|
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 ... |
5078-5346 |
2.47e-124 |
|
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: 393.64 E-value: 2.47e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5078 LAMGLCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFKKDKIWLRRTKPSKRQYQVMISVDDSKSMSESHSVQ 5157
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5158 LAYEALSLISKALSQLEVGDISITSFGERVRLLHPFDQPFTAESGANVIQQFTFAQQKTYVKNLIETSVGLFESAkhSSG 5237
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDA--RTQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5238 PGNAELWQLQLIISDGICEDHNTL-RALVRNALDQQIMMIFIVVDNKPEKDSILNMTNVKYtiKDGKYGiQMNPYLETFP 5316
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAqKVRLREAREQNVFVVFIIIDNPDNKQSILDIKVVSF--KNDKSG-VITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|
gi 758354136 5317 FQYFMVLRDINSLPEVLSDALRQYFSFVSA 5346
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 ... |
951-1056 |
9.36e-45 |
|
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: 158.90 E-value: 9.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 951 DLLQIVKQYLAGIaSGDERSYDDVAEFYMNAKKLAaEHKLVDGANQRPHFSMRTLARALTYVAQIFPVYGLRRSLYEGFC 1030
Cdd:pfam17865 1 DLELLVKAYLKGV-SSDDDLVRDIVKFYLEAKKLA-EKSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90 100
....*....|....*....|....*.
gi 758354136 1031 MTFLTQLDKESEVLMRDLIFKTILRG 1056
Cdd:pfam17865 79 MSFLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1418-1568 |
1.30e-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: 122.40 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1418 PVLLVGETGCGKTTVCQMLAE-TYNRELHIVNCHQNTETGDLLGGqRPVRNREAnddpekqqqlfEWHDGPLVQAMKEGH 1496
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGR-RNIDPGGA-----------SWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758354136 1497 LFLLDEISLADDSVLERLNSVLEPSRLLVlaEKGGKhvEELYGAANFQFLATMNPgGDYGKKELSPALRNRF 1568
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 ... |
1119-1255 |
6.12e-25 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
:
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 103.14 E-value: 6.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1119 PVLIQGPTSAGKTSMVEYMAKKT-GHRFVRINNHEHTDLQEYLGTYVSNNEGKlVFQEGVLVEALRNGYWIVLDELNLAP 1197
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 758354136 1198 SDVLEALNRLLDDNRELLIPETQEIVKPHPHFMLFATQNPagLYGGRKALSRAFRNRF 1255
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 ... |
1903-2001 |
3.51e-23 |
|
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: 97.37 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1903 DLLFICSHLFSeFEPSIMAKMIDFNNKMYEETMMRCSFGRKGSPWEFNLRDVFRWLELMQ--------KDRVTDPAEYLD 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSsllptllsPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*..
gi 758354136 1975 IIYMQRMRTHEDRVQIVQLYESVFQVK 2001
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 ... |
511-626 |
8.74e-22 |
|
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: 93.14 E-value: 8.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 511 ELETVVRQKFTHIGDFATHVMTLFQTVVGMYQDPNFSTLASStmGRFLSTRDLMKWCHRVDLLIGEKLNDTTevgmdltl 590
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGS--PREFNLRDLLRWCRRLSSLLPTLLSPTV-------- 70
|
90 100 110
....*....|....*....|....*....|....*.
gi 758354136 591 RQDLFSEANDCFCGMIPDYNVWMTVLETLGRPLQIS 626
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 ... |
1267-1361 |
4.11e-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: 82.73 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1267 ELETILSKRCAIAPSYCKKLVKVYKELMERRQSTRIFEQKHG--FITLRDLFRWAGR---------DPQGYQELAENGYM 1335
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCRRlssllptllSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 758354136 1336 LLAERCRKDEEKKVVKQVLEQVMKVK 1361
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
356-487 |
7.64e-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: 7.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 356 PTLLEGVTGAGKTALIEELASRTgRGAELVKIHLGDQTDPKVLLGTYVSTstPGSFRWQAGVLTTAVLEGRWVLIEDIDL 435
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL-SNRPVFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEINR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 758354136 436 APAEVLSVLLPLLETRHLFIPSRGEKIKAK-EGFQLFGTrSFVPTRSGKGMSS 487
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 ... |
1752-1891 |
1.08e-16 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 79.64 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1752 PILLEGSPGVGKTSLVSALAAA-SGHHLVRINLSEQTDLMDLFGSDLPVEGGnsgeFAWRDAPFLQAMKAGDWVLLDELN 1830
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNIDPGG----ASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758354136 1831 LASQSVLEGLNSCLDHRgAVYIPELDREFFCAKE-FRVFGAQNPLQQGGgrKGLPKSFVNRF 1891
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDgFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4418-5067 |
1.81e-11 |
|
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: 71.20 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4418 MPAGADDGEEGDADGTMSGTGMGEGEGTKDVSEEIEDEEQVLGTQNEERNNDDKQDTKEEKNGMDMENDFDGNLEDIEQD 4497
Cdd:COG5271 371 EAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEAD 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4498 DDKEEDDSDSDSDEEDPDEQIGDVDDMDPDAVDDKMWGDEAEENLKESDKTVEDQGnqDQQQESEIVA--KEEEDQQQNE 4575
Cdd:COG5271 451 SLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADS--DELTAEETSAddGADTDAAADP 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4576 AKGEKPEKSDKNDKQqeadgeegdgdeEMDDDENQGSGDEDQQEDDAEGEGQDEDDVENKPG-EQLNADipeaETLELPD 4654
Cdd:COG5271 529 EDSDEDALEDETEGE------------ENAPGSDQDADETDEPEATAEEDEPDEAEAETEDAtENADAD----ETEESAD 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4655 DLNMDGDDDDNGDEEGQEGQDMNDPmdmDEQPAKGEDEQLPEEDENAEAFHDALDDVDQAPQEDEEMADASAQmDTeqge 4734
Cdd:COG5271 593 ESEEAEASEDEAAEEEEADDDEADA---DADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASA-DE---- 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4735 geeqdeeeNGEDKEENEELAPEVGDSEQQQKSGQIEEDDQgEEENKAQNREQPNSDATADNQFGVQGESGKQSKSSAGKK 4814
Cdd:COG5271 665 --------SEEEAEDESETSSEDAEEDADAAAAEASDDEE-ETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEA 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4815 EGEDDTADINEDADD--DIAEKKEQKGKSERGANQTNDEED------PDADNEQGDQDDQDQEAKEAQSNPQrslGDALE 4886
Cdd:COG5271 736 ESADEEAASLPDEADaeEEAEEAEEAEEDDADGLEEALEEEkadaeeAATDEEAEAAAEEKEKVADEDQDTD---EDALL 812
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4887 KwrrrladlddaadeEEEDENADKEKKTEDQDTEQAQVNEEDSFEYVKNDEDAHDMQTMGNAQPDQVQDLKMGGMDEEKE 4966
Cdd:COG5271 813 D--------------EAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEA 878
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4967 DTKETSGEMDVDQQADNVDTMPLPRDTLEMSGATDVQGAILSKKLPEQQLVDETEVLTMDESVVAREPLEQEDI-ERMRD 5045
Cdd:COG5271 879 QEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALdEAGDE 958
|
650 660
....*....|....*....|..
gi 758354136 5046 ELETQVSDWREDGRDINKAREL 5067
Cdd:COG5271 959 ESDDAAADDAGDDSLADDDEAL 980
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
701-937 |
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 758354136 701 PVLLVGETGTGKTTVVQHLADMIH-QNLIVVNLSQQSDSSDLLGGFKPVDGKvlaipmkeeferlfektfsvkknakfle 779
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDPGG---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 780 mvrktfihqkwsnfvtllkqavkmsqqkfeaeqnaeskrvsaptlrnawktfakkveefevqqvqsqnkfvFNFMEGSLV 859
Cdd:pfam07728 53 -----------------------------------------------------------------------ASWVDGPLV 61
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758354136 860 KAVRQGDWILLDEINLATTETLECLSGLLQDAHgsLLLTEKGDVEPIKRhPNFRLFACMNPAtDVGKRDLPPGLRNRF 937
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 ... |
2228-2314 |
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 758354136 2228 GKFEWIDGLLINALEKGYWLLIDNANMCNPSVLDRLNPLFENdgvlmvNERGLVDGTVKVIKPHPNFRMFMTVDPQNG-- 2305
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 758354136 2306 -ELSRAMRNR 2314
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| Zinc_peptidase_like super family |
cl14876 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
29-232 |
5.27e-05 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
The actual alignment was detected with superfamily member cd05677:
Pssm-ID: 472712 [Multi-domain] Cd Length: 436 Bit Score: 49.26 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 29 VSQLSTLIGSStfGSVDLEVLHQATIATTSTNKSQLLDTVSRAMLKPEWTlsvvrlfrpiVIDLVARWTLPSFTdfLDSA 108
Cdd:cd05677 222 IKLLSKLQDPD--GRILIPHFYDPVKPLTEAERARFTAIAETALIHEDTT----------VDSLIAKWRKPSLT--VHTV 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 109 SASPNANRTVykIELVAKAiSVVLPIVP-----QVKSLAVTYFTHSASLFERLNHLnnyrELEVTSSLTAELQDLLLTTY 183
Cdd:cd05677 288 KVSGPGNTTV--IPKSASA-SVSIRLVPdqdldVIKQDLTDYIQSCFAELKSQNHL----DIEVLNEAEPWLGDPDNPAY 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 758354136 184 RLLSfstSTFTPLWNWGPLVqllqFQE----PCIRYitvlcLSKVYGLSDAQV 232
Cdd:cd05677 361 QILR---EAVTAAWGVEPLY----IREggsiPTIRF-----LEKEFNAPAVQL 401
|
|
| COG2842 super family |
cl34499 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
653-742 |
3.69e-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: 45.71 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 653 VNLSSIAASGKQKQKQALIKREKKRPFATTGHALRLMERIAVCIHLTEPVLLVGETGTGKTTVVQHLADMiHQNLIVVNL 732
Cdd:COG2842 4 KTQAAVAKEIGNEKLEAKIARWEAPSFVETKNVRRFAEALDEARALPGIGVVYGESGVGKTTAAREYANR-NPNVIYVTA 82
|
90
....*....|
gi 758354136 733 SQQSDSSDLL 742
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 ... |
5078-5346 |
2.47e-124 |
|
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: 393.64 E-value: 2.47e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5078 LAMGLCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFKKDKIWLRRTKPSKRQYQVMISVDDSKSMSESHSVQ 5157
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5158 LAYEALSLISKALSQLEVGDISITSFGERVRLLHPFDQPFTAESGANVIQQFTFAQQKTYVKNLIETSVGLFESAkhSSG 5237
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDA--RTQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5238 PGNAELWQLQLIISDGICEDHNTL-RALVRNALDQQIMMIFIVVDNKPEKDSILNMTNVKYtiKDGKYGiQMNPYLETFP 5316
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAqKVRLREAREQNVFVVFIIIDNPDNKQSILDIKVVSF--KNDKSG-VITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|
gi 758354136 5317 FQYFMVLRDINSLPEVLSDALRQYFSFVSA 5346
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 ... |
951-1056 |
9.36e-45 |
|
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: 158.90 E-value: 9.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 951 DLLQIVKQYLAGIaSGDERSYDDVAEFYMNAKKLAaEHKLVDGANQRPHFSMRTLARALTYVAQIFPVYGLRRSLYEGFC 1030
Cdd:pfam17865 1 DLELLVKAYLKGV-SSDDDLVRDIVKFYLEAKKLA-EKSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90 100
....*....|....*....|....*.
