|
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 ... |
5315-5585 |
1.16e-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: 434.86 E-value: 1.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5315 LSQQLCEQLRLLLEPTQAAKLRGDYRTGKRLNMRKIIPYIASQFRKDRIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5394
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5395 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFNDSSGSQILRLCKFQQRKTKIAQFLESVAIMFAAAQKlsQ 5474
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDART--Q 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5475 NTSPETAQLLLIVSDGRGLFLEGKDRVLaaVQAAQNANIFVIFVVLDNPNSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5554
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 1958779119 5555 FPFYIILRDVNALPETLSDALRQWFELVTAS 5585
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 ... |
913-1015 |
9.32e-42 |
|
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: 150.04 E-value: 9.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 913 DLHILIVDYLKGLSVSRSAVQGIVNFYTALRKESKTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGNIQRSLYEGFCLG 991
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 1958779119 992 FLTQLDRASHPVVQKLICQHIISG 1015
Cdd:pfam17865 81 FLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1383-1537 |
5.98e-29 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
:
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 114.70 E-value: 5.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1383 PVLLVGDTGCGKTTVCQLFS-ALSNQKLYSVNCHLNMETSDFLGGLrpvrqkpndkeEPDTRLFEWHDGPLVLAMKEDSF 1461
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDPGGASWVDGPLVRAAREGEI 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958779119 1462 FLLDEISLADDSVLERLNSVLEvEKCLVLAEKGSPESKdtevelltAGKHFRILATMNPgGDFGKKELSPALRNRF 1537
Cdd:pfam07728 70 AVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKA--------APDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1897-1995 |
3.56e-23 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 465540 Cd Length: 106 Bit Score: 97.37 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1897 DMEFIASTLFPaIDRNIVKKMVAFNNHIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1971
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....
gi 1958779119 1972 LIYGERMRTREDKEKVITVFKDVF 1995
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVL 103
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1077-1213 |
1.04e-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: 96.98 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1077 PVLIQGETSVGKTSLIRWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDTSGKlVFNEGVLIDAMRKGYWIVLDELNLAP 1155
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779119 1156 TDVLEALNRLLDDNRELLITETQEVVRAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 1213
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 ... |
1225-1326 |
6.14e-22 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 465540 Cd Length: 106 Bit Score: 93.91 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1225 ELETILHKRCSLPPSYCSKLVKVMLELQSYRRRSSVFA--GKQGFIALRDLFRWAERYRLAEQTEKDYDWLQHLANDGFM 1302
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 1958779119 1303 LLAGRVRKQEEADVIQEVLEKHFK 1326
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 ... |
481-602 |
1.50e-18 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 465540 Cd Length: 106 Bit Score: 83.89 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 481 DLREVLQNRYPSLLTATDHLLDIYieltgekhccpsigcdeapQEVSEAEGENRRVALEG--RELSLRDLLNWCNRVAHG 558
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVY-------------------SRLQELVSSSRSFGSSGspREFNLRDLLRWCRRLSSL 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958779119 559 F-DSTSSTALLNVFQEALDCFTAMLSEQTKKLKMAEIIGSKLNIS 602
Cdd:pfam17867 62 LpTLLSPTVREEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
326-454 |
7.25e-18 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 83.11 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 326 VLLEGPIGSGKTSLVEHLAAVTGRTKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATKGHWILLEDID 405
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958779119 406 YAPLDVVSVLIPLLENGELLIP-GQGDCLKVAPTFQLFATRRLLSCGGSW 454
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1745-1885 |
4.84e-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: 80.80 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1745 PILLEGSPGVGKTSLVAALAKA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWCDGPLLAALKAGHWVVLDELN 1823
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779119 1824 LASQSILEGLNACFDHRgEIYVPELGMSFQVQHEKTRIFGCQNPfrQGGGRKGLPKSFLNRF 1885
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4698-5249 |
2.40e-10 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
:
