|
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 ... |
5071-5339 |
2.40e-123 |
|
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: 390.56 E-value: 2.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 5071 LAMGLCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFKKDKIWLRRTKPSKRQYQVMISVDDSKSMSESHSVQ 5150
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 5151 LAYEALSLISKALSQLEVGDISITSFGERVRLLHPFDQPFTAESGANVIQQFTFAQQKTYVKNLIETSVGLFESAkhSSG 5230
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDA--RTQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 5231 PGNAELWQLQLIISDGICEDHNTL-RALVRNALDQQIMMIFIVVDNKPEKDSILNMTNVKYtvKDGKYGiQMNPYLETFP 5309
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAqKVRLREAREQNVFVVFIIIDNPDNKQSILDIKVVSF--KNDKSG-VITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|
gi 1964352332 5310 FQYFMVLRDINSLPEALSDALRQYFSFVSA 5339
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 ... |
949-1054 |
1.67e-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: 1.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 949 DLLQIVKQYIAGIaSGDERSYDDVAEFYMNAKKLAaEHKLVDGANQRPHFSMRTLARALTYVTQIFPVYGLRRSLYEGFC 1028
Cdd:pfam17865 1 DLELLVKAYLKGV-SSDDDLVRDIVKFYLEAKKLA-EKSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90 100
....*....|....*....|....*.
gi 1964352332 1029 MTFLTQLDKESEVLMRDLIFKTILRG 1054
Cdd:pfam17865 79 MSFLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1416-1566 |
4.23e-31 |
|
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: 120.86 E-value: 4.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1416 PVLLVGETGCGKTTVCQMLAE-TYNRELHIVNCHQNTETGDLLGGqRPVRNREAnedpekqqqlfEWHDGPLVQAMKDGH 1494
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGR-RNIDPGGA-----------SWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1964352332 1495 LFLLDEISLADDSVLERLNSVLEPSRLLVlaEKGGKhvEELYGATNFQFLATMNPgGDYGKKELSPALRNRF 1566
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLDERRLLL--PDGGE--LVKAAPDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1117-1253 |
9.92e-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: 102.76 E-value: 9.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1117 PVLIQGPTSAGKTSMVEYMAKKT-GHRFVRINNHEHTDLQEYLGTYVSNNEGKlIFQEGVLVEALRNGYWIVLDELNLAP 1195
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1964352332 1196 SDVLEALNRLLDDNRELLIPETQEIVKPHPHFMLFATQNPagLYGGRKALSRAFRNRF 1253
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 ... |
1901-1999 |
7.26e-24 |
|
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: 99.30 E-value: 7.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1901 DLLFICSHLFSeFEPSTMAKMIDFNNKMYEETMIRCSFGRKGSPWEFNLRDVFRWLELMQ--------KDNVIDPAEYLD 1972
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSsllptllsPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*..
gi 1964352332 1973 IIYMQRMRTHDDRVQIVQLYESVFNVK 1999
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 ... |
509-624 |
1.42e-20 |
|
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: 89.67 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 509 ELETVVRQKFIHIGDFATHVMTLFQTVVGMYQDPNFSTLASStmGRFLSTRDLMKWCHRVDILIGEKLNDNTevgmdlal 588
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGS--PREFNLRDLLRWCRRLSSLLPTLLSPTV-------- 70
|
90 100 110
....*....|....*....|....*....|....*.
gi 1964352332 589 RQDLFSEANDCFCGMIPDYNVWMTVLENLGRPLQIS 624
Cdd:pfam17867 71 REEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1265-1359 |
3.41e-18 |
|
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: 83.12 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1265 ELETILSKRCAIAPSYCKKLVKVYKELMERRQSTRIFEQKHG--FITLRDLFRWAGR---------DPQGYQELAENGYM 1333
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCRRlssllptllSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 1964352332 1334 LLAERCRKDEEKKVVKQVLEQVMKVK 1359
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
354-485 |
7.63e-18 |
|
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: 83.11 E-value: 7.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 354 PTLLEGVTGAGKTALIEELASRTgRGAELVKIHLGDQTDPKVLLGTYVSTstPGSFRWQAGVLTTAVLEGRWVLIEDIDL 433
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL-SNRPVFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEINR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1964352332 434 APAEVLSVLLPLLETRHLFIPSRGEKIKAK-EGFQLFGTrSFVPTRSGKGMSS 485
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 ... |
1750-1889 |
1.34e-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: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1750 PILLEGSPGVGKTSLVSALAAA-SGHNLVRINLSEQTDLMDLFGSDLPVEGGnsgeFAWRDAPFLQAMKAGDWVLLDELN 1828
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNIDPGG----ASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1964352332 1829 LASQSVLEGLNSCLDHRgAVYIPELDREFFCAKE-FRVFGAQNPLQQGGgrKGLPKSFVNRF 1889
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 ... |
699-935 |
1.02e-09 |
|
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: 59.61 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 699 PVLLVGETGTGKTTVVQHLADMIH-QNLIVVNLSQQSDSSDLLGGFKPVDGKvlaipmkeeferlfektfsvkkngkfle 777
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDPGG---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 778 mvrktfihqkwpnfvtllkqavkmsqqkfeaeqnaeskrvssptlrnawktftkkveefevqqvqsqnkfvFNFMEGSLV 857
Cdd:pfam07728 53 -----------------------------------------------------------------------ASWVDGPLV 61
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1964352332 858 KAVRQGDWILLDEINLATTETLECLSGLLQDAHgsLLLTEKGDVEPIKRhPNFRLFACMNPAtDVGKRDLPPGLRNRF 935
Cdd:pfam07728 62 RAAREGEIAVLDEINRANPDVLNSLLSLLDERR--LLLPDGGELVKAAP-DGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
2226-2312 |
1.77e-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: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 2226 GKFEWIDGLLINALEKGYWLLIDNANMCNPSVLDRLNPLFENdgvlmvNERGLVDGTVKVIKPHPNFRMFMTVDPQNG-- 2303
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 1964352332 2304 -ELSRAMRNR 2312
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| MDN1 super family |
cl34967 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4414-5053 |
8.85e-05 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
The actual alignment was detected with superfamily member COG5271:
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 49.24 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4414 AGADDGEEGDADGMMAGTGMGEGEGNKDVSEEIEDEEQVLGTQNEERNNDDKQDTKEEKNGMDMENDFDGNLEDIEQDED 4493
Cdd:COG5271 167 ADEGDELAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4494 KEEDDSDDSDSDEEDPDEQIGDVDDMDPDAVDDKMWGDEAEENLKESDKTVEDQGNQDQQQESEIVAKEEDDQQNDSKGE 4573
Cdd:COG5271 247 TLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIAT 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4574 KPEKSDKNDKQQEADGEEGDGDEEMDDENQDGGDDEEDNEAEGEGEDEDDVENKAGEQLNAEIPEAETLELPDDLNMDGD 4653
Cdd:COG5271 327 ADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGG 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4654 DNGDEEGEEGQEMNDPMDMDEQPANQGEEEQLPEEDENAEAFHDALDDVDQNPNEDEEMADASAQMDTEQGEGEEDEENN 4733
Cdd:COG5271 407 TSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDD 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4734 ASGDEEEKEENEELAPEvGDSEQQQKSGQIE-EDEQNDEEENKAQNREQPNSDATADNQFGVQGESgKQSKSSAGKKEGE 4812
Cdd:COG5271 487 ASDDGDEEEAEEDAEAE-ADSDELTAEETSAdDGADTDAAADPEDSDEDALEDETEGEENAPGSDQ-DADETDEPEATAE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4813 DDTADTNDAEDETAEKKEQKGKSERGANQANEEEDDENEEQGDQEAEDQEAKEAQSNPQRSLGDALEKWRRRLADLDDEA 4892
Cdd:COG5271 565 EDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDA 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4893 ENEEEET--DADKEKKTDDPDTEDAKVNEEDSFEYVKNDEDAHDMQTMGNAQPDQVQDLKMGGMDEEKEDLKETSgemDV 4970
Cdd:COG5271 645 SEAADEDadAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADAEEADT---EA 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4971 DQQAEDVDtmplprDTLEMSGSTDNQGAilskklPEQQLIDEtevltmDESVVAREPLEQEDIERMRDELETQVSDWREE 5050
Cdd:COG5271 722 DGTAEEAE------EAAEEAESADEEAA------SLPDEADA------EEEAEEAEEAEEDDADGLEEALEEEKADAEEA 783
|
...
