHDK-LRSLVRSALEQRIMIIFIVVDNKPEKD 4963
Cdd:smart00327 78 GTNLGAALQYALENLFSKSAGSRRGAP---KVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVGVGNDVDEE 148
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
795-1021 |
9.38e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 51.66 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 795 TQLDKESEKLMHDLIHKtilrniqnpqqlitRIPRQPAENFIQFGHFWLEQGQFTPEEDTRYILTQSIEVKL---YNLAR 871
Cdd:PHA02244 46 EKAETEGKEIAIDDIKK--------------EIEDSPEEQFFELPVKIELQQEGKPAGDISGIDTTKIASNPtfhYETAD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 872 V--IMSRKFPVLIQGPTSAGKTSMVEYMAKKTGHRFVRINnhehTDLQEYLGTYVSNNEGKlvFQEGVLVEALRNGYWIV 949
Cdd:PHA02244 112 IakIVNANIPVFLKGGAGSGKNHIAEQIAEALDLDFYFMN----AIMDEFELKGFIDANGK--FHETPFYEAFKKGGLFF 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1954487186 950 LDELNLAPSDVLEALNRLLDDNRELLIPETqevVKPHPHFMLFATQNPAG-----LYGGRKALSRAFRNRFLELHFD 1021
Cdd:PHA02244 186 IDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1162-1271 |
1.94e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 44.83 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1162 LVARCLRYDEPVLLVGDTGCGKTTVCQMLA---ETYGRELHIVNCHQNTEtgdllggqRPVRGQDEDMDKPKQLFEwhdg 1238
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLE--------GLVVAELFGHFLVRLLFE---- 78
|
90 100 110
....*....|....*....|....*....|...
gi 1954487186 1239 plVQSMKDGHLFLLDEISLADDSVLERLNSVLE 1271
Cdd:cd00009 79 --LAEKAKPGVLFIDEIDSLSRGAQNALLRVLE 109
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
884-972 |
2.10e-04 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 45.25 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 884 GPTSAGKTSMVEYMAKK---TGHRFVRIN------NHEHTDLQEYLGTYVSNNEGklvfqeGVLVEAL-RNGYWIVL-DE 952
Cdd:cd19499 48 GPTGVGKTELAKALAELlfgDEDNLIRIDmseymeKHSVSRLIGAPPGYVGYTEG------GQLTEAVrRKPYSVVLlDE 121
|
90 100
....*....|....*....|
gi 1954487186 953 LNLAPSDVLEALNRLLDDNR 972
Cdd:cd19499 122 IEKAHPDVQNLLLQVLDDGR 141
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
876-1015 |
6.75e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 876 RKFPVLIQGPTSAGKTSMVEYMAK---KTGHRFVRIN--NHEHTDLQEYLGTYVSNNEGKLVF---QEGVLVEALRNGY- 946
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDgeDILEEVLDQLLLIIVGGKKASGSGelrLRLALALARKLKPd 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1954487186 947 WIVLDELNLAPSDVLEALNRLLDDNRELLIPETQEVVkphphFMLFATQNPAGLygGRKALSRAFRNRF 1015
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNL-----TVILTTNDEKDL--GPALLRRRFDRRI 142
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
435-502 |
7.11e-04 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 44.78 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 435 KQRPFATT----------GHAlRLMEKIAVTIHLNEP-VLLVGETGTGKTTVVQHLADMIHQNLIVVNLSQ-QSDSSDLL 502
Cdd:COG3267 9 KEKPFSLTpdprflflspSHR-EALARLEYALAQGGGfVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNpQLSPAELL 87
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
459-541 |
8.65e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 459 NEPVLLVGETGTGKTTVVQHLADMI---HQNLIVVNLSQQSDSSDLLGGFKPVDGKVLAIPLNDEFERLFEKTFSVKKNV 535
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
|
....*.
gi 1954487186 536 KFLDMV 541
Cdd:smart00382 82 LILDEI 87
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
446-494 |
1.37e-03 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 42.66 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1954487186 446 LRLMEKIAVTIHLNEPVLLVGETGTGKTTVVQHLADMIHQNLIVVNLSQ 494
Cdd:cd19481 13 RRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4219-4573 |
2.61e-03 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 44.13 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4219 EEGEDNLNESDK-TVEDQGQQQDKQEESDIVAKEEEEGAQDDKKENKPDKNQQKDSA-DKDENGDDKEEGEQGEDEGQEG 4296
Cdd:NF033609 581 DSGSDSTSDSGSdSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSAsDSDSDSDSDSDSDSDSDSDSDS 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4297 DEKDEGEEGAEEDEddvqnrpgeqlDTEIPEAETLELPEDMNMEGDDGEDKEGDDGEDKEGDENEETGMDDPMDMDETPA 4376
Cdd:NF033609 661 DSDSDSDSDSDSDS-----------DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4377 EEQNEEGEAFHDVLDDLNEGEQGEQEDEEMADASAQMDTEqNEQEGDQENGEEESEEKGEEEGKEEVADATGDQeDSKNG 4456
Cdd:NF033609 730 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSD 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4457 AQIEQDEDEDIESTAQNREQPNSDAAADNQFGVQGQSGKQSKSSAGKKEGEDDTADMAEGEDEAEKKENKGKSssGSNEA 4536
Cdd:NF033609 808 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKN--GTNAS 885
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1954487186 4537 NEEDNEESAEGAEDEPKREEANPQ------RSLGdALEKWRRR 4573
Cdd:NF033609 886 NKNEAKDSKEPLPDTGSEDEANTSliwgllASLG-SLLLFRRK 927
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4104-4281 |
2.62e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 44.22 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4104 PAGLEGEEGDADGKQS-----GTGIGEGEGAKDVSHEIEDEEQVLGTQNEERSDEKQDTKEEK----------------- 4161
Cdd:TIGR00927 652 PTEAEGENGEESGGEAeqegeTETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEvehegeteaegtedege 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4162 -----NGMDMDNDFEGNLEDMEQDQDEEDESDSSDDEDNEPDEQIGDVDDMDPDAVDDKMWGEEGEDNLNESDKTVEDQG 4236
Cdd:TIGR00927 732 ietgeEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGE 811
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1954487186 4237 QQQDKQEESDIVAKEE---EEGAQDDKKENKPDKNQQKDSADKDENGD 4281
Cdd:TIGR00927 812 KDEHEGQSETQADDTEvkdETGEQELNAENQGEAKQDEKGVDGGGGSD 859
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
4091-4283 |
2.80e-03 |
|
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) or RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II.