gi 758354136 1031 MTFLTQLDKESEVLMRDLIFKTILRG 1056
Cdd:pfam17865 79 MSFLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1418-1568 |
1.30e-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: 122.40 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1418 PVLLVGETGCGKTTVCQMLAE-TYNRELHIVNCHQNTETGDLLGGqRPVRNREAnddpekqqqlfEWHDGPLVQAMKEGH 1496
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGR-RNIDPGGA-----------SWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758354136 1497 LFLLDEISLADDSVLERLNSVLEPSRLLVlaEKGGKhvEELYGAANFQFLATMNPgGDYGKKELSPALRNRF 1568
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 ... |
1119-1255 |
6.12e-25 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 103.14 E-value: 6.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1119 PVLIQGPTSAGKTSMVEYMAKKT-GHRFVRINNHEHTDLQEYLGTYVSNNEGKlVFQEGVLVEALRNGYWIVLDELNLAP 1197
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 758354136 1198 SDVLEALNRLLDDNRELLIPETQEIVKPHPHFMLFATQNPagLYGGRKALSRAFRNRF 1255
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 ... |
1903-2001 |
3.51e-23 |
|
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: 97.37 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1903 DLLFICSHLFSeFEPSIMAKMIDFNNKMYEETMMRCSFGRKGSPWEFNLRDVFRWLELMQ--------KDRVTDPAEYLD 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSsllptllsPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*..
gi 758354136 1975 IIYMQRMRTHEDRVQIVQLYESVFQVK 2001
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 ... |
511-626 |
8.74e-22 |
|
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: 93.14 E-value: 8.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 511 ELETVVRQKFTHIGDFATHVMTLFQTVVGMYQDPNFSTLASStmGRFLSTRDLMKWCHRVDLLIGEKLNDTTevgmdltl 590
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGS--PREFNLRDLLRWCRRLSSLLPTLLSPTV-------- 70
|
90 100 110
....*....|....*....|....*....|....*.
gi 758354136 591 RQDLFSEANDCFCGMIPDYNVWMTVLETLGRPLQIS 626
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 ... |
1267-1361 |
4.11e-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: 82.73 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1267 ELETILSKRCAIAPSYCKKLVKVYKELMERRQSTRIFEQKHG--FITLRDLFRWAGR---------DPQGYQELAENGYM 1335
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCRRlssllptllSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 758354136 1336 LLAERCRKDEEKKVVKQVLEQVMKVK 1361
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
356-487 |
7.64e-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: 7.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 356 PTLLEGVTGAGKTALIEELASRTgRGAELVKIHLGDQTDPKVLLGTYVSTstPGSFRWQAGVLTTAVLEGRWVLIEDIDL 435
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL-SNRPVFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEINR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 758354136 436 APAEVLSVLLPLLETRHLFIPSRGEKIKAK-EGFQLFGTrSFVPTRSGKGMSS 487
Cdd:pfam07728 78 ANPDVLNSLLSLLDERRLLLPDGGELVKAApDGFRLIAT-MNPLDRGLNELSP 129
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1752-1891 |
1.08e-16 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 79.64 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1752 PILLEGSPGVGKTSLVSALAAA-SGHHLVRINLSEQTDLMDLFGSDLPVEGGnsgeFAWRDAPFLQAMKAGDWVLLDELN 1830
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNIDPGG----ASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758354136 1831 LASQSVLEGLNSCLDHRgAVYIPELDREFFCAKE-FRVFGAQNPLQQGGgrKGLPKSFVNRF 1891
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDgFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1740-1891 |
1.57e-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: 71.74 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1740 AMRVIRSMQLKKPILLEGSPGVGKTSLVSALAAASGHHLVRINLSEqtDLM--DLFGSDLPVEggNSGEFAWRDAPFLQA 1817
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTP--DLLpsDILGTYIYDQ--QTGEFEFRPGPLFAN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758354136 1818 MkagdwVLLDELNLAS---QSV-LEglnsCLDHRgAVYIPelDREFFCAKEFRVFGAQNPLQQGGGRKgLPKSFVNRF 1891
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 ... |
1119-1275 |
9.47e-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: 69.43 E-value: 9.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1119 PVLIQGPTSAGKTSMVEYMAKKTGHRFVRINNHEHTDLQEYLGTYVSN-NEGKLVFQEGVLveaLRNgywIVL-DELNLA 1196
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDqQTGEFEFRPGPL---FAN---VLLaDEINRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1197 P----SDVLEALnrlldDNRELLIPEtQEIVKPHPhFMLFATQNPAGLYGGRkALSRAFRNRFL-ELHFD--DiPEDELE 1269
Cdd:COG0714 107 PpktqSALLEAM-----EERQVTIPG-GTYKLPEP-FLVIATQNPIEQEGTY-PLPEAQLDRFLlKLYIGypD-AEEERE 177
|
....*.
gi 758354136 1270 tILSKR 1275
Cdd:COG0714 178 -ILRRH 182
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4418-5067 |
1.81e-11 |
|
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: 71.20 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4418 MPAGADDGEEGDADGTMSGTGMGEGEGTKDVSEEIEDEEQVLGTQNEERNNDDKQDTKEEKNGMDMENDFDGNLEDIEQD 4497
Cdd:COG5271 371 EAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEAD 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4498 DDKEEDDSDSDSDEEDPDEQIGDVDDMDPDAVDDKMWGDEAEENLKESDKTVEDQGnqDQQQESEIVA--KEEEDQQQNE 4575
Cdd:COG5271 451 SLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADS--DELTAEETSAddGADTDAAADP 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4576 AKGEKPEKSDKNDKQqeadgeegdgdeEMDDDENQGSGDEDQQEDDAEGEGQDEDDVENKPG-EQLNADipeaETLELPD 4654
Cdd:COG5271 529 EDSDEDALEDETEGE------------ENAPGSDQDADETDEPEATAEEDEPDEAEAETEDAtENADAD----ETEESAD 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4655 DLNMDGDDDDNGDEEGQEGQDMNDPmdmDEQPAKGEDEQLPEEDENAEAFHDALDDVDQAPQEDEEMADASAQmDTeqge 4734
Cdd:COG5271 593 ESEEAEASEDEAAEEEEADDDEADA---DADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASA-DE---- 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4735 geeqdeeeNGEDKEENEELAPEVGDSEQQQKSGQIEEDDQgEEENKAQNREQPNSDATADNQFGVQGESGKQSKSSAGKK 4814
Cdd:COG5271 665 --------SEEEAEDESETSSEDAEEDADAAAAEASDDEE-ETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEA 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4815 EGEDDTADINEDADD--DIAEKKEQKGKSERGANQTNDEED------PDADNEQGDQDDQDQEAKEAQSNPQrslGDALE 4886
Cdd:COG5271 736 ESADEEAASLPDEADaeEEAEEAEEAEEDDADGLEEALEEEkadaeeAATDEEAEAAAEEKEKVADEDQDTD---EDALL 812
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4887 KwrrrladlddaadeEEEDENADKEKKTEDQDTEQAQVNEEDSFEYVKNDEDAHDMQTMGNAQPDQVQDLKMGGMDEEKE 4966
Cdd:COG5271 813 D--------------EAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEA 878
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4967 DTKETSGEMDVDQQADNVDTMPLPRDTLEMSGATDVQGAILSKKLPEQQLVDETEVLTMDESVVAREPLEQEDI-ERMRD 5045
Cdd:COG5271 879 QEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALdEAGDE 958
|
650 660
....*....|....*....|..
gi 758354136 5046 ELETQVSDWREDGRDINKAREL 5067
Cdd:COG5271 959 ESDDAAADDAGDDSLADDDEAL 980
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1415-1568 |
7.93e-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: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1415 HNEPVLLVGETGCGKTTVCQMLAETYNRELH---IVNCHQNTETGDLLGGQRPVRNREANDDPEKQQ-QLFEwhdgpLVQ 1490
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrLALA-----LAR 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758354136 1491 AMKEGhLFLLDEISLADDSVLERLNSVLEPSRLLVLAEKGGkhveelygaaNFQFLATMNPGGDYGKKELSPALRNRF 1568
Cdd:smart00382 76 KLKPD-VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK----------NLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1418-1587 |
4.10e-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: 64.42 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1418 PVLLVGETGCGKTTVCQMLAETYNRELHIVNCHQNTETGDLLGGQrpvrnreandDPEKQQQLFEWHDGPLVQamkegHL 1497
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTY----------IYDQQTGEFEFRPGPLFA-----NV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1498 FLLDEISLADDSVlerlnsvlePSRLL-VLAEK----GGKHVEelygAAN-FQFLATMNPGGDYGKKELSPALRNRFT-E 1570
Cdd:COG0714 98 LLADEINRAPPKT---------QSALLeAMEERqvtiPGGTYK----LPEpFLVIATQNPIEQEGTYPLPEAQLDRFLlK 164
|
170
....*....|....*....