gi 1964352332 5051 GRD 5053
Cdd:COG5271 784 ATD 786
|
|
| COG2842 super family |
cl34499 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
651-740 |
3.05e-04 |
|
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: 46.10 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 651 VNLSSIAASGKQKQKQALIKREKKRPFATTGHALRLMERIAVCIHLTEPVLLVGETGTGKTTVVQHLADMiHQNLIVVNL 730
Cdd:COG2842 4 KTQAAVAKEIGNEKLEAKIARWEAPSFVETKNVRRFAEALDEARALPGIGVVYGESGVGKTTAAREYANR-NPNVIYVTA 82
|
90
....*....|
gi 1964352332 731 SQQSDSSDLL 740
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 ... |
5071-5339 |
2.40e-123 |
|
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: 390.56 E-value: 2.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 5071 LAMGLCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFKKDKIWLRRTKPSKRQYQVMISVDDSKSMSESHSVQ 5150
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 5151 LAYEALSLISKALSQLEVGDISITSFGERVRLLHPFDQPFTAESGANVIQQFTFAQQKTYVKNLIETSVGLFESAkhSSG 5230
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDA--RTQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 5231 PGNAELWQLQLIISDGICEDHNTL-RALVRNALDQQIMMIFIVVDNKPEKDSILNMTNVKYtvKDGKYGiQMNPYLETFP 5309
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAqKVRLREAREQNVFVVFIIIDNPDNKQSILDIKVVSF--KNDKSG-VITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|
gi 1964352332 5310 FQYFMVLRDINSLPEALSDALRQYFSFVSA 5339
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 ... |
949-1054 |
1.67e-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: 1.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 949 DLLQIVKQYIAGIaSGDERSYDDVAEFYMNAKKLAaEHKLVDGANQRPHFSMRTLARALTYVTQIFPVYGLRRSLYEGFC 1028
Cdd:pfam17865 1 DLELLVKAYLKGV-SSDDDLVRDIVKFYLEAKKLA-EKSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90 100
....*....|....*....|....*.
gi 1964352332 1029 MTFLTQLDKESEVLMRDLIFKTILRG 1054
Cdd:pfam17865 79 MSFLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1416-1566 |
4.23e-31 |
|
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: 120.86 E-value: 4.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1416 PVLLVGETGCGKTTVCQMLAE-TYNRELHIVNCHQNTETGDLLGGqRPVRNREAnedpekqqqlfEWHDGPLVQAMKDGH 1494
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGR-RNIDPGGA-----------SWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1964352332 1495 LFLLDEISLADDSVLERLNSVLEPSRLLVlaEKGGKhvEELYGATNFQFLATMNPgGDYGKKELSPALRNRF 1566
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLDERRLLL--PDGGE--LVKAAPDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1117-1253 |
9.92e-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: 102.76 E-value: 9.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1117 PVLIQGPTSAGKTSMVEYMAKKT-GHRFVRINNHEHTDLQEYLGTYVSNNEGKlIFQEGVLVEALRNGYWIVLDELNLAP 1195
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1964352332 1196 SDVLEALNRLLDDNRELLIPETQEIVKPHPHFMLFATQNPagLYGGRKALSRAFRNRF 1253
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 ... |
1901-1999 |
7.26e-24 |
|
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: 99.30 E-value: 7.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1901 DLLFICSHLFSeFEPSTMAKMIDFNNKMYEETMIRCSFGRKGSPWEFNLRDVFRWLELMQ--------KDNVIDPAEYLD 1972
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSsllptllsPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*..
gi 1964352332 1973 IIYMQRMRTHDDRVQIVQLYESVFNVK 1999
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 ... |
509-624 |
1.42e-20 |
|
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: 89.67 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 509 ELETVVRQKFIHIGDFATHVMTLFQTVVGMYQDPNFSTLASStmGRFLSTRDLMKWCHRVDILIGEKLNDNTevgmdlal 588
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGS--PREFNLRDLLRWCRRLSSLLPTLLSPTV-------- 70
|
90 100 110
....*....|....*....|....*....|....*.
gi 1964352332 589 RQDLFSEANDCFCGMIPDYNVWMTVLENLGRPLQIS 624
Cdd:pfam17867 71 REEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1265-1359 |
3.41e-18 |
|
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: 83.12 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1265 ELETILSKRCAIAPSYCKKLVKVYKELMERRQSTRIFEQKHG--FITLRDLFRWAGR---------DPQGYQELAENGYM 1333
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCRRlssllptllSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 1964352332 1334 LLAERCRKDEEKKVVKQVLEQVMKVK 1359
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
354-485 |
7.63e-18 |
|
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: 83.11 E-value: 7.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 354 PTLLEGVTGAGKTALIEELASRTgRGAELVKIHLGDQTDPKVLLGTYVSTstPGSFRWQAGVLTTAVLEGRWVLIEDIDL 433
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL-SNRPVFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEINR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1964352332 434 APAEVLSVLLPLLETRHLFIPSRGEKIKAK-EGFQLFGTrSFVPTRSGKGMSS 485
Cdd:pfam07728 78 ANPDVLNSLLSLLDERRLLLPDGGELVKAApDGFRLIAT-MNPLDRGLNELSP 129
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1750-1889 |
1.34e-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: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1750 PILLEGSPGVGKTSLVSALAAA-SGHNLVRINLSEQTDLMDLFGSDLPVEGGnsgeFAWRDAPFLQAMKAGDWVLLDELN 1828
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNIDPGG----ASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1964352332 1829 LASQSVLEGLNSCLDHRgAVYIPELDREFFCAKE-FRVFGAQNPLQQGGgrKGLPKSFVNRF 1889
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDgFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1738-1889 |
1.31e-12 |
|
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: 72.12 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1738 AMRVIRSMQLKKPILLEGSPGVGKTSLVSALAAASGHNLVRINLSEqtDLM--DLFGSDLPVEggNSGEFAWRDAPFLQA 1815
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTP--DLLpsDILGTYIYDQ--QTGEFEFRPGPLFAN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1964352332 1816 MkagdwVLLDELNLAS---QSV-LEglnsCLDHRgAVYIPelDREFFCAKEFRVFGAQNPLQQGGGRKgLPKSFVNRF 1889
Cdd:COG0714 97 V-----LLADEINRAPpktQSAlLE----AMEER-QVTIP--GGTYKLPEPFLVIATQNPIEQEGTYP-LPEAQLDRF 161
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1117-1273 |
1.48e-11 |
|
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: 68.66 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1117 PVLIQGPTSAGKTSMVEYMAKKTGHRFVRINNHEHTDLQEYLGTYVSN-NEGKLIFQEGVLveaLRNgywIVL-DELNLA 1194
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDqQTGEFEFRPGPL---FAN---VLLaDEINRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1195 P----SDVLEALnrlldDNRELLIPEtQEIVKPHPhFMLFATQNPAGLYGGRkALSRAFRNRFL-ELHFD--DiPEDELE 1267
Cdd:COG0714 107 PpktqSALLEAM-----EERQVTIPG-GTYKLPEP-FLVIATQNPIEQEGTY-PLPEAQLDRFLlKLYIGypD-AEEERE 177
|
....*.