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 67.73 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4698 EDTFQKGQEKDKEDLDSKPDTKGEDSAVEMSEDfDGKMHDGELEQEDDEKSDSEDGDLDKQmgnlnGEEADKLDERLwgd 4777
Cdd:COG5271 422 EDASAGETEDESTDVTSAEDDIATDEEADSLAD-EEEEAEAELDTEEDTESAEEDADGDEA-----TDEDDASDDGD--- 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4778 deeedEDDDGKGEEAGPGMDEEDSELVAKDDNL--DAGNLNKNKKHQGEEEDSEPEDVEQGqekineqmDEREYDESEvD 4855
Cdd:COG5271 493 -----EEEAEEDAEAEADSDELTAEETSADDGAdtDAAADPEDSDEDALEDETEGEENAPG--------SDQDADETD-E 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4856 PYHGSQEQLPEPEALDLPDDLKLDSEDRSAgedtdneeaEEENPLEIKEKTVDmEEIDREVEEPDAAQSEGERppAPDEG 4935
Cdd:COG5271 559 PEATAEEDEPDEAEAETEDATENADADETE---------ESADESEEAEASED-EAAEEEEADDDEADADADG--AADEE 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4936 PGEGEESMDTGA-DDQDKDTAShaeeqeeeeegeegeeeeeeedRAATDGSGESGVSPvDKDLQPQKEEEEGEKSDAEEQ 5014
Cdd:COG5271 627 ETEEEAAEDEAAePETDASEAA----------------------DEDADAETEAEASA-DESEEEAEDESETSSEDAEED 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5015 VPEATERKEHDScgqtgvdnvqsaQAVELAGAAPEKEqgkeehgSGAADANQAEghesnfiarlSSQQHTNKNTQSFKRR 5094
Cdd:COG5271 684 ADAAAAEASDDE------------EETEEADEDAETA-------SEEADAEEAD----------TEADGTAEEAEEAAEE 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5095 PGQADNErsiGDPNEhvrkrlrtVDTDRKTEQEPAQPQAQvEDADTFEhiqqgsdayDAQTYDVASSEQQQTtkasgedq 5174
Cdd:COG5271 735 AESADEE---AASLP--------DEADAEEEAEEAEEAEE-DDADGLE---------EALEEEKADAEEAAT-------- 785
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958779119 5175 eeeekedilmDTEEELIRAEDTEQLKPEAVRSETATASGSSEMEVDMQTLKTKEDEDPRTTTSHQEIESERPERS 5249
Cdd:COG5271 786 ----------DEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDD 850
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
670-900 |
6.19e-09 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 57.69 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 670 PVLLVGETGTGKTSAVQHLAHAT-GQHLRVVNMNQQSDTADLLGGFKPvdhkliwlplretfeelfvqtfskkqnftflg 748
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 749 hiqtcyrqkrwhdllklmqhvqksaitkegkesqpglllkekweafglrlnhaqqqmkmteNALLFAFVEGTLAQAIKKG 828
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779119 829 EWILLDEINLAAPETLECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 900
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
2217-2303 |
4.70e-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: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 2217 GSFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPggvltiNERGMVDGSTCTVTPNPNFRLFLSMDPVHG-- 2294
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 1958779119 2295 -EISRAMRNR 2303
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 ... |
5315-5585 |
1.16e-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: 434.86 E-value: 1.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5315 LSQQLCEQLRLLLEPTQAAKLRGDYRTGKRLNMRKIIPYIASQFRKDRIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5394
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5395 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFNDSSGSQILRLCKFQQRKTKIAQFLESVAIMFAAAQKlsQ 5474
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDART--Q 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5475 NTSPETAQLLLIVSDGRGLFLEGKDRVLaaVQAAQNANIFVIFVVLDNPNSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5554
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 1958779119 5555 FPFYIILRDVNALPETLSDALRQWFELVTAS 5585
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 ... |
913-1015 |
9.32e-42 |
|
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: 150.04 E-value: 9.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 913 DLHILIVDYLKGLSVSRSAVQGIVNFYTALRKESKTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGNIQRSLYEGFCLG 991
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 1958779119 992 FLTQLDRASHPVVQKLICQHIISG 1015
Cdd:pfam17865 81 FLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1383-1537 |
5.98e-29 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 114.70 E-value: 5.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1383 PVLLVGDTGCGKTTVCQLFS-ALSNQKLYSVNCHLNMETSDFLGGLrpvrqkpndkeEPDTRLFEWHDGPLVLAMKEDSF 1461
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDPGGASWVDGPLVRAAREGEI 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958779119 1462 FLLDEISLADDSVLERLNSVLEvEKCLVLAEKGSPESKdtevelltAGKHFRILATMNPgGDFGKKELSPALRNRF 1537
Cdd:pfam07728 70 AVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKA--------APDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1897-1995 |
3.56e-23 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 97.37 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1897 DMEFIASTLFPaIDRNIVKKMVAFNNHIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1971
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....
