|
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 ... |
5316-5586 |
2.16e-138 |
|
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: 434.09 E-value: 2.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5316 LSQQLCEQLRLLLEPTQAAKLRGDYRTGKRLNMRKIIPYIASQFRKDRIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5395
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5396 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFNDSSGTHILRLCTFQQRKTKIAQFLETVAKMFAAAQKLSQ 5475
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5476 NVSPEtaQLLLIVSDGRGLFLEGKDRVLaaVQAAQNANIFVIFVVLDNPNSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5555
Cdd:cd01460 161 SGSLW--QLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 568925788 5556 FPFYIILRDVNALPETLSDALRQWFELVTAS 5586
Cdd:cd01460 236 FPYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
911-1013 |
9.21e-41 |
|
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: 147.34 E-value: 9.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 911 DLQILIVDYLKGLNVSKNTVQGIVNFYTALRKESGTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGSIQRSLYEGFCLG 989
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 568925788 990 FLTQLDRASHPVVQKLICQHIISG 1013
Cdd:pfam17865 81 FLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1381-1535 |
3.56e-28 |
|
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: 112.77 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1381 PVLLVGDTGCGKTTVCQMFS-ALANQKLYSVNCHLNMETSDFLGGLrpvrqkpndkdELDTRLFEWHDGPLVLAMKEDSF 1459
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDPGGASWVDGPLVRAAREGEI 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568925788 1460 FLLDEISLADDSVLERLNSVLEvEKCLVLAEKGSPESKDNevelltagKHFRILATMNPgGDFGKKELSPALRNRF 1535
Cdd:pfam07728 70 AVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKAAP--------DGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1895-1993 |
1.24e-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: 98.53 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1895 DMEFIASTLFPtIDKDIVKKMVAFNNHIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLI-----LVDQSPGCYDPGQHVF 1969
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....
gi 568925788 1970 LVYGERMRTREDKEKVVAVFKDVF 1993
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVL 103
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1075-1211 |
8.42e-22 |
|
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: 94.28 E-value: 8.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1075 PVLIQGETSVGKTSLIRWLAAASGNHCVR-INNHEHTDIQEYIGCYTSDTSGKlVFNEGVLIDAMRKGYWIVLDELNLAP 1153
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568925788 1154 TDVLEALNRLLDDNRELLITETQEVVRAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 1211
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPL--DRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1223-1324 |
1.89e-21 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 465540 Cd Length: 106 Bit Score: 92.36 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1223 ELETILHKRCSLPPSYCSKLVKVMLDLQSYRRRSSVFA--GKQGFIALRDLFRWAERYRLAEQTQEDYDWLQHLANDGFM 1300
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 568925788 1301 LLAGRVRKQEEADVIQEVLEKHFK 1324
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
480-601 |
2.88e-19 |
|
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: 86.20 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 480 DLNEVLQSKYPSLLAATDHLLDIYieltgekhccpsvaydkapQEVSEAERENRRVVLEG--RELSLRDLLNWCNRVAHG 557
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVY-------------------SRLQELVSSSRSFGSSGspREFNLRDLLRWCRRLSSL 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568925788 558 F-DPTSSTALLHIFQEAMDCFTAMLSEQTKKLRMAEVIGSRLNIS 601
Cdd:pfam17867 62 LpTLLSPTVREEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
325-453 |
4.97e-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: 83.50 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 325 VLLEGPIGSGKTSLVEHLAAVTGRTKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATKGYWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 568925788 405 YAPLDVVSVLIPLLEHGELLIP-GHGDCLKVAPTFQLFATRRLLSCGGSW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1743-1883 |
3.48e-17 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 81.18 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1743 PILLEGSPGVGKTSLVAALAKA-SGNTLVRINLSEQTDITDLFGADLPveggRGGEFAWCDGPLLAALKAGHWVVLDELN 1821
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568925788 1822 LASQSILEGLNACFDHRgEIYVPELGMSFQVQHEKTRIFGCQNPfrQGGGRKGLPKSFLNRF 1883
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4684-5254 |
3.34e-09 |
|
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: 63.88 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4684 DVSDRIENEEQVEDTFQKGQEkDEEDLDSKPDTKGeDNAIEMSEDFDGKMHDGELEQEEDDEKSDSEDgDLDKQMGNLNG 4763
Cdd:COG5271 473 EEDADGDEATDEDDASDDGDE-EEAEEDAEAEADS-DELTAEETSADDGADTDAAADPEDSDEDALED-ETEGEENAPGS 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4764 -EEADKLDERLwgddeeededgdgrAEETGPGVDEEDSELVAKDDSLDAGNLNKNKKHQDEKEDSEPEDVEqGQEKINEQ 4842
Cdd:COG5271 550 dQDADETDEPE--------------ATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAE-EEEADDDE 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4843 IDEREydENEVDPYHGNQEKLPEPEALDLPDDLKLDSEDksggedtdneeaeeenpleikektvdmeeTDHEIEEPGAG- 4921
Cdd:COG5271 615 ADADA--DGAADEEETEEEAAEDEAAEPETDASEAADED-----------------------------ADAETEAEASAd 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4922 ------QDEGESphePEEGPSEDKENMDMDTGAD-------DQDRDTSSHAEEHSLEEEAEEEEEKGEKEEDKATTDGGG 4988
Cdd:COG5271 664 eseeeaEDESET---SSEDAEEDADAAAAEASDDeeeteeaDEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADE 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4989 ESGVNPVDQGLQPQKEEEEEGEQSDAEEqVPEATERkEHATCGQTGVDNVQSAQAVELAGAAPEKEQGKEEHGSGAADAN 5068
Cdd:COG5271 741 EAASLPDEADAEEEAEEAEEAEEDDADG-LEEALEE-EKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEAD 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5069 QAEGHESNLIARLSSQQHTNKNTQSFKRRPGQADNERSVGDYNERVRKRLRTVGTDRETEQEPTQAQVEDADAFEHVKQG 5148
Cdd:COG5271 819 EEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSG 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5149 SDAYDA----QTYDVASSEQQQTAKASGQDQEEEEIEDILMDTEEELMRAEDTEQLKPEAVQSETAA---TSGSSEMEVD 5221
Cdd:COG5271 899 ESSAAAedddAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEESDDAAAddaGDDSLADDDE 978
|
570 580 590
....*....|....*....|....*....|...
gi 568925788 5222 MQTLKTKEDQDPRTTTPHQETENERPERSRDST 5254
Cdd:COG5271 979 ALADAADDAEADDSELDASESTGEAEGDEDDDE 1011
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
669-898 |
5.13e-08 |
|
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: 54.99 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 669 PVLLVGETGTGKTSAVQYLAYAT-GQHLRVVNMNQQSDTADLLGGFKPvdhkliwlplretfeelfvqtfskkqnftflg 747
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 748 hiqtcyrqkrwhdllklmlhvqksastkggeqsqpgllkekweafglrlnhaqqqmkmteNALLFAFVEGTLAQAIKKGE 827
Cdd:pfam07728 49 ------------------------------------------------------------DPGGASWVDGPLVRAAREGE 68
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568925788 828 WILLDEINLAAPETLECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 898
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
2215-2301 |
1.07e-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: 53.84 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 2215 GSFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPggvltiNERGMVDGSTCTVTPNPNFRLFLSMDPIHG-- 2292
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 568925788 2293 -EISRAMRNR 2301
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| |
|
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 ... |
5316-5586 |
2.16e-138 |
|
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: 434.09 E-value: 2.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5316 LSQQLCEQLRLLLEPTQAAKLRGDYRTGKRLNMRKIIPYIASQFRKDRIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5395
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5396 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFNDSSGTHILRLCTFQQRKTKIAQFLETVAKMFAAAQKLSQ 5475
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5476 NVSPEtaQLLLIVSDGRGLFLEGKDRVLaaVQAAQNANIFVIFVVLDNPNSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5555
Cdd:cd01460 161 SGSLW--QLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 568925788 5556 FPFYIILRDVNALPETLSDALRQWFELVTAS 5586
Cdd:cd01460 236 FPYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
911-1013 |
9.21e-41 |
|
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: 147.34 E-value: 9.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 911 DLQILIVDYLKGLNVSKNTVQGIVNFYTALRKESGTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGSIQRSLYEGFCLG 989
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 568925788 990 FLTQLDRASHPVVQKLICQHIISG 1013
Cdd:pfam17865 81 FLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1381-1535 |
3.56e-28 |
|
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: 112.77 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1381 PVLLVGDTGCGKTTVCQMFS-ALANQKLYSVNCHLNMETSDFLGGLrpvrqkpndkdELDTRLFEWHDGPLVLAMKEDSF 1459
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDPGGASWVDGPLVRAAREGEI 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568925788 1460 FLLDEISLADDSVLERLNSVLEvEKCLVLAEKGSPESKDNevelltagKHFRILATMNPgGDFGKKELSPALRNRF 1535
Cdd:pfam07728 70 AVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKAAP--------DGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1895-1993 |
1.24e-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: 98.53 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1895 DMEFIASTLFPtIDKDIVKKMVAFNNHIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLI-----LVDQSPGCYDPGQHVF 1969
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....