gi 1964352332 1268 tILSKR 1273
Cdd:COG0714 178 -ILRRH 182
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1413-1566 |
7.92e-11 |
|
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: 63.55 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1413 HNEPVLLVGETGCGKTTVCQMLAETYNRELH---IVNCHQNTETGDLLGGQRPVRNREANEDPEKQQ-QLFEwhdgpLVQ 1488
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrLALA-----LAR 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1964352332 1489 AMKDGhLFLLDEISLADDSVLERLNSVLEPSRLLVLAEKggkhveelygATNFQFLATMNPGGDYGKKELSPALRNRF 1566
Cdd:smart00382 76 KLKPD-VLILDEITSLLDAEQEALLLLLEELRLLLLLKS----------EKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1416-1585 |
1.20e-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: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1416 PVLLVGETGCGKTTVCQMLAETYNRELHIVNCHQNTETGDLLGgqrpvrnreaNEDPEKQQQLFEWHDGPLVQamkdgHL 1495
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILG----------TYIYDQQTGEFEFRPGPLFA-----NV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1496 FLLDEISLADDSVlerlnsvlePSRLL-VLAEK----GGKHVEElygATNFQFLATMNPGGDYGKKELSPALRNRFT-EI 1569
Cdd:COG0714 98 LLADEINRAPPKT---------QSALLeAMEERqvtiPGGTYKL---PEPFLVIATQNPIEQEGTYPLPEAQLDRFLlKL 165
|
170
....*....|....*...
gi 1964352332 1570 WV--PsvtDRDDLIKIID 1585
Cdd:COG0714 166 YIgyP---DAEEEREILR 180
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
699-935 |
1.02e-09 |
|
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: 59.61 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 699 PVLLVGETGTGKTTVVQHLADMIH-QNLIVVNLSQQSDSSDLLGGFKPVDGKvlaipmkeeferlfektfsvkkngkfle 777
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDPGG---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 778 mvrktfihqkwpnfvtllkqavkmsqqkfeaeqnaeskrvssptlrnawktftkkveefevqqvqsqnkfvFNFMEGSLV 857
Cdd:pfam07728 53 -----------------------------------------------------------------------ASWVDGPLV 61
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1964352332 858 KAVRQGDWILLDEINLATTETLECLSGLLQDAHgsLLLTEKGDVEPIKRhPNFRLFACMNPAtDVGKRDLPPGLRNRF 935
Cdd:pfam07728 62 RAAREGEIAVLDEINRANPDVLNSLLSLLDERR--LLLPDGGELVKAAP-DGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
344-472 |
1.08e-07 |
|
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: 57.10 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 344 AVSLALSIGAPTLLEGVTGAGKTALIEELASRTGRGAELV--KIHLgdqtDPKVLLGTYVSTSTPGSFRWQAGVLTTAVL 421
Cdd:COG0714 23 LVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIqfTPDL----LPSDILGTYIYDQQTGEFEFRPGPLFANVL 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1964352332 422 egrwvLIEDIDLAPAEVLSVLLPLLETRHLFIPsrGEKIKAKEGFQLFGTR 472
Cdd:COG0714 99 -----LADEINRAPPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIATQ 142
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2226-2312 |
1.77e-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: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 2226 GKFEWIDGLLINALEKGYWLLIDNANMCNPSVLDRLNPLFENdgvlmvNERGLVDGTVKVIKPHPNFRMFMTVDPQNG-- 2303
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 1964352332 2304 -ELSRAMRNR 2312
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1748-1890 |
3.98e-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: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1748 KKPILLEGSPGVGKTSLVSALAAAS---GHNLVRINLSeqtdlmDLFGSDlpVEGGNSGEFAWRDAPFLQAMKAGDWVLL 1824
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFI 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1964352332 1825 DELNLASQSVLEGLNSCLDhrgavyipELDREFFCAKEFRVFGAQNPLQQGGGRKGLPKSFVNRFT 1890
Cdd:cd00009 91 DEIDSLSRGAQNALLRVLE--------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIV 148
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1064-1259 |
3.20e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 53.20 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1064 QIPRQPHEDFIQFGYFWLQQGQFPPEDDTRYILTN---SVETKLYNLARV--IMSRKFPVLIQGPTSAGKTSMVEYMAKK 1138
Cdd:PHA02244 63 EIEDSPEEQFFELPVKIELQQEGKPAGDISGIDTTkiaSNPTFHYETADIakIVNANIPVFLKGGAGSGKNHIAEQIAEA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1139 TGHRFVRINnhehTDLQEYLGTYVSNNEGKliFQEGVLVEALRNGYWIVLDELNLAPSDVLEALNRLLDDNRELLIPETq 1218
Cdd:PHA02244 143 LDLDFYFMN----AIMDEFELKGFIDANGK--FHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANKFFDFADER- 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1964352332 1219 eiVKPHPHFMLFATQNPAG-----LYGGRKALSRAFRNRFLELHFD 1259
Cdd:PHA02244 216 --VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1716-1901 |
2.04e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 50.50 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1716 PRGQLAKTDIKFTLLAPTTADNAMRVIRSMQLKKPILLEGSPGVGKTSLVSALAAAsghnlVRINLSEQTDLMDLFgsdl 1795
Cdd:PHA02244 87 PAGDISGIDTTKIASNPTFHYETADIAKIVNANIPVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAIMDEF---- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1796 PVEGGNSGEFAWRDAPFLQAMKAGDWVLLDELNLASQSVLEGLNSCLDHRgavYIPELDREFFCAKEFRVFGAQNPLQQG 1875
Cdd:PHA02244 158 ELKGFIDANGKFHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANK---FFDFADERVTAHEDFRVISAGNTLGKG 234
|
170 180 190
....*....|....*....|....*....|....*...
gi 1964352332 1876 G-----GRKGLPKSFVNRFTQVYVE-------QLTSDD 1901
Cdd:PHA02244 235 AdhiyvARNKIDGATLDRFAPIEFDydekiehLISNGD 272
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1406-1569 |
2.79e-05 |
|
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: 47.53 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1406 LVARCLQHNEPVLLVGETGCGKTTVCQMLA---ETYNRELHIVNCHQNTETGDLLGGQRPVRNREANEDPEKqqqlfewh 1482
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1483 dgplvqamKDGHLFLLDEIsladDSVLERLNSVLEpsRLLVLAEKGGKHVEELygatnFQFLATMNPGGDygkkELSPAL 1562
Cdd:cd00009 83 --------AKPGVLFIDEI----DSLSRGAQNALL--RVLETLNDLRIDRENV-----RVIGATNRPLLG----DLDRAL 139
|
....*..