Pssm-ID: 310411 [Multi-domain] Cd Length: 528 Bit Score: 43.78 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4091 NSFNIIITKGFCMPAGLEGEEG-DADGKQSGTGIGEGEGAKDVSHEIEDEEQVLGTQNEERSDEKQ-------------- 4155
Cdd:pfam05793 175 NGFSLMMMKAAKNGPAAFGEHDeETEGEKGGGGRGKDLKIKDLEGDDEDDGDESDKGGEDGDEEKKkkkkkklaknkkkl 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4156 -DTKEEKNGMDmDNDFEGNLEDMEQDQDEEDESDSSDDEDNEPDEQIGDVDDMDpdavddkmwGEEGEDNLNESDKTVED 4234
Cdd:pfam05793 255 dDDKKKKRGGD-DDAFEYDSDDGDDEGREEDYISDSSASGNDPEEREDKLSPEE---------PAKGEIEQSDDSEESEE 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1954487186 4235 qgqqqDKQEESDIVAKEEEEGAQDDKKENKPDKNQQKDSADKDENGDDK 4283
Cdd:pfam05793 325 -----EKNEEEGKLSKKGKKAKKLKGKKNGKDKSESSDGDDSDDSDIDD 368
|
|
| COG2842 |
COG2842 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
413-502 |
5.78e-03 |
|
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];
Pssm-ID: 442090 [Multi-domain] Cd Length: 254 Bit Score: 41.86 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 413 VNLSSIAASGKQKKKASLIKREKQRPFATTGHALRLMEKIAVTIHLNEPVLLVGETGTGKTTVVQHLADMiHQNLIVVNL 492
Cdd:COG2842 4 KTQAAVAKEIGNEKLEAKIARWEAPSFVETKNVRRFAEALDEARALPGIGVVYGESGVGKTTAAREYANR-NPNVIYVTA 82
|
90
....*....|
gi 1954487186 493 SQQSDSSDLL 502
Cdd:COG2842 83 SPSWTSKELL 92
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1501-1591 |
6.25e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1501 RKPILLEGSPGVGKTSLVSALAA---ASGHHLVRINLSEQTDLMDLFGSDLPVEGGNSGEFAWRDAPFLQAM---KRGDW 1574
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALarkLKPDV 81
|
90
....*....|....*..
gi 1954487186 1575 VLLDELNLASQSVLEGL 1591
Cdd:smart00382 82 LILDEITSLLDAEQEAL 98
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| vWA_midasin |
cd01460 |
VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are ... |
4754-5022 |
2.02e-121 |
|
VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are unified by their common archetectural organization that is based upon a conserved ATPase domain. The AAA domain of midasin contains six tandem AAA protomers. The AAA domains in midasin is followed by a D/E rich domain that is following by a VWA domain. The members of this subgroup have a conserved MIDAS motif. The function of this domain is not exactly known although it has been speculated to play a crucial role in midasin function.
Pssm-ID: 238737 Cd Length: 266 Bit Score: 385.17 E-value: 2.02e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4754 LAMGLCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFKKDKIWLRRTKMSKRQYQIMISVDDSKSMSESRSVQ 4833
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4834 LAYETLALISKALTQLEVGDISISSFGERVRLLHPFGQPFTAESGASVLQQFTFAQQKTYVKNLIETSLGLFENAKHTSg 4913
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4914 pGKDDLWQLQLVISDGICEDH-DKLRSLVRSALEQRIMIIFIVVDNKPEKDSILNMTNITYtiDDGKYGiQMKPYLETFP 4992
Cdd:cd01460 160 -SSGSLWQLLLIISDGRGEFSeGAQKVRLREAREQNVFVVFIIIDNPDNKQSILDIKVVSF--KNDKSG-VITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|
gi 1954487186 4993 FQYFMIVRDVASLPEALSDALRQYFSFVAS 5022
Cdd:cd01460 236 FPYYVIVRDLNQLPSVLSDALRQWFELVNS 265
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
711-816 |
1.52e-43 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 407722 Cd Length: 104 Bit Score: 155.05 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 711 DLLQIVKQYIYGIASGDERCyDDVAEFYMSAKKLAnEHKLVDGANQRPHFSMRTLARALTYVVQICPTYGLRRSLYEGFC 790
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLV-RDIVKFYLEAKKLA-EKSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90 100
....*....|....*....|....*.
gi 1954487186 791 MTFLTQLDKESEKLMHDLIHKTILRN 816
Cdd:pfam17865 79 MSFLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1172-1320 |
1.33e-29 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 116.62 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1172 PVLLVGDTGCGKTTVCQMLAE-TYGRELHIVNCHQNTETGDLLGGQRPVRGqdedmdkpkqLFEWHDGPLVQSMKDGHLF 1250
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNIDPG----------GASWVDGPLVRAAREGEIA 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1954487186 1251 LLDEISLADDSVLERLNSVLEPSRLLVlaEKGGkhvEELYGAPE-FKFLATMNPgGDYGKKELSPALRNRF 1320
Cdd:pfam07728 71 VLDEINRANPDVLNSLLSLLDERRLLL--PDGG---ELVKAAPDgFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
879-1015 |
5.47e-25 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 103.53 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 879 PVLIQGPTSAGKTSMVEYMAKKT-GHRFVRINNHEHTDLQEYLGTYVSNNEGKlVFQEGVLVEALRNGYWIVLDELNLAP 957
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1954487186 958 SDVLEALNRLLDDNRELLIPETQEVVKPHPHFMLFATQNPagLYGGRKALSRAFRNRF 1015
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1654-1752 |
7.59e-25 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 101.99 E-value: 7.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1654 DLLFICSHLFSeFEPAVLAKMIEFNNQMYQETMVRCSFGRKGSPWEFNLRDVFRWLELMR--------QNNTVDPAEYLD 1725
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSsllptllsPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*..