gi 568925788 1970 LVYGERMRTREDKEKVVAVFKDVF 1993
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVL 103
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1075-1211 |
8.42e-22 |
|
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: 94.28 E-value: 8.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1075 PVLIQGETSVGKTSLIRWLAAASGNHCVR-INNHEHTDIQEYIGCYTSDTSGKlVFNEGVLIDAMRKGYWIVLDELNLAP 1153
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568925788 1154 TDVLEALNRLLDDNRELLITETQEVVRAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 1211
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPL--DRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1223-1324 |
1.89e-21 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 92.36 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1223 ELETILHKRCSLPPSYCSKLVKVMLDLQSYRRRSSVFA--GKQGFIALRDLFRWAERYRLAEQTQEDYDWLQHLANDGFM 1300
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 568925788 1301 LLAGRVRKQEEADVIQEVLEKHFK 1324
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
480-601 |
2.88e-19 |
|
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: 86.20 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 480 DLNEVLQSKYPSLLAATDHLLDIYieltgekhccpsvaydkapQEVSEAERENRRVVLEG--RELSLRDLLNWCNRVAHG 557
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVY-------------------SRLQELVSSSRSFGSSGspREFNLRDLLRWCRRLSSL 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568925788 558 F-DPTSSTALLHIFQEAMDCFTAMLSEQTKKLRMAEVIGSRLNIS 601
Cdd:pfam17867 62 LpTLLSPTVREEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
325-453 |
4.97e-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: 83.50 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 325 VLLEGPIGSGKTSLVEHLAAVTGRTKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATKGYWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 568925788 405 YAPLDVVSVLIPLLEHGELLIP-GHGDCLKVAPTFQLFATRRLLSCGGSW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1743-1883 |
3.48e-17 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 81.18 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1743 PILLEGSPGVGKTSLVAALAKA-SGNTLVRINLSEQTDITDLFGADLPveggRGGEFAWCDGPLLAALKAGHWVVLDELN 1821
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568925788 1822 LASQSILEGLNACFDHRgEIYVPELGMSFQVQHEKTRIFGCQNPfrQGGGRKGLPKSFLNRF 1883
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1731-1883 |
8.13e-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: 63.65 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1731 AQRLLRAAKLNKPILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQTDITDLFGADLPVEggRGGEFAWCDGPLLAAlk 1810
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQ--QTGEFEFRPGPLFAN-- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568925788 1811 aghwVVL-DELNLAS---QS-ILEGLNacfdhRGEIYVPelGMSFQVQHeKTRIFGCQNPFRQGGGRKgLPKSFLNRF 1883
Cdd:COG0714 97 ----VLLaDEINRAPpktQSaLLEAME-----ERQVTIP--GGTYKLPE-PFLVIATQNPIEQEGTYP-LPEAQLDRF 161
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4684-5254 |
3.34e-09 |
|
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: 63.88 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4684 DVSDRIENEEQVEDTFQKGQEkDEEDLDSKPDTKGeDNAIEMSEDFDGKMHDGELEQEEDDEKSDSEDgDLDKQMGNLNG 4763
Cdd:COG5271 473 EEDADGDEATDEDDASDDGDE-EEAEEDAEAEADS-DELTAEETSADDGADTDAAADPEDSDEDALED-ETEGEENAPGS 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4764 -EEADKLDERLwgddeeededgdgrAEETGPGVDEEDSELVAKDDSLDAGNLNKNKKHQDEKEDSEPEDVEqGQEKINEQ 4842
Cdd:COG5271 550 dQDADETDEPE--------------ATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAE-EEEADDDE 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4843 IDEREydENEVDPYHGNQEKLPEPEALDLPDDLKLDSEDksggedtdneeaeeenpleikektvdmeeTDHEIEEPGAG- 4921
Cdd:COG5271 615 ADADA--DGAADEEETEEEAAEDEAAEPETDASEAADED-----------------------------ADAETEAEASAd 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4922 ------QDEGESphePEEGPSEDKENMDMDTGAD-------DQDRDTSSHAEEHSLEEEAEEEEEKGEKEEDKATTDGGG 4988
Cdd:COG5271 664 eseeeaEDESET---SSEDAEEDADAAAAEASDDeeeteeaDEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADE 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4989 ESGVNPVDQGLQPQKEEEEEGEQSDAEEqVPEATERkEHATCGQTGVDNVQSAQAVELAGAAPEKEQGKEEHGSGAADAN 5068
Cdd:COG5271 741 EAASLPDEADAEEEAEEAEEAEEDDADG-LEEALEE-EKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEAD 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5069 QAEGHESNLIARLSSQQHTNKNTQSFKRRPGQADNERSVGDYNERVRKRLRTVGTDRETEQEPTQAQVEDADAFEHVKQG 5148
Cdd:COG5271 819 EEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSG 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5149 SDAYDA----QTYDVASSEQQQTAKASGQDQEEEEIEDILMDTEEELMRAEDTEQLKPEAVQSETAA---TSGSSEMEVD 5221
Cdd:COG5271 899 ESSAAAedddAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEESDDAAAddaGDDSLADDDE 978
|
570 580 590
....*....|....*....|....*....|...
gi 568925788 5222 MQTLKTKEDQDPRTTTPHQETENERPERSRDST 5254
Cdd:COG5271 979 ALADAADDAEADDSELDASESTGEAEGDEDDDE 1011
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1075-1231 |
4.38e-09 |
|
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: 61.34 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1075 PVLIQGETSVGKTSLIRWLAAASGNHCVRINNHEHTDIQEyiGCYTSDT---SGKLVFNEG------VLIdamrkgywiv 1145
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSD--ILGTYIYdqqTGEFEFRPGplfanvLLA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1146 lDELNLAPTDVLEALNRLLDDNRellITETQEVVRAHPRFMLFATQNPPGLYGGRkVLSRAFRNRF-VELHFDeLPSSEL 1224
Cdd:COG0714 101 -DEINRAPPKTQSALLEAMEERQ---VTIPGGTYKLPEPFLVIATQNPIEQEGTY-PLPEAQLDRFlLKLYIG-YPDAEE 174
|
....*...
gi 568925788 1225 ET-ILHKR 1231
Cdd:COG0714 175 EReILRRH 182
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
669-898 |
5.13e-08 |
|
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: 54.99 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 669 PVLLVGETGTGKTSAVQYLAYAT-GQHLRVVNMNQQSDTADLLGGFKPvdhkliwlplretfeelfvqtfskkqnftflg 747
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 748 hiqtcyrqkrwhdllklmlhvqksastkggeqsqpgllkekweafglrlnhaqqqmkmteNALLFAFVEGTLAQAIKKGE 827
Cdd:pfam07728 49 ------------------------------------------------------------DPGGASWVDGPLVRAAREGE 68
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568925788 828 WILLDEINLAAPETLECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 898
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2215-2301 |
1.07e-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: 53.84 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 2215 GSFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPggvltiNERGMVDGSTCTVTPNPNFRLFLSMDPIHG-- 2292
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 568925788 2293 -EISRAMRNR 2301
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1379-1535 |
1.54e-07 |
|
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: 53.92 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1379 GEPVLLVGDTGCGKTTVCQMFSALANQKLYSVnCHLNMETSdFLGGLRPVRQKPNDKDELDTRLFEWHDGPLVLAMKED- 1457
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-IYIDGEDI-LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKp 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568925788 1458 SFFLLDEISLADDSVLERLNSVLEVekclvlaekgspeskDNEVELLTAGKHFRILATMNPGGDFGKKELSPALRNRF 1535
Cdd:smart00382 80 DVLILDEITSLLDAEQEALLLLLEE---------------LRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1732-1891 |
8.98e-07 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 51.76 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1732 QRLLRAAKLN--KPILLEGSPGVGKTSLVAALAKAS---GNTLVRINLSEqtDITDLFGADLPVEGGRGGEFAwcdgplL 1806
Cdd:cd00009 8 EALREALELPppKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASD--LLEGLVVAELFGHFLVRLLFE------L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1807 AALKAGHWVVLDELNLASQSILEGLNACFdhrgeiyvpELGMSFQVQHEKTRIFG-CQNPFRQgggrkGLPKSFLNRFTQ 1885
Cdd:cd00009 80 AEKAKPGVLFIDEIDSLSRGAQNALLRVL---------ETLNDLRIDRENVRVIGaTNRPLLG-----DLDRALYDRLDI 145
|
....*.
gi 568925788 1886 VFVDPL 1891
Cdd:cd00009 146 RIVIPL 151
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1012-1313 |
4.05e-06 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 53.23 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1012 SGNVKSLLKQPIPEPKGGRLIQVEGYWISVGDKEPKIDETYVLTPSVKLNLRDIARVVSAGTYP--VLIQGETSVGKTSL 1089
Cdd:COG1401 158 LEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKTKknVILAGPPGTGKTYL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1090 IRWLAAASG---NHCVRI-----NNHEHTDIQEYigcYTSDTSGKLVFNEGVLIDAMRKG-------YWIVLDELNLAPT 1154
Cdd:COG1401 238 ARRLAEALGgedNGRIEFvqfhpSWSYEDFLLGY---RPSLDEGKYEPTPGIFLRFCLKAeknpdkpYVLIIDEINRANV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1155 D--------VLEALNRLLDDNRELLITETQEVVRAHPRFMLFATQNPP--GLYGGRKVLSRAFRNRFVELHFDELPSSEL 1224
Cdd:COG1401 315 EkyfgellsLLESDKRGEELSIELPYSGEGEEFSIPPNLYIIGTMNTDdrSLALSDKALRRRFTFEFLDPDLDKLSNEEV 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1225 ETILHKrcslppsyCSKLVKVMLDLQSYRRrssvFAGKQGFIALRDLFRWAERYRLAEQTQEDYDWLQHLANDGFMLLAG 1304
Cdd:COG1401 395 VDLLEE--------LNEILEKRDFQIGHRA----LLLLDGLLSGDLDLLLLLLLLLLELLLLLLDKLDLLGMAEFEDRLE 462
|
....*....
gi 568925788 1305 RVRKQEEAD 1313
Cdd:COG1401 463 LSEYLPLLL 471
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1368-1535 |
2.02e-05 |
|
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: 50.17 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1368 LAVLVGRalefgePVLLVGDTGCGKTTVCQMFSALANQKLYSVNCHLNMETSDFLGGLRPVRQkpndkdeldTRLFEWHD 1447
Cdd:COG0714 26 IALLAGG------HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQ---------TGEFEFRP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1448 GPlVLAmkedSFFLLDEISLADDSVLerlNSVLEVekclvLAEKgspeskdnEV----ELLTAGKHFRILATMNPGGDFG 1523
Cdd:COG0714 91 GP-LFA----NVLLADEINRAPPKTQ---SALLEA-----MEER--------QVtipgGTYKLPEPFLVIATQNPIEQEG 149
|
170
....*....|..
gi 568925788 1524 KKELSPALRNRF 1535
Cdd:COG0714 150 TYPLPEAQLDRF 161
|
|
| Mpp10 |
pfam04006 |
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The ... |
4695-4851 |
8.21e-05 |
|
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The U3 small nucleolar ribonucleoprotein (snoRNP) is required for three cleavage events that generate the mature 18S rRNA from the pre-rRNA. In Saccharomyces cerevisiae, depletion of Mpp10, a U3 snoRNP-specific protein, halts 18S rRNA production and impairs cleavage at the three U3 snoRNP-dependent sites.