gi 1964352332 1563 RNRFTEI 1569
Cdd:cd00009 140 YDRLDIR 146
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4414-5053 |
8.85e-05 |
|
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: 49.24 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4414 AGADDGEEGDADGMMAGTGMGEGEGNKDVSEEIEDEEQVLGTQNEERNNDDKQDTKEEKNGMDMENDFDGNLEDIEQDED 4493
Cdd:COG5271 167 ADEGDELAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4494 KEEDDSDDSDSDEEDPDEQIGDVDDMDPDAVDDKMWGDEAEENLKESDKTVEDQGNQDQQQESEIVAKEEDDQQNDSKGE 4573
Cdd:COG5271 247 TLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIAT 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4574 KPEKSDKNDKQQEADGEEGDGDEEMDDENQDGGDDEEDNEAEGEGEDEDDVENKAGEQLNAEIPEAETLELPDDLNMDGD 4653
Cdd:COG5271 327 ADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGG 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4654 DNGDEEGEEGQEMNDPMDMDEQPANQGEEEQLPEEDENAEAFHDALDDVDQNPNEDEEMADASAQMDTEQGEGEEDEENN 4733
Cdd:COG5271 407 TSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDD 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4734 ASGDEEEKEENEELAPEvGDSEQQQKSGQIE-EDEQNDEEENKAQNREQPNSDATADNQFGVQGESgKQSKSSAGKKEGE 4812
Cdd:COG5271 487 ASDDGDEEEAEEDAEAE-ADSDELTAEETSAdDGADTDAAADPEDSDEDALEDETEGEENAPGSDQ-DADETDEPEATAE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4813 DDTADTNDAEDETAEKKEQKGKSERGANQANEEEDDENEEQGDQEAEDQEAKEAQSNPQRSLGDALEKWRRRLADLDDEA 4892
Cdd:COG5271 565 EDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDA 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4893 ENEEEET--DADKEKKTDDPDTEDAKVNEEDSFEYVKNDEDAHDMQTMGNAQPDQVQDLKMGGMDEEKEDLKETSgemDV 4970
Cdd:COG5271 645 SEAADEDadAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADAEEADT---EA 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4971 DQQAEDVDtmplprDTLEMSGSTDNQGAilskklPEQQLIDEtevltmDESVVAREPLEQEDIERMRDELETQVSDWREE 5050
Cdd:COG5271 722 DGTAEEAE------EAAEEAESADEEAA------SLPDEADA------EEEAEEAEEAEEDDADGLEEALEEEKADAEEA 783
|
...
gi 1964352332 5051 GRD 5053
Cdd:COG5271 784 ATD 786
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1114-1253 |
1.99e-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: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1114 RKFPVLIQGPTSAGKTSMVEYMAK---KTGHRFVRINNHEhtdlqEYLGTYVSNNEGKLIFQEGVLVEALRNGYWIVLDE 1190
Cdd:cd00009 18 PPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASD-----LLEGLVVAELFGHFLVRLLFELAEKAKPGVLFIDE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1964352332 1191 LNLAPSDVLEALNRLLDDnrellipETQEIVKPHPHFMLFATQNPAGLyggrkALSRAFRNRF 1253
Cdd:cd00009 93 IDSLSRGAQNALLRVLET-------LNDLRIDRENVRVIGATNRPLLG-----DLDRALYDRL 143
|
|
| COG2842 |
COG2842 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
651-740 |
3.05e-04 |
|
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];
Pssm-ID: 442090 [Multi-domain] Cd Length: 254 Bit Score: 46.10 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 651 VNLSSIAASGKQKQKQALIKREKKRPFATTGHALRLMERIAVCIHLTEPVLLVGETGTGKTTVVQHLADMiHQNLIVVNL 730
Cdd:COG2842 4 KTQAAVAKEIGNEKLEAKIARWEAPSFVETKNVRRFAEALDEARALPGIGVVYGESGVGKTTAAREYANR-NPNVIYVTA 82
|
90
....*....|
gi 1964352332 731 SQQSDSSDLL 740
Cdd:COG2842 83 SPSWTSKELL 92
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5133-5280 |
3.09e-04 |
|
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: 44.75 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 5133 VMISVDDSKSMSESHsvqlAYEALSLISKALSQLEVGD----ISITSFGERVRLLHPFDQPFTAESGANVIQQFT-FAQQ 5207
Cdd:smart00327 2 VVFLLDGSGSMGGNR----FELAKEFVLKLVEQLDIGPdgdrVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1964352332 5208 KTYVKNLIETSVGLFESAKHSSGPGNAelwQLQLIISDGICEDHNT-LRALVRNALDQQIMMIFIVVDNKPEKD 5280
Cdd:smart00327 78 GTNLGAALQYALENLFSKSAGSRRGAP---KVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVGVGNDVDEE 148
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
677-740 |
3.60e-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: 45.93 E-value: 3.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1964352332 677 FATTGHAlRLMERIAVCIHLTEP-VLLVGETGTGKTTVVQHLADMIHQNLIVVNLSQ-QSDSSDLL 740
Cdd:COG3267 23 FLSPSHR-EALARLEYALAQGGGfVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNpQLSPAELL 87
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1114-1253 |
5.35e-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: 43.52 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1114 RKFPVLIQGPTSAGKTSMVEYMAK---KTGHRFVRIN--NHEHTDLQEYLGTYVSNNEGKLIF---QEGVLVEALRNGY- 1184
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDgeDILEEVLDQLLLIIVGGKKASGSGelrLRLALALARKLKPd 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1964352332 1185 WIVLDELNLAPSDVLEALNRLLDDNRELLIPETQEIVkphphFMLFATQNPAGLygGRKALSRAFRNRF 1253
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNL-----TVILTTNDEKDL--GPALLRRRFDRRI 142
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
684-732 |
1.23e-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: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1964352332 684 LRLMERIAVCIHLTEPVLLVGETGTGKTTVVQHLADMIHQNLIVVNLSQ 732
Cdd:cd19481 13 RRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| |
|
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 ... |
5071-5339 |
2.40e-123 |
|
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: 390.56 E-value: 2.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 5071 LAMGLCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFKKDKIWLRRTKPSKRQYQVMISVDDSKSMSESHSVQ 5150
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 5151 LAYEALSLISKALSQLEVGDISITSFGERVRLLHPFDQPFTAESGANVIQQFTFAQQKTYVKNLIETSVGLFESAkhSSG 5230
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDA--RTQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 5231 PGNAELWQLQLIISDGICEDHNTL-RALVRNALDQQIMMIFIVVDNKPEKDSILNMTNVKYtvKDGKYGiQMNPYLETFP 5309
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAqKVRLREAREQNVFVVFIIIDNPDNKQSILDIKVVSF--KNDKSG-VITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|
gi 1964352332 5310 FQYFMVLRDINSLPEALSDALRQYFSFVSA 5339
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 ... |
949-1054 |
1.67e-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: 1.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 949 DLLQIVKQYIAGIaSGDERSYDDVAEFYMNAKKLAaEHKLVDGANQRPHFSMRTLARALTYVTQIFPVYGLRRSLYEGFC 1028
Cdd:pfam17865 1 DLELLVKAYLKGV-SSDDDLVRDIVKFYLEAKKLA-EKSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90 100
....*....|....*....|....*.