gi 1954487186 1726 IIYMQRMRTQEDRKHIAQLFETVFGVK 1752
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
272-386 |
4.32e-21 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 91.21 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 272 ELEQVIRQKFQHIQDFAPHAMELFQTVVGIYEDPNFSSLSSssMGRFLSTRDLMKWCHRVDLLmgekledSNLGMDLTLR 351
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSG--SPREFNLRDLLRWCRRLSSL-------LPTLLSPTVR 71
|
90 100 110
....*....|....*....|....*....|....*
gi 1954487186 352 QDLFNEANDCFCGMISDYNIWMTVLQTIGRPLQIS 386
Cdd:pfam17867 72 EEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1027-1121 |
1.37e-17 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 81.19 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1027 ELETILSKRCAIAPSYCKKLVKVYQDLMAHRQSTRIFEQKHG--FITLRDLFRWAGR---------DPQGYQELAENGYM 1095
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCRRlssllptllSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 1954487186 1096 LLAERCRREEEKKVVKQVLEQVMKVK 1121
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1503-1642 |
1.40e-17 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 82.34 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1503 PILLEGSPGVGKTSLVSALAAA-SGHHLVRINLSEQTDLMDLFGSDLPVEGGnsgeFAWRDAPFLQAMKRGDWVLLDELN 1581
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNIDPGG----ASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954487186 1582 LASQSVLEGLNSCLDHRgavYIPELDREFFCHAE---FRVFGAQNPLQQGGgrKGLPKSFVNRF 1642
Cdd:pfam07728 77 RANPDVLNSLLSLLDER---RLLLPDGGELVKAApdgFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
117-248 |
6.36e-16 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 77.33 E-value: 6.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 117 PTLLEGVTGAGKTCLVEELAWRTgRGAGLVKIHLGDQTDPKVLLGTYVSTstPGSFRWQAGVLTTAVLEGRWVLIEDIDL 196
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL-SNRPVFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEINR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1954487186 197 APAEVLSVLLPLLETGHLFIPSRGEKIKAKA-GFHLFGTrSFVPSRSGKGVSA 248
Cdd:pfam07728 78 ANPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIAT-MNPLDRGLNELSP 129
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1491-1642 |
3.52e-13 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 73.66 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1491 AMRVVRAMQLRKPILLEGSPGVGKTSLVSALAAASGHHLVRINLSEqtDLM--DLFGSDLPVEggNSGEFAWRDAPFLQA 1568
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTP--DLLpsDILGTYIYDQ--QTGEFEFRPGPLFAN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1569 MkrgdwVLLDELNLAS---QSV-LEglnsCLDHRgAVYIP----ELDREFFchaefrVFGAQNPLQQGGGRKgLPKSFVN 1640
Cdd:COG0714 97 V-----LLADEINRAPpktQSAlLE----AMEER-QVTIPggtyKLPEPFL------VIATQNPIEQEGTYP-LPEAQLD 159
|
..
gi 1954487186 1641 RF 1642
Cdd:COG0714 160 RF 161
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
851-1035 |
5.19e-13 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 72.89 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 851 EEDTRYILTQSIEVKLYNLArvIMSRKfPVLIQGPTSAGKTSMVEYMAKKTGHRFVRINNHEHTDLQEYLGTYVSN-NEG 929
Cdd:COG0714 8 AEIGKVYVGQEELIELVLIA--LLAGG-HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDqQTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 930 KLVFQEGVLveaLRNgywIVL-DELNLAP----SDVLEALnrlldDNRELLIPEtqEVVK-PHPhFMLFATQNPAGLYGG 1003
Cdd:COG0714 85 EFEFRPGPL---FAN---VLLaDEINRAPpktqSALLEAM-----EERQVTIPG--GTYKlPEP-FLVIATQNPIEQEGT 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1954487186 1004 RkALSRAFRNRFL-ELHFD--DiPEDELEtILSKR 1035
Cdd:COG0714 151 Y-PLPEAQLDRFLlKLYIGypD-AEEERE-ILRRH 182
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1172-1339 |
1.14e-10 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 65.96 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1172 PVLLVGDTGCGKTTVCQMLAETYGRELHIVNCHQNTETGDLLGgqrpvrgqDEDMDKPKQLFEWHDGPLVQSmkdghLFL 1251
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILG--------TYIYDQQTGEFEFRPGPLFAN-----VLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1252 LDEISLADDSVlerlnsvlePSRLL-VLAEK----GGKHVEelygAPE-FKFLATMNPGGDYGKKELSPALRNRFT-EIW 1324
Cdd:COG0714 100 ADEINRAPPKT---------QSALLeAMEERqvtiPGGTYK----LPEpFLVIATQNPIEQEGTYPLPEAQLDRFLlKLY 166
|
170
....*....|....*..
gi 1954487186 1325 V--PsvtDRDDLINIID 1339
Cdd:COG0714 167 IgyP---DAEEEREILR 180
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
461-697 |
7.10e-10 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 60.00 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 461 PVLLVGETGTGKTTVVQHLADMIH-QNLIVVNLSQQSDSSDLLGGFKPVDGKvlaiplndeferlfektfsvkknvkfld 539
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDPGG---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 540 mvrkmfvhqkwtsfvallkqsvkmsqqkfeaeqnvenkkvsgpqlrnawkmfakhveefevqqvqsqnkfvFSFMEGSLV 619
Cdd:pfam07728 53 -----------------------------------------------------------------------ASWVDGPLV 61
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954487186 620 KAVRNGDWILLDEINLATTETLECLSGLLQDvnGSLLLTEKGDVEPIQRhPNFRLFACMNPAtDVGKRDLPPGLRNRF 697
Cdd:pfam07728 62 RAAREGEIAVLDEINRANPDVLNSLLSLLDE--RRLLLPDGGELVKAAP-DGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1171-1320 |
5.95e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.77 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1171 EPVLLVGDTGCGKTTVCQMLAETYGRELH---IVNCHQNTETGDLLGGQRPVRG---QDEDMDKPKQLFEwhdgpLVQSM 1244
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGgviYIDGEDILEEVLDQLLLIIVGGkkaSGSGELRLRLALA-----LARKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1954487186 1245 KDGhLFLLDEISLADDSVLERLNSVLEPSRLLVLAEKGGKhveelygapeFKFLATMNPGGDYGKKELSPALRNRF 1320
Cdd:smart00382 78 KPD-VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKN----------LTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
1504-1642 |
4.60e-08 |
|
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 429622 [Multi-domain] Cd Length: 131 Bit Score: 54.87 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1504 ILLEGSPGVGKTSLVSALAAASGHHLVRINLSeqTDLM--DLFGSDLPVEggNSGEFAWRDAPFLqamkrGDWVLLDELN 1581
Cdd:pfam07726 2 VLLEGVPGLAKTLLVRTLARSLGLDFRRIQFT--PDLLpsDITGTEVFDQ--KTREFEFRPGPVF-----ANVLLADEIN 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954487186 1582 LAS---QSVLegLNSCLDHR----GAVYipELDREFFchaefrVFGAQNPLQQGGGRKgLPKSFVNRF 1642
Cdd:pfam07726 73 RAPpktQSAL--LEAMQERQvtidGETH--PLPEPFF------VLATQNPIEQEGTYP-LPEAQLDRF 129
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1971-2061 |
1.65e-07 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 53.45 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1971 DTIAGKFEWIDGLLINALEKGHWLLIDNANLCNPSVLDRLNPLFENdgvlmvNERGLVDGTVKVIKPHPNFRMFMTVDPQ 2050
Cdd:pfam07728 47 NIDPGGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPL 120
|
90
....*....|....