Pssm-ID: 461128 [Multi-domain] Cd Length: 506 Bit Score: 49.19 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4695 VEDTFQKGQE-----KDEEDLD-SKPDTKGEDNAIEMSEDFDGKMHDGELEQE-------EDDEKSDSEDGDLDKQMGNL 4761
Cdd:pfam04006 159 VDDKFFKLDEmekflEDEEKKEeRKDKGKEDEDDIDYFEDDDSEDDEDDGARNlkyedffDPPEEEDEKETKKKKDKKKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4762 NGEEADKLDErlwgddeeededgdgraEETGPGVDEEDSELVAKDDSLDAGNLNKNKKHQDEKEDSEPEDVEQGQEKINE 4841
Cdd:pfam04006 239 EDEKDDEEEE-----------------DEEDDAMEEEKEDEFAEDEDEEEDDDEDSDDEEEEASPEELSSFEKRQEKLQE 301
|
170
....*....|
gi 568925788 4842 QIDEREyDEN 4851
Cdd:pfam04006 302 RIRKLE-EEN 310
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1048-1217 |
8.78e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 48.58 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1048 IDETYVLT-PSVKLNLRDIARVVSAGTyPVLIQGETSVGKTSLIRWLAAAsgnhcVRINNHEHTDI-QEYIGCYTSDTSG 1125
Cdd:PHA02244 94 IDTTKIASnPTFHYETADIAKIVNANI-PVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAImDEFELKGFIDANG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1126 KlvFNEGVLIDAMRKGYWIVLDELNLAPTDVLEALNRLLDDNRELLITETqevVRAHPRFMLFATQNPPG-----LYGGR 1200
Cdd:PHA02244 168 K--FHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVAR 242
|
170
....*....|....*..
gi 568925788 1201 KVLSRAFRNRFVELHFD 1217
Cdd:PHA02244 243 NKIDGATLDRFAPIEFD 259
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1381-1538 |
1.55e-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: 45.21 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1381 PVLLVGDTGCGKTTVCQmfsALANQ------KLYSVNCHLNMEtsdflgglrpvrqkpNDKDELDTRLFEWHDGPLVLAM 1454
Cdd:cd00009 21 NLLLYGPPGTGKTTLAR---AIANElfrpgaPFLYLNASDLLE---------------GLVVAELFGHFLVRLLFELAEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1455 KEDSFFLLDEISLADDSVLERLNSVLEVekclvlaekgspeskdnEVELLTAGKHFRILATMNPGGDFgkkELSPALRNR 1534
Cdd:cd00009 83 AKPGVLFIDEIDSLSRGAQNALLRVLET-----------------LNDLRIDRENVRVIGATNRPLLG---DLDRALYDR 142
|
....
gi 568925788 1535 FTEI 1538
Cdd:cd00009 143 LDIR 146
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5378-5524 |
3.27e-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: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5378 ICLAIDDSSSMVDNhTKQLAFESLAVIGNALTLLEVG-QIAVCSFGESVKLLHPFHeqfNDSSGTHILRLCTFQQRK--- 5453
Cdd:smart00327 2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgg 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568925788 5454 -TKIAQFLETVAKMFAAAQKLSQnvsPETAQLLLIVSDGRGLFLEGKDRVLAAVQAAQNANIFVIFVVLDNP 5524
Cdd:smart00327 78 gTNLGAALQYALENLFSKSAGSR---RGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVD 146
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1381-1557 |
3.30e-04 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 46.65 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1381 PVLLVGDTGCGKTTVCQMFSALANQKLYSvnchLNMETSDF-LGGLRPVRQKpndkdeldtrlfeWHDGPLVLAMKEDSF 1459
Cdd:PHA02244 121 PVFLKGGAGSGKNHIAEQIAEALDLDFYF----MNAIMDEFeLKGFIDANGK-------------FHETPFYEAFKKGGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1460 FLLDEISLADDSVLERLNSVLevekclvlaekgSPESKDNEVELLTAGKHFRILA---TMNPGGD---FGKKELSPALRN 1533
Cdd:PHA02244 184 FFIDEIDASIPEALIIINSAI------------ANKFFDFADERVTAHEDFRVISagnTLGKGADhiyVARNKIDGATLD 251
|
170 180
....*....|....*....|....
gi 568925788 1534 RFTEIWCPQSTKREDLIQIINHNL 1557
Cdd:PHA02244 252 RFAPIEFDYDEKIEHLISNGDEDL 275
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
316-432 |
6.23e-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: 43.67 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 316 AVSVASQNAVLLEGPIGSGKTSLVEHLAAVTGRTKPPqLLKVQLGDqtdskMLLGMYRCTDVpGEFVWQPGTLTQAATKG 395
Cdd:cd00009 13 ALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNASD-----LLEGLVVAELF-GHFLVRLLFELAEKAKP 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 568925788 396 YWILLEDIDYAPLDVVSVLIPLLEHGELLIPGHGDCL 432
Cdd:cd00009 86 GVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVR 122
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1742-1777 |
6.50e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 46.07 E-value: 6.50e-04
10 20 30
....*....|....*....|....*....|....*.
gi 568925788 1742 KPILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQ 1777
Cdd:PRK04195 40 KALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4687-4918 |
7.81e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 46.14 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4687 DRIENEEQVEDtfqKGQEKDEEDLDS--KPDTKGEDNAIEMSEDFDGKMHDGELEQEEDDEksdsEDGDLDKQMGNLNGE 4764
Cdd:TIGR00927 665 GEAEQEGETET---KGENESEGEIPAerKGEQEGEGEIEAKEADHKGETEAEEVEHEGETE----AEGTEDEGEIETGEE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4765 EADKLDE-------RLWGDDEEEDEDGDGRAEETGPGV-DEEDSELVAKDDSLDAGNLNKNKKHQDEKEDSEPEDVEQGQ 4836
Cdd:TIGR00927 738 GEEVEDEgegeaegKHEVETEGDRKETEHEGETEAEGKeDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEG 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4837 EKINEQIDEREYDENevdpyhGNQEKLPEPEALDLPDDLKLDSEDKSGGEDTDNEEAEEENPLEIKEKTVDMEETDHEIE 4916
Cdd:TIGR00927 818 QSETQADDTEVKDET------GEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENE 891
|
..
gi 568925788 4917 EP 4918
Cdd:TIGR00927 892 EP 893
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
4683-4850 |
1.39e-03 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 45.55 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4683 KDVSDRIEN--EEQVEDTFQKGQEKD-EEDLDSKPDTKGEDNAIEMSEDFDgkmHDGELEQEEDDEKSDSEDGDLDKQMG 4759
Cdd:PTZ00341 973 ENVEENVEEnvEENVEENVEENVEENvEENIEENVEENVEENIEENVEEYD---EENVEEVEENVEEYDEENVEEIEENA 1049
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4760 NLNGEEadKLDERLWGDDEEEDEDGDGRAEETgpgVDEEDSELVAKDDSLDAGNLNKNKkhQDEKEDSEPEDVEQGQEKI 4839
Cdd:PTZ00341 1050 EENVEE--NIEENIEEYDEENVEEIEENIEEN---IEENVEENVEENVEEIEENVEENV--EENAEENAEENAEENAEEY 1122
|
170
....*....|....