gi 1964352332 1029 MTFLTQLDKESEVLMRDLIFKTILRG 1054
Cdd:pfam17865 79 MSFLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1416-1566 |
4.23e-31 |
|
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: 120.86 E-value: 4.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1416 PVLLVGETGCGKTTVCQMLAE-TYNRELHIVNCHQNTETGDLLGGqRPVRNREAnedpekqqqlfEWHDGPLVQAMKDGH 1494
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGR-RNIDPGGA-----------SWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1964352332 1495 LFLLDEISLADDSVLERLNSVLEPSRLLVlaEKGGKhvEELYGATNFQFLATMNPgGDYGKKELSPALRNRF 1566
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLDERRLLL--PDGGE--LVKAAPDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1117-1253 |
9.92e-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: 102.76 E-value: 9.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1117 PVLIQGPTSAGKTSMVEYMAKKT-GHRFVRINNHEHTDLQEYLGTYVSNNEGKlIFQEGVLVEALRNGYWIVLDELNLAP 1195
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1964352332 1196 SDVLEALNRLLDDNRELLIPETQEIVKPHPHFMLFATQNPagLYGGRKALSRAFRNRF 1253
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 ... |
1901-1999 |
7.26e-24 |
|
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: 99.30 E-value: 7.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1901 DLLFICSHLFSeFEPSTMAKMIDFNNKMYEETMIRCSFGRKGSPWEFNLRDVFRWLELMQ--------KDNVIDPAEYLD 1972
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSsllptllsPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*..
gi 1964352332 1973 IIYMQRMRTHDDRVQIVQLYESVFNVK 1999
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 ... |
509-624 |
1.42e-20 |
|
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: 89.67 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 509 ELETVVRQKFIHIGDFATHVMTLFQTVVGMYQDPNFSTLASStmGRFLSTRDLMKWCHRVDILIGEKLNDNTevgmdlal 588
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGS--PREFNLRDLLRWCRRLSSLLPTLLSPTV-------- 70
|
90 100 110
....*....|....*....|....*....|....*.
gi 1964352332 589 RQDLFSEANDCFCGMIPDYNVWMTVLENLGRPLQIS 624
Cdd:pfam17867 71 REEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1265-1359 |
3.41e-18 |
|
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: 83.12 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1265 ELETILSKRCAIAPSYCKKLVKVYKELMERRQSTRIFEQKHG--FITLRDLFRWAGR---------DPQGYQELAENGYM 1333
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCRRlssllptllSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 1964352332 1334 LLAERCRKDEEKKVVKQVLEQVMKVK 1359
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
354-485 |
7.63e-18 |
|
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: 83.11 E-value: 7.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 354 PTLLEGVTGAGKTALIEELASRTgRGAELVKIHLGDQTDPKVLLGTYVSTstPGSFRWQAGVLTTAVLEGRWVLIEDIDL 433
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL-SNRPVFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEINR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1964352332 434 APAEVLSVLLPLLETRHLFIPSRGEKIKAK-EGFQLFGTrSFVPTRSGKGMSS 485
Cdd:pfam07728 78 ANPDVLNSLLSLLDERRLLLPDGGELVKAApDGFRLIAT-MNPLDRGLNELSP 129
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1750-1889 |
1.34e-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: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1750 PILLEGSPGVGKTSLVSALAAA-SGHNLVRINLSEQTDLMDLFGSDLPVEGGnsgeFAWRDAPFLQAMKAGDWVLLDELN 1828
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNIDPGG----ASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1964352332 1829 LASQSVLEGLNSCLDHRgAVYIPELDREFFCAKE-FRVFGAQNPLQQGGgrKGLPKSFVNRF 1889
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDgFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1738-1889 |
1.31e-12 |
|
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: 72.12 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1738 AMRVIRSMQLKKPILLEGSPGVGKTSLVSALAAASGHNLVRINLSEqtDLM--DLFGSDLPVEggNSGEFAWRDAPFLQA 1815
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTP--DLLpsDILGTYIYDQ--QTGEFEFRPGPLFAN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1964352332 1816 MkagdwVLLDELNLAS---QSV-LEglnsCLDHRgAVYIPelDREFFCAKEFRVFGAQNPLQQGGGRKgLPKSFVNRF 1889
Cdd:COG0714 97 V-----LLADEINRAPpktQSAlLE----AMEER-QVTIP--GGTYKLPEPFLVIATQNPIEQEGTYP-LPEAQLDRF 161
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1117-1273 |
1.48e-11 |
|
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: 68.66 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1117 PVLIQGPTSAGKTSMVEYMAKKTGHRFVRINNHEHTDLQEYLGTYVSN-NEGKLIFQEGVLveaLRNgywIVL-DELNLA 1194
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDqQTGEFEFRPGPL---FAN---VLLaDEINRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1195 P----SDVLEALnrlldDNRELLIPEtQEIVKPHPhFMLFATQNPAGLYGGRkALSRAFRNRFL-ELHFD--DiPEDELE 1267
Cdd:COG0714 107 PpktqSALLEAM-----EERQVTIPG-GTYKLPEP-FLVIATQNPIEQEGTY-PLPEAQLDRFLlKLYIGypD-AEEERE 177
|
....*.
gi 1964352332 1268 tILSKR 1273
Cdd:COG0714 178 -ILRRH 182
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1413-1566 |
7.92e-11 |
|
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: 63.55 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1413 HNEPVLLVGETGCGKTTVCQMLAETYNRELH---IVNCHQNTETGDLLGGQRPVRNREANEDPEKQQ-QLFEwhdgpLVQ 1488
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrLALA-----LAR 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1964352332 1489 AMKDGhLFLLDEISLADDSVLERLNSVLEPSRLLVLAEKggkhveelygATNFQFLATMNPGGDYGKKELSPALRNRF 1566
Cdd:smart00382 76 KLKPD-VLILDEITSLLDAEQEALLLLLEELRLLLLLKS----------EKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1416-1585 |
1.20e-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: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1416 PVLLVGETGCGKTTVCQMLAETYNRELHIVNCHQNTETGDLLGgqrpvrnreaNEDPEKQQQLFEWHDGPLVQamkdgHL 1495
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILG----------TYIYDQQTGEFEFRPGPLFA-----NV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1496 FLLDEISLADDSVlerlnsvlePSRLL-VLAEK----GGKHVEElygATNFQFLATMNPGGDYGKKELSPALRNRFT-EI 1569
Cdd:COG0714 98 LLADEINRAPPKT---------QSALLeAMEERqvtiPGGTYKL---PEPFLVIATQNPIEQEGTYPLPEAQLDRFLlKL 165
|
170
....*....|....*...