gi 1954487186 2051 NG---ELSRAMRNR 2061
Cdd:pfam07728 121 DRglnELSPALRSR 134
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4108-4681 |
1.74e-07 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 58.10 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4108 EGEEGDADGKQSGTGIGEGEGAKDVSHEIEDEEQvLGTQNEERSDEKQDTKEEKNGMDMDNDFEGNLEDMEQDQDEEDES 4187
Cdd:COG5271 297 QAADPESDDDADDSTLAALEGAAEDTEIATADEL-AAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4188 DSSDDEDNEPDEQIGDVDDMDPDAVDDKMWGEEGEDNLNESDKTVEDQGQQQDKQEESDIVAKEEEEGAQDDKKENKPDK 4267
Cdd:COG5271 376 SEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4268 NQQ----------KDSADKDENGDDKEEGEQGEDEGQEGDEKDEGEEGAEEDEDDVQNR---PGEQLDT-EIPEAETLEL 4333
Cdd:COG5271 456 EEEaeaeldteedTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETsadDGADTDAaADPEDSDEDA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4334 PEDmnmEGDDGEDKEGDDGEDKEGDENEETGMDDPMDMDETPAEEQNEEGEAfhdvlDDLNEGEQGEQEDEEMADASAQM 4413
Cdd:COG5271 536 LED---ETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADA-----DETEESADESEEAEASEDEAAEE 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4414 DTEQNEQegdqengeeeseekgeeegkeEVADATGDQEDSKNGAQIEQDEDEDIESTAQNREQPNSDAAADNQF---GVQ 4490
Cdd:COG5271 608 EEADDDE---------------------ADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEAsadESE 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4491 GQSGKQSKSSAGKKEGEDDTADMAEGEDEAEKKENKGKSSSGSNEANEEDNEESAEGAEDEPkrEEANPQRSLGDAlekw 4570
Cdd:COG5271 667 EEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADAEEADTEADGTAEEA--EEAAEEAESADE---- 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4571 rrrlanlndelnneeeenEKTEDKDTEDAQVKEDDAFEYVKNDEDAHDmqamgNAQADQVQDLKTAAMDEDQQD---ENQ 4647
Cdd:COG5271 741 ------------------EAASLPDEADAEEEAEEAEEAEEDDADGLE-----EALEEEKADAEEAATDEEAEAaaeEKE 797
|
570 580 590
....*....|....*....|....*....|....
gi 1954487186 4648 VSGEMNVDQPEDIETMPLPRDTLDMSGSTDQQGA 4681
Cdd:COG5271 798 KVADEDQDTDEDALLDEAEADEEEDLDGEDEETA 831
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
4814-4972 |
2.09e-07 |
|
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.
Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 53.72 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4814 YQIMISVDDSKSMSESRsVQLAYETLALISKALTQLEVGD-ISISSFGERVRLLHPFGQPFTAESGASVLQQFTF-AQQK 4891
Cdd:cd00198 1 ADIVFLLDVSGSMGGEK-LDKAKEALKALVSSLSASPPGDrVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4892 TYVKNLIETSLGLFENAKHTSGPgkddlwQLQLVISDGICEDH-DKLRSLVRSALEQRIMIIFIVVDNKPEKDSILNMTN 4970
Cdd:cd00198 80 TNIGAALRLALELLKSAKRPNAR------RVIILLTDGEPNDGpELLAEAARELRKLGITVYTIGIGDDANEDELKEIAD 153
|
..
gi 1954487186 4971 IT 4972
Cdd:cd00198 154 KT 155
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1501-1643 |
3.78e-07 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 52.92 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1501 RKPILLEGSPGVGKTSLVSALAAAS---GHHLVRINLSeqtdlmDLFGSDlpVEGGNSGEFAWRDAPFLQAMKRGDWVLL 1577
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFI 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1954487186 1578 DELNLASQSVLEGLNSCLDhrgavyipELDREFFCHAEFRVFGAQNPLQQGGGRKGLPKSFVNRFT 1643
Cdd:cd00009 91 DEIDSLSRGAQNALLRVLE--------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIV 148
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4220-4736 |
5.47e-07 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 56.56 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4220 EGEDNLNESDKTVEDQGQQQDKQEESDIVAKEEEEGAQDDKKENKPDKNQQKDSADKDENGDDKEEGEQGEDEGQEGDEK 4299
Cdd:COG5271 284 AEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQD 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4300 DEGEEGAEEDEDDVQNRPGEQLDTEIPEAETLELPEDMNMEGDDGEDKEGDDGEDKEGDeNEETGMDDPMDMDETPAEEQ 4379
Cdd:COG5271 364 AEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADE-DASAGETEDESTDVTSAEDD 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4380 NEEGEAFHDVLDDLNEGEQGEQEDEEMADASAQMD----TEQNEQEGDQENGEEESEEKGEEEGKEEVADAT-GDQEDSK 4454
Cdd:COG5271 443 IATDEEADSLADEEEEAEAELDTEEDTESAEEDADgdeaTDEDDASDDGDEEEAEEDAEAEADSDELTAEETsADDGADT 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4455 NGAQIEQDEDEDIES--TAQNREQPNSDAAADNqfgvqgqsgkqskSSAGKKEGEDDTADMAEGEDEAEKKENKGKSSSG 4532
Cdd:COG5271 523 DAAADPEDSDEDALEdeTEGEENAPGSDQDADE-------------TDEPEATAEEDEPDEAEAETEDATENADADETEE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4533 SneaneEDNEESAEGAEDEPKR-EEANPQRSLGDAlekwrRRLANLNDELNNEEEENEKTEDKDTEDAQVKEDDAFEYVK 4611
Cdd:COG5271 590 S-----ADESEEAEASEDEAAEeEEADDDEADADA-----DGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAE 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4612 NDEDAHDMQAMGNA-----QADQVQDLKTAAMDEDQQDENqvsgemNVDQpeDIETMPLPRDTLDMSGSTDQQGAILSKK 4686
Cdd:COG5271 660 ASADESEEEAEDESetsseDAEEDADAAAAEASDDEEETE------EADE--DAETASEEADAEEADTEADGTAEEAEEA 731
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1954487186 4687 LPENQLLDETQILTMDES-----VVSREPLEQQDIELMREELETRVSDWREEGRD 4736
Cdd:COG5271 732 AEEAESADEEAASLPDEAdaeeeAEEAEEAEEDDADGLEEALEEEKADAEEAATD 786
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1504-1539 |
1.49e-06 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 50.28 E-value: 1.49e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1954487186 1504 ILLEGSPGVGKTSLVSALAAASGHHLVRINLSEQTD 1539
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS 36
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1469-1645 |
2.61e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 53.20 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1469 PRGNLAHTTVKFTLAAPTTSDNAMRVVRAMQLRKPILLEGSPGVGKTSLVSALAAAsghhlVRINLSEQTDLMDLFgsdl 1548
Cdd:PHA02244 87 PAGDISGIDTTKIASNPTFHYETADIAKIVNANIPVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAIMDEF---- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1549 PVEGGNSGEFAWRDAPFLQAMKRGDWVLLDELNLASQSVLEGLNSCLDHRgavYIPELDREFFCHAEFRVFGAQNPLQQG 1628
Cdd:PHA02244 158 ELKGFIDANGKFHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANK---FFDFADERVTAHEDFRVISAGNTLGKG 234
|
170 180
....*....|....*....|..