gi 568925788 4840 NEQIDE---REYDE 4850
Cdd:PTZ00341 1123 DDENPEehnEEYDE 1136
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1075-1217 |
1.76e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.36 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1075 PVLIQGETSVGKTSLIR---WLAAASGNHCVRIN----NHEHTDIQEYIGCYTSDTSGKLVFNEGVLIDAMRKGYW--IV 1145
Cdd:smart00382 4 VILIVGPPGSGKTTLARalaRELGPPGGGVIYIDgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568925788 1146 LDELNLAPTDVLEALNRLLDDNRELLITETQEVVRAhprfmLFATQNPPGLygGRKVLSRAFRNRFVELHFD 1217
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV-----ILTTNDEKDL--GPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1075-1211 |
1.81e-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: 42.13 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1075 PVLIQGETSVGKTSLIR---WLAAASGNHCVRINNHEHTDIQEYIGCYTSDTSGKLVFnegvlIDAMRKGYWIVLDELNL 1151
Cdd:cd00009 21 NLLLYGPPGTGKTTLARaiaNELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFE-----LAEKAKPGVLFIDEIDS 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1152 APTDVLEALNRLLDDnRELLITETQEVvrahpRFMLFATQNPPGLyggrkvLSRAFRNRF 1211
Cdd:cd00009 96 LSRGAQNALLRVLET-LNDLRIDRENV-----RVIGATNRPLLGD------LDRALYDRL 143
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
812-915 |
9.52e-03 |
|
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: 41.69 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 812 FAFVEGTLAQAIkkgewILLDEINLAAPETLeclSGLLEgssgslVLLDR-----GDTEPLvRHPdFRLFACMNPATDVG 886
Cdd:COG0714 86 FEFRPGPLFANV-----LLADEINRAPPKTQ---SALLE------AMEERqvtipGGTYKL-PEP-FLVIATQNPIEQEG 149
|
90 100 110
....*....|....*....|....*....|
gi 568925788 887 KRNLPPGIRNRFT-ELYVEELESKEDLQIL 915
Cdd:COG0714 150 TYPLPEAQLDRFLlKLYIGYPDAEEEREIL 179
|
|
| |
|
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 ... |
5316-5586 |
2.16e-138 |
|
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: 434.09 E-value: 2.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5316 LSQQLCEQLRLLLEPTQAAKLRGDYRTGKRLNMRKIIPYIASQFRKDRIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5395
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5396 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFNDSSGTHILRLCTFQQRKTKIAQFLETVAKMFAAAQKLSQ 5475
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5476 NVSPEtaQLLLIVSDGRGLFLEGKDRVLaaVQAAQNANIFVIFVVLDNPNSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5555
Cdd:cd01460 161 SGSLW--QLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 568925788 5556 FPFYIILRDVNALPETLSDALRQWFELVTAS 5586
Cdd:cd01460 236 FPYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
911-1013 |
9.21e-41 |
|
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: 147.34 E-value: 9.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 911 DLQILIVDYLKGLNVSKNTVQGIVNFYTALRKESGTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGSIQRSLYEGFCLG 989
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 568925788 990 FLTQLDRASHPVVQKLICQHIISG 1013
Cdd:pfam17865 81 FLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1381-1535 |
3.56e-28 |
|
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: 112.77 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1381 PVLLVGDTGCGKTTVCQMFS-ALANQKLYSVNCHLNMETSDFLGGLrpvrqkpndkdELDTRLFEWHDGPLVLAMKEDSF 1459
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDPGGASWVDGPLVRAAREGEI 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568925788 1460 FLLDEISLADDSVLERLNSVLEvEKCLVLAEKGSPESKDNevelltagKHFRILATMNPgGDFGKKELSPALRNRF 1535
Cdd:pfam07728 70 AVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKAAP--------DGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1895-1993 |
1.24e-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: 98.53 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1895 DMEFIASTLFPtIDKDIVKKMVAFNNHIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLI-----LVDQSPGCYDPGQHVF 1969
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....
gi 568925788 1970 LVYGERMRTREDKEKVVAVFKDVF 1993
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVL 103
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1075-1211 |
8.42e-22 |
|
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: 94.28 E-value: 8.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1075 PVLIQGETSVGKTSLIRWLAAASGNHCVR-INNHEHTDIQEYIGCYTSDTSGKlVFNEGVLIDAMRKGYWIVLDELNLAP 1153
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568925788 1154 TDVLEALNRLLDDNRELLITETQEVVRAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 1211
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPL--DRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1223-1324 |
1.89e-21 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 92.36 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1223 ELETILHKRCSLPPSYCSKLVKVMLDLQSYRRRSSVFA--GKQGFIALRDLFRWAERYRLAEQTQEDYDWLQHLANDGFM 1300
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 568925788 1301 LLAGRVRKQEEADVIQEVLEKHFK 1324
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
480-601 |
2.88e-19 |
|
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: 86.20 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 480 DLNEVLQSKYPSLLAATDHLLDIYieltgekhccpsvaydkapQEVSEAERENRRVVLEG--RELSLRDLLNWCNRVAHG 557
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVY-------------------SRLQELVSSSRSFGSSGspREFNLRDLLRWCRRLSSL 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568925788 558 F-DPTSSTALLHIFQEAMDCFTAMLSEQTKKLRMAEVIGSRLNIS 601
Cdd:pfam17867 62 LpTLLSPTVREEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
325-453 |
4.97e-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: 83.50 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 325 VLLEGPIGSGKTSLVEHLAAVTGRTKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATKGYWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 568925788 405 YAPLDVVSVLIPLLEHGELLIP-GHGDCLKVAPTFQLFATRRLLSCGGSW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1743-1883 |
3.48e-17 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 81.18 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1743 PILLEGSPGVGKTSLVAALAKA-SGNTLVRINLSEQTDITDLFGADLPveggRGGEFAWCDGPLLAALKAGHWVVLDELN 1821
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568925788 1822 LASQSILEGLNACFDHRgEIYVPELGMSFQVQHEKTRIFGCQNPfrQGGGRKGLPKSFLNRF 1883
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1731-1883 |
8.13e-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: 63.65 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1731 AQRLLRAAKLNKPILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQTDITDLFGADLPVEggRGGEFAWCDGPLLAAlk 1810
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQ--QTGEFEFRPGPLFAN-- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568925788 1811 aghwVVL-DELNLAS---QS-ILEGLNacfdhRGEIYVPelGMSFQVQHeKTRIFGCQNPFRQGGGRKgLPKSFLNRF 1883
Cdd:COG0714 97 ----VLLaDEINRAPpktQSaLLEAME-----ERQVTIP--GGTYKLPE-PFLVIATQNPIEQEGTYP-LPEAQLDRF 161
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4684-5254 |
3.34e-09 |
|
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: 63.88 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4684 DVSDRIENEEQVEDTFQKGQEkDEEDLDSKPDTKGeDNAIEMSEDFDGKMHDGELEQEEDDEKSDSEDgDLDKQMGNLNG 4763
Cdd:COG5271 473 EEDADGDEATDEDDASDDGDE-EEAEEDAEAEADS-DELTAEETSADDGADTDAAADPEDSDEDALED-ETEGEENAPGS 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4764 -EEADKLDERLwgddeeededgdgrAEETGPGVDEEDSELVAKDDSLDAGNLNKNKKHQDEKEDSEPEDVEqGQEKINEQ 4842
Cdd:COG5271 550 dQDADETDEPE--------------ATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAE-EEEADDDE 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4843 IDEREydENEVDPYHGNQEKLPEPEALDLPDDLKLDSEDksggedtdneeaeeenpleikektvdmeeTDHEIEEPGAG- 4921
Cdd:COG5271 615 ADADA--DGAADEEETEEEAAEDEAAEPETDASEAADED-----------------------------ADAETEAEASAd 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4922 ------QDEGESphePEEGPSEDKENMDMDTGAD-------DQDRDTSSHAEEHSLEEEAEEEEEKGEKEEDKATTDGGG 4988
Cdd:COG5271 664 eseeeaEDESET---SSEDAEEDADAAAAEASDDeeeteeaDEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADE 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4989 ESGVNPVDQGLQPQKEEEEEGEQSDAEEqVPEATERkEHATCGQTGVDNVQSAQAVELAGAAPEKEQGKEEHGSGAADAN 5068
Cdd:COG5271 741 EAASLPDEADAEEEAEEAEEAEEDDADG-LEEALEE-EKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEAD 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5069 QAEGHESNLIARLSSQQHTNKNTQSFKRRPGQADNERSVGDYNERVRKRLRTVGTDRETEQEPTQAQVEDADAFEHVKQG 5148
Cdd:COG5271 819 EEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSG 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5149 SDAYDA----QTYDVASSEQQQTAKASGQDQEEEEIEDILMDTEEELMRAEDTEQLKPEAVQSETAA---TSGSSEMEVD 5221
Cdd:COG5271 899 ESSAAAedddAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEESDDAAAddaGDDSLADDDE 978
|
570 580 590
....*....|....*....|....*....|...
gi 568925788 5222 MQTLKTKEDQDPRTTTPHQETENERPERSRDST 5254
Cdd:COG5271 979 ALADAADDAEADDSELDASESTGEAEGDEDDDE 1011
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1075-1231 |
4.38e-09 |
|
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: 61.34 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1075 PVLIQGETSVGKTSLIRWLAAASGNHCVRINNHEHTDIQEyiGCYTSDT---SGKLVFNEG------VLIdamrkgywiv 1145
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSD--ILGTYIYdqqTGEFEFRPGplfanvLLA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1146 lDELNLAPTDVLEALNRLLDDNRellITETQEVVRAHPRFMLFATQNPPGLYGGRkVLSRAFRNRF-VELHFDeLPSSEL 1224
Cdd:COG0714 101 -DEINRAPPKTQSALLEAMEERQ---VTIPGGTYKLPEPFLVIATQNPIEQEGTY-PLPEAQLDRFlLKLYIG-YPDAEE 174
|
....*...