gi 758354136 1571 IWV--PsvtDRDDLIKIID 1587
Cdd:COG0714 165 LYIgyP---DAEEEREILR 180
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
701-937 |
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 758354136 701 PVLLVGETGTGKTTVVQHLADMIH-QNLIVVNLSQQSDSSDLLGGFKPVDGKvlaipmkeeferlfektfsvkknakfle 779
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDPGG---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 780 mvrktfihqkwsnfvtllkqavkmsqqkfeaeqnaeskrvsaptlrnawktfakkveefevqqvqsqnkfvFNFMEGSLV 859
Cdd:pfam07728 53 -----------------------------------------------------------------------ASWVDGPLV 61
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758354136 860 KAVRQGDWILLDEINLATTETLECLSGLLQDAHgsLLLTEKGDVEPIKRhPNFRLFACMNPAtDVGKRDLPPGLRNRF 937
Cdd:pfam07728 62 RAAREGEIAVLDEINRANPDVLNSLLSLLDERR--LLLPDGGELVKAAP-DGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4558-4842 |
3.17e-08 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 60.78 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4558 QQESEIVAKEEEDQQQNEAKGEKPEKSDkNDKQQEADGEEGDGdeemdddeNQGSGD-EDQQEDDAEGEGQDEDDVENKP 4636
Cdd:TIGR00927 637 EAEHTGERTGEEGERPTEAEGENGEESG-GEAEQEGETETKGE--------NESEGEiPAERKGEQEGEGEIEAKEADHK 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4637 GEQlnadipEAETLELPDDLNMDGDDDDNGDEEGQEGQDMNDPMDMDEQpAKGEDEQLPEEDE-NAEAFHDALDDVDQAP 4715
Cdd:TIGR00927 708 GET------EAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAE-GKHEVETEGDRKEtEHEGETEAEGKEDEDE 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4716 QEDEEMADASAQMDTEQGEGEEQDEEENGEDKEeneelapEVGDSEQQQKSGQIEEDDQGEEENKAQNReqpnsDATADN 4795
Cdd:TIGR00927 781 GEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKD-------EHEGQSETQADDTEVKDETGEQELNAENQ-----GEAKQD 848
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 758354136 4796 QFGVQGESGkqskSSAGKKEGEDDTADINEDADDDIAEKKEQKGKSE 4842
Cdd:TIGR00927 849 EKGVDGGGG----SDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENE 891
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
346-474 |
1.61e-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: 56.33 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 346 AVSLALSIGAPTLLEGVTGAGKTALIEELASRTGRGAELV--KIHLgdqtDPKVLLGTYVSTSTPGSFRWQAGVLTTAVL 423
Cdd:COG0714 23 LVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIqfTPDL----LPSDILGTYIYDQQTGEFEFRPGPLFANVL 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 758354136 424 egrwvLIEDIDLAPAEVLSVLLPLLETRHLFIPsrGEKIKAKEGFQLFGTR 474
Cdd:COG0714 99 -----LADEINRAPPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIATQ 142
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2228-2314 |
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 758354136 2228 GKFEWIDGLLINALEKGYWLLIDNANMCNPSVLDRLNPLFENdgvlmvNERGLVDGTVKVIKPHPNFRMFMTVDPQNG-- 2305
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 758354136 2306 -ELSRAMRNR 2314
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1750-1892 |
5.17e-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: 52.53 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1750 KKPILLEGSPGVGKTSLVSALAAAS---GHHLVRINLSeqtdlmDLFGSDlpVEGGNSGEFAWRDAPFLQAMKAGDWVLL 1826
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFI 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758354136 1827 DELNLASQSVLEGLNSCLDhrgavyipELDREFFCAKEFRVFGAQNPLQQGGGRKGLPKSFVNRFT 1892
Cdd:cd00009 91 DEIDSLSRGAQNALLRVLE--------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIV 148
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1066-1261 |
2.81e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 53.20 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1066 QIPRQPHEDFIQFGYFWLQQGQFPPEDDTRYILTN---SVETKLYNLARV--IMSRKFPVLIQGPTSAGKTSMVEYMAKK 1140
Cdd:PHA02244 63 EIEDSPEEQFFELPVKIELQQEGKPAGDISGIDTTkiaSNPTFHYETADIakIVNANIPVFLKGGAGSGKNHIAEQIAEA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1141 TGHRFVRINnhehTDLQEYLGTYVSNNEGKlvFQEGVLVEALRNGYWIVLDELNLAPSDVLEALNRLLDDNRELLIPETq 1220
Cdd:PHA02244 143 LDLDFYFMN----AIMDEFELKGFIDANGK--FHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANKFFDFADER- 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 758354136 1221 eiVKPHPHFMLFATQNPAG-----LYGGRKALSRAFRNRFLELHFD 1261
Cdd:PHA02244 216 --VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4673-5035 |
1.81e-05 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 51.45 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4673 GQDMNDPMdMDEQPAK-GEDEQLPEE------------------------DENAEAFHDALDDVDQAPQEDEEmADASAQ 4727
Cdd:NF033609 536 GDGIDKPV-VPEQPDEpGEIEPIPEDsdsdpgsdsgsdssnsdsgsdsgsDSTSDSGSDSASDSDSASDSDSA-SDSDSA 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4728 MDTEQGEGEEQDEEENGEDKEENEELAPEVGDSEQQQKSGQIEEDDQGEEENKAQNREqpnSDATADNQFGVQGESGKQS 4807
Cdd:NF033609 614 SDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD---SDSDSDSDSDSDSDSDSDS 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4808 KSSAGKKEGEDDTADINEDADDDIAEKKEQKGKSERGANQTND-EEDPDADNEQGDQDDQDQEAKEAQSNPQRSLGDAle 4886
Cdd:NF033609 691 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-- 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4887 kwrrrladlddaaDEEEEDENADKEKKTEDQDTEQAQVNEEDSFEYVKNDEDAhDMQTMGNAQPDQVQDlkmggMDEEKE 4966
Cdd:NF033609 769 -------------DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSD-----SDSDSD 829
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 758354136 4967 DTKETSGEMDVDQQADNVDTMPLPRDTlEMSGATDVQGAILSKKLPEQQLVDETEVLTMDESVVAREPL 5035
Cdd:NF033609 830 SDSDSDSDSDSDSDSDSDSDSDSDSDS-ESDSNSDSESGSNNNVVPPNSPKNGTNASNKNEAKDSKEPL 897
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1718-1903 |
1.85e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 50.89 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1718 PRGQLAKTDIKFTLLAPTTADNAMRVIRSMQLKKPILLEGSPGVGKTSLVSALAAAsghhlVRINLSEQTDLMDLFgsdl 1797
Cdd:PHA02244 87 PAGDISGIDTTKIASNPTFHYETADIAKIVNANIPVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAIMDEF---- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1798 PVEGGNSGEFAWRDAPFLQAMKAGDWVLLDELNLASQSVLEGLNSCLDHRgavYIPELDREFFCAKEFRVFGAQNPLQQG 1877
Cdd:PHA02244 158 ELKGFIDANGKFHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANK---FFDFADERVTAHEDFRVISAGNTLGKG 234
|
170 180 190
....*....|....*....|....*....|....*...
gi 758354136 1878 G-----GRKGLPKSFVNRFTQVYVE-------QLTSDD 1903
Cdd:PHA02244 235 AdhiyvARNKIDGATLDRFAPIEFDydekiehLISNGD 272
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1408-1571 |
3.13e-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: 47.14 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1408 LVARCLQHNEPVLLVGETGCGKTTVCQMLA---ETYNRELHIVNCHQNTETGDLLGGQRPVRNReanddpekqqQLFEwh 1484
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAELFGHFLVR----------LLFE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1485 dgplVQAMKEGHLFLLDEIsladDSVLERLNSVLEpsRLLVLAEKGGKHVEELygaanFQFLATMNPGGDygkkELSPAL 1564
Cdd:cd00009 79 ----LAEKAKPGVLFIDEI----DSLSRGAQNALL--RVLETLNDLRIDRENV-----RVIGATNRPLLG----DLDRAL 139
|
....*..
gi 758354136 1565 RNRFTEI 1571
Cdd:cd00009 140 YDRLDIR 146
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
29-232 |
5.27e-05 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 49.26 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 29 VSQLSTLIGSStfGSVDLEVLHQATIATTSTNKSQLLDTVSRAMLKPEWTlsvvrlfrpiVIDLVARWTLPSFTdfLDSA 108
Cdd:cd05677 222 IKLLSKLQDPD--GRILIPHFYDPVKPLTEAERARFTAIAETALIHEDTT----------VDSLIAKWRKPSLT--VHTV 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 109 SASPNANRTVykIELVAKAiSVVLPIVP-----QVKSLAVTYFTHSASLFERLNHLnnyrELEVTSSLTAELQDLLLTTY 183
Cdd:cd05677 288 KVSGPGNTTV--IPKSASA-SVSIRLVPdqdldVIKQDLTDYIQSCFAELKSQNHL----DIEVLNEAEPWLGDPDNPAY 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 758354136 184 RLLSfstSTFTPLWNWGPLVqllqFQE----PCIRYitvlcLSKVYGLSDAQV 232
Cdd:cd05677 361 QILR---EAVTAAWGVEPLY----IREggsiPTIRF-----LEKEFNAPAVQL 401
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1124-1212 |
2.30e-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: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1124 GPTSAGKTSMVEYMAKK---TGHRFVRIN------NHEHTDLQEYLGTYVSNNEGklvfqeGVLVEAL-RNGYWIVL-DE 1192
Cdd:cd19499 48 GPTGVGKTELAKALAELlfgDEDNLIRIDmseymeKHSVSRLIGAPPGYVGYTEG------GQLTEAVrRKPYSVVLlDE 121
|
90 100
....*....|....*....|
gi 758354136 1193 LNLAPSDVLEALNRLLDDNR 1212
Cdd:cd19499 122 IEKAHPDVQNLLLQVLDDGR 141
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5140-5287 |
3.01e-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: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5140 VMISVDDSKSMSESHsvqlAYEALSLISKALSQLEVGD----ISITSFGERVRLLHPFDQPFTAESGANVIQQFT-FAQQ 5214
Cdd:smart00327 2 VVFLLDGSGSMGGNR----FELAKEFVLKLVEQLDIGPdgdrVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758354136 5215 KTYVKNLIETSVGLFESAKHSSGPGNAelwQLQLIISDGICEDHNT-LRALVRNALDQQIMMIFIVVDNKPEKD 5287
Cdd:smart00327 78 GTNLGAALQYALENLFSKSAGSRRGAP---KVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVGVGNDVDEE 148
|
|
| COG2842 |
COG2842 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
653-742 |
3.69e-04 |
|
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];
Pssm-ID: 442090 [Multi-domain] Cd Length: 254 Bit Score: 45.71 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 653 VNLSSIAASGKQKQKQALIKREKKRPFATTGHALRLMERIAVCIHLTEPVLLVGETGTGKTTVVQHLADMiHQNLIVVNL 732
Cdd:COG2842 4 KTQAAVAKEIGNEKLEAKIARWEAPSFVETKNVRRFAEALDEARALPGIGVVYGESGVGKTTAAREYANR-NPNVIYVTA 82
|
90
....*....|
gi 758354136 733 SQQSDSSDLL 742
Cdd:COG2842 83 SPSWTSKELL 92
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
679-742 |
4.39e-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: 45.55 E-value: 4.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758354136 679 FATTGHAlRLMERIAVCIHLTEP-VLLVGETGTGKTTVVQHLADMIHQNLIVVNLSQ-QSDSSDLL 742
Cdd:COG3267 23 FLSPSHR-EALARLEYALAQGGGfVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNpQLSPAELL 87
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4537-4720 |
5.44e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 46.12 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4537 EAEENLKESDKTVEDQGNQDQQQESEI---------VAKEEEDQQQNEAKGEKPEKSDKNDKQQEADGEEGDGDEEMDDD 4607
Cdd:PHA03169 74 ETAEESRHGEKEERGQGGPSGSGSESVgsptpspsgSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4608 ENQGSGdEDQQEDDAEGEGQDEDDVENKPGEQLNADIPEAEtlelpddlnmdgddddnGDEEGQEGQDMNDPMDMDEQPA 4687
Cdd:PHA03169 154 SHNPSP-NQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPP-----------------QSETPTSSPPPQSPPDEPGEPQ 215
|
170 180 190
....*....|....*....|....*....|...
gi 758354136 4688 KGEDEQLPEEDENAEAFHDALDDVDQAPQEDEE 4720
Cdd:PHA03169 216 SPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFP 248
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1116-1255 |
5.83e-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: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1116 RKFPVLIQGPTSAGKTSMVEYMAK---KTGHRFVRIN--NHEHTDLQEYLGTYVSNNEGKLVF---QEGVLVEALRNGY- 1186
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDgeDILEEVLDQLLLIIVGGKKASGSGelrLRLALALARKLKPd 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 758354136 1187 WIVLDELNLAPSDVLEALNRLLDDNRELLIPETQEIVkphphFMLFATQNPAGLygGRKALSRAFRNRF 1255
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNL-----TVILTTNDEKDL--GPALLRRRFDRRI 142
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
4536-4844 |
9.53e-04 |
|
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) or RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II.
Pssm-ID: 310411 [Multi-domain] Cd Length: 528 Bit Score: 45.71 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4536 DEAEENLKESDKTVE-------DQGNQDQQQESEivaKEEEDQQQNEAKGEKPEK--SDKNDKQQEadgeegdgdeemdd 4606
Cdd:pfam05793 161 EEAEEEMERRKKTANgfslmmmKAAKNGPAAFGE---HDEETEGEKGGGGRGKDLkiKDLEGDDED-------------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4607 denqgSGDEDQQEDDAEGEGQD--------------EDDVENKPGEQLNADIPEAETLElpddlnmdgddddngdEEGQE 4672
Cdd:pfam05793 224 -----DGDESDKGGEDGDEEKKkkkkkklaknkkklDDDKKKKRGGDDDAFEYDSDDGD----------------DEGRE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4673 GQDMNDpmdmdeqpaKGEDEQLPEEDEnaeafhDALDDVDQAPQEDEemadasaqmdteqgegeeqdeeengedkeenee 4752
Cdd:pfam05793 283 EDYISD---------SSASGNDPEERE------DKLSPEEPAKGEIE--------------------------------- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4753 lapEVGDSEQQQKSGQIEEDDQGEEENKAQnreqpnsdatadnqfGVQGESGKQSKSSAGKKEGEDDTADINEDADDDIA 4832
Cdd:pfam05793 315 ---QSDDSEESEEEKNEEEGKLSKKGKKAK---------------KLKGKKNGKDKSESSDGDDSDDSDIDDEDSVPLFT 376
|
330
....*....|..