gi 1958779119 1972 LIYGERMRTREDKEKVITVFKDVF 1995
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVL 103
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1077-1213 |
1.04e-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: 96.98 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1077 PVLIQGETSVGKTSLIRWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDTSGKlVFNEGVLIDAMRKGYWIVLDELNLAP 1155
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779119 1156 TDVLEALNRLLDDNRELLITETQEVVRAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 1213
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 ... |
1225-1326 |
6.14e-22 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 93.91 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1225 ELETILHKRCSLPPSYCSKLVKVMLELQSYRRRSSVFA--GKQGFIALRDLFRWAERYRLAEQTEKDYDWLQHLANDGFM 1302
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 1958779119 1303 LLAGRVRKQEEADVIQEVLEKHFK 1326
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 ... |
481-602 |
1.50e-18 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 83.89 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 481 DLREVLQNRYPSLLTATDHLLDIYieltgekhccpsigcdeapQEVSEAEGENRRVALEG--RELSLRDLLNWCNRVAHG 558
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVY-------------------SRLQELVSSSRSFGSSGspREFNLRDLLRWCRRLSSL 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958779119 559 F-DSTSSTALLNVFQEALDCFTAMLSEQTKKLKMAEIIGSKLNIS 602
Cdd:pfam17867 62 LpTLLSPTVREEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
326-454 |
7.25e-18 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 83.11 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 326 VLLEGPIGSGKTSLVEHLAAVTGRTKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATKGHWILLEDID 405
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958779119 406 YAPLDVVSVLIPLLENGELLIP-GQGDCLKVAPTFQLFATRRLLSCGGSW 454
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1745-1885 |
4.84e-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: 80.80 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1745 PILLEGSPGVGKTSLVAALAKA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWCDGPLLAALKAGHWVVLDELN 1823
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779119 1824 LASQSILEGLNACFDHRgEIYVPELGMSFQVQHEKTRIFGCQNPfrQGGGRKGLPKSFLNRF 1885
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4698-5249 |
2.40e-10 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 67.73 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4698 EDTFQKGQEKDKEDLDSKPDTKGEDSAVEMSEDfDGKMHDGELEQEDDEKSDSEDGDLDKQmgnlnGEEADKLDERLwgd 4777
Cdd:COG5271 422 EDASAGETEDESTDVTSAEDDIATDEEADSLAD-EEEEAEAELDTEEDTESAEEDADGDEA-----TDEDDASDDGD--- 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4778 deeedEDDDGKGEEAGPGMDEEDSELVAKDDNL--DAGNLNKNKKHQGEEEDSEPEDVEQGqekineqmDEREYDESEvD 4855
Cdd:COG5271 493 -----EEEAEEDAEAEADSDELTAEETSADDGAdtDAAADPEDSDEDALEDETEGEENAPG--------SDQDADETD-E 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4856 PYHGSQEQLPEPEALDLPDDLKLDSEDRSAgedtdneeaEEENPLEIKEKTVDmEEIDREVEEPDAAQSEGERppAPDEG 4935
Cdd:COG5271 559 PEATAEEDEPDEAEAETEDATENADADETE---------ESADESEEAEASED-EAAEEEEADDDEADADADG--AADEE 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4936 PGEGEESMDTGA-DDQDKDTAShaeeqeeeeegeegeeeeeeedRAATDGSGESGVSPvDKDLQPQKEEEEGEKSDAEEQ 5014
Cdd:COG5271 627 ETEEEAAEDEAAePETDASEAA----------------------DEDADAETEAEASA-DESEEEAEDESETSSEDAEED 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5015 VPEATERKEHDScgqtgvdnvqsaQAVELAGAAPEKEqgkeehgSGAADANQAEghesnfiarlSSQQHTNKNTQSFKRR 5094
Cdd:COG5271 684 ADAAAAEASDDE------------EETEEADEDAETA-------SEEADAEEAD----------TEADGTAEEAEEAAEE 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5095 PGQADNErsiGDPNEhvrkrlrtVDTDRKTEQEPAQPQAQvEDADTFEhiqqgsdayDAQTYDVASSEQQQTtkasgedq 5174
Cdd:COG5271 735 AESADEE---AASLP--------DEADAEEEAEEAEEAEE-DDADGLE---------EALEEEKADAEEAAT-------- 785
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958779119 5175 eeeekedilmDTEEELIRAEDTEQLKPEAVRSETATASGSSEMEVDMQTLKTKEDEDPRTTTSHQEIESERPERS 5249
Cdd:COG5271 786 ----------DEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDD 850
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1733-1885 |
1.13e-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: 63.26 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1733 AQRLLRAAKLNKPILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWCDGPLLAAlk 1812
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQ--QTGEFEFRPGPLFAN-- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779119 1813 aghwVVL-DELNLAS---QS-ILEGLNacfdhRGEIYVPelGMSFQVQHeKTRIFGCQNPFRQGGGRKgLPKSFLNRF 1885
Cdd:COG0714 97 ----VLLaDEINRAPpktQSaLLEAME-----ERQVTIP--GGTYKLPE-PFLVIATQNPIEQEGTYP-LPEAQLDRF 161
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1077-1233 |
2.24e-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: 62.11 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1077 PVLIQGETSVGKTSLIRWLAAATGNHCVRINNHEHTDIQEyiGCYTSDT---SGKLVFNEG------VLIdamrkgywiv 1147
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSD--ILGTYIYdqqTGEFEFRPGplfanvLLA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1148 lDELNLAPTDVLEALNRLLDDNRellITETQEVVRAHPRFMLFATQNPPGLYGGRkVLSRAFRNRF-VELHFDeLPSSEL 1226
Cdd:COG0714 101 -DEINRAPPKTQSALLEAMEERQ---VTIPGGTYKLPEPFLVIATQNPIEQEGTY-PLPEAQLDRFlLKLYIG-YPDAEE 174
|
....*...