gi 568925788 1225 ET-ILHKR 1231
Cdd:COG0714 175 EReILRRH 182
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4684-5232 |
1.80e-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: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4684 DVSDRIENEEQVEDTFQKGQEKDEEDLDSKP------DTKGEDNAIEMSEDFDGKMHDGELEQEEDDEKSDSEDGDLDKQ 4757
Cdd:COG5271 480 EATDEDDASDDGDEEEAEEDAEAEADSDELTaeetsaDDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEP 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4758 MGNLNGEEADKLDERLWGDDEEE----DEDGDGRAEETGPGVDEEDSELVAKDDSLDA---GNLNKNKKHQDEKEDSEPE 4830
Cdd:COG5271 560 EATAEEDEPDEAEAETEDATENAdadeTEESADESEEAEASEDEAAEEEEADDDEADAdadGAADEEETEEEAAEDEAAE 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4831 DVEQGQEKINEQIDEREYDENEVDpyhgNQEKLPEPEALDLPDDLKLDSEDKSGGEDTDNEEAEEENpleiKEKTVDMEE 4910
Cdd:COG5271 640 PETDASEAADEDADAETEAEASAD----ESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEAD----EDAETASEE 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4911 TDHEIEEPGAGQDEGESPHEPEEGPSEDKENMDMDTGADDQDRDTSSHAEEHSLEEEAEEEEEKGEKEEDKATTDGGGES 4990
Cdd:COG5271 712 ADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEEAEA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4991 GVNPVDQGLQPQKEEEEEGEQSDAEEQVPEATERKEhatcgQTGVDNVQSAQAVELAGAAPEKEQGKEEHGSGAADANQA 5070
Cdd:COG5271 792 AAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGED-----EETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDA 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5071 EGHESNLIARLSSQQHT-NKNTQSFKRRPGQADNERSVGDYNERVRKRLRTVGTDretEQEPTQAQVEDADAFEHVKQGS 5149
Cdd:COG5271 867 DLAADEHEAEEAQEAETdADADADAGEADSSGESSAAAEDDDAAEDADSDDGAND---EDDDDDAEEERKDAEEDELGAA 943
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5150 DAYDAQTY--DVASSEQQQTAKASGQDQEEEEIEDILMDTEEELMRAEDTEQLKPEAVQSETAATSGSSEMEVDMQTLKT 5227
Cdd:COG5271 944 EDDLDALAldEAGDEESDDAAADDAGDDSLADDDEALADAADDAEADDSELDASESTGEAEGDEDDDELEDGEAAAGEAT 1023
|
....*
gi 568925788 5228 KEDQD 5232
Cdd:COG5271 1024 ADLAA 1028
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
669-898 |
5.13e-08 |
|
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: 54.99 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 669 PVLLVGETGTGKTSAVQYLAYAT-GQHLRVVNMNQQSDTADLLGGFKPvdhkliwlplretfeelfvqtfskkqnftflg 747
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 748 hiqtcyrqkrwhdllklmlhvqksastkggeqsqpgllkekweafglrlnhaqqqmkmteNALLFAFVEGTLAQAIKKGE 827
Cdd:pfam07728 49 ------------------------------------------------------------DPGGASWVDGPLVRAAREGE 68
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568925788 828 WILLDEINLAAPETLECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 898
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2215-2301 |
1.07e-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: 53.84 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 2215 GSFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPggvltiNERGMVDGSTCTVTPNPNFRLFLSMDPIHG-- 2292
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 568925788 2293 -EISRAMRNR 2301
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4684-5257 |
1.16e-07 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 58.87 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4684 DVSDRIENEEQVEDTFQKGQEKDEEDLDSKPDTKGEDNAIemSEDFDGKMHDGELEQEEDDEKSDSEDGDLDKqmGNLNG 4763
Cdd:COG5271 324 IATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQD--AEDEAAGEAADESEGADTDAAADEADAAADD--SADDE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4764 EEADKLDERLWGDDEEEDEDGDGRAEETGPGVDEEDSELVAKDDSLDAgnlNKNKKHQDEKEDSEPEDVEQGQEKINEQI 4843
Cdd:COG5271 400 EASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDE---EADSLADEEEEAEAELDTEEDTESAEEDA 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4844 DERE-YDENEVDPYHGNQEKLPEPEAldlpddlkldsedksggedtdneeaeeenpleikEKTVDMEETDHEIEEPGAGQ 4922
Cdd:COG5271 477 DGDEaTDEDDASDDGDEEEAEEDAEA----------------------------------EADSDELTAEETSADDGADT 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4923 DEGESPHEPEEGPSEDKENMDMDTGADDQDRDtsshaeehsleeeaeeeeekgekeedkATTDGGGESGVNPVDQGlQPQ 5002
Cdd:COG5271 523 DAAADPEDSDEDALEDETEGEENAPGSDQDAD---------------------------ETDEPEATAEEDEPDEA-EAE 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5003 KEEEEEGEQSDAEEQVPEATERKEHAT-CGQTGVDNVQSAQAVELAGAAPEKEQGKEEhgsgAADANQAEGHESNLIARl 5081
Cdd:COG5271 575 TEDATENADADETEESADESEEAEASEdEAAEEEEADDDEADADADGAADEEETEEEA----AEDEAAEPETDASEAAD- 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5082 ssqqhtnKNTQSFKRRPGQADNER-SVGDYNErvrkrlrTVGTDRETEQE-PTQAQVEDADAFEHVKQgsdayDAQTYDV 5159
Cdd:COG5271 650 -------EDADAETEAEASADESEeEAEDESE-------TSSEDAEEDADaAAAEASDDEEETEEADE-----DAETASE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5160 ASSEQQQTAKASGQDQEEEEIEDILMDTEEELMRAEDTEQLKPEAVQSETAATSGSSEME---VDMQTLKTKEDQDPRtt 5236
Cdd:COG5271 711 EADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEealEEEKADAEEAATDEE-- 788
|
570 580
....*....|....*....|.
gi 568925788 5237 tphQETENERPERSRDSTIHT 5257
Cdd:COG5271 789 ---AEAAAEEKEKVADEDQDT 806
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1379-1535 |
1.54e-07 |
|
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: 53.92 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1379 GEPVLLVGDTGCGKTTVCQMFSALANQKLYSVnCHLNMETSdFLGGLRPVRQKPNDKDELDTRLFEWHDGPLVLAMKED- 1457
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-IYIDGEDI-LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKp 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568925788 1458 SFFLLDEISLADDSVLERLNSVLEVekclvlaekgspeskDNEVELLTAGKHFRILATMNPGGDFGKKELSPALRNRF 1535
Cdd:smart00382 80 DVLILDEITSLLDAEQEALLLLLEE---------------LRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1732-1891 |
8.98e-07 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 51.76 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1732 QRLLRAAKLN--KPILLEGSPGVGKTSLVAALAKAS---GNTLVRINLSEqtDITDLFGADLPVEGGRGGEFAwcdgplL 1806
Cdd:cd00009 8 EALREALELPppKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASD--LLEGLVVAELFGHFLVRLLFE------L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1807 AALKAGHWVVLDELNLASQSILEGLNACFdhrgeiyvpELGMSFQVQHEKTRIFG-CQNPFRQgggrkGLPKSFLNRFTQ 1885
Cdd:cd00009 80 AEKAKPGVLFIDEIDSLSRGAQNALLRVL---------ETLNDLRIDRENVRVIGaTNRPLLG-----DLDRALYDRLDI 145
|
....*.
gi 568925788 1886 VFVDPL 1891
Cdd:cd00009 146 RIVIPL 151
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4683-5250 |
1.03e-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: 55.79 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4683 KDVSDRIENEEQVEDTFQKGQEKDEEDLDSKPDTKGEDNAIEMSEDFDGKMHDGELEQEEDDEKSDSEDGDLDKQMGNLN 4762
Cdd:COG5271 285 EDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDA 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4763 GEEADKLDERLWGDDEEEDEDGDGRAEETGPGVDEEDSELVAKDDSLDAGNLNKNKKHQDEKEDSEPE--DVEQGQEKI- 4839
Cdd:COG5271 365 EDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDEstDVTSAEDDIa 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4840 NEQIDEREYDENEVDPYHGNQEKLPEPEALDLPDDLKLDSEDKSGGEDTDNEEAEEENpleikEKTVDMEETDHEIEEPG 4919
Cdd:COG5271 445 TDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEA-----EADSDELTAEETSADDG 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4920 AGQDEGESPHEPEEGPSEDKENMDMDTGADDQDRD-----TSSHAEEHSLEEEAEEEEEKGEKEEDKATTDGGGESGVNP 4994
Cdd:COG5271 520 ADTDAAADPEDSDEDALEDETEGEENAPGSDQDADetdepEATAEEDEPDEAEAETEDATENADADETEESADESEEAEA 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4995 VDQGLQPQKEEEEEGEQSDAEEQVPEATERKEHATCGQTGVDNVQSAQAVELAGAAPEKEQGKEEHGSGAADANQAEGHE 5074
Cdd:COG5271 600 SEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDESETSSED 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5075 SN-----LIARLS----SQQHTNKNTQSFKRRPGQADNERSVGDYNERVRK-RLRTVGTDRETEQEPTQAQVEDADAFEH 5144
Cdd:COG5271 680 AEedadaAAAEASddeeETEEADEDAETASEEADAEEADTEADGTAEEAEEaAEEAESADEEAASLPDEADAEEEAEEAE 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5145 VKQGSDAYDAQTYDVASSEQQQTAKAsgqdqeeeeiedilmDTEEELMRAEDTEQLKPEAVQSETAATSGSSEMEVDMQT 5224
Cdd:COG5271 760 EAEEDDADGLEEALEEEKADAEEAAT---------------DEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLD 824
|
570 580
....*....|....*....|....*.
gi 568925788 5225 LKTKEDQDPRTTTPHQETENERPERS 5250
Cdd:COG5271 825 GEDEETADEALEDIEAGIAEDDEEDD 850
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1744-1779 |
2.85e-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: 49.90 E-value: 2.85e-06
10 20 30
....*....|....*....|....*....|....*.