gi 758354136 4833 EKKEQKGKSERG 4844
Cdd:pfam05793 377 AKKKKEPKKEEP 388
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
686-734 |
1.24e-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: 1.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 758354136 686 LRLMERIAVCIHLTEPVLLVGETGTGKTTVVQHLADMIHQNLIVVNLSQ 734
Cdd:cd19481 13 RRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4615-4859 |
8.84e-03 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 42.59 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4615 EDQQEDDAEGEGQDED--DVENKPGEQLNADIPEAETLELPDDLNMDGDDDDNGDEEGQEGQDMNDPMDMD-EQPAKGED 4691
Cdd:NF033609 559 EDSDSDPGSDSGSDSSnsDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDsASDSDSAS 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4692 EQLPEEDENAEAFHDALDDVDQAPQEDEEmADASAQMDTEQGEGEEQDEEENGEDKEENEELAPEVGDSEQQQKSgqiEE 4771
Cdd:NF033609 639 DSDSDSDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS---DS 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4772 DDQGEEENKAQNREQPNSDATADNQFGVQGESGKQSKSSAGKKEGEDDTADINEDADDDIAEKKEQKGKSERGANQTND- 4850
Cdd:NF033609 715 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDs 794
|
....*....
gi 758354136 4851 EEDPDADNE 4859
Cdd:NF033609 795 DSDSDSDSD 803
|
|
| |
|
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 ... |
5078-5346 |
2.47e-124 |
|
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: 393.64 E-value: 2.47e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5078 LAMGLCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFKKDKIWLRRTKPSKRQYQVMISVDDSKSMSESHSVQ 5157
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5158 LAYEALSLISKALSQLEVGDISITSFGERVRLLHPFDQPFTAESGANVIQQFTFAQQKTYVKNLIETSVGLFESAkhSSG 5237
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDA--RTQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5238 PGNAELWQLQLIISDGICEDHNTL-RALVRNALDQQIMMIFIVVDNKPEKDSILNMTNVKYtiKDGKYGiQMNPYLETFP 5316
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAqKVRLREAREQNVFVVFIIIDNPDNKQSILDIKVVSF--KNDKSG-VITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|
gi 758354136 5317 FQYFMVLRDINSLPEVLSDALRQYFSFVSA 5346
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 ... |
951-1056 |
9.36e-45 |
|
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: 158.90 E-value: 9.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 951 DLLQIVKQYLAGIaSGDERSYDDVAEFYMNAKKLAaEHKLVDGANQRPHFSMRTLARALTYVAQIFPVYGLRRSLYEGFC 1030
Cdd:pfam17865 1 DLELLVKAYLKGV-SSDDDLVRDIVKFYLEAKKLA-EKSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90 100
....*....|....*....|....*.
gi 758354136 1031 MTFLTQLDKESEVLMRDLIFKTILRG 1056
Cdd:pfam17865 79 MSFLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1418-1568 |
1.30e-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: 122.40 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1418 PVLLVGETGCGKTTVCQMLAE-TYNRELHIVNCHQNTETGDLLGGqRPVRNREAnddpekqqqlfEWHDGPLVQAMKEGH 1496
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGR-RNIDPGGA-----------SWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758354136 1497 LFLLDEISLADDSVLERLNSVLEPSRLLVlaEKGGKhvEELYGAANFQFLATMNPgGDYGKKELSPALRNRF 1568
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 ... |
1119-1255 |
6.12e-25 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 103.14 E-value: 6.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1119 PVLIQGPTSAGKTSMVEYMAKKT-GHRFVRINNHEHTDLQEYLGTYVSNNEGKlVFQEGVLVEALRNGYWIVLDELNLAP 1197
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 758354136 1198 SDVLEALNRLLDDNRELLIPETQEIVKPHPHFMLFATQNPagLYGGRKALSRAFRNRF 1255
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 ... |
1903-2001 |
3.51e-23 |
|
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: 97.37 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1903 DLLFICSHLFSeFEPSIMAKMIDFNNKMYEETMMRCSFGRKGSPWEFNLRDVFRWLELMQ--------KDRVTDPAEYLD 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSsllptllsPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*..
gi 758354136 1975 IIYMQRMRTHEDRVQIVQLYESVFQVK 2001
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 ... |
511-626 |
8.74e-22 |
|
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: 93.14 E-value: 8.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 511 ELETVVRQKFTHIGDFATHVMTLFQTVVGMYQDPNFSTLASStmGRFLSTRDLMKWCHRVDLLIGEKLNDTTevgmdltl 590
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGS--PREFNLRDLLRWCRRLSSLLPTLLSPTV-------- 70
|
90 100 110
....*....|....*....|....*....|....*.
gi 758354136 591 RQDLFSEANDCFCGMIPDYNVWMTVLETLGRPLQIS 626
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 ... |
1267-1361 |
4.11e-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: 82.73 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1267 ELETILSKRCAIAPSYCKKLVKVYKELMERRQSTRIFEQKHG--FITLRDLFRWAGR---------DPQGYQELAENGYM 1335
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCRRlssllptllSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 758354136 1336 LLAERCRKDEEKKVVKQVLEQVMKVK 1361
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
356-487 |
7.64e-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: 7.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 356 PTLLEGVTGAGKTALIEELASRTgRGAELVKIHLGDQTDPKVLLGTYVSTstPGSFRWQAGVLTTAVLEGRWVLIEDIDL 435
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL-SNRPVFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEINR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 758354136 436 APAEVLSVLLPLLETRHLFIPSRGEKIKAK-EGFQLFGTrSFVPTRSGKGMSS 487
Cdd:pfam07728 78 ANPDVLNSLLSLLDERRLLLPDGGELVKAApDGFRLIAT-MNPLDRGLNELSP 129
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1752-1891 |
1.08e-16 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 79.64 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1752 PILLEGSPGVGKTSLVSALAAA-SGHHLVRINLSEQTDLMDLFGSDLPVEGGnsgeFAWRDAPFLQAMKAGDWVLLDELN 1830
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNIDPGG----ASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758354136 1831 LASQSVLEGLNSCLDHRgAVYIPELDREFFCAKE-FRVFGAQNPLQQGGgrKGLPKSFVNRF 1891
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDgFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1740-1891 |
1.57e-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: 71.74 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1740 AMRVIRSMQLKKPILLEGSPGVGKTSLVSALAAASGHHLVRINLSEqtDLM--DLFGSDLPVEggNSGEFAWRDAPFLQA 1817
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTP--DLLpsDILGTYIYDQ--QTGEFEFRPGPLFAN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758354136 1818 MkagdwVLLDELNLAS---QSV-LEglnsCLDHRgAVYIPelDREFFCAKEFRVFGAQNPLQQGGGRKgLPKSFVNRF 1891
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 ... |
1119-1275 |
9.47e-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: 69.43 E-value: 9.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1119 PVLIQGPTSAGKTSMVEYMAKKTGHRFVRINNHEHTDLQEYLGTYVSN-NEGKLVFQEGVLveaLRNgywIVL-DELNLA 1196
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDqQTGEFEFRPGPL---FAN---VLLaDEINRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1197 P----SDVLEALnrlldDNRELLIPEtQEIVKPHPhFMLFATQNPAGLYGGRkALSRAFRNRFL-ELHFD--DiPEDELE 1269
Cdd:COG0714 107 PpktqSALLEAM-----EERQVTIPG-GTYKLPEP-FLVIATQNPIEQEGTY-PLPEAQLDRFLlKLYIGypD-AEEERE 177
|
....*.
gi 758354136 1270 tILSKR 1275
Cdd:COG0714 178 -ILRRH 182
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4418-5067 |
1.81e-11 |
|
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: 71.20 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4418 MPAGADDGEEGDADGTMSGTGMGEGEGTKDVSEEIEDEEQVLGTQNEERNNDDKQDTKEEKNGMDMENDFDGNLEDIEQD 4497
Cdd:COG5271 371 EAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEAD 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4498 DDKEEDDSDSDSDEEDPDEQIGDVDDMDPDAVDDKMWGDEAEENLKESDKTVEDQGnqDQQQESEIVA--KEEEDQQQNE 4575
Cdd:COG5271 451 SLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADS--DELTAEETSAddGADTDAAADP 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4576 AKGEKPEKSDKNDKQqeadgeegdgdeEMDDDENQGSGDEDQQEDDAEGEGQDEDDVENKPG-EQLNADipeaETLELPD 4654
Cdd:COG5271 529 EDSDEDALEDETEGE------------ENAPGSDQDADETDEPEATAEEDEPDEAEAETEDAtENADAD----ETEESAD 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4655 DLNMDGDDDDNGDEEGQEGQDMNDPmdmDEQPAKGEDEQLPEEDENAEAFHDALDDVDQAPQEDEEMADASAQmDTeqge 4734
Cdd:COG5271 593 ESEEAEASEDEAAEEEEADDDEADA---DADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASA-DE---- 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4735 geeqdeeeNGEDKEENEELAPEVGDSEQQQKSGQIEEDDQgEEENKAQNREQPNSDATADNQFGVQGESGKQSKSSAGKK 4814
Cdd:COG5271 665 --------SEEEAEDESETSSEDAEEDADAAAAEASDDEE-ETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEA 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4815 EGEDDTADINEDADD--DIAEKKEQKGKSERGANQTNDEED------PDADNEQGDQDDQDQEAKEAQSNPQrslGDALE 4886
Cdd:COG5271 736 ESADEEAASLPDEADaeEEAEEAEEAEEDDADGLEEALEEEkadaeeAATDEEAEAAAEEKEKVADEDQDTD---EDALL 812
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4887 KwrrrladlddaadeEEEDENADKEKKTEDQDTEQAQVNEEDSFEYVKNDEDAHDMQTMGNAQPDQVQDLKMGGMDEEKE 4966
Cdd:COG5271 813 D--------------EAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEA 878
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4967 DTKETSGEMDVDQQADNVDTMPLPRDTLEMSGATDVQGAILSKKLPEQQLVDETEVLTMDESVVAREPLEQEDI-ERMRD 5045
Cdd:COG5271 879 QEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALdEAGDE 958
|
650 660
....*....|....*....|..
gi 758354136 5046 ELETQVSDWREDGRDINKAREL 5067
Cdd:COG5271 959 ESDDAAADDAGDDSLADDDEAL 980
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1415-1568 |
7.93e-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: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1415 HNEPVLLVGETGCGKTTVCQMLAETYNRELH---IVNCHQNTETGDLLGGQRPVRNREANDDPEKQQ-QLFEwhdgpLVQ 1490
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrLALA-----LAR 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758354136 1491 AMKEGhLFLLDEISLADDSVLERLNSVLEPSRLLVLAEKGGkhveelygaaNFQFLATMNPGGDYGKKELSPALRNRF 1568
Cdd:smart00382 76 KLKPD-VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK----------NLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4420-5060 |
1.00e-10 |
|
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: 68.89 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4420 AGADDGEEGDADGTMSGTGMGEGEGTKDVSEEIEDEEQVLGTQNEERNNDDKQDTKEEKNGM-DMENDFDGNLEDIEQDD 4498
Cdd:COG5271 167 ADEGDELAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASaVVEEEDASEDAVAAADE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4499 DKEEDDSDSDSDEEDPDEQIGDVDDMDPDAVDDKMWGDEAEENLKESDKTVEDQGNQDQQQESEIVAKEEEDQQQNEAKG 4578
Cdd:COG5271 247 TLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIAT 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4579 EKPEKSDKNDkqqeadgeegdgdeemdddenqgsgDEDQQEDDAEGEGQDEDDVENKPGEQLNADIPEAETLELPDDLNM 4658
Cdd:COG5271 327 ADELAAADDE-------------------------DDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADT 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4659 DGDDDDNGDEEGQEGQDMNDPMDMDEQPAKGEDEQLPEEDENAEAFHDALDDVDQAPQEDEEMADASAqmdteqgEGEEQ 4738
Cdd:COG5271 382 DAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEA-------DSLAD 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4739 DEEENGEDKEENEELAPEVGDSEQqqkSGQIEEDDQGEEENKAQNREQPNSDATADNQ--------FGVQGESGKQSKSS 4810
Cdd:COG5271 455 EEEEAEAELDTEEDTESAEEDADG---DEATDEDDASDDGDEEEAEEDAEAEADSDELtaeetsadDGADTDAAADPEDS 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4811 AGKKEGEDDTADINE-DADDDIAEKKEQKGKSERG------ANQTNDEEDPDADNEQGDQDDQDQE-------AKEAQSN 4876
Cdd:COG5271 532 DEDALEDETEGEENApGSDQDADETDEPEATAEEDepdeaeAETEDATENADADETEESADESEEAeasedeaAEEEEAD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4877 PQRSLGDALEKWRRRLADLDDAADEEEEDENADKEKKTEDQDTEQAQVNEEDSfEYVKNDEDAHDMQTMGNAQPDQVqdl 4956
Cdd:COG5271 612 DDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASADE-SEEEAEDESETSSEDAEEDADAA--- 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4957 kmggMDEEKEDTKETsGEMDVDQQADNVDTMPLPRDTLEMSGATDVQGAILSKKLPEQQLVDETEVLTMDESVVAREPLE 5036
Cdd:COG5271 688 ----AAEASDDEEET-EEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAE 762
|
650 660
....*....|....*....|....