gi 1958779119 1227 ET-ILHKR 1233
Cdd:COG0714 175 EReILRRH 182
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
670-900 |
6.19e-09 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 57.69 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 670 PVLLVGETGTGKTSAVQHLAHAT-GQHLRVVNMNQQSDTADLLGGFKPvdhkliwlplretfeelfvqtfskkqnftflg 748
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 749 hiqtcyrqkrwhdllklmqhvqksaitkegkesqpglllkekweafglrlnhaqqqmkmteNALLFAFVEGTLAQAIKKG 828
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779119 829 EWILLDEINLAAPETLECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 900
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2217-2303 |
4.70e-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: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 2217 GSFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPggvltiNERGMVDGSTCTVTPNPNFRLFLSMDPVHG-- 2294
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 1958779119 2295 -EISRAMRNR 2303
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1381-1537 |
3.90e-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: 52.76 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1381 GEPVLLVGDTGCGKTTVCQLFSALSNQKLYSVnCHLNMETSdFLGGLRPVRQKPNDKEEPDTRLFEWHDGPLVLAMKED- 1459
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-IYIDGEDI-LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKp 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779119 1460 SFFLLDEISLADDSVLERLNSVLEVEKclvlaekgspeskdtEVELLTAGKHFRILATMNPGGDFGKKELSPALRNRF 1537
Cdd:smart00382 80 DVLILDEITSLLDAEQEALLLLLEELR---------------LLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1734-1893 |
8.08e-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: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1734 QRLLRAAKLN--KPILLEGSPGVGKTSLVAALAKAS---GNTLVRINLSeqtditDLFGADlpVEGGKGGEFAWCDGPLL 1808
Cdd:cd00009 8 EALREALELPppKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1809 AALKAGHWVVLDELNLASQSILEGLNACFdhrgeiyvpELGMSFQVQHEKTRIFG-CQNPFRQgggrkGLPKSFLNRFTQ 1887
Cdd:cd00009 80 AEKAKPGVLFIDEIDSLSRGAQNALLRVL---------ETLNDLRIDRENVRVIGaTNRPLLG-----DLDRALYDRLDI 145
|
....*.
gi 1958779119 1888 VFVDPL 1893
Cdd:cd00009 146 RIVIPL 151
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1370-1606 |
1.15e-06 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 54.02 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1370 LAVLVGRalefgePVLLVGDTGCGKTTVCQLFSALSNQKLYSVNCHLNMETSDFLGglrpvRQKPNdkeePDTRLFEWHD 1449
Cdd:COG0714 26 IALLAGG------HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILG-----TYIYD----QQTGEFEFRP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1450 GPlVLAmkedSFFLLDEISLADDSVLerlNSVLEVekclvLAEKgspeskdtEV----ELLTAGKHFRILATMNPGGDFG 1525
Cdd:COG0714 91 GP-LFA----NVLLADEINRAPPKTQ---SALLEA-----MEER--------QVtipgGTYKLPEPFLVIATQNPIEQEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1526 KKELSPALRNRFT-EIWC--PQstkREDLVQIIN-------HNLRPGLS---------LARAGHKGADIAEVMLDFITWL 1586
Cdd:COG0714 150 TYPLPEAQLDRFLlKLYIgyPD---AEEEREILRrhtgrhlAEVEPVLSpeellalqeLVRQVHVSEAVLDYIVDLVRAT 226
|
250 260
....*....|....*....|.
gi 1958779119 1587 -THQEFGRKcvVSIRDILSWV 1606
Cdd:COG0714 227 rEHPDLRKG--PSPRASIALL 245
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1014-1315 |
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 1958779119 1014 SGNVKSLLKQPIPEPKGGRLIQVEGYWISVGDKEPKIDETYVLTPSVKLNLRDIARVVSAGTYP--VLIQGETSVGKTSL 1091
Cdd:COG1401 158 LEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKTKknVILAGPPGTGKTYL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1092 IRWLAAATG---NHCVRI-----NNHEHTDIQEYigcYTSDTSGKLVFNEGVLIDAMRKG-------YWIVLDELNLAPT 1156
Cdd:COG1401 238 ARRLAEALGgedNGRIEFvqfhpSWSYEDFLLGY---RPSLDEGKYEPTPGIFLRFCLKAeknpdkpYVLIIDEINRANV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1157 D--------VLEALNRLLDDNRELLITETQEVVRAHPRFMLFATQNPP--GLYGGRKVLSRAFRNRFVELHFDELPSSEL 1226
Cdd:COG1401 315 EkyfgellsLLESDKRGEELSIELPYSGEGEEFSIPPNLYIIGTMNTDdrSLALSDKALRRRFTFEFLDPDLDKLSNEEV 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1227 ETILHKrcslppsycsklVKVMLELQSYRRRSSVFAGKQGFIALRDLFRWAERYRLAEQTEKDYDWLQHLANDGFMLLAG 1306
Cdd:COG1401 395 VDLLEE------------LNEILEKRDFQIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLLDKLDLLGMAEFEDRLE 462
|
....*....