gi 1954487186 1629 G-----GRKGLPKSFVNRFTQV 1645
Cdd:PHA02244 235 AdhiyvARNKIDGATLDRFAPI 256
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1498-1536 |
4.28e-06 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 49.97 E-value: 4.28e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1954487186 1498 MQLRKPILLEGSPGVGKTSLVSALAAASGHHLVRINLSE 1536
Cdd:cd19481 23 LGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
110-235 |
7.94e-06 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 51.32 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 110 LALSIGAPTLLEGVTGAGKTCLVEELAWRTGRGAGLV--KIHLgdqtDPKVLLGTYVSTSTPGSFRWQAGVLTTAVLegr 187
Cdd:COG0714 26 IALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIqfTPDL----LPSDILGTYIYDQQTGEFEFRPGPLFANVL--- 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1954487186 188 wvLIEDIDLAPAEVLSVLLPLLETGHLFIPsrGEKIKAKAGFHLFGTR 235
Cdd:COG0714 99 --LADEINRAPPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIATQ 142
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
4816-4963 |
8.23e-06 |
|
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 49.38 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4816 IMISVDDSKSMSESRsvqlAYETLALISKALTQLEVGD----ISISSFGERVRLLHPFGQPFTAESGASVLQQFT-FAQQ 4890
Cdd:smart00327 2 VVFLLDGSGSMGGNR----FELAKEFVLKLVEQLDIGPdgdrVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954487186 4891 KTYVKNLIETSLGLFENAKHTSGPGKDdlwQLQLVISDGICEDHDK-LRSLVRSALEQRIMIIFIVVDNKPEKD 4963
Cdd:smart00327 78 GTNLGAALQYALENLFSKSAGSRRGAP---KVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVGVGNDVDEE 148
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
795-1021 |
9.38e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 51.66 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 795 TQLDKESEKLMHDLIHKtilrniqnpqqlitRIPRQPAENFIQFGHFWLEQGQFTPEEDTRYILTQSIEVKL---YNLAR 871
Cdd:PHA02244 46 EKAETEGKEIAIDDIKK--------------EIEDSPEEQFFELPVKIELQQEGKPAGDISGIDTTKIASNPtfhYETAD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 872 V--IMSRKFPVLIQGPTSAGKTSMVEYMAKKTGHRFVRINnhehTDLQEYLGTYVSNNEGKlvFQEGVLVEALRNGYWIV 949
Cdd:PHA02244 112 IakIVNANIPVFLKGGAGSGKNHIAEQIAEALDLDFYFMN----AIMDEFELKGFIDANGK--FHETPFYEAFKKGGLFF 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1954487186 950 LDELNLAPSDVLEALNRLLDDNRELLIPETqevVKPHPHFMLFATQNPAG-----LYGGRKALSRAFRNRFLELHFD 1021
Cdd:PHA02244 186 IDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1481-1583 |
4.28e-05 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 49.77 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1481 TLAAPTTSDNAMRVVRAMQLRKPILLEGSPGVGKTSLVSALAAA------SGHHLV--RINLSEQTDLMDLFgsdlPVEG 1552
Cdd:COG1401 201 DLLREKFEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEAlggednGRIEFVqfHPSWSYEDFLLGYR----PSLD 276
|
90 100 110
....*....|....*....|....*....|....*...
gi 1954487186 1553 gnSGEFAWRDAPFLQAMKRGD-------WVLLDELNLA 1583
Cdd:COG1401 277 --EGKYEPTPGIFLRFCLKAEknpdkpyVLIIDEINRA 312
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
1173-1295 |
7.70e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 45.41 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1173 VLLVGDTGCGKTTVCQMLAETY---GRELHIVNCHQNTETGDL-------LGGQRPVRGQDEDMdkpKQLFEWHdgplVQ 1242
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSPKDLlrallraLGLPLSGRLSKEEL---LAALQQL----LL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1954487186 1243 SMKDGHLFLLDEISLADDSVLERLnsvlepSRLLVLAEKGGKHVeeLYGAPEF 1295
Cdd:pfam13401 81 ALAVAVVLIIDEAQHLSLEALEEL------RDLLNLSSKLLQLI--LVGTPEL 125
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
448-501 |
1.71e-04 |
|
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).
Pssm-ID: 463698 [Multi-domain] Cd Length: 179 Bit Score: 45.46 E-value: 1.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1954487186 448 LMEKIavtIHLNEPVLLVGETGTGKTTVVQHLADMIHQN---LIVVNLSQQSDSSDL 501
Cdd:pfam12775 23 LLDLL---LKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEkylPLFINFSAQTTSNQT 76
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1162-1271 |
1.94e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 44.83 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1162 LVARCLRYDEPVLLVGDTGCGKTTVCQMLA---ETYGRELHIVNCHQNTEtgdllggqRPVRGQDEDMDKPKQLFEwhdg 1238
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLE--------GLVVAELFGHFLVRLLFE---- 78
|
90 100 110
....*....|....*....|....*....|...