gi 758354136 5037 QEDIERMRDELETQVSDWREDGRD 5060
Cdd:COG5271 763 EDDADGLEEALEEEKADAEEAATD 786
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1418-1587 |
4.10e-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: 64.42 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1418 PVLLVGETGCGKTTVCQMLAETYNRELHIVNCHQNTETGDLLGGQrpvrnreandDPEKQQQLFEWHDGPLVQamkegHL 1497
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTY----------IYDQQTGEFEFRPGPLFA-----NV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1498 FLLDEISLADDSVlerlnsvlePSRLL-VLAEK----GGKHVEelygAAN-FQFLATMNPGGDYGKKELSPALRNRFT-E 1570
Cdd:COG0714 98 LLADEINRAPPKT---------QSALLeAMEERqvtiPGGTYK----LPEpFLVIATQNPIEQEGTYPLPEAQLDRFLlK 164
|
170
....*....|....*....
gi 758354136 1571 IWV--PsvtDRDDLIKIID 1587
Cdd:COG0714 165 LYIgyP---DAEEEREILR 180
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
701-937 |
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 758354136 701 PVLLVGETGTGKTTVVQHLADMIH-QNLIVVNLSQQSDSSDLLGGFKPVDGKvlaipmkeeferlfektfsvkknakfle 779
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDPGG---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 780 mvrktfihqkwsnfvtllkqavkmsqqkfeaeqnaeskrvsaptlrnawktfakkveefevqqvqsqnkfvFNFMEGSLV 859
Cdd:pfam07728 53 -----------------------------------------------------------------------ASWVDGPLV 61
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758354136 860 KAVRQGDWILLDEINLATTETLECLSGLLQDAHgsLLLTEKGDVEPIKRhPNFRLFACMNPAtDVGKRDLPPGLRNRF 937
Cdd:pfam07728 62 RAAREGEIAVLDEINRANPDVLNSLLSLLDERR--LLLPDGGELVKAAP-DGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4536-5079 |
1.23e-08 |
|
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: 61.95 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4536 DEAEENLKESDKTVEDQGNQDQQQESEIVAKEEEDQQQNEAKGEKPEKSDK--------NDKQQEADGEEGDGDEEMDDD 4607
Cdd:COG5271 386 DEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVtsaeddiaTDEEADSLADEEEEAEAELDT 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4608 ENqgSGDEDQQEDDAEGEGQDEDDVENKPGEQLNADIPEAETLELPDDLNMDGDDDD----NGDEEGQEGQDMNDPMDmD 4683
Cdd:COG5271 466 EE--DTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGAdtdaAADPEDSDEDALEDETE-G 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4684 EQPAKGEDEQLPEEDENAEAFHDALDD---VDQAPQEDEEMADASAQMDTEQGEGEEQDEEENGEDKEENEELAPEV-GD 4759
Cdd:COG5271 543 EENAPGSDQDADETDEPEATAEEDEPDeaeAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADAdGA 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4760 SEQQQKSGQIEEDDQGEEENKAQNREQPNSDATADNQF-----GVQGESGKQSKSSAGKKEGEDDTADINED------AD 4828
Cdd:COG5271 623 ADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEAsadesEEEAEDESETSSEDAEEDADAAAAEASDDeeeteeAD 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4829 DDIAEKKEQKGKSERGANQ--------TNDEEDPDADNEQGDQDDQDQEAKEAQSNPQRSLGDA---LEKWRRRLADLDD 4897
Cdd:COG5271 703 EDAETASEEADAEEADTEAdgtaeeaeEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDAdglEEALEEEKADAEE 782
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4898 AADEEEEDENADKEKKTED-----------QDTEQAQVNEEDSFEYVKNDEDAHDMQTMGNAQPDQVQDLKMGGMDEEKE 4966
Cdd:COG5271 783 AATDEEAEAAAEEKEKVADedqdtdedallDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADL 862
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4967 DTKETS----GEMDVDQQADNVDTMPLPRDTLEMSGATDVQGAILSKKLPEQQLVDETEVLTMDESVVAREPLEQEDIER 5042
Cdd:COG5271 863 DLDADLaadeHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGA 942
|
570 580 590
....*....|....*....|....*....|....*..
gi 758354136 5043 MRDELETQVSDWREDGRDINKArELWQGYENLTHDLA 5079
Cdd:COG5271 943 AEDDLDALALDEAGDEESDDAA-ADDAGDDSLADDDE 978
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4536-4985 |
1.65e-08 |
|
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: 61.57 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4536 DEAEENLKESDKTVEDQGNQDQQQESEivAKEEEDQQ-QNEAKGEKPEKSDKNDKQQeadgeegdGDEEMDDDENQGSGD 4614
Cdd:COG5271 592 DESEEAEASEDEAAEEEEADDDEADAD--ADGAADEEeTEEEAAEDEAAEPETDASE--------AADEDADAETEAEAS 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4615 EDQQEDDAEGEGQDEDDVENKPGEQLNADIP--EAETLELPDDLNMDGDDDDNGDEEGQEgqdmndpmDMDEQPAKGEDE 4692
Cdd:COG5271 662 ADESEEEAEDESETSSEDAEEDADAAAAEASddEEETEEADEDAETASEEADAEEADTEA--------DGTAEEAEEAAE 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4693 QLPEEDENAEAFHDALD-DVDQAPQEDEEMADASAQMDTEQGEGEEQDEEENGEDKEENEELAPEVGDSEQQQKSGQIEE 4771
Cdd:COG5271 734 EAESADEEAASLPDEADaEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLD 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4772 DDQGEEENKAQNREQPNSDATADNQFGVQGESGKQSKSSAGKKEGEDDTADINEDADDDIAEKKEQKGKSERGANQTNDE 4851
Cdd:COG5271 814 EAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGE 893
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4852 EDPDADNEQGDQDDQDQEAKEAQSNPQRSLGDALEKWRRRLADLDDAADEEEEDENADKEKKTEDQDTEQAQVNEEDSFE 4931
Cdd:COG5271 894 ADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEESDDAAADDAGDDSL 973
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 758354136 4932 YvKNDEDAHDMQTMGNAQPDQVQDLKMGGMDEEKEDTKETSGEMDVDQQADNVD 4985
Cdd:COG5271 974 A-DDDEALADAADDAEADDSELDASESTGEAEGDEDDDELEDGEAAAGEATADL 1026
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4558-4842 |
3.17e-08 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 60.78 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4558 QQESEIVAKEEEDQQQNEAKGEKPEKSDkNDKQQEADGEEGDGdeemdddeNQGSGD-EDQQEDDAEGEGQDEDDVENKP 4636
Cdd:TIGR00927 637 EAEHTGERTGEEGERPTEAEGENGEESG-GEAEQEGETETKGE--------NESEGEiPAERKGEQEGEGEIEAKEADHK 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4637 GEQlnadipEAETLELPDDLNMDGDDDDNGDEEGQEGQDMNDPMDMDEQpAKGEDEQLPEEDE-NAEAFHDALDDVDQAP 4715
Cdd:TIGR00927 708 GET------EAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAE-GKHEVETEGDRKEtEHEGETEAEGKEDEDE 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4716 QEDEEMADASAQMDTEQGEGEEQDEEENGEDKEeneelapEVGDSEQQQKSGQIEEDDQGEEENKAQNReqpnsDATADN 4795
Cdd:TIGR00927 781 GEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKD-------EHEGQSETQADDTEVKDETGEQELNAENQ-----GEAKQD 848
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 758354136 4796 QFGVQGESGkqskSSAGKKEGEDDTADINEDADDDIAEKKEQKGKSE 4842
Cdd:TIGR00927 849 EKGVDGGGG----SDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENE 891
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
1753-1891 |
5.77e-08 |
|
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 429622 [Multi-domain] Cd Length: 131 Bit Score: 54.49 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1753 ILLEGSPGVGKTSLVSALAAASGHHLVRINLSeqTDLM--DLFGSDLPVEggNSGEFAWRDAPFLqamkaGDWVLLDELN 1830
Cdd:pfam07726 2 VLLEGVPGLAKTLLVRTLARSLGLDFRRIQFT--PDLLpsDITGTEVFDQ--KTREFEFRPGPVF-----ANVLLADEIN 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758354136 1831 LAS---QSVLegLNSCLDHR----GAVYipELDREFFcakefrVFGAQNPLQQGGGRKgLPKSFVNRF 1891
Cdd:pfam07726 73 RAPpktQSAL--LEAMQERQvtidGETH--PLPEPFF------VLATQNPIEQEGTYP-LPEAQLDRF 129
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
5138-5293 |
1.09e-07 |
|
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.
Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 54.49 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5138 YQVMISVDDSKSMSEShSVQLAYEALSLISKALSQLEVGD-ISITSFGERVRLLHPFDQPFTAESGANVIQQFTF-AQQK 5215
Cdd:cd00198 1 ADIVFLLDVSGSMGGE-KLDKAKEALKALVSSLSASPPGDrVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 758354136 5216 TYVKNLIETSVGLFESAKHSSGPGNAelwqlqLIISDGICEDHNT-LRALVRNALDQQIMMIFIVVDNKPEKDSILNMT 5293
Cdd:cd00198 80 TNIGAALRLALELLKSAKRPNARRVI------ILLTDGEPNDGPElLAEAARELRKLGITVYTIGIGDDANEDELKEIA 152
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
346-474 |
1.61e-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: 56.33 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 346 AVSLALSIGAPTLLEGVTGAGKTALIEELASRTGRGAELV--KIHLgdqtDPKVLLGTYVSTSTPGSFRWQAGVLTTAVL 423
Cdd:COG0714 23 LVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIqfTPDL----LPSDILGTYIYDQQTGEFEFRPGPLFANVL 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 758354136 424 egrwvLIEDIDLAPAEVLSVLLPLLETRHLFIPsrGEKIKAKEGFQLFGTR 474
Cdd:COG0714 99 -----LADEINRAPPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIATQ 142
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2228-2314 |
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 758354136 2228 GKFEWIDGLLINALEKGYWLLIDNANMCNPSVLDRLNPLFENdgvlmvNERGLVDGTVKVIKPHPNFRMFMTVDPQNG-- 2305
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 758354136 2306 -ELSRAMRNR 2314
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1750-1892 |
5.17e-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: 52.53 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1750 KKPILLEGSPGVGKTSLVSALAAAS---GHHLVRINLSeqtdlmDLFGSDlpVEGGNSGEFAWRDAPFLQAMKAGDWVLL 1826
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFI 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758354136 1827 DELNLASQSVLEGLNSCLDhrgavyipELDREFFCAKEFRVFGAQNPLQQGGGRKGLPKSFVNRFT 1892
Cdd:cd00009 91 DEIDSLSRGAQNALLRVLE--------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIV 148
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1753-1788 |
1.66e-06 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 50.28 E-value: 1.66e-06
10 20 30
....*....|....*....|....*....|....*.