gi 1958779119 1307 RVRKQEEAD 1315
Cdd:COG1401 463 LSEYLPLLL 471
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4825-5245 |
3.77e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4825 EEDSEPEDVEQGQEKINEQMDEREYDESEVDPYHGSQEQLPEPEALDLPDDLKLDSEDRSAGEDTDNEEAEEENPLEIKE 4904
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4905 KTVDMEEIDREVEEPDAAQSEGERPPAPDEGPGEGEESMDTGADDQDKDTASHAEEQEEEEEGEEGEEEEEEEDRAATDG 4984
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK 1498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4985 SGES-GVSPVDKDLQPQKEEEEGEKSD----AEE-----QVPEATERKEHDSCGQTgvDNVQSAQAVELAGAAPEKEQGK 5054
Cdd:PTZ00121 1499 ADEAkKAAEAKKKADEAKKAEEAKKADeakkAEEakkadEAKKAEEKKKADELKKA--EELKKAEEKKKAEEAKKAEEDK 1576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5055 EEHGSGAADANQAEGHESNFIARLSSQQHTNKNTQSFKRRPGQADNERSigDPNEHVRKRlrtVDTDRKTEQEPAQPQAQ 5134
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL--KKAEEEKKK---VEQLKKKEAEEKKKAEE 1651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5135 VEDADTFEHIQQGSDAYDAQtydvasSEQQQTTKASGEDQEEEEKEDILMDTEEELIRAEDTEQLKPEAVRSETATASGS 5214
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAE------EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
410 420 430
....*....|....*....|....*....|.
gi 1958779119 5215 SEMEVDMQTLKTKEDEDPRTTTSHQEIESER 5245
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1383-1540 |
8.03e-05 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 45.99 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1383 PVLLVGDTGCGKTTVCQLF---SALSNQKLYSVNCHLNMEtsdflgglrpvrqkpNDKEEPDTRLFEWHDGPLVLAMKED 1459
Cdd:cd00009 21 NLLLYGPPGTGKTTLARAIaneLFRPGAPFLYLNASDLLE---------------GLVVAELFGHFLVRLLFELAEKAKP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1460 SFFLLDEISLADDSVLERLNSVLEvekclvlaekgspeskdTEVELLTAGKHFRILATMNPGGDFgkkELSPALRNRFTE 1539
Cdd:cd00009 86 GVLFIDEIDSLSRGAQNALLRVLE-----------------TLNDLRIDRENVRVIGATNRPLLG---DLDRALYDRLDI 145
|
.
gi 1958779119 1540 I 1540
Cdd:cd00009 146 R 146
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1050-1219 |
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 1958779119 1050 IDETYVLT-PSVKLNLRDIARVVSAGTyPVLIQGETSVGKTSLIRWLAAAtgnhcVRINNHEHTDI-QEYIGCYTSDTSG 1127
Cdd:PHA02244 94 IDTTKIASnPTFHYETADIAKIVNANI-PVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAImDEFELKGFIDANG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1128 KlvFNEGVLIDAMRKGYWIVLDELNLAPTDVLEALNRLLDDNRELLITETqevVRAHPRFMLFATQNPPG-----LYGGR 1202
Cdd:PHA02244 168 K--FHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVAR 242
|
170
....*....|....*..
gi 1958779119 1203 KVLSRAFRNRFVELHFD 1219
Cdd:PHA02244 243 NKIDGATLDRFAPIEFD 259
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5377-5523 |
1.44e-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: 45.91 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5377 ICLAIDDSSSMVDNhTKQLAFESLAVIGNALTLLEVG-QIAVCSFGESVKLLHPFHeqfNDSSGSQILRLCKFQQRK--- 5452
Cdd:smart00327 2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgg 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779119 5453 -TKIAQFLESVAIMFAAAqklSQNTSPETAQLLLIVSDGRGLFLEGKDRVLAAVQAAQNANIFVIFVVLDNP 5523
Cdd:smart00327 78 gTNLGAALQYALENLFSK---SAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVD 146
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1744-1779 |
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 1958779119 1744 KPILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQ 1779
Cdd:PRK04195 40 KALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1383-1559 |
9.81e-04 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 45.11 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1383 PVLLVGDTGCGKTTVCQLFSALSNQKLYSvnchLNMETSDF-LGGLRPVRQKpndkeepdtrlfeWHDGPLVLAMKEDSF 1461
Cdd:PHA02244 121 PVFLKGGAGSGKNHIAEQIAEALDLDFYF----MNAIMDEFeLKGFIDANGK-------------FHETPFYEAFKKGGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1462 FLLDEISLADDSVLERLNSVLevekclvlaekgSPESKDTEVELLTAGKHFRILA---TMNPGGD---FGKKELSPALRN 1535
Cdd:PHA02244 184 FFIDEIDASIPEALIIINSAI------------ANKFFDFADERVTAHEDFRVISagnTLGKGADhiyVARNKIDGATLD 251
|
170 180
....*....|....*....|....