gi 1964352332 1570 WV--PsvtDRDDLIKIID 1585
Cdd:COG0714 166 YIgyP---DAEEEREILR 180
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
699-935 |
1.02e-09 |
|
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: 59.61 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 699 PVLLVGETGTGKTTVVQHLADMIH-QNLIVVNLSQQSDSSDLLGGFKPVDGKvlaipmkeeferlfektfsvkkngkfle 777
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDPGG---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 778 mvrktfihqkwpnfvtllkqavkmsqqkfeaeqnaeskrvssptlrnawktftkkveefevqqvqsqnkfvFNFMEGSLV 857
Cdd:pfam07728 53 -----------------------------------------------------------------------ASWVDGPLV 61
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1964352332 858 KAVRQGDWILLDEINLATTETLECLSGLLQDAHgsLLLTEKGDVEPIKRhPNFRLFACMNPAtDVGKRDLPPGLRNRF 935
Cdd:pfam07728 62 RAAREGEIAVLDEINRANPDVLNSLLSLLDERR--LLLPDGGELVKAAP-DGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
1751-1889 |
1.26e-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: 56.41 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1751 ILLEGSPGVGKTSLVSALAAASGHNLVRINLSeqTDLM--DLFGSDLPVEggNSGEFAWRDAPFLqamkaGDWVLLDELN 1828
Cdd:pfam07726 2 VLLEGVPGLAKTLLVRTLARSLGLDFRRIQFT--PDLLpsDITGTEVFDQ--KTREFEFRPGPVF-----ANVLLADEIN 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1964352332 1829 LAS---QSVLegLNSCLDHR----GAVYipELDREFFcakefrVFGAQNPLQQGGGRKgLPKSFVNRF 1889
Cdd:pfam07726 73 RAPpktQSAL--LEAMQERQvtidGETH--PLPEPFF------VLATQNPIEQEGTYP-LPEAQLDRF 129
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
344-472 |
1.08e-07 |
|
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: 57.10 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 344 AVSLALSIGAPTLLEGVTGAGKTALIEELASRTGRGAELV--KIHLgdqtDPKVLLGTYVSTSTPGSFRWQAGVLTTAVL 421
Cdd:COG0714 23 LVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIqfTPDL----LPSDILGTYIYDQQTGEFEFRPGPLFANVL 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1964352332 422 egrwvLIEDIDLAPAEVLSVLLPLLETRHLFIPsrGEKIKAKEGFQLFGTR 472
Cdd:COG0714 99 -----LADEINRAPPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIATQ 142
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
5131-5286 |
1.31e-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: 54.49 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 5131 YQVMISVDDSKSMSEShSVQLAYEALSLISKALSQLEVGD-ISITSFGERVRLLHPFDQPFTAESGANVIQQFTF-AQQK 5208
Cdd:cd00198 1 ADIVFLLDVSGSMGGE-KLDKAKEALKALVSSLSASPPGDrVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1964352332 5209 TYVKNLIETSVGLFESAKHSSGPGNAelwqlqLIISDGICEDHNT-LRALVRNALDQQIMMIFIVVDNKPEKDSILNMT 5286
Cdd:cd00198 80 TNIGAALRLALELLKSAKRPNARRVI------ILLTDGEPNDGPElLAEAARELRKLGITVYTIGIGDDANEDELKEIA 152
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2226-2312 |
1.77e-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: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 2226 GKFEWIDGLLINALEKGYWLLIDNANMCNPSVLDRLNPLFENdgvlmvNERGLVDGTVKVIKPHPNFRMFMTVDPQNG-- 2303
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 1964352332 2304 -ELSRAMRNR 2312
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1748-1890 |
3.98e-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: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1748 KKPILLEGSPGVGKTSLVSALAAAS---GHNLVRINLSeqtdlmDLFGSDlpVEGGNSGEFAWRDAPFLQAMKAGDWVLL 1824
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFI 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1964352332 1825 DELNLASQSVLEGLNSCLDhrgavyipELDREFFCAKEFRVFGAQNPLQQGGGRKGLPKSFVNRFT 1890
Cdd:cd00009 91 DEIDSLSRGAQNALLRVLE--------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIV 148
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1751-1786 |
2.00e-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: 2.00e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1964352332 1751 ILLEGSPGVGKTSLVSALAAASGHNLVRINLSEQTD 1786
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS 36
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1064-1259 |
3.20e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 53.20 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1064 QIPRQPHEDFIQFGYFWLQQGQFPPEDDTRYILTN---SVETKLYNLARV--IMSRKFPVLIQGPTSAGKTSMVEYMAKK 1138
Cdd:PHA02244 63 EIEDSPEEQFFELPVKIELQQEGKPAGDISGIDTTkiaSNPTFHYETADIakIVNANIPVFLKGGAGSGKNHIAEQIAEA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1139 TGHRFVRINnhehTDLQEYLGTYVSNNEGKliFQEGVLVEALRNGYWIVLDELNLAPSDVLEALNRLLDDNRELLIPETq 1218
Cdd:PHA02244 143 LDLDFYFMN----AIMDEFELKGFIDANGK--FHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANKFFDFADER- 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1964352332 1219 eiVKPHPHFMLFATQNPAG-----LYGGRKALSRAFRNRFLELHFD 1259
Cdd:PHA02244 216 --VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1743-1783 |
3.42e-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: 50.36 E-value: 3.42e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1964352332 1743 RSMQLKKPILLEGSPGVGKTSLVSALAAASGHNLVRINLSE 1783
Cdd:cd19481 21 YGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1716-1901 |
2.04e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 50.50 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1716 PRGQLAKTDIKFTLLAPTTADNAMRVIRSMQLKKPILLEGSPGVGKTSLVSALAAAsghnlVRINLSEQTDLMDLFgsdl 1795
Cdd:PHA02244 87 PAGDISGIDTTKIASNPTFHYETADIAKIVNANIPVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAIMDEF---- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1796 PVEGGNSGEFAWRDAPFLQAMKAGDWVLLDELNLASQSVLEGLNSCLDHRgavYIPELDREFFCAKEFRVFGAQNPLQQG 1875
Cdd:PHA02244 158 ELKGFIDANGKFHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANK---FFDFADERVTAHEDFRVISAGNTLGKG 234
|
170 180 190
....*....|....*....|....*....|....*...
gi 1964352332 1876 G-----GRKGLPKSFVNRFTQVYVE-------QLTSDD 1901
Cdd:PHA02244 235 AdhiyvARNKIDGATLDRFAPIEFDydekiehLISNGD 272
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
1394-1522 |
2.71e-05 |
|
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: 49.40 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1394 LVWTKAMRRLFNLVARCLQHNEP-VLLVGETGCGKTTVCQMLAETYNRE---LHIVNCHQNTET-----GDLLGGQRPVR 1464
Cdd:COG3267 22 LFLSPSHREALARLEYALAQGGGfVVLTGEVGTGKTTLLRRLLERLPDDvkvAYIPNPQLSPAEllraiADELGLEPKGA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1465 NREanedpEKQQQLFEWhdgpLVQAMKDG--HLFLLDEISLADDSVLERLnsvlepsRLL 1522
Cdd:COG3267 102 SKA-----DLLRQLQEF----LLELAAAGrrVVLIIDEAQNLPPETLEEL-------RLL 145
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1406-1569 |
2.79e-05 |
|
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: 47.53 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1406 LVARCLQHNEPVLLVGETGCGKTTVCQMLA---ETYNRELHIVNCHQNTETGDLLGGQRPVRNREANEDPEKqqqlfewh 1482
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1483 dgplvqamKDGHLFLLDEIsladDSVLERLNSVLEpsRLLVLAEKGGKHVEELygatnFQFLATMNPGGDygkkELSPAL 1562
Cdd:cd00009 83 --------AKPGVLFIDEI----DSLSRGAQNALL--RVLETLNDLRIDRENV-----RVIGATNRPLLG----DLDRAL 139
|
....*..
gi 1964352332 1563 RNRFTEI 1569
Cdd:cd00009 140 YDRLDIR 146
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1685-1830 |
2.90e-05 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 50.54 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1685 KPNATELEILGETKDKVQTAGDKFAIGPFQIPRGQLAKTDIKF-TLLAPTTADNAMRVIRSMQLKKPILLEGSPGVGKTS 1763
Cdd:COG1401 157 ALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLkDLLREKFEETLEAFLAALKTKKNVILAGPPGTGKTY 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1764 LVSALAAA-SGHNLVRINL-------SEQTDLMDLFgsdlPVEGgnSGEFAWRDAPFLQAM-KAGD------WVLLDELN 1828
Cdd:COG1401 237 LARRLAEAlGGEDNGRIEFvqfhpswSYEDFLLGYR----PSLD--EGKYEPTPGIFLRFClKAEKnpdkpyVLIIDEIN 310
|
..