gi 568925788 1744 ILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQTD 1779
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS 36
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1012-1313 |
4.05e-06 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 53.23 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1012 SGNVKSLLKQPIPEPKGGRLIQVEGYWISVGDKEPKIDETYVLTPSVKLNLRDIARVVSAGTYP--VLIQGETSVGKTSL 1089
Cdd:COG1401 158 LEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKTKknVILAGPPGTGKTYL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1090 IRWLAAASG---NHCVRI-----NNHEHTDIQEYigcYTSDTSGKLVFNEGVLIDAMRKG-------YWIVLDELNLAPT 1154
Cdd:COG1401 238 ARRLAEALGgedNGRIEFvqfhpSWSYEDFLLGY---RPSLDEGKYEPTPGIFLRFCLKAeknpdkpYVLIIDEINRANV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1155 D--------VLEALNRLLDDNRELLITETQEVVRAHPRFMLFATQNPP--GLYGGRKVLSRAFRNRFVELHFDELPSSEL 1224
Cdd:COG1401 315 EkyfgellsLLESDKRGEELSIELPYSGEGEEFSIPPNLYIIGTMNTDdrSLALSDKALRRRFTFEFLDPDLDKLSNEEV 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1225 ETILHKrcslppsyCSKLVKVMLDLQSYRRrssvFAGKQGFIALRDLFRWAERYRLAEQTQEDYDWLQHLANDGFMLLAG 1304
Cdd:COG1401 395 VDLLEE--------LNEILEKRDFQIGHRA----LLLLDGLLSGDLDLLLLLLLLLLELLLLLLDKLDLLGMAEFEDRLE 462
|
....*....
gi 568925788 1305 RVRKQEEAD 1313
Cdd:COG1401 463 LSEYLPLLL 471
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
1744-1883 |
6.46e-06 |
|
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: 48.71 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1744 ILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQTDITDLFGADLPVEggRGGEFAWCDGPLLAALkaghwVVLDELNLA 1823
Cdd:pfam07726 2 VLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQ--KTREFEFRPGPVFANV-----LLADEINRA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568925788 1824 S---QSILegLNACFDHR----GEIY-VPELGMsfqvqhektrIFGCQNPFRQGGGRKgLPKSFLNRF 1883
Cdd:pfam07726 75 PpktQSAL--LEAMQERQvtidGETHpLPEPFF----------VLATQNPIEQEGTYP-LPEAQLDRF 129
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1739-1776 |
7.68e-06 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 49.20 E-value: 7.68e-06
10 20 30
....*....|....*....|....*....|....*...
gi 568925788 1739 KLNKPILLEGSPGVGKTSLVAALAKASGNTLVRINLSE 1776
Cdd:cd19481 24 GLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1368-1535 |
2.02e-05 |
|
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: 50.17 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1368 LAVLVGRalefgePVLLVGDTGCGKTTVCQMFSALANQKLYSVNCHLNMETSDFLGGLRPVRQkpndkdeldTRLFEWHD 1447
Cdd:COG0714 26 IALLAGG------HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQ---------TGEFEFRP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1448 GPlVLAmkedSFFLLDEISLADDSVLerlNSVLEVekclvLAEKgspeskdnEV----ELLTAGKHFRILATMNPGGDFG 1523
Cdd:COG0714 91 GP-LFA----NVLLADEINRAPPKTQ---SALLEA-----MEER--------QVtipgGTYKLPEPFLVIATQNPIEQEG 149
|
170
....*....|..
gi 568925788 1524 KKELSPALRNRF 1535
Cdd:COG0714 150 TYPLPEAQLDRF 161
|
|
| Mpp10 |
pfam04006 |
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The ... |
4695-4851 |
8.21e-05 |
|
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The U3 small nucleolar ribonucleoprotein (snoRNP) is required for three cleavage events that generate the mature 18S rRNA from the pre-rRNA. In Saccharomyces cerevisiae, depletion of Mpp10, a U3 snoRNP-specific protein, halts 18S rRNA production and impairs cleavage at the three U3 snoRNP-dependent sites.
Pssm-ID: 461128 [Multi-domain] Cd Length: 506 Bit Score: 49.19 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4695 VEDTFQKGQE-----KDEEDLD-SKPDTKGEDNAIEMSEDFDGKMHDGELEQE-------EDDEKSDSEDGDLDKQMGNL 4761
Cdd:pfam04006 159 VDDKFFKLDEmekflEDEEKKEeRKDKGKEDEDDIDYFEDDDSEDDEDDGARNlkyedffDPPEEEDEKETKKKKDKKKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4762 NGEEADKLDErlwgddeeededgdgraEETGPGVDEEDSELVAKDDSLDAGNLNKNKKHQDEKEDSEPEDVEQGQEKINE 4841
Cdd:pfam04006 239 EDEKDDEEEE-----------------DEEDDAMEEEKEDEFAEDEDEEEDDDEDSDDEEEEASPEELSSFEKRQEKLQE 301
|
170
....*....|
gi 568925788 4842 QIDEREyDEN 4851
Cdd:pfam04006 302 RIRKLE-EEN 310
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1048-1217 |
8.78e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 48.58 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1048 IDETYVLT-PSVKLNLRDIARVVSAGTyPVLIQGETSVGKTSLIRWLAAAsgnhcVRINNHEHTDI-QEYIGCYTSDTSG 1125
Cdd:PHA02244 94 IDTTKIASnPTFHYETADIAKIVNANI-PVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAImDEFELKGFIDANG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1126 KlvFNEGVLIDAMRKGYWIVLDELNLAPTDVLEALNRLLDDNRELLITETqevVRAHPRFMLFATQNPPG-----LYGGR 1200
Cdd:PHA02244 168 K--FHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVAR 242
|
170
....*....|....*..
gi 568925788 1201 KVLSRAFRNRFVELHFD 1217
Cdd:PHA02244 243 NKIDGATLDRFAPIEFD 259
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1733-1823 |
1.14e-04 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 48.61 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1733 RLLRAAKLNKPILLEGSPGVGKTSLVAALAKA-SGNTLVRINLseqtdIT---DLFGADLpVEG----GRGGEFAWCDGP 1804
Cdd:COG1401 213 AFLAALKTKKNVILAGPPGTGKTYLARRLAEAlGGEDNGRIEF-----VQfhpSWSYEDF-LLGyrpsLDEGKYEPTPGI 286
|
90 100
....*....|....*....|....*.
gi 568925788 1805 LL-AALKAG------HWVVLDELNLA 1823
Cdd:COG1401 287 FLrFCLKAEknpdkpYVLIIDEINRA 312
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1381-1538 |
1.55e-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: 45.21 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1381 PVLLVGDTGCGKTTVCQmfsALANQ------KLYSVNCHLNMEtsdflgglrpvrqkpNDKDELDTRLFEWHDGPLVLAM 1454
Cdd:cd00009 21 NLLLYGPPGTGKTTLAR---AIANElfrpgaPFLYLNASDLLE---------------GLVVAELFGHFLVRLLFELAEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1455 KEDSFFLLDEISLADDSVLERLNSVLEVekclvlaekgspeskdnEVELLTAGKHFRILATMNPGGDFgkkELSPALRNR 1534
Cdd:cd00009 83 AKPGVLFIDEIDSLSRGAQNALLRVLET-----------------LNDLRIDRENVRVIGATNRPLLG---DLDRALYDR 142
|
....
gi 568925788 1535 FTEI 1538
Cdd:cd00009 143 LDIR 146
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5378-5524 |
3.27e-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: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5378 ICLAIDDSSSMVDNhTKQLAFESLAVIGNALTLLEVG-QIAVCSFGESVKLLHPFHeqfNDSSGTHILRLCTFQQRK--- 5453
Cdd:smart00327 2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgg 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568925788 5454 -TKIAQFLETVAKMFAAAQKLSQnvsPETAQLLLIVSDGRGLFLEGKDRVLAAVQAAQNANIFVIFVVLDNP 5524
Cdd:smart00327 78 gTNLGAALQYALENLFSKSAGSR---RGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVD 146
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1381-1557 |
3.30e-04 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 46.65 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1381 PVLLVGDTGCGKTTVCQMFSALANQKLYSvnchLNMETSDF-LGGLRPVRQKpndkdeldtrlfeWHDGPLVLAMKEDSF 1459
Cdd:PHA02244 121 PVFLKGGAGSGKNHIAEQIAEALDLDFYF----MNAIMDEFeLKGFIDANGK-------------FHETPFYEAFKKGGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1460 FLLDEISLADDSVLERLNSVLevekclvlaekgSPESKDNEVELLTAGKHFRILA---TMNPGGD---FGKKELSPALRN 1533
Cdd:PHA02244 184 FFIDEIDASIPEALIIINSAI------------ANKFFDFADERVTAHEDFRVISagnTLGKGADhiyVARNKIDGATLD 251
|
170 180
....*....|....*....|....
gi 568925788 1534 RFTEIWCPQSTKREDLIQIINHNL 1557
Cdd:PHA02244 252 RFAPIEFDYDEKIEHLISNGDEDL 275
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
4690-4940 |
3.47e-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: 46.87 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4690 ENEEQVEDTFQKGQEK-----DEEDLDSKPDTKGEDNAIEMSEDFDGKMHDGELEQEEDDEKSDSEDGD--LDKQMGNLN 4762
Cdd:pfam05793 168 ERRKKTANGFSLMMMKaakngPAAFGEHDEETEGEKGGGGRGKDLKIKDLEGDDEDDGDESDKGGEDGDeeKKKKKKKKL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4763 GEEADKLDERLWGDDEEEDEDGDGRAEETgpgvDEEDSELVAKDDSLDAGNLNKNKKHQDEKEDSEPEDVEQgqekiNEQ 4842
Cdd:pfam05793 248 AKNKKKLDDDKKKKRGGDDDAFEYDSDDG----DDEGREEDYISDSSASGNDPEEREDKLSPEEPAKGEIEQ-----SDD 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4843 IDEREYDENEVDpyHGNQEKLPEPEALDLPDDLKLDSEDKSGGEDTDNEEAEEENPLEIKEKtvdmEETDHEIEEPGAGQ 4922
Cdd:pfam05793 319 SEESEEEKNEEE--GKLSKKGKKAKKLKGKKNGKDKSESSDGDDSDDSDIDDEDSVPLFTAK----KKKEPKKEEPVDSG 392
|
250
....*....|....*...
gi 568925788 4923 DEGESPHEPEEGPSEDKE 4940
Cdd:pfam05793 393 PSSPGNSGPARPSPESGS 410
|
|
| Mpp10 |
pfam04006 |
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The ... |
4701-4868 |
3.60e-04 |
|
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The U3 small nucleolar ribonucleoprotein (snoRNP) is required for three cleavage events that generate the mature 18S rRNA from the pre-rRNA. In Saccharomyces cerevisiae, depletion of Mpp10, a U3 snoRNP-specific protein, halts 18S rRNA production and impairs cleavage at the three U3 snoRNP-dependent sites.