gi 1958779119 1536 RFTEIWCPQSTKREDLVQIINHNL 1559
Cdd:PHA02244 252 RFAPIEFDYDEKIEHLISNGDEDL 275
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
317-433 |
1.55e-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: 42.52 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 317 AVAVASQNAVLLEGPIGSGKTSLVEHLAAVTGRTKPPqLLKVQLGDqtdskMLLGMYRCTDVpGEFVWQPGTLTQAATKG 396
Cdd:cd00009 13 ALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNASD-----LLEGLVVAELF-GHFLVRLLFELAEKAKP 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958779119 397 HWILLEDIDYAPLDVVSVLIPLLENGELLIPGQGDCL 433
Cdd:cd00009 86 GVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVR 122
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1077-1219 |
1.60e-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: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1077 PVLIQGETSVGKTSLIR---WLAAATGNHCVRIN----NHEHTDIQEYIGCYTSDTSGKLVFNEGVLIDAMRKGYW--IV 1147
Cdd:smart00382 4 VILIVGPPGSGKTTLARalaRELGPPGGGVIYIDgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779119 1148 LDELNLAPTDVLEALNRLLDDNRELLITETQEVVRAhprfmLFATQNPPGLygGRKVLSRAFRNRFVELHFD 1219
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV-----ILTTNDEKDL--GPALLRRRFDRRIVLLLIL 148
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
4692-4942 |
3.23e-03 |
|
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) or RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II.
Pssm-ID: 310411 [Multi-domain] Cd Length: 528 Bit Score: 43.78 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4692 ENEEQVEDTFQKGQEK-----DKEDLDSKPDTKGEDSAVEMSEDFDGKMHDGELEQE-DDEKSDSEDGD--LDKQMGNLN 4763
Cdd:pfam05793 168 ERRKKTANGFSLMMMKaakngPAAFGEHDEETEGEKGGGGRGKDLKIKDLEGDDEDDgDESDKGGEDGDeeKKKKKKKKL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4764 GEEADKLDERlwgDDEEEDEDDDGKGEEAGPGmDEEDSELVAKDDNLDAGNlnknkKHQGEEEDSEPEDVEQGQEKINEQ 4843
Cdd:pfam05793 248 AKNKKKLDDD---KKKKRGGDDDAFEYDSDDG-DDEGREEDYISDSSASGN-----DPEEREDKLSPEEPAKGEIEQSDD 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4844 MDEREYDESEvdpyHGSQEQLPEPEALDLPDDLKLDSEDRSAgedtdneeaeeenpleiKEKTVDMEEIDREVEEPDAAQ 4923
Cdd:pfam05793 319 SEESEEEKNE----EEGKLSKKGKKAKKLKGKKNGKDKSESS-----------------DGDDSDDSDIDDEDSVPLFTA 377
|
250
....*....|....*....
gi 1958779119 4924 SEgERPPAPDEGPGEGEES 4942
Cdd:pfam05793 378 KK-KKEPKKEEPVDSGPSS 395
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1077-1213 |
4.58e-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: 40.98 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1077 PVLIQGETSVGKTSLIR---WLAAATGNHCVRINNHEHTDIQEYIGCYTSDTSGKLVFnegvlIDAMRKGYWIVLDELNL 1153
Cdd:cd00009 21 NLLLYGPPGTGKTTLARaiaNELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFE-----LAEKAKPGVLFIDEIDS 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1154 APTDVLEALNRLLDDnRELLITETQEVvrahpRFMLFATQNPPGLyggrkvLSRAFRNRF 1213
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 ... |
657-712 |
6.19e-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: 42.46 E-value: 6.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779119 657 LLEQLAVCVSQGEPVLLVGETGTGKTSAVQHLAHATGQHLRVVNMNqqSDT--ADLLG 712
Cdd:COG0714 20 LIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFT--PDLlpSDILG 75
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4826-5071 |
7.45e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.06 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4826 EDSEPEDVEQGQ---EKINEQMDEREYDESEVDPYHGSQEQLPEpealdlpdDLKLDSEDRSAGEDTDNEEAEEENPLEI 4902
Cdd:TIGR00927 628 GDLSKGDVAEAEhtgERTGEEGERPTEAEGENGEESGGEAEQEG--------ETETKGENESEGEIPAERKGEQEGEGEI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4903 KEKTVDM--EEIDREVEEPDAAQSEGERPPAPDEGPGEGEESMDTGADDQDKDTASHAEEQEEEEEGEEGEEEEEEEDRA 4980
Cdd:TIGR00927 700 EAKEADHkgETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDED 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4981 ATDGSGESGVSPVDKDLQPQKEEEEGEKSDAEEQVPEATERKEHDSCGQTGVDNVQSAQAvELAGAAPEKEQGKEehGSG 5060
Cdd:TIGR00927 780 EGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNA-ENQGEAKQDEKGVD--GGG 856
|
250
....*....|.