gi 758354136 1753 ILLEGSPGVGKTSLVSALAAASGHHLVRINLSEQTD 1788
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS 36
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4616-4859 |
1.86e-06 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 54.62 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4616 DQQEDDAEGEGQDEDDVENK-----PGEQLNADIPEAETLElpDDLNMDGDDDDNGDEEGQEGQDMNDPmDMDEQPAKGE 4690
Cdd:TIGR00927 661 EESGGEAEQEGETETKGENEsegeiPAERKGEQEGEGEIEA--KEADHKGETEAEEVEHEGETEAEGTE-DEGEIETGEE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4691 DEQLPEEDEN-AEAFHDALDDVDQAPQEDEEMADASAQMDTEQGEGEEQdeeengedkeeneelapevGDSEQQQKSGQI 4769
Cdd:TIGR00927 738 GEEVEDEGEGeAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAG-------------------EDGEMKGDEGAE 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4770 EEDDQGEEENKAQNREQPNSDATADNQFGVQGESGKQSKSSAGKKEGEDDTADINEDADDDIAEKKEQKGKSERGANQTN 4849
Cdd:TIGR00927 799 GKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEE 878
|
250
....*....|
gi 758354136 4850 DEEDPDADNE 4859
Cdd:TIGR00927 879 EEEEEEEEEE 888
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1066-1261 |
2.81e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 53.20 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1066 QIPRQPHEDFIQFGYFWLQQGQFPPEDDTRYILTN---SVETKLYNLARV--IMSRKFPVLIQGPTSAGKTSMVEYMAKK 1140
Cdd:PHA02244 63 EIEDSPEEQFFELPVKIELQQEGKPAGDISGIDTTkiaSNPTFHYETADIakIVNANIPVFLKGGAGSGKNHIAEQIAEA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1141 TGHRFVRINnhehTDLQEYLGTYVSNNEGKlvFQEGVLVEALRNGYWIVLDELNLAPSDVLEALNRLLDDNRELLIPETq 1220
Cdd:PHA02244 143 LDLDFYFMN----AIMDEFELKGFIDANGK--FHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANKFFDFADER- 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 758354136 1221 eiVKPHPHFMLFATQNPAG-----LYGGRKALSRAFRNRFLELHFD 1261
Cdd:PHA02244 216 --VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1745-1785 |
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 758354136 1745 RSMQLKKPILLEGSPGVGKTSLVSALAAASGHHLVRINLSE 1785
Cdd:cd19481 21 YGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4535-4886 |
4.16e-06 |
|
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: 53.48 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4535 GDEAEENLKESDKTVEDQGNQDQQqesEIVAKEEEDQQQNEAKGEKPEKSDKNDKQQeadgeEGDGDEEMDDDENQGSGD 4614
Cdd:COG5271 662 ADESEEEAEDESETSSEDAEEDAD---AAAAEASDDEEETEEADEDAETASEEADAE-----EADTEADGTAEEAEEAAE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4615 EDQQEDDAEGEGQDEDDVENKPGEQLNADIPEAETLELPDDLNMDGDDDDNGDEEGQEGQDMNDPMDmDEQPAKGEDEQL 4694
Cdd:COG5271 734 EAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVA-DEDQDTDEDALL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4695 PEEDENAEAfhdALDDVDQAPQEDEEMADASAQMDTEQGEGEEQDEEENGEDKEENEELAPEVGDSEQQQKS-------- 4766
Cdd:COG5271 813 DEAEADEEE---DLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAetdadada 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4767 ------GQIEEDDQGEEENKAQNREQPNSDATADNQFGVQGESGKQSKSSAGKKEGEDDTADINEDADDDIAEKKEQKGK 4840
Cdd:COG5271 890 dageadSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEESDDAAADDAG 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 758354136 4841 SERgaNQTNDEEDPDADNEQGDQDDQDQEAKEAQSNPQRSLGDALE 4886
Cdd:COG5271 970 DDS--LADDDEALADAADDAEADDSELDASESTGEAEGDEDDDELE 1013
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4532-4789 |
7.14e-06 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 52.69 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4532 KMWGDEAE-ENLKESDKTVEDQGNQDQQQESEIVAKEE-EDQQQNEAKGEKPEKSDKNDKQqEADGEEGDGDEEMDDDEN 4609
Cdd:TIGR00927 643 ERTGEEGErPTEAEGENGEESGGEAEQEGETETKGENEsEGEIPAERKGEQEGEGEIEAKE-ADHKGETEAEEVEHEGET 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4610 QGSGDEDQQEDDAEGEGQDEDDVENKPGEQLNADIPEAETLELPDDLNMDGDDDDNGDE---EGQEGQDMNDPMDMDEQP 4686
Cdd:TIGR00927 722 EAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEgeiQAGEDGEMKGDEGAEGKV 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4687 AKGEDEQLPEEDENAEAFHDALDDVDQAPQEDEEMADASAQMDTEQGEGEEQDEEengedkeeneelAPEVGDSE----- 4761
Cdd:TIGR00927 802 EHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGG------------GSDGGDSEeeeee 869
|
250 260 270
....*....|....*....|....*....|
gi 758354136 4762 --QQQKSGQIEEDDQGEEENKaqnrEQPNS 4789
Cdd:TIGR00927 870 eeEEEEEEEEEEEEEEEEEEN----EEPLS 895
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1687-1832 |
9.35e-06 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 52.08 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1687 KPNATELEILGETKDKVHTAGDKFTIGPFEIPRGQLAKTDIKF-TLLAPTTADNAMRVIRSMQLKKPILLEGSPGVGKTS 1765
Cdd:COG1401 157 ALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLkDLLREKFEETLEAFLAALKTKKNVILAGPPGTGKTY 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1766 LVSALAAA------SGHHLV--RINLSEQTDLMDLFgsdlPVEGgnSGEFAWRDAPFLQAM-KAGD------WVLLDELN 1830
Cdd:COG1401 237 LARRLAEAlggednGRIEFVqfHPSWSYEDFLLGYR----PSLD--EGKYEPTPGIFLRFClKAEKnpdkpyVLIIDEIN 310
|
..
gi 758354136 1831 LA 1832
Cdd:COG1401 311 RA 312
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4673-5035 |
1.81e-05 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 51.45 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4673 GQDMNDPMdMDEQPAK-GEDEQLPEE------------------------DENAEAFHDALDDVDQAPQEDEEmADASAQ 4727
Cdd:NF033609 536 GDGIDKPV-VPEQPDEpGEIEPIPEDsdsdpgsdsgsdssnsdsgsdsgsDSTSDSGSDSASDSDSASDSDSA-SDSDSA 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4728 MDTEQGEGEEQDEEENGEDKEENEELAPEVGDSEQQQKSGQIEEDDQGEEENKAQNREqpnSDATADNQFGVQGESGKQS 4807
Cdd:NF033609 614 SDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD---SDSDSDSDSDSDSDSDSDS 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4808 KSSAGKKEGEDDTADINEDADDDIAEKKEQKGKSERGANQTND-EEDPDADNEQGDQDDQDQEAKEAQSNPQRSLGDAle 4886
Cdd:NF033609 691 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-- 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4887 kwrrrladlddaaDEEEEDENADKEKKTEDQDTEQAQVNEEDSFEYVKNDEDAhDMQTMGNAQPDQVQDlkmggMDEEKE 4966
Cdd:NF033609 769 -------------DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSD-----SDSDSD 829
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 758354136 4967 DTKETSGEMDVDQQADNVDTMPLPRDTlEMSGATDVQGAILSKKLPEQQLVDETEVLTMDESVVAREPL 5035
Cdd:NF033609 830 SDSDSDSDSDSDSDSDSDSDSDSDSDS-ESDSNSDSESGSNNNVVPPNSPKNGTNASNKNEAKDSKEPL 897
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1718-1903 |
1.85e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 50.89 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1718 PRGQLAKTDIKFTLLAPTTADNAMRVIRSMQLKKPILLEGSPGVGKTSLVSALAAAsghhlVRINLSEQTDLMDLFgsdl 1797
Cdd:PHA02244 87 PAGDISGIDTTKIASNPTFHYETADIAKIVNANIPVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAIMDEF---- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1798 PVEGGNSGEFAWRDAPFLQAMKAGDWVLLDELNLASQSVLEGLNSCLDHRgavYIPELDREFFCAKEFRVFGAQNPLQQG 1877
Cdd:PHA02244 158 ELKGFIDANGKFHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANK---FFDFADERVTAHEDFRVISAGNTLGKG 234
|
170 180 190
....*....|....*....|....*....|....*...
gi 758354136 1878 G-----GRKGLPKSFVNRFTQVYVE-------QLTSDD 1903
Cdd:PHA02244 235 AdhiyvARNKIDGATLDRFAPIEFDydekiehLISNGD 272
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
1396-1524 |
1.89e-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: 49.79 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1396 LVWTKAMRRLFSLVARCLQHNEP-VLLVGETGCGKTTVCQMLAETYNRE---LHIVNCHQNTET-----GDLLGGQRPVR 1466
Cdd:COG3267 22 LFLSPSHREALARLEYALAQGGGfVVLTGEVGTGKTTLLRRLLERLPDDvkvAYIPNPQLSPAEllraiADELGLEPKGA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1467 NREanddpEKQQQLFEWhdgpLVQAMKEG--HLFLLDEISLADDSVLERLnsvlepsRLL 1524
Cdd:COG3267 102 SKA-----DLLRQLQEF----LLELAAAGrrVVLIIDEAQNLPPETLEEL-------RLL 145
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1408-1571 |
3.13e-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: 47.14 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1408 LVARCLQHNEPVLLVGETGCGKTTVCQMLA---ETYNRELHIVNCHQNTETGDLLGGQRPVRNReanddpekqqQLFEwh 1484
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAELFGHFLVR----------LLFE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1485 dgplVQAMKEGHLFLLDEIsladDSVLERLNSVLEpsRLLVLAEKGGKHVEELygaanFQFLATMNPGGDygkkELSPAL 1564
Cdd:cd00009 79 ----LAEKAKPGVLFIDEI----DSLSRGAQNALL--RVLETLNDLRIDRENV-----RVIGATNRPLLG----DLDRAL 139
|
....*..