gi 1954487186 1239 plVQSMKDGHLFLLDEISLADDSVLERLNSVLE 1271
Cdd:cd00009 79 --LAEKAKPGVLFIDEIDSLSRGAQNALLRVLE 109
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
884-972 |
2.10e-04 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 45.25 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 884 GPTSAGKTSMVEYMAKK---TGHRFVRIN------NHEHTDLQEYLGTYVSNNEGklvfqeGVLVEAL-RNGYWIVL-DE 952
Cdd:cd19499 48 GPTGVGKTELAKALAELlfgDEDNLIRIDmseymeKHSVSRLIGAPPGYVGYTEG------GQLTEAVrRKPYSVVLlDE 121
|
90 100
....*....|....*....|
gi 1954487186 953 LNLAPSDVLEALNRLLDDNR 972
Cdd:cd19499 122 IEKAHPDVQNLLLQVLDDGR 141
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
857-1034 |
2.23e-04 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 47.46 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 857 ILTQSIEVKLYNLARVIMSRKFpVLIQGPTSAGKTSMVEYMAKKTG----HRFVRINNHehtdlQEY------LGTYVSN 926
Cdd:COG1401 202 LLREKFEETLEAFLAALKTKKN-VILAGPPGTGKTYLARRLAEALGgednGRIEFVQFH-----PSWsyedflLGYRPSL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 927 NEGKLVFQEGVLVEALR-------NGYWIVLDELNLAPSD--------VLEALNRLLDDNRELLIPETQEVVKPHPHFML 991
Cdd:COG1401 276 DEGKYEPTPGIFLRFCLkaeknpdKPYVLIIDEINRANVEkyfgellsLLESDKRGEELSIELPYSGEGEEFSIPPNLYI 355
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1954487186 992 FATQNPA--GLYGGRKALSRAFRNRFLELHFDDIPEDELETILSK 1034
Cdd:COG1401 356 IGTMNTDdrSLALSDKALRRRFTFEFLDPDLDKLSNEEVVDLLEE 400
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
876-1015 |
3.71e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 44.06 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 876 RKFPVLIQGPTSAGKTSMVEYMAK---KTGHRFVRINNHEhtdlqEYLGTYVSNNEGKLVFQEGVLVEALRNGYWIVLDE 952
Cdd:cd00009 18 PPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASD-----LLEGLVVAELFGHFLVRLLFELAEKAKPGVLFIDE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1954487186 953 LNLAPSDVLEALNRLLDDnrellipETQEVVKPHPHFMLFATQNPAGLyggrkALSRAFRNRF 1015
Cdd:cd00009 93 IDSLSRGAQNALLRVLET-------LNDLRIDRENVRVIGATNRPLLG-----DLDRALYDRL 143
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
876-1015 |
6.75e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 876 RKFPVLIQGPTSAGKTSMVEYMAK---KTGHRFVRIN--NHEHTDLQEYLGTYVSNNEGKLVF---QEGVLVEALRNGY- 946
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDgeDILEEVLDQLLLIIVGGKKASGSGelrLRLALALARKLKPd 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1954487186 947 WIVLDELNLAPSDVLEALNRLLDDNRELLIPETQEVVkphphFMLFATQNPAGLygGRKALSRAFRNRF 1015
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNL-----TVILTTNDEKDL--GPALLRRRFDRRI 142
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
435-502 |
7.11e-04 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 44.78 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 435 KQRPFATT----------GHAlRLMEKIAVTIHLNEP-VLLVGETGTGKTTVVQHLADMIHQNLIVVNLSQ-QSDSSDLL 502
Cdd:COG3267 9 KEKPFSLTpdprflflspSHR-EALARLEYALAQGGGfVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNpQLSPAELL 87
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
1493-1580 |
7.14e-04 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 45.67 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1493 RVVRAMQLRKP--ILLEGSPGVGKTSLVSALAAASGHHLVRINLSeqtdlmDLFGSDLpvegGNSgEFAWRDApFLQAMK 1570
Cdd:COG0464 181 ELREEYGLPPPrgLLLYGPPGTGKTLLARALAGELGLPLIEVDLS------DLVSKYV----GET-EKNLREV-FDKARG 248
|
90
....*....|.
gi 1954487186 1571 RGDWVLL-DEL 1580
Cdd:COG0464 249 LAPCVLFiDEA 259
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
459-541 |
8.65e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 459 NEPVLLVGETGTGKTTVVQHLADMI---HQNLIVVNLSQQSDSSDLLGGFKPVDGKVLAIPLNDEFERLFEKTFSVKKNV 535
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
|
....*.
gi 1954487186 536 KFLDMV 541
Cdd:smart00382 82 LILDEI 87
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1501-1537 |
9.00e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 45.30 E-value: 9.00e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1954487186 1501 RKPILLEGSPGVGKTSLVSALAAASGHHLVRINLSEQ 1537
Cdd:PRK04195 39 KKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4110-4755 |
9.80e-04 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 45.78 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4110 EEGDADGKQSGTGIGEGEGAKDVSHEIEDEEQVLGTQNEERSDEKQDTKEEKNGMDMDNDFEGNLEDMEQDQDEEDESDS 4189
Cdd:COG5271 360 DTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4190 SDDEDNepDEQIGDVDDMDPDAVDDKMWGEEGEDNlnESDKTVEDQGQQQDKQEESD---IVAKEEEEGAQDDKKEN--K 4264
Cdd:COG5271 440 EDDIAT--DEEADSLADEEEEAEAELDTEEDTESA--EEDADGDEATDEDDASDDGDeeeAEEDAEAEADSDELTAEetS 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4265 PDKNQQKDSADKDENGDDKEEGEQGEDEGQEGDEKdegeegaeededdvQNRPGEQLDTEIPEAETLELPEDMNMEGDDG 4344
Cdd:COG5271 516 ADDGADTDAAADPEDSDEDALEDETEGEENAPGSD--------------QDADETDEPEATAEEDEPDEAEAETEDATEN 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4345 EDKEGDDGEDKEGDENEETGmDDPMDMDETPAEEQNEEGEAfhdvLDDLNEGEQGEQedeemADASAQMDTEQNEQEGDQ 4424
Cdd:COG5271 582 ADADETEESADESEEAEASE-DEAAEEEEADDDEADADADG----AADEEETEEEAA-----EDEAAEPETDASEAADED 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4425 engeeeseekgeeegkeevADATGDQEDSKNGAQIEQDEDEDIESTAQ--NREQPNSDAAADNQ----------FGVQGQ 4492
Cdd:COG5271 652 -------------------ADAETEAEASADESEEEAEDESETSSEDAeeDADAAAAEASDDEEeteeadedaeTASEEA 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4493 SGKQSKSSAGKKEGEDDTADMAEGEDEAEKKENKGKSSSGSNEANEEDNEES-AEGAEDEPKREEANPQRSLGDA-LEKW 4570
Cdd:COG5271 713 DAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDdADGLEEALEEEKADAEEAATDEeAEAA 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4571 RRRLANLNDELNNEEEENEKTEDKDTEDAQVKEDDAfeyVKNDEDAHDMQAMGNAQADQVQDLKTA----AMDEDQQDEN 4646
Cdd:COG5271 793 AEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDE---ETADEALEDIEAGIAEDDEEDDDAAAAkdvdADLDLDADLA 869
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4647 QVSGEMNVDQPEDIET-MPLPRDTLDMSGSTDQQGAILSKKLPENQLLDETQILTMDESVVSREPLEQQDIELMREELET 4725
Cdd:COG5271 870 ADEHEAEEAQEAETDAdADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDA 949
|
650 660 670
....*....|....*....|....*....|
gi 1954487186 4726 RVSDWREEGRDINKArELWQGYENLTHDLA 4755
Cdd:COG5271 950 LALDEAGDEESDDAA-ADDAGDDSLADDDE 978
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1156-1278 |
1.21e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 42.88 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1156 MRRLFSLVARCLRYDEP-VLLVGDTGCGKTTVCQMLAETYGRELHIV---NCHQNTETGDLLG--GQRPVRGQDEDMDKP 1229
Cdd:pfam13191 9 LEQLLDALDRVRSGRPPsVLLTGEAGTGKTTLLRELLRALERDGGYFlrgKCDENLPYSPLLEalTREGLLRQLLDELES 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1954487186 1230 KQLFEWHDGP-------------------------LVQSMKDGH--LFLLDEISLADDS---VLERLNSVLEPSRLLVL 1278
Cdd:pfam13191 89 SLLEAWRAALlealapvpelpgdlaerlldlllrlLDLLARGERplVLVLDDLQWADEAslqLLAALLRLLESLPLLVV 167
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
446-494 |
1.37e-03 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 42.66 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1954487186 446 LRLMEKIAVTIHLNEPVLLVGETGTGKTTVVQHLADMIHQNLIVVNLSQ 494
Cdd:cd19481 13 RRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
1155-1203 |
1.38e-03 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 44.89 E-value: 1.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1954487186 1155 AMRRLFSLVARCLRYDEPVLLVGDTGCGKTTVCQMLAETYGRE---LHIVNC 1203
Cdd:COG3284 329 AMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRAdgpFVAVNC 380
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
1150-1276 |
1.58e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 43.62 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1150 LVWTKAMRRLFSLVARCLRYDEP-VLLVGDTGCGKTTVCQMLAETYGRE---LHIVNCHQNTET-----GDLLGGqrPVR 1220
Cdd:COG3267 22 LFLSPSHREALARLEYALAQGGGfVVLTGEVGTGKTTLLRRLLERLPDDvkvAYIPNPQLSPAEllraiADELGL--EPK 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1954487186 1221 GQDEDmDKPKQLFEWhdgpLVQSMKDG--HLFLLDEISLADDSVLERLnsvlepsRLL 1276
Cdd:COG3267 100 GASKA-DLLRQLQEF----LLELAAAGrrVVLIIDEAQNLPPETLEEL-------RLL 145
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1501-1542 |
1.97e-03 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 42.55 E-value: 1.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1954487186 1501 RKPI---LLEGSPGVGKTSLVSALAAA---SGHHLVRINLSEQTDLMD 1542
Cdd:cd19499 38 NRPIgsfLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKHS 85
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
461-557 |
2.37e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 41.75 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 461 PVLLVGETGTGKTTVVQHLA-DMIHQNLIVVNLsqqsDSSDLLGGFKpVDGKVLAIPLNDEFERLFEKtfsvKKNVKFLD 539
Cdd:cd00009 21 NLLLYGPPGTGKTTLARAIAnELFRPGAPFLYL----NASDLLEGLV-VAELFGHFLVRLLFELAEKA----KPGVLFID 91
|
90
....*....|....*...