gi 1958779119 5061 AADANQAEGHE 5071
Cdd:TIGR00927 857 GSDGGDSEEEE 867
|
|
| |
|
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 ... |
5315-5585 |
1.16e-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: 434.86 E-value: 1.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5315 LSQQLCEQLRLLLEPTQAAKLRGDYRTGKRLNMRKIIPYIASQFRKDRIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5394
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5395 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFNDSSGSQILRLCKFQQRKTKIAQFLESVAIMFAAAQKlsQ 5474
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDART--Q 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5475 NTSPETAQLLLIVSDGRGLFLEGKDRVLaaVQAAQNANIFVIFVVLDNPNSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5554
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 1958779119 5555 FPFYIILRDVNALPETLSDALRQWFELVTAS 5585
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 ... |
913-1015 |
9.32e-42 |
|
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: 150.04 E-value: 9.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 913 DLHILIVDYLKGLSVSRSAVQGIVNFYTALRKESKTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGNIQRSLYEGFCLG 991
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 1958779119 992 FLTQLDRASHPVVQKLICQHIISG 1015
Cdd:pfam17865 81 FLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1383-1537 |
5.98e-29 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 114.70 E-value: 5.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1383 PVLLVGDTGCGKTTVCQLFS-ALSNQKLYSVNCHLNMETSDFLGGLrpvrqkpndkeEPDTRLFEWHDGPLVLAMKEDSF 1461
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDPGGASWVDGPLVRAAREGEI 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958779119 1462 FLLDEISLADDSVLERLNSVLEvEKCLVLAEKGSPESKdtevelltAGKHFRILATMNPgGDFGKKELSPALRNRF 1537
Cdd:pfam07728 70 AVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKA--------APDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1897-1995 |
3.56e-23 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 97.37 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1897 DMEFIASTLFPaIDRNIVKKMVAFNNHIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1971
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....
gi 1958779119 1972 LIYGERMRTREDKEKVITVFKDVF 1995
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVL 103
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1077-1213 |
1.04e-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: 96.98 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1077 PVLIQGETSVGKTSLIRWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDTSGKlVFNEGVLIDAMRKGYWIVLDELNLAP 1155
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779119 1156 TDVLEALNRLLDDNRELLITETQEVVRAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 1213
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 ... |
1225-1326 |
6.14e-22 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 93.91 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1225 ELETILHKRCSLPPSYCSKLVKVMLELQSYRRRSSVFA--GKQGFIALRDLFRWAERYRLAEQTEKDYDWLQHLANDGFM 1302
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 1958779119 1303 LLAGRVRKQEEADVIQEVLEKHFK 1326
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 ... |
481-602 |
1.50e-18 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 83.89 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 481 DLREVLQNRYPSLLTATDHLLDIYieltgekhccpsigcdeapQEVSEAEGENRRVALEG--RELSLRDLLNWCNRVAHG 558
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVY-------------------SRLQELVSSSRSFGSSGspREFNLRDLLRWCRRLSSL 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958779119 559 F-DSTSSTALLNVFQEALDCFTAMLSEQTKKLKMAEIIGSKLNIS 602
Cdd:pfam17867 62 LpTLLSPTVREEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
326-454 |
7.25e-18 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 83.11 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 326 VLLEGPIGSGKTSLVEHLAAVTGRTKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATKGHWILLEDID 405
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958779119 406 YAPLDVVSVLIPLLENGELLIP-GQGDCLKVAPTFQLFATRRLLSCGGSW 454
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1745-1885 |