gi 758354136 1565 RNRFTEI 1571
Cdd:cd00009 140 YDRLDIR 146
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4536-5048 |
4.29e-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: 50.40 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4536 DEAEENLKESDKTVEDQGNQDQQQESEIVAKEEEDQQQNEAKGEKPEKSDKNDKQQEADGEEGDGDEEMDDDENQGSGDE 4615
Cdd:COG5271 135 LATDTLGGGDLDLATKDGDELLPSLADNDEAAADEGDELAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4616 DQQEDDAEGEGQDEDDVENKPGEQL-NADIPEAETLELPDDLNMDGDDDDNGDEEGQEGQDMNDPMDMDEQPAKGEDEQL 4694
Cdd:COG5271 215 VAADDDLAAEEGASAVVEEEDASEDaVAAADETLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELT 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4695 PEEDENAEAFHDALDDVDQAPQEDEEMADASAQMDTEQGEGEEQDEEENGEDKEENEELAPEVGD----------SEQQQ 4764
Cdd:COG5271 295 AAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEdtqdaedeaaGEAAD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4765 KSGQIEEDDQGEEENKAQNREQPNSDATADNQFGVQGESGKQSKS-------SAGKKEGEDDTADINEDADDDIAEK-KE 4836
Cdd:COG5271 375 ESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEadedasaGETEDESTDVTSAEDDIATDEEADSlAD 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4837 QKGKSERGANQTNDEEDPDADneqgdqddqdqEAKEAQSNPQRSLGDALEKwrrrladlddaadeeeedenadkeKKTED 4916
Cdd:COG5271 455 EEEEAEAELDTEEDTESAEED-----------ADGDEATDEDDASDDGDEE------------------------EAEED 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4917 QDTEqaqvNEEDSFEYVKNDEDAhdmqtmgNAQPDQVQDLKMGGMDEEKEDTKETSGEMDVDQQADNVDTmplpRDTLEM 4996
Cdd:COG5271 500 AEAE----ADSDELTAEETSADD-------GADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDE----PEATAE 564
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 758354136 4997 SGATDvqgailskkLPEQQLVDETEVLTMDESvvAREPLEQEDIERMRDELE 5048
Cdd:COG5271 565 EDEPD---------EAEAETEDATENADADET--EESADESEEAEASEDEAA 605
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
29-232 |
5.27e-05 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 49.26 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 29 VSQLSTLIGSStfGSVDLEVLHQATIATTSTNKSQLLDTVSRAMLKPEWTlsvvrlfrpiVIDLVARWTLPSFTdfLDSA 108
Cdd:cd05677 222 IKLLSKLQDPD--GRILIPHFYDPVKPLTEAERARFTAIAETALIHEDTT----------VDSLIAKWRKPSLT--VHTV 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 109 SASPNANRTVykIELVAKAiSVVLPIVP-----QVKSLAVTYFTHSASLFERLNHLnnyrELEVTSSLTAELQDLLLTTY 183
Cdd:cd05677 288 KVSGPGNTTV--IPKSASA-SVSIRLVPdqdldVIKQDLTDYIQSCFAELKSQNHL----DIEVLNEAEPWLGDPDNPAY 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 758354136 184 RLLSfstSTFTPLWNWGPLVqllqFQE----PCIRYitvlcLSKVYGLSDAQV 232
Cdd:cd05677 361 QILR---EAVTAAWGVEPLY----IREggsiPTIRF-----LEKEFNAPAVQL 401
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
1404-1448 |
1.58e-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: 45.85 E-value: 1.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 758354136 1404 RLFSLVARCLQHNEPVLLVGETGCGKTTVCQMLAETYNRELHIVN 1448
Cdd:pfam12775 19 RYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPL 63
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1091-1274 |
1.66e-04 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 47.84 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1091 EDDTRYILTNSVETKLYNLARVIMSRKFpVLIQGPTSAGKTSMVEYMAKKTG----HRFVRINNHehtdlQEY------L 1160
Cdd:COG1401 196 DDYLKDLLREKFEETLEAFLAALKTKKN-VILAGPPGTGKTYLARRLAEALGgednGRIEFVQFH-----PSWsyedflL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1161 GTYVSNNEGKLVFQEGVLVEALR-------NGYWIVLDELNLAPSD--------VLEALNRLLDDNRELLIPETQEIVKP 1225
Cdd:COG1401 270 GYRPSLDEGKYEPTPGIFLRFCLkaeknpdKPYVLIIDEINRANVEkyfgellsLLESDKRGEELSIELPYSGEGEEFSI 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 758354136 1226 HPHFMLFATQNPA--GLYGGRKALSRAFRNRFLELHFDDIPEDELETILSK 1274
Cdd:COG1401 350 PPNLYIIGTMNTDdrSLALSDKALRRRFTFEFLDPDLDKLSNEEVVDLLEE 400
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
1401-1449 |
1.77e-04 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 47.97 E-value: 1.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 758354136 1401 AMRRLFSLVARCLQHNEPVLLVGETGCGKTTVCQMLAETYNRE---LHIVNC 1449
Cdd:COG3284 329 AMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRAdgpFVAVNC 380
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
701-741 |
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 758354136 701 PVLLVGETGTGKTTVVQHLADMIHQN---LIVVNLSQQSDSSDL 741
Cdd:pfam12775 33 PVLLVGPTGTGKTVIIQNLLRKLDKEkylPLFINFSAQTTSNQT 76
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1124-1212 |
2.30e-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: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1124 GPTSAGKTSMVEYMAKK---TGHRFVRIN------NHEHTDLQEYLGTYVSNNEGklvfqeGVLVEAL-RNGYWIVL-DE 1192
Cdd:cd19499 48 GPTGVGKTELAKALAELlfgDEDNLIRIDmseymeKHSVSRLIGAPPGYVGYTEG------GQLTEAVrRKPYSVVLlDE 121
|
90 100
....*....|....*....|
gi 758354136 1193 LNLAPSDVLEALNRLLDDNR 1212
Cdd:cd19499 122 IEKAHPDVQNLLLQVLDDGR 141
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1116-1255 |
2.39e-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: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1116 RKFPVLIQGPTSAGKTSMVEYMAK---KTGHRFVRINNHEhtdlqEYLGTYVSNNEGKLVFQEGVLVEALRNGYWIVLDE 1192
Cdd:cd00009 18 PPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASD-----LLEGLVVAELFGHFLVRLLFELAEKAKPGVLFIDE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 758354136 1193 LNLAPSDVLEALNRLLDDnrellipETQEIVKPHPHFMLFATQNPAGLyggrkALSRAFRNRF 1255
Cdd:cd00009 93 IDSLSRGAQNALLRVLET-------LNDLRIDRENVRVIGATNRPLLG-----DLDRALYDRL 143
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5140-5287 |
3.01e-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: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5140 VMISVDDSKSMSESHsvqlAYEALSLISKALSQLEVGD----ISITSFGERVRLLHPFDQPFTAESGANVIQQFT-FAQQ 5214
Cdd:smart00327 2 VVFLLDGSGSMGGNR----FELAKEFVLKLVEQLDIGPdgdrVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758354136 5215 KTYVKNLIETSVGLFESAKHSSGPGNAelwQLQLIISDGICEDHNT-LRALVRNALDQQIMMIFIVVDNKPEKD 5287
Cdd:smart00327 78 GTNLGAALQYALENLFSKSAGSRRGAP---KVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVGVGNDVDEE 148
|
|
| COG2842 |
COG2842 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
653-742 |
3.69e-04 |
|
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];
Pssm-ID: 442090 [Multi-domain] Cd Length: 254 Bit Score: 45.71 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 653 VNLSSIAASGKQKQKQALIKREKKRPFATTGHALRLMERIAVCIHLTEPVLLVGETGTGKTTVVQHLADMiHQNLIVVNL 732
Cdd:COG2842 4 KTQAAVAKEIGNEKLEAKIARWEAPSFVETKNVRRFAEALDEARALPGIGVVYGESGVGKTTAAREYANR-NPNVIYVTA 82
|
90
....*....|
gi 758354136 733 SQQSDSSDLL 742
Cdd:COG2842 83 SPSWTSKELL 92
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
679-742 |
4.39e-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: 45.55 E-value: 4.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758354136 679 FATTGHAlRLMERIAVCIHLTEP-VLLVGETGTGKTTVVQHLADMIHQNLIVVNLSQ-QSDSSDLL 742
Cdd:COG3267 23 FLSPSHR-EALARLEYALAQGGGfVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNpQLSPAELL 87
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1750-1786 |
4.41e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 46.45 E-value: 4.41e-04
10 20 30
....*....|....*....|....*....|....*..
gi 758354136 1750 KKPILLEGSPGVGKTSLVSALAAASGHHLVRINLSEQ 1786
Cdd:PRK04195 39 KKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4537-4720 |
5.44e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 46.12 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4537 EAEENLKESDKTVEDQGNQDQQQESEI---------VAKEEEDQQQNEAKGEKPEKSDKNDKQQEADGEEGDGDEEMDDD 4607
Cdd:PHA03169 74 ETAEESRHGEKEERGQGGPSGSGSESVgsptpspsgSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4608 ENQGSGdEDQQEDDAEGEGQDEDDVENKPGEQLNADIPEAEtlelpddlnmdgddddnGDEEGQEGQDMNDPMDMDEQPA 4687
Cdd:PHA03169 154 SHNPSP-NQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPP-----------------QSETPTSSPPPQSPPDEPGEPQ 215
|
170 180 190
....*....|....*....|....*....|...
gi 758354136 4688 KGEDEQLPEEDENAEAFHDALDDVDQAPQEDEE 4720
Cdd:PHA03169 216 SPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFP 248
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1116-1255 |
5.83e-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: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1116 RKFPVLIQGPTSAGKTSMVEYMAK---KTGHRFVRIN--NHEHTDLQEYLGTYVSNNEGKLVF---QEGVLVEALRNGY- 1186
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDgeDILEEVLDQLLLIIVGGKKASGSGelrLRLALALARKLKPd 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 758354136 1187 WIVLDELNLAPSDVLEALNRLLDDNRELLIPETQEIVkphphFMLFATQNPAGLygGRKALSRAFRNRF 1255
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNL-----TVILTTNDEKDL--GPALLRRRFDRRI 142
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
1742-1829 |
5.98e-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: 46.06 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1742 RVIRSMQLKKP--ILLEGSPGVGKTSLVSALAAASGHHLVRINLSeqtdlmDLFGSDLpvegGNSgEFAWRDApFLQAMK 1819
Cdd:COG0464 181 ELREEYGLPPPrgLLLYGPPGTGKTLLARALAGELGLPLIEVDLS------DLVSKYV----GET-EKNLREV-FDKARG 248
|
90
....*....|.
gi 758354136 1820 AGDWVLL-DEL 1829
Cdd:COG0464 249 LAPCVLFiDEA 259
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1402-1526 |
8.76e-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: 43.26 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1402 MRRLFSLVARCLQHNEP-VLLVGETGCGKTTVCQMLAETYNRELHIV---NCHQNTETGDLLGGQRPVRNREANDDPEKQ 1477
Cdd:pfam13191 9 LEQLLDALDRVRSGRPPsVLLTGEAGTGKTTLLRELLRALERDGGYFlrgKCDENLPYSPLLEALTREGLLRQLLDELES 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 758354136 1478 QQLFEWHDGP-------------------------LVQAMKEGH--LFLLDEISLADDS---VLERLNSVLEPSRLLVL 1526
Cdd:pfam13191 89 SLLEAWRAALlealapvpelpgdlaerlldlllrlLDLLARGERplVLVLDDLQWADEAslqLLAALLRLLESLPLLVV 167
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
4536-4844 |
9.53e-04 |
|
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) or RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II.