gi 1954487186 540 MVRKMFVHQKWTSFVALL 557
Cdd:cd00009 92 EIDSLSRGAQNALLRVLE 109
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4219-4573 |
2.61e-03 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 44.13 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4219 EEGEDNLNESDK-TVEDQGQQQDKQEESDIVAKEEEEGAQDDKKENKPDKNQQKDSA-DKDENGDDKEEGEQGEDEGQEG 4296
Cdd:NF033609 581 DSGSDSTSDSGSdSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSAsDSDSDSDSDSDSDSDSDSDSDS 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4297 DEKDEGEEGAEEDEddvqnrpgeqlDTEIPEAETLELPEDMNMEGDDGEDKEGDDGEDKEGDENEETGMDDPMDMDETPA 4376
Cdd:NF033609 661 DSDSDSDSDSDSDS-----------DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4377 EEQNEEGEAFHDVLDDLNEGEQGEQEDEEMADASAQMDTEqNEQEGDQENGEEESEEKGEEEGKEEVADATGDQeDSKNG 4456
Cdd:NF033609 730 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSD 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4457 AQIEQDEDEDIESTAQNREQPNSDAAADNQFGVQGQSGKQSKSSAGKKEGEDDTADMAEGEDEAEKKENKGKSssGSNEA 4536
Cdd:NF033609 808 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKN--GTNAS 885
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1954487186 4537 NEEDNEESAEGAEDEPKREEANPQ------RSLGdALEKWRRR 4573
Cdd:NF033609 886 NKNEAKDSKEPLPDTGSEDEANTSliwgllASLG-SLLLFRRK 927
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4104-4281 |
2.62e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 44.22 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4104 PAGLEGEEGDADGKQS-----GTGIGEGEGAKDVSHEIEDEEQVLGTQNEERSDEKQDTKEEK----------------- 4161
Cdd:TIGR00927 652 PTEAEGENGEESGGEAeqegeTETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEvehegeteaegtedege 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4162 -----NGMDMDNDFEGNLEDMEQDQDEEDESDSSDDEDNEPDEQIGDVDDMDPDAVDDKMWGEEGEDNLNESDKTVEDQG 4236
Cdd:TIGR00927 732 ietgeEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGE 811
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1954487186 4237 QQQDKQEESDIVAKEE---EEGAQDDKKENKPDKNQQKDSADKDENGD 4281
Cdd:TIGR00927 812 KDEHEGQSETQADDTEvkdETGEQELNAENQGEAKQDEKGVDGGGGSD 859
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
4091-4283 |
2.80e-03 |
|
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) or RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II.
Pssm-ID: 310411 [Multi-domain] Cd Length: 528 Bit Score: 43.78 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4091 NSFNIIITKGFCMPAGLEGEEG-DADGKQSGTGIGEGEGAKDVSHEIEDEEQVLGTQNEERSDEKQ-------------- 4155
Cdd:pfam05793 175 NGFSLMMMKAAKNGPAAFGEHDeETEGEKGGGGRGKDLKIKDLEGDDEDDGDESDKGGEDGDEEKKkkkkkklaknkkkl 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4156 -DTKEEKNGMDmDNDFEGNLEDMEQDQDEEDESDSSDDEDNEPDEQIGDVDDMDpdavddkmwGEEGEDNLNESDKTVED 4234
Cdd:pfam05793 255 dDDKKKKRGGD-DDAFEYDSDDGDDEGREEDYISDSSASGNDPEEREDKLSPEE---------PAKGEIEQSDDSEESEE 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1954487186 4235 qgqqqDKQEESDIVAKEEEEGAQDDKKENKPDKNQQKDSADKDENGDDK 4283
Cdd:pfam05793 325 -----EKNEEEGKLSKKGKKAKKLKGKKNGKDKSESSDGDDSDDSDIDD 368
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
444-491 |
4.75e-03 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 41.23 E-value: 4.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1954487186 444 HALRLMEKIAVTihlNEPVLLVGETGTGKTtvvqHLADMIHQN-------LIVVN 491
Cdd:pfam00158 10 EVLEQAKRVAPT---DAPVLITGESGTGKE----LFARAIHQLspradgpFVAVN 57
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4110-4652 |
4.82e-03 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 43.46 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4110 EEGDADGKQSGTGIGEGEGAKDVSHEIEDEEQvlGTQNEERSDE-KQDTKEEKNGMDMDNDfegNLEDMEQDQDEEDESD 4188
Cdd:COG5271 529 EDSDEDALEDETEGEENAPGSDQDADETDEPE--ATAEEDEPDEaEAETEDATENADADET---EESADESEEAEASEDE 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4189 SSDDEDNEPDEQIGDvddmdpdavddkmwGEEGEDNLNESDKTVEDQGQQQDK------QEESDivaKEEEEGAQDDKKE 4262
Cdd:COG5271 604 AAEEEEADDDEADAD--------------ADGAADEEETEEEAAEDEAAEPETdaseaaDEDAD---AETEAEASADESE 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4263 NKPDKNQQKDSADKDENGDDKEEGEqgedegqegdekdegeegaeededdvqnrPGEQLDTEIPEAETLELPEDMNMEGD 4342
Cdd:COG5271 667 EEAEDESETSSEDAEEDADAAAAEA-----------------------------SDDEEETEEADEDAETASEEADAEEA 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4343 DGEDKEGDDGEDKEGDENEETgmDDPMDMDETPAEEQNEEGEAFHDVLDDLNEGeqgeqedeemADASAQMDTEQNEQEG 4422
Cdd:COG5271 718 DTEADGTAEEAEEAAEEAESA--DEEAASLPDEADAEEEAEEAEEAEEDDADGL----------EEALEEEKADAEEAAT 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4423 DQengeeesEEKGEEEGKEEVADATGDQED--SKNGAQIEQDEDEDIESTAQNREQPNSDAAADNQFGVQGQSGKQSKSS 4500
Cdd:COG5271 786 DE-------EAEAAAEEKEKVADEDQDTDEdaLLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDV 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 4501 AGKKEGEDDTADMAEGEDEAEKKENKGKSSSGSNEANEEDNEESAEGAEDEPKREEANPQRSLGDALEKWRRRLANLNDE 4580
Cdd:COG5271 859 DADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEED 938