Pssm-ID: 461128 [Multi-domain] Cd Length: 506 Bit Score: 46.88 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4701 KGQEKDEEDLDSKPDTKGEDNAIEMSEDFDGKMHDGELEQEEDDEKSDSEDGDLD------KQMGNLNG----------- 4763
Cdd:pfam04006 87 DSEQDDEEDEDEEEDEEDEEDEEEDEDEEEEEEEEEEDDEDEDSDDEGLEEEDVKeleqktKKDAKKGRksvvddkffkl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4764 -------EEADKLDERlwgddeeededgdgraeETGPGVDEEDSELVAKDDS-----LDAGNLN---------------- 4815
Cdd:pfam04006 167 demekflEDEEKKEER-----------------KDKGKEDEDDIDYFEDDDSeddedDGARNLKyedffdppeeedeket 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568925788 4816 ----KNKKHQDEKEDSEPED-VEQGQEKINEQIDEREYDENEVDPYHGNQEKLPEPEA 4868
Cdd:pfam04006 230 kkkkDKKKEEDEKDDEEEEDeEDDAMEEEKEDEFAEDEDEEEDDDEDSDDEEEEASPE 287
|
|
| COG5137 |
COG5137 |
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ... |
4684-4827 |
4.34e-04 |
|
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];
Pssm-ID: 227466 [Multi-domain] Cd Length: 279 Bit Score: 45.76 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4684 DVSDRIENEEQVEDTFQKGQEKDEEDLDSKPDTKGEDNAiEMSEDFDGKmhdgELEQEEDDEKSDSEDGDLDKQMGNLNG 4763
Cdd:COG5137 139 DVEREILAEKPRVTRFNIVWDNDEDNDEAPPAQPDVDNE-EEERLEESD----GREEEEDEEVGSDSYGEGNRELNEEEE 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568925788 4764 EEADKLD--ERLWGDDEEEDEDGDGRAEETGPGVDEEDSELVAKDDSLDAGNLNKNKKHQDEKEDS 4827
Cdd:COG5137 214 EEAEGSDdgEDVVDYEGERIDKKQGEEEEMEEEVINLFEIEWEEESPSEEVPRNNEESPAKKQKVE 279
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
316-432 |
6.23e-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: 43.67 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 316 AVSVASQNAVLLEGPIGSGKTSLVEHLAAVTGRTKPPqLLKVQLGDqtdskMLLGMYRCTDVpGEFVWQPGTLTQAATKG 395
Cdd:cd00009 13 ALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNASD-----LLEGLVVAELF-GHFLVRLLFELAEKAKP 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 568925788 396 YWILLEDIDYAPLDVVSVLIPLLEHGELLIPGHGDCL 432
Cdd:cd00009 86 GVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVR 122
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1742-1777 |
6.50e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 46.07 E-value: 6.50e-04
10 20 30
....*....|....*....|....*....|....*.
gi 568925788 1742 KPILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQ 1777
Cdd:PRK04195 40 KALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
1734-1785 |
7.03e-04 |
|
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: 44.09 E-value: 7.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568925788 1734 LLRAAKLNKPIL-LEGSPGVGKTSLVAALAKASGNTLVRINLSEQTDITDLFG 1785
Cdd:cd19500 29 RKLKGSMKGPILcLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRG 81
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4687-4918 |
7.81e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 46.14 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4687 DRIENEEQVEDtfqKGQEKDEEDLDS--KPDTKGEDNAIEMSEDFDGKMHDGELEQEEDDEksdsEDGDLDKQMGNLNGE 4764
Cdd:TIGR00927 665 GEAEQEGETET---KGENESEGEIPAerKGEQEGEGEIEAKEADHKGETEAEEVEHEGETE----AEGTEDEGEIETGEE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4765 EADKLDE-------RLWGDDEEEDEDGDGRAEETGPGV-DEEDSELVAKDDSLDAGNLNKNKKHQDEKEDSEPEDVEQGQ 4836
Cdd:TIGR00927 738 GEEVEDEgegeaegKHEVETEGDRKETEHEGETEAEGKeDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEG 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4837 EKINEQIDEREYDENevdpyhGNQEKLPEPEALDLPDDLKLDSEDKSGGEDTDNEEAEEENPLEIKEKTVDMEETDHEIE 4916
Cdd:TIGR00927 818 QSETQADDTEVKDET------GEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENE 891
|
..
gi 568925788 4917 EP 4918
Cdd:TIGR00927 892 EP 893
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4652-4852 |
9.96e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 45.76 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4652 LPKELMEDSAGEGATQFH------DYEGGGIGDGEGMKDVSDRIENEEQVEDTFQKGQEKDEEDLDSKP--DTKGEDNAI 4723
Cdd:TIGR00927 685 IPAERKGEQEGEGEIEAKeadhkgETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHevETEGDRKET 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4724 EMSEDFDGKM----HDGELEQEEDDEKSDSEDGDLDKQMGNLngEEADKLDErlwgddeeEDEDGDGRAEETGPGVDEED 4799
Cdd:TIGR00927 765 EHEGETEAEGkedeDEGEIQAGEDGEMKGDEGAEGKVEHEGE--TEAGEKDE--------HEGQSETQADDTEVKDETGE 834
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568925788 4800 SELVAkDDSLDAGNLNKNKKHQDEKEDSEPEDVEQGQEKINEQIDEREYDENE 4852
Cdd:TIGR00927 835 QELNA-ENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEE 886
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1719-1787 |
1.06e-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: 43.32 E-value: 1.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568925788 1719 DYALTAGTTAMNAQRLLrAAKLNKPI---LLEGSPGVGKTSLVAALAKA---SGNTLVRINLSEQT---DITDLFGAD 1787
Cdd:cd19499 17 DEAVKAVSDAIRRARAG-LSDPNRPIgsfLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMekhSVSRLIGAP 93
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1076-1211 |
1.18e-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: 42.20 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1076 VLIQGETSVGKTSLIRWLAAASGNHCVRINNHEHTDiqEYIGcytsDTSGKLvfnEGVLIDAMRKGYWIV-LDELNLAPT 1154
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS--KYVG----ESEKRL---RELFEAAKKLAPCVIfIDEIDALAG 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568925788 1155 DVLEALNRLLDDNRELLITETQEVVRAHPRFMLFATQNPPGLyggrkvLSRAFRNRF 1211
Cdd:pfam00004 72 SRGSGGDSESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDK------LDPALLGRF 122
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
4683-4850 |
1.39e-03 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 45.55 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4683 KDVSDRIEN--EEQVEDTFQKGQEKD-EEDLDSKPDTKGEDNAIEMSEDFDgkmHDGELEQEEDDEKSDSEDGDLDKQMG 4759
Cdd:PTZ00341 973 ENVEENVEEnvEENVEENVEENVEENvEENIEENVEENVEENIEENVEEYD---EENVEEVEENVEEYDEENVEEIEENA 1049
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4760 NLNGEEadKLDERLWGDDEEEDEDGDGRAEETgpgVDEEDSELVAKDDSLDAGNLNKNKkhQDEKEDSEPEDVEQGQEKI 4839
Cdd:PTZ00341 1050 EENVEE--NIEENIEEYDEENVEEIEENIEEN---IEENVEENVEENVEEIEENVEENV--EENAEENAEENAEENAEEY 1122
|
170
....*....|....