Pssm-ID: 310411 [Multi-domain] Cd Length: 528 Bit Score: 45.71 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4536 DEAEENLKESDKTVE-------DQGNQDQQQESEivaKEEEDQQQNEAKGEKPEK--SDKNDKQQEadgeegdgdeemdd 4606
Cdd:pfam05793 161 EEAEEEMERRKKTANgfslmmmKAAKNGPAAFGE---HDEETEGEKGGGGRGKDLkiKDLEGDDED-------------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4607 denqgSGDEDQQEDDAEGEGQD--------------EDDVENKPGEQLNADIPEAETLElpddlnmdgddddngdEEGQE 4672
Cdd:pfam05793 224 -----DGDESDKGGEDGDEEKKkkkkkklaknkkklDDDKKKKRGGDDDAFEYDSDDGD----------------DEGRE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4673 GQDMNDpmdmdeqpaKGEDEQLPEEDEnaeafhDALDDVDQAPQEDEemadasaqmdteqgegeeqdeeengedkeenee 4752
Cdd:pfam05793 283 EDYISD---------SSASGNDPEERE------DKLSPEEPAKGEIE--------------------------------- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4753 lapEVGDSEQQQKSGQIEEDDQGEEENKAQnreqpnsdatadnqfGVQGESGKQSKSSAGKKEGEDDTADINEDADDDIA 4832
Cdd:pfam05793 315 ---QSDDSEESEEEKNEEEGKLSKKGKKAK---------------KLKGKKNGKDKSESSDGDDSDDSDIDDEDSVPLFT 376
|
330
....*....|..
gi 758354136 4833 EKKEQKGKSERG 4844
Cdd:pfam05793 377 AKKKKEPKKEEP 388
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
686-734 |
1.24e-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: 1.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 758354136 686 LRLMERIAVCIHLTEPVLLVGETGTGKTTVVQHLADMIHQNLIVVNLSQ 734
Cdd:cd19481 13 RRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
1419-1522 |
1.34e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.94 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1419 VLLVGETGCGKTTVCQMLAETY---NRELHIVNCHQNTETGDL-------LGGQRPVRNREANDDPEKQQQLfewhdgpl 1488
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSPKDLlrallraLGLPLSGRLSKEELLAALQQLL-------- 79
|
90 100 110
....*....|....*....|....*....|....
gi 758354136 1489 vQAMKEGHLFLLDEISLADDSVLERLNSVLEPSR 1522
Cdd:pfam13401 80 -LALAVAVVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
691-771 |
2.97e-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: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 691 RIAVCIHLTEPVLLVGETGTGKTTVVQHLA-DMIHQNLIVVNLsqqsDSSDLLGGFKpVDGKVLAIPMKEEFERLFEKTF 769
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIAnELFRPGAPFLYL----NASDLLEGLV-VAELFGHFLVRLLFELAEKAKP 85
|
..
gi 758354136 770 SV 771
Cdd:cd00009 86 GV 87
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4550-4724 |
3.23e-03 |
|
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443611 [Multi-domain] Cd Length: 608 Bit Score: 44.01 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4550 EDQGNQDQQQESEivaKEEEDQQQNEAKGEkpeksDKNDKQQeadgeegdgdeemdddenqgSGDEDQQEDDAEGEGQDE 4629
Cdd:COG4547 208 AEELGEDEDEEDE---DDEDDSGEQEEDEE-----DGEDEDE--------------------ESDEGAEAEDAEASGDDA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4630 DDVENKPGEQLNADIpeaetlelpddlnmdgddddngdEEGQEGQDMNDPMDMDEQPAKGEDEqlpEEDENAEAFHDALD 4709
Cdd:COG4547 260 EEGESEAAEAESDEM-----------------------AEEAEGEDSEEPGEPWRPNAPPPDD---PADPDYKVFTTAFD 313
|
170
....*....|....*
gi 758354136 4710 DVDQApqedEEMADA 4724
Cdd:COG4547 314 EVVAA----EDLCDP 324
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1419-1574 |
3.26e-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: 41.04 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1419 VLLVGETGCGKTTVCQMLAETYNRELHIVNCHQntetgdllggqrpVRNREANDDPEKQQQLFEwhdgplvQAMKEG-HL 1497
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-------------LVSKYVGESEKRLRELFE-------AAKKLApCV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 1498 FLLDEIsladDSVLERLNSVLEPSRLLVLAE-----KGGKHVEelygaANFQFLATMN-PGgdygkkELSPALRNRFT-E 1570
Cdd:pfam00004 61 IFIDEI----DALAGSRGSGGDSESRRVVNQlltelDGFTSSN-----SKVIVIAATNrPD------KLDPALLGRFDrI 125
|
....
gi 758354136 1571 IWVP 1574
Cdd:pfam00004 126 IEFP 129
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4537-5087 |
3.48e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4537 EAEENLKESDKTVEDQGNQDQQQESEIVAKEEEDQQQNEAKGEKPEKSDKNDKQqeadgeegdgdeemdddenqgsGDED 4616
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK----------------------AEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4617 QQEDDAEGEGQDEDDVENKPGEQLNadipEAETLElpddlnmdgddddnGDEEGQEGQDMNDPmdmdEQPAKGEDEQLPE 4696
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEVRKAEELR----KAEDAR--------------KAEAARKAEEERKA----EEARKAEDAKKAE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4697 EDENAEafhDALDDVDQAPQEDEEMADasAQMDTEQGEGEEQDEEENGEDKEENEELAPEVGDSEQQQKSgqiEEDDQGE 4776
Cdd:PTZ00121 1228 AVKKAE---EAKKDAEEAKKAEEERNN--EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA---DEAKKAE 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4777 EENKAQNREQPNSDATADNQFGVQGESGKQSKSSAGKKEGEDDTADINEDADDDIAEKKEQKGKSERGANQTNDEEDPDA 4856
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4857 DNEQGDQDDQDQEAKEAQSNPQ--RSLGDALEKWRRRLADLDDAADEEEEDENADKEKKT--EDQDTEQAQVNEEDSFEY 4932
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEedKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKaeEAKKADEAKKKAEEAKKA 1459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4933 VKNDEDAHDMQTMGNAQPDQVQDLKMGGMDEEKEDTKETSGEM----DVDQQADNVDTMPLPRDTLEMSGATDVQGAILS 5008
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAkkaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 5009 KKLPEQQLVDEtevLTMDESVvaREPLEQEDIERMRDELETQVSDWR--EDGRDINKAR--ELWQGYENLTHDLAmglcE 5084
Cdd:PTZ00121 1540 KKAEEKKKADE---LKKAEEL--KKAEEKKKAEEAKKAEEDKNMALRkaEEAKKAEEARieEVMKLYEEEKKMKA----E 1610
|
...
gi 758354136 5085 QLR 5087
Cdd:PTZ00121 1611 EAK 1613
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4535-4787 |
3.73e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.42 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4535 GDEAEENLKESDKTVEDQGNQDQQQESEIVAKEEEDQQQNE--AKGEKPEKSDKNDKQQEADGEEGDGDEEMDDDENQGS 4612
Cdd:PHA03169 37 RGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEesRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELAS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4613 GDEDQqeddAEGEGQDEDDVENKPGEQLNADIPEAETLElpddlnmdgDDDDNGD-EEGQEGQDMNDPMDMDEqPAKGED 4691
Cdd:PHA03169 117 GLSPE----NTSGSSPESPASHSPPPSPPSHPGPHEPAP---------PESHNPSpNQQPSSFLQPSHEDSPE-EPEPPT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4692 EQLPEEDENAEAFHDALDDVDQAPQEDEEMADASAQmdteqgegeeqdeeengedkeeneelaPEVGDSEQQQKSGQIEE 4771
Cdd:PHA03169 183 SEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPT---------------------------PQQAPSPNTQQAVEHED 235
|
250
....*....|....*.
gi 758354136 4772 DdqgEEENKAQNREQP 4787
Cdd:PHA03169 236 E---PTEPEREGPPFP 248
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4453-4828 |
4.31e-03 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 43.85 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4453 EDEEQVLGTQNEERNNDDK---QDTKEEKNGMDMENDFDGNLEDIEQDDDKEEDDSDSDSDEEDPDEQIGDVDDMDP--D 4527
Cdd:COG5271 662 ADESEEEAEDESETSSEDAeedADAAAAEASDDEEETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESAdeE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4528 AVDDKMWGDEAEENLKESDKTVEDQGNQDQQQESEIVAKEEE--DQQQNEAKGEKPEKSDKNDKQQE--ADGEEGDGDEE 4603
Cdd:COG5271 742 AASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAatDEEAEAAAEEKEKVADEDQDTDEdaLLDEAEADEEE 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4604 MDDDENQGSGDEDQQEDDAEGEGQDEDDVENKPGEQLNADIPEAETLELPDDLNMDGDDDDNGDEEGQEGQDMND----- 4678
Cdd:COG5271 822 DLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSsgess 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4679 ----PMDMDEQPAKGEDEQLPEEDENAEAFHDALDDVDQAPQEDEEMADASAqmdteqgegeeqdeeengedkeeneelA 4754
Cdd:COG5271 902 aaaeDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALD---------------------------E 954
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758354136 4755 PEVGDSEQQQKSGQIEEDDQGEEENKAQNREQPNSDATADNQFGVQGESGKQSKSSAGKKEGEDDTADINEDAD 4828
Cdd:COG5271 955 AGDEESDDAAADDAGDDSLADDDEALADAADDAEADDSELDASESTGEAEGDEDDDELEDGEAAAGEATADLAA 1028
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4420-4857 |
4.42e-03 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 43.85 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4420 AGADDGEEGDADGTMSGTGMGEGEGTKDVSEEIEDEEQVLGTQNEERNNDDKQDTKEEKNGMDMENDF----DGNLEDIE 4495
Cdd:COG5271 591 ADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAeasaDESEEEAE 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4496 QDDDKEEDDSDS----DSDEEDP----DEQIGDVDDMDPDAVDDKMWGDEAEENLKESDKTVEDQGNQDQQQESEIVAKE 4567
Cdd:COG5271 671 DESETSSEDAEEdadaAAAEASDdeeeTEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEAD 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4568 EEDQQQNEAKGEKPEKSDKNDKQQeadgeegdgdeEMDDDENQGSGDEDQQEDDAEGEGQDEDDVENKPGEQLNADIPEA 4647
Cdd:COG5271 751 AEEEAEEAEEAEEDDADGLEEALE-----------EEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADE 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4648 ETLELPDDLNMDGDDDDNGDEEGQEGQDmnDPMDMDEQPAKGEDEQLPEEDENAEAFHDALDDVDQAPQEDEEMADAsaq 4727
Cdd:COG5271 820 EEDLDGEDEETADEALEDIEAGIAEDDE--EDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEA--- 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4728 mDTEQGEGEEQDEEENGEDKEENEELAPEVGDSEQQQKSGQIEEDDQGEEENKAQNREQPNSDATADNQfgVQGESGKQS 4807
Cdd:COG5271 895 -DSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEESDD--AAADDAGDD 971
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 758354136 4808 KSSAGKKEGEDDTADINEDADDDIAEKKEQKGKSERGANQTNDEEDPDAD 4857
Cdd:COG5271 972 SLADDDEALADAADDAEADDSELDASESTGEAEGDEDDDELEDGEAAAGE 1021
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1750-1791 |
4.43e-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: 41.39 E-value: 4.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 758354136 1750 KKPI---LLEGSPGVGKTSLVSALAAA---SGHHLVRINLSEQTDLMD 1791
Cdd:cd19499 38 NRPIgsfLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKHS 85
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
1742-1782 |
4.57e-03 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 41.12 E-value: 4.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 758354136 1742 RVIRSMQLKKP--ILLEGSPGVGKTSLVSALAAASGHHLVRIN 1782
Cdd:cd19503 24 ELFRALGLKPPrgVLLHGPPGTGKTLLARAVANEAGANFLSIS 66
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
1748-1783 |
5.00e-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: 41.39 E-value: 5.00e-03
10 20 30
....*....|....*....|....*....|....*..
gi 758354136 1748 QLKKPIL-LEGSPGVGKTSLVSALAAASGHHLVRINL 1783
Cdd:cd19500 34 SMKGPILcLVGPPGVGKTSLGKSIARALGRKFVRISL 70
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
702-742 |
5.18e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 40.40 E-value: 5.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 758354136 702 VLLVGETGTGKTTVVQHLADMIHQ---NLIVVNLSQQSDSSDLL 742
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLPEvrdSVVFVDLPSGTSPKDLL 51
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4615-4859 |
8.84e-03 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 42.59 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4615 EDQQEDDAEGEGQDED--DVENKPGEQLNADIPEAETLELPDDLNMDGDDDDNGDEEGQEGQDMNDPMDMD-EQPAKGED 4691
Cdd:NF033609 559 EDSDSDPGSDSGSDSSnsDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDsASDSDSAS 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4692 EQLPEEDENAEAFHDALDDVDQAPQEDEEmADASAQMDTEQGEGEEQDEEENGEDKEENEELAPEVGDSEQQQKSgqiEE 4771
Cdd:NF033609 639 DSDSDSDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS---DS 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758354136 4772 DDQGEEENKAQNREQPNSDATADNQFGVQGESGKQSKSSAGKKEGEDDTADINEDADDDIAEKKEQKGKSERGANQTND- 4850
Cdd:NF033609 715 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDs 794
|
....*....
gi 758354136 4851 EEDPDADNE 4859
Cdd:NF033609 795 DSDSDSDSD 803
|
|
| |