gi 1964352332 1829 LA 1830
Cdd:COG1401 311 RA 312
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4414-5053 |
8.85e-05 |
|
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: 49.24 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4414 AGADDGEEGDADGMMAGTGMGEGEGNKDVSEEIEDEEQVLGTQNEERNNDDKQDTKEEKNGMDMENDFDGNLEDIEQDED 4493
Cdd:COG5271 167 ADEGDELAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4494 KEEDDSDDSDSDEEDPDEQIGDVDDMDPDAVDDKMWGDEAEENLKESDKTVEDQGNQDQQQESEIVAKEEDDQQNDSKGE 4573
Cdd:COG5271 247 TLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIAT 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4574 KPEKSDKNDKQQEADGEEGDGDEEMDDENQDGGDDEEDNEAEGEGEDEDDVENKAGEQLNAEIPEAETLELPDDLNMDGD 4653
Cdd:COG5271 327 ADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGG 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4654 DNGDEEGEEGQEMNDPMDMDEQPANQGEEEQLPEEDENAEAFHDALDDVDQNPNEDEEMADASAQMDTEQGEGEEDEENN 4733
Cdd:COG5271 407 TSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDD 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4734 ASGDEEEKEENEELAPEvGDSEQQQKSGQIE-EDEQNDEEENKAQNREQPNSDATADNQFGVQGESgKQSKSSAGKKEGE 4812
Cdd:COG5271 487 ASDDGDEEEAEEDAEAE-ADSDELTAEETSAdDGADTDAAADPEDSDEDALEDETEGEENAPGSDQ-DADETDEPEATAE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4813 DDTADTNDAEDETAEKKEQKGKSERGANQANEEEDDENEEQGDQEAEDQEAKEAQSNPQRSLGDALEKWRRRLADLDDEA 4892
Cdd:COG5271 565 EDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDA 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4893 ENEEEET--DADKEKKTDDPDTEDAKVNEEDSFEYVKNDEDAHDMQTMGNAQPDQVQDLKMGGMDEEKEDLKETSgemDV 4970
Cdd:COG5271 645 SEAADEDadAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADAEEADT---EA 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 4971 DQQAEDVDtmplprDTLEMSGSTDNQGAilskklPEQQLIDEtevltmDESVVAREPLEQEDIERMRDELETQVSDWREE 5050
Cdd:COG5271 722 DGTAEEAE------EAAEEAESADEEAA------SLPDEADA------EEEAEEAEEAEEDDADGLEEALEEEKADAEEA 783
|
...
gi 1964352332 5051 GRD 5053
Cdd:COG5271 784 ATD 786
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
1399-1447 |
1.45e-04 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 48.36 E-value: 1.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1964352332 1399 AMRRLFNLVARCLQHNEPVLLVGETGCGKTTVCQMLAETYNRE---LHIVNC 1447
Cdd:COG3284 329 AMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRAdgpFVAVNC 380
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
699-739 |
1.87e-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: 1.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1964352332 699 PVLLVGETGTGKTTVVQHLADMIHQN---LIVVNLSQQSDSSDL 739
Cdd:pfam12775 33 PVLLVGPTGTGKTVIIQNLLRKLDKEkylPLFINFSAQTTSNQT 76
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1114-1253 |
1.99e-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: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1114 RKFPVLIQGPTSAGKTSMVEYMAK---KTGHRFVRINNHEhtdlqEYLGTYVSNNEGKLIFQEGVLVEALRNGYWIVLDE 1190
Cdd:cd00009 18 PPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASD-----LLEGLVVAELFGHFLVRLLFELAEKAKPGVLFIDE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1964352332 1191 LNLAPSDVLEALNRLLDDnrellipETQEIVKPHPHFMLFATQNPAGLyggrkALSRAFRNRF 1253
Cdd:cd00009 93 IDSLSRGAQNALLRVLET-------LNDLRIDRENVRVIGATNRPLLG-----DLDRALYDRL 143
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1122-1210 |
2.38e-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: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1122 GPTSAGKTSMVEYMAKK---TGHRFVRIN------NHEHTDLQEYLGTYVSNNEGklifqeGVLVEAL-RNGYWIVL-DE 1190
Cdd:cd19499 48 GPTGVGKTELAKALAELlfgDEDNLIRIDmseymeKHSVSRLIGAPPGYVGYTEG------GQLTEAVrRKPYSVVLlDE 121
|
90 100
....*....|....*....|
gi 1964352332 1191 LNLAPSDVLEALNRLLDDNR 1210
Cdd:cd19499 122 IEKAHPDVQNLLLQVLDDGR 141
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1400-1524 |
2.74e-04 |
|
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: 44.80 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1400 MRRLFNLVARCLQHNEP-VLLVGETGCGKTTVCQMLAETYNRELHIV---NCHQNTETGDLLGGQRPVRNREANEDPEKQ 1475
Cdd:pfam13191 9 LEQLLDALDRVRSGRPPsVLLTGEAGTGKTTLLRELLRALERDGGYFlrgKCDENLPYSPLLEALTREGLLRQLLDELES 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1964352332 1476 QQLFEWHDGP-------------------------LVQAMKDGH--LFLLDEISLADD---SVLERLNSVLEPSRLLVL 1524
Cdd:pfam13191 89 SLLEAWRAALlealapvpelpgdlaerlldlllrlLDLLARGERplVLVLDDLQWADEaslQLLAALLRLLESLPLLVV 167
|
|
| COG2842 |
COG2842 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
651-740 |
3.05e-04 |
|
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];
Pssm-ID: 442090 [Multi-domain] Cd Length: 254 Bit Score: 46.10 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 651 VNLSSIAASGKQKQKQALIKREKKRPFATTGHALRLMERIAVCIHLTEPVLLVGETGTGKTTVVQHLADMiHQNLIVVNL 730
Cdd:COG2842 4 KTQAAVAKEIGNEKLEAKIARWEAPSFVETKNVRRFAEALDEARALPGIGVVYGESGVGKTTAAREYANR-NPNVIYVTA 82
|
90
....*....|
gi 1964352332 731 SQQSDSSDLL 740
Cdd:COG2842 83 SPSWTSKELL 92
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5133-5280 |
3.09e-04 |
|
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: 44.75 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 5133 VMISVDDSKSMSESHsvqlAYEALSLISKALSQLEVGD----ISITSFGERVRLLHPFDQPFTAESGANVIQQFT-FAQQ 5207
Cdd:smart00327 2 VVFLLDGSGSMGGNR----FELAKEFVLKLVEQLDIGPdgdrVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1964352332 5208 KTYVKNLIETSVGLFESAKHSSGPGNAelwQLQLIISDGICEDHNT-LRALVRNALDQQIMMIFIVVDNKPEKD 5280
Cdd:smart00327 78 GTNLGAALQYALENLFSKSAGSRRGAP---KVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVGVGNDVDEE 148
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
677-740 |
3.60e-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: 45.93 E-value: 3.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1964352332 677 FATTGHAlRLMERIAVCIHLTEP-VLLVGETGTGKTTVVQHLADMIHQNLIVVNLSQ-QSDSSDLL 740
Cdd:COG3267 23 FLSPSHR-EALARLEYALAQGGGfVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNpQLSPAELL 87
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1089-1272 |
4.11e-04 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 46.69 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1089 EDDTRYILTNSVETKLYNLARVIMSRKFpVLIQGPTSAGKTSMVEYMAKKTG----HRFVRINNHehtdlQEY------L 1158