gi 568925788 4840 NEQIDE---REYDE 4850
Cdd:PTZ00341 1123 DDENPEehnEEYDE 1136
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1075-1217 |
1.76e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.36 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1075 PVLIQGETSVGKTSLIR---WLAAASGNHCVRIN----NHEHTDIQEYIGCYTSDTSGKLVFNEGVLIDAMRKGYW--IV 1145
Cdd:smart00382 4 VILIVGPPGSGKTTLARalaRELGPPGGGVIYIDgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568925788 1146 LDELNLAPTDVLEALNRLLDDNRELLITETQEVVRAhprfmLFATQNPPGLygGRKVLSRAFRNRFVELHFD 1217
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV-----ILTTNDEKDL--GPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1075-1211 |
1.81e-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: 42.13 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1075 PVLIQGETSVGKTSLIR---WLAAASGNHCVRINNHEHTDIQEYIGCYTSDTSGKLVFnegvlIDAMRKGYWIVLDELNL 1151
Cdd:cd00009 21 NLLLYGPPGTGKTTLARaiaNELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFE-----LAEKAKPGVLFIDEIDS 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 1152 APTDVLEALNRLLDDnRELLITETQEVvrahpRFMLFATQNPPGLyggrkvLSRAFRNRF 1211
Cdd:cd00009 96 LSRGAQNALLRVLET-LNDLRIDRENV-----RVIGATNRPLLGD------LDRALYDRL 143
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4683-5251 |
2.06e-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: 45.01 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4683 KDVSDRIENEEQVEDTFQKGQEKDEEDLDSKPDTKGEDNAIEMSEDFDGKMHDGELEQEEDDEKSDSEDGDLDKQMGNLN 4762
Cdd:COG5271 175 ADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADETLLADDDD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4763 GEEADKLDERLWGDDEEEDEDGDGRA------EETGPGVDEEDSELVAKDDSLDAGNLNKNK--------KHQDEKEDSE 4828
Cdd:COG5271 255 TESAGATAEVGGTPDTDDEATDDADGleaaedDALDAELTAAQAADPESDDDADDSTLAALEgaaedteiATADELAAAD 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4829 PEDVEQGQEKINEQIDEREYDENEVDPYHGNQEKLPEpEALDLPDDLKLDSEDKSGGEDTDNEEAEEENPLEIKEKTVDM 4908
Cdd:COG5271 335 DEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGE-AADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDT 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4909 EETDHEIEEPGAGQ---DEGESPHEPEEGPSEDKE-----------NMDMDTGADDQDRDTSSHAEEHSLEEEAEEEEEK 4974
Cdd:COG5271 414 DEEEEEADEDASAGeteDESTDVTSAEDDIATDEEadsladeeeeaEAELDTEEDTESAEEDADGDEATDEDDASDDGDE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4975 GEKEEDKATTDGGGESGVNPVDQGLQPQKEEEEEGEQSDaEEQVPEATERKEHATCGQTGVDNVQSAQA-VELAGAAPEK 5053
Cdd:COG5271 494 EEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSD-EDALEDETEGEENAPGSDQDADETDEPEAtAEEDEPDEAE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5054 EQGKEEHGSGAADANQAEGHESNliarlSSQQHTNKNTqsfkrRPGQADNERSVGDYNERVRKRLRTVGT----DRETEQ 5129
Cdd:COG5271 573 AETEDATENADADETEESADESE-----EAEASEDEAA-----EEEEADDDEADADADGAADEEETEEEAaedeAAEPET 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 5130 EPTQAQVEDADAFEHVKQGSD------AYDAQTYDVASSEQQQTAKASGQD---QEEEEIEDILMDTEEELMRAEDTEQl 5200
Cdd:COG5271 643 DASEAADEDADAETEAEASADeseeeaEDESETSSEDAEEDADAAAAEASDdeeETEEADEDAETASEEADAEEADTEA- 721
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 568925788 5201 kPEAVQSETAATSGSSEMEVDMQTLKTKEDQDPRTTTPHQETENERPERSR 5251
Cdd:COG5271 722 -DGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEE 771
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
4686-4866 |
3.34e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 43.92 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4686 SDRIENE--------------EQVEDTFQK-GQEKDEEDLDSKPDTKGEDNAIEmSEDFDGKMHDGELEQEEDDEKSDSE 4750
Cdd:COG5644 107 SDKLENEgsvssidenelvdlDTLLDNDQPeKNESGNNDHATDKENLLESDASS-SNDSESEESDSESEIESSDSDHDDE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4751 DGDldkqmgnlngeeaDKLDerlwgddeeededgDGRAEETGPGVDEEDSELVAKDDSLDAGNLNKNKKHQDEKEDSEPE 4830
Cdd:COG5644 186 NSD-------------SKLD--------------NLRNYIVSLKKDEADAESVLSSDDNDSIEEIKYDPHETNKESGSSE 238
|
170 180 190
....*....|....*....|....*....|....*.
gi 568925788 4831 DVEqgQEKINEQIDEREYDENeVDPYHGNQEKLPEP 4866
Cdd:COG5644 239 TID--ITDLLDSIPMEQLKVS-LKPLVSESSKLDAP 271
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1736-1785 |
3.70e-03 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 43.77 E-value: 3.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568925788 1736 RAAKLNKPIL-LEGSPGVGKTSLVAALAKASGNTLVRINLSEQTDITDLFG 1785
Cdd:PRK10787 343 RVNKIKGPILcLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRG 393
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
656-685 |
4.19e-03 |
|
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).
Pssm-ID: 463698 [Multi-domain] Cd Length: 179 Bit Score: 41.61 E-value: 4.19e-03
10 20 30
....*....|....*....|....*....|
gi 568925788 656 LLEQLavcVSQGEPVLLVGETGTGKTSAVQ 685
Cdd:pfam12775 23 LLDLL---LKNGKPVLLVGPTGTGKTVIIQ 49
|
|
| DNA_pol_phi |
pfam04931 |
DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7. ... |
4684-4825 |
6.01e-03 |
|
DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7.7. Pol5p is localized exclusively to the nucleolus and binds near or at the enhancer region of rRNA-encoding DNA repeating units.
Pssm-ID: 461488 Cd Length: 765 Bit Score: 43.00 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4684 DVSDRIENEEQVEDTFQKGQEKDEEDLDSKPDTKGEDNAIEMSEDFDgkmhDGELEQEEDDEKSDSEDGDLDKQMGNLNG 4763
Cdd:pfam04931 621 DVLDARENPEGQQELFEDEDEDEEDDDEEEDDDDEDDEDSEEDDDED----DDDEDEEDDDDEDVDEIDELRAKLAEALG 696
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568925788 4764 EEADKLDErlwgddeeededgdgrAEEtgpGVDEE--DSELVAKDDSL--------DAGNlNKNKKHQDEKE 4825
Cdd:pfam04931 697 EHGDDADD----------------DDS---DSDEDmdDEQMMALDEQLaeifkerkKAGN-DKKKKKKDAKE 748
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
4686-4861 |
7.02e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 43.15 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4686 SDRIENEEQVEDTFQKGQEKDEEDLDSKPDTKG------EDNAIEMSEDFDgkmhDGELEQEEDDEKSDSEDGDLDKQMG 4759
Cdd:COG5644 13 KKQLENKILHSYEEESAGFDSEELEDNDEQGYSfgvnseDDEEIDSDEAFD----EEDEKRFADWSFNASKSGKSNKDHK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4760 NLNGEEADKLDERlwgddeeEDEDGDGRAEETG--PGVDEEDseLVAKDDSLDAGNLNKNKKHQDEkEDSEPE------D 4831
Cdd:COG5644 89 NLNNTKEISLNDS-------DDSVNSDKLENEGsvSSIDENE--LVDLDTLLDNDQPEKNESGNND-HATDKEnllesdA 158
|
170 180 190
....*....|....*....|....*....|
gi 568925788 4832 VEQGQEKINEQIDEREYDENEVDPYHGNQE 4861
Cdd:COG5644 159 SSSNDSESEESDSESEIESSDSDHDDENSD 188
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
4706-4953 |
7.39e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 43.19 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4706 DEEDLDSKPDTKGEDNAIEMSEDFDGKMHDGELEQEEDDEKSDSEDGDLDKQMGNLNGEEADKLDERLWGDDEEEDEDGD 4785
Cdd:COG5192 431 DDSDVSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFDESEGNLRWKEGLASKLAYSQSGKRGRNIQKIFYDESL 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4786 GR----AEETGPGVDEEDSELVAKDDSLDAGNLNK--NKKHQDEKEDSEPEDVEQGQEKIN--EQIDEREYDENEVDPYH 4857
Cdd:COG5192 511 SPeeciEEYKGESAKSSESDLVVQDEPEDFFDVSKvaNESISSNHEKLMESEFEELKKKWSslAQLKSRFQKDATLDSIE 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 4858 GNQEKLPEPEaldlpDDLKLDSEDKSGGEDTDNEEAEEENPLEIKEKTVDMEETDHEIEEPGAGQDEGESPHEPEEgpSE 4937
Cdd:COG5192 591 GEEELIQDDE-----KGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEELRGNFELEE--RG 663
|
250
....*....|....*.
gi 568925788 4938 DKENMDMDTGADDQDR 4953
Cdd:COG5192 664 DPEKKDVDWYTEEKRK 679
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
1733-1776 |
8.45e-03 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 42.21 E-value: 8.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568925788 1733 RLLRAAKLNKP--ILLEGSPGVGKTSLVAALAKASGNTLVRINLSE 1776
Cdd:COG0464 181 ELREEYGLPPPrgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSD 226
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
812-915 |
9.52e-03 |
|
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: 41.69 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568925788 812 FAFVEGTLAQAIkkgewILLDEINLAAPETLeclSGLLEgssgslVLLDR-----GDTEPLvRHPdFRLFACMNPATDVG 886
Cdd:COG0714 86 FEFRPGPLFANV-----LLADEINRAPPKTQ---SALLE------AMEERqvtipGGTYKL-PEP-FLVIATQNPIEQEG 149
|
90 100 110
....*....|....*....|....*....|
gi 568925788 887 KRNLPPGIRNRFT-ELYVEELESKEDLQIL 915
Cdd:COG0714 150 TYPLPEAQLDRFLlKLYIGYPDAEEEREIL 179
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
1742-1779 |
9.74e-03 |
|
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. 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: 410928 [Multi-domain] Cd Length: 166 Bit Score: 40.49 E-value: 9.74e-03
10 20 30
....*....|....*....|....*....|....*...
gi 568925788 1742 KPILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQTD 1779
Cdd:cd19520 36 KGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTD 73
|
|
| |