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1954487186 4581 LNN----EEEENEKTEDKDTEDAQVKEDDAFEYVKNDEDAHDMQAMGNAQADQVQDLKTAAMDEDQQDENQVSGEM 4652
Cdd:COG5271 939 ELGaaedDLDALALDEAGDEESDDAAADDAGDDSLADDDEALADAADDAEADDSELDASESTGEAEGDEDDDELED 1014
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
1497-1533 |
5.32e-03 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 41.12 E-value: 5.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1497 AMQLRKP-------------ILLEGSPGVGKTSLVSALAAASGHHLVRIN 1533
Cdd:cd19503 17 ELPLKYPelfralglkpprgVLLHGPPGTGKTLLARAVANEAGANFLSIS 66
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
462-502 |
5.51e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 40.02 E-value: 5.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1954487186 462 VLLVGETGTGKTTVVQHLADMIHQ---NLIVVNLSQQSDSSDLL 502
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLPEvrdSVVFVDLPSGTSPKDLL 51
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
1480-1588 |
5.75e-03 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 42.97 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1480 FTLAAPTTSDNAM-----RVVRAMQLRKPILLEGSPGVGKTSLVSALAAASGHH---LVRIN---LSEQTDLMDLFGSdl 1548
Cdd:COG3284 318 AALAALAGGDPAMrralrRARRLADRDIPVLILGETGTGKELFARAIHAASPRAdgpFVAVNcaaIPEELIESELFGY-- 395
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1954487186 1549 pVEGGNSGEFAW-RDAPFLQAMkrGDWVLLDE---LNLASQSVL 1588
Cdd:COG3284 396 -EPGAFTGARRKgRPGKIEQAD--GGTLFLDEigdMPLALQARL 436
|
|
| COG2842 |
COG2842 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
413-502 |
5.78e-03 |
|
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];
Pssm-ID: 442090 [Multi-domain] Cd Length: 254 Bit Score: 41.86 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 413 VNLSSIAASGKQKKKASLIKREKQRPFATTGHALRLMEKIAVTIHLNEPVLLVGETGTGKTTVVQHLADMiHQNLIVVNL 492
Cdd:COG2842 4 KTQAAVAKEIGNEKLEAKIARWEAPSFVETKNVRRFAEALDEARALPGIGVVYGESGVGKTTAAREYANR-NPNVIYVTA 82
|
90
....*....|
gi 1954487186 493 SQQSDSSDLL 502
Cdd:COG2842 83 SPSWTSKELL 92
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1501-1591 |
6.25e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1501 RKPILLEGSPGVGKTSLVSALAA---ASGHHLVRINLSEQTDLMDLFGSDLPVEGGNSGEFAWRDAPFLQAM---KRGDW 1574
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALarkLKPDV 81
|
90
....*....|....*..
gi 1954487186 1575 VLLDELNLASQSVLEGL 1591
Cdd:smart00382 82 LILDEITSLLDAEQEAL 98
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
1158-1202 |
6.64e-03 |
|
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).
Pssm-ID: 463698 [Multi-domain] Cd Length: 179 Bit Score: 40.84 E-value: 6.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1954487186 1158 RLFSLVARCLRYDEPVLLVGDTGCGKTTVCQMLAETYGRELHIVN 1202
Cdd:pfam12775 19 RYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPL 63
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
1501-1536 |
7.16e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 42.30 E-value: 7.16e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1954487186 1501 RKPILLEGSPGVGKTSLVSALAAASGHHLVRINLSE 1536
Cdd:COG1222 112 PKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSE 147
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1173-1326 |
7.99e-03 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 39.88 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1173 VLLVGDTGCGKTTVCQMLAETYGRELHIVNChqntetGDLLGGqrpvrGQDEDMDKPKQLFEWhdgplVQSMKdGHLFLL 1252
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISG------SELVSK-----YVGESEKRLRELFEA-----AKKLA-PCVIFI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954487186 1253 DEIsladDSVLERLNSVLEPSRLLVLAE-----KGGKHVEelygaPEFKFLATMN-PGgdygkkELSPALRNRFT-EIWV 1325
Cdd:pfam00004 64 DEI----DALAGSRGSGGDSESRRVVNQlltelDGFTSSN-----SKVIVIAATNrPD------KLDPALLGRFDrIIEF 128
|
.
gi 1954487186 1326 P 1326
Cdd:pfam00004 129 P 129
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
462-505 |
9.15e-03 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 42.21 E-value: 9.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1954487186 462 VLLVGETGTGKTTVVQHLADMIHQNLIVVNLsqqsdsSDLLGGF 505
Cdd:COG0464 194 LLLYGPPGTGKTLLARALAGELGLPLIEVDL------SDLVSKY 231
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
444-491 |
9.25e-03 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 42.19 E-value: 9.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1954487186 444 HALRLMEKIAvtiHLNEPVLLVGETGTGKTtvvqHLADMIHQN-------LIVVN 491
Cdd:COG3284 332 RALRRARRLA---DRDIPVLILGETGTGKE----LFARAIHAAspradgpFVAVN 379
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
1498-1534 |
9.68e-03 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410908 [Multi-domain] Cd Length: 182 Bit Score: 40.62 E-value: 9.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1954487186 1498 MQLRK----PIL-LEGSPGVGKTSLVSALAAASGHHLVRINL 1534
Cdd:cd19500 29 RKLKGsmkgPILcLVGPPGVGKTSLGKSIARALGRKFVRISL 70
|
|
| |