Cdd:COG1401 196 DDYLKDLLREKFEETLEAFLAALKTKKN-VILAGPPGTGKTYLARRLAEALGgednGRIEFVQFH-----PSWsyedflL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1159 GTYVSNNEGKLIFQEGVLVEALR-------NGYWIVLDELNLAPSD--------VLEALNRLLDDNRELLIPETQEIVKP 1223
Cdd:COG1401 270 GYRPSLDEGKYEPTPGIFLRFCLkaeknpdKPYVLIIDEINRANVEkyfgellsLLESDKRGEELSIELPYSGEGEEFSI 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1964352332 1224 HPHFMLFATQNPA--GLYGGRKALSRAFRNRFLELHFDDIPEDELETILSK 1272
Cdd:COG1401 350 PPNLYIIGTMNTDdrSLALSDKALRRRFTFEFLDPDLDKLSNEEVVDLLEE 400
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1748-1784 |
4.18e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 46.45 E-value: 4.18e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1964352332 1748 KKPILLEGSPGVGKTSLVSALAAASGHNLVRINLSEQ 1784
Cdd:PRK04195 39 KKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
1417-1520 |
4.29e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 43.48 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1417 VLLVGETGCGKTTVCQMLAETY---NRELHIVNCHQNTETGDLLggqRPVRN---REANEDPEKQQQLFEWHDgpLVQAM 1490
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSPKDLL---RALLRalgLPLSGRLSKEELLAALQQ--LLLAL 82
|
90 100 110
....*....|....*....|....*....|
gi 1964352332 1491 KDGHLFLLDEISLADDSVLERLNSVLEPSR 1520
Cdd:pfam13401 83 AVAVVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
1406-1446 |
4.52e-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: 44.30 E-value: 4.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1964352332 1406 LVARCLQHNEPVLLVGETGCGKTTVCQMLAETYNRELHIVN 1446
Cdd:pfam12775 23 LLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPL 63
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1114-1253 |
5.35e-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: 43.52 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1114 RKFPVLIQGPTSAGKTSMVEYMAK---KTGHRFVRIN--NHEHTDLQEYLGTYVSNNEGKLIF---QEGVLVEALRNGY- 1184
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDgeDILEEVLDQLLLIIVGGKKASGSGelrLRLALALARKLKPd 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1964352332 1185 WIVLDELNLAPSDVLEALNRLLDDNRELLIPETQEIVkphphFMLFATQNPAGLygGRKALSRAFRNRF 1253
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNL-----TVILTTNDEKDL--GPALLRRRFDRRI 142
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
1740-1827 |
6.46e-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: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1740 RVIRSMQLKKP--ILLEGSPGVGKTSLVSALAAASGHNLVRINLSeqtdlmDLFGSDLpvegGNSgEFAWRDApFLQAMK 1817
Cdd:COG0464 181 ELREEYGLPPPrgLLLYGPPGTGKTLLARALAGELGLPLIEVDLS------DLVSKYV----GET-EKNLREV-FDKARG 248
|
90
....*....|.
gi 1964352332 1818 AGDWVLL-DEL 1827
Cdd:COG0464 249 LAPCVLFiDEA 259
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
684-732 |
1.23e-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: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1964352332 684 LRLMERIAVCIHLTEPVLLVGETGTGKTTVVQHLADMIHQNLIVVNLSQ 732
Cdd:cd19481 13 RRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1417-1572 |
1.76e-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: 41.81 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1417 VLLVGETGCGKTTVCQMLAETYNRELHIVNCHQntetgdllggqrpVRNREANEDPEKQQQLFEwhdgplvQAMKDG-HL 1495
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-------------LVSKYVGESEKRLRELFE-------AAKKLApCV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1496 FLLDEI-SLA------DDSVLERLNSVlepsrLLVLAEKGGKHVEELY--GATNFQFLatmnpggdygkkeLSPALRNRF 1566
Cdd:pfam00004 61 IFIDEIdALAgsrgsgGDSESRRVVNQ-----LLTELDGFTSSNSKVIviAATNRPDK-------------LDPALLGRF 122
|
....*..
gi 1964352332 1567 T-EIWVP 1572
Cdd:pfam00004 123 DrIIEFP 129
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1748-1789 |
2.46e-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: 42.16 E-value: 2.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1964352332 1748 KKPI---LLEGSPGVGKTSLVSALAAA---SGHNLVRINLSEQTDLMD 1789
Cdd:cd19499 38 NRPIgsfLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKHS 85
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
1746-1781 |
2.62e-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: 42.16 E-value: 2.62e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1964352332 1746 QLKKPIL-LEGSPGVGKTSLVSALAAASGHNLVRINL 1781
Cdd:cd19500 34 SMKGPILcLVGPPGVGKTSLGKSIARALGRKFVRISL 70
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
689-769 |
3.79e-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: 41.36 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 689 RIAVCIHLTEPVLLVGETGTGKTTVVQHLA-DMIHQNLIVVNLsqqsDSSDLLGGFKpVDGKVLAIPMKEEFERLFEKTF 767
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIAnELFRPGAPFLYL----NASDLLEGLV-VAELFGHFLVRLLFELAEKAKP 85
|
..
gi 1964352332 768 SV 769
Cdd:cd00009 86 GV 87
|
|
| Sigma54_activ_2 |
pfam14532 |
Sigma-54 interaction domain; |
1397-1481 |
4.42e-03 |
|
Sigma-54 interaction domain;
Pssm-ID: 434021 [Multi-domain] Cd Length: 138 Bit Score: 40.79 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 1397 TKAMRRLFNLVARCLQHNEPVLLVGETGCGKTTVCQMLAETYNRELHIVNC----HQNTETGDLLGGQRPVRNREANEDP 1472
Cdd:pfam14532 4 SAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIeylaHAPLELLEQAKGGTLYLKDIADLSK 83
|
....*....
gi 1964352332 1473 EKQQQLFEW 1481
Cdd:pfam14532 84 ALQKGLLLL 92
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
700-740 |
4.75e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 40.40 E-value: 4.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1964352332 700 VLLVGETGTGKTTVVQHLADMIHQ---NLIVVNLSQQSDSSDLL 740
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLPEvrdSVVFVDLPSGTSPKDLL 51
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
611-743 |
7.15e-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: 42.59 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964352332 611 MTVLENLGRPLQISEELVRNYVDQYKPVLEIDESTIRIgrvnLSSIAasGKQKQKQALIKREKkrpFATTGHALRLMERI 690
Cdd:COG0464 118 LLELLRESAEALALAAPLVTYEDIGGLEEELLELREAI----LDDLG--GLEEVKEELRELVA---LPLKRPELREEYGL 188
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1964352332 691 AVCIHltepVLLVGETGTGKTTVVQHLADMIHQNLIVVNLsqqsdsSDLLGGF 743
Cdd:COG0464 189 PPPRG----LLLYGPPGTGKTLLARALAGELGLPLIEVDL------SDLVSKY 231
|
|
| |