4.84e-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: 80.80 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1745 PILLEGSPGVGKTSLVAALAKA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWCDGPLLAALKAGHWVVLDELN 1823
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779119 1824 LASQSILEGLNACFDHRgEIYVPELGMSFQVQHEKTRIFGCQNPfrQGGGRKGLPKSFLNRF 1885
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4698-5249 |
2.40e-10 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 67.73 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4698 EDTFQKGQEKDKEDLDSKPDTKGEDSAVEMSEDfDGKMHDGELEQEDDEKSDSEDGDLDKQmgnlnGEEADKLDERLwgd 4777
Cdd:COG5271 422 EDASAGETEDESTDVTSAEDDIATDEEADSLAD-EEEEAEAELDTEEDTESAEEDADGDEA-----TDEDDASDDGD--- 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4778 deeedEDDDGKGEEAGPGMDEEDSELVAKDDNL--DAGNLNKNKKHQGEEEDSEPEDVEQGqekineqmDEREYDESEvD 4855
Cdd:COG5271 493 -----EEEAEEDAEAEADSDELTAEETSADDGAdtDAAADPEDSDEDALEDETEGEENAPG--------SDQDADETD-E 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4856 PYHGSQEQLPEPEALDLPDDLKLDSEDRSAgedtdneeaEEENPLEIKEKTVDmEEIDREVEEPDAAQSEGERppAPDEG 4935
Cdd:COG5271 559 PEATAEEDEPDEAEAETEDATENADADETE---------ESADESEEAEASED-EAAEEEEADDDEADADADG--AADEE 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4936 PGEGEESMDTGA-DDQDKDTAShaeeqeeeeegeegeeeeeeedRAATDGSGESGVSPvDKDLQPQKEEEEGEKSDAEEQ 5014
Cdd:COG5271 627 ETEEEAAEDEAAePETDASEAA----------------------DEDADAETEAEASA-DESEEEAEDESETSSEDAEED 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5015 VPEATERKEHDScgqtgvdnvqsaQAVELAGAAPEKEqgkeehgSGAADANQAEghesnfiarlSSQQHTNKNTQSFKRR 5094
Cdd:COG5271 684 ADAAAAEASDDE------------EETEEADEDAETA-------SEEADAEEAD----------TEADGTAEEAEEAAEE 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5095 PGQADNErsiGDPNEhvrkrlrtVDTDRKTEQEPAQPQAQvEDADTFEhiqqgsdayDAQTYDVASSEQQQTtkasgedq 5174
Cdd:COG5271 735 AESADEE---AASLP--------DEADAEEEAEEAEEAEE-DDADGLE---------EALEEEKADAEEAAT-------- 785
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958779119 5175 eeeekedilmDTEEELIRAEDTEQLKPEAVRSETATASGSSEMEVDMQTLKTKEDEDPRTTTSHQEIESERPERS 5249
Cdd:COG5271 786 ----------DEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDD 850
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1733-1885 |
1.13e-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: 63.26 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1733 AQRLLRAAKLNKPILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWCDGPLLAAlk 1812
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQ--QTGEFEFRPGPLFAN-- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779119 1813 aghwVVL-DELNLAS---QS-ILEGLNacfdhRGEIYVPelGMSFQVQHeKTRIFGCQNPFRQGGGRKgLPKSFLNRF 1885
Cdd:COG0714 97 ----VLLaDEINRAPpktQSaLLEAME-----ERQVTIP--GGTYKLPE-PFLVIATQNPIEQEGTYP-LPEAQLDRF 161
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1077-1233 |
2.24e-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: 62.11 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1077 PVLIQGETSVGKTSLIRWLAAATGNHCVRINNHEHTDIQEyiGCYTSDT---SGKLVFNEG------VLIdamrkgywiv 1147
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSD--ILGTYIYdqqTGEFEFRPGplfanvLLA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1148 lDELNLAPTDVLEALNRLLDDNRellITETQEVVRAHPRFMLFATQNPPGLYGGRkVLSRAFRNRF-VELHFDeLPSSEL 1226
Cdd:COG0714 101 -DEINRAPPKTQSALLEAMEERQ---VTIPGGTYKLPEPFLVIATQNPIEQEGTY-PLPEAQLDRFlLKLYIG-YPDAEE 174
|
....*...
gi 1958779119 1227 ET-ILHKR 1233
Cdd:COG0714 175 EReILRRH 182
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4684-5231 |
5.58e-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: 63.11 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4684 VKDVSDRIENEEQVEDTFQKG---QEKDKEDLDSKPDTKGEDSAvEMSEDFDGkmhDGELEQEDDEKSDSEDGDLDKQMG 4760
Cdd:COG5271 502 AEADSDELTAEETSADDGADTdaaADPEDSDEDALEDETEGEEN-APGSDQDA---DETDEPEATAEEDEPDEAEAETED 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4761 NLNGEEADKlderlwgddeeeDEDDDGKGEEAGPGMDEEDSELVAKDDNLDAgnlnknkkhqgeEEDSEPEDVEQGQEki 4840
Cdd:COG5271 578 ATENADADE------------TEESADESEEAEASEDEAAEEEEADDDEADA------------DADGAADEEETEEE-- 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4841 nEQMDEREYDESEVDPYH-----GSQEQLPEPEALDLPDDLKLDSEDRSAGEDTDNEEAEEENPLEIKEKTVDMEEIDRE 4915
Cdd:COG5271 632 -AAEDEAAEPETDASEAAdedadAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASE 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4916 VEEPDAAQSEGERPPAPDEGPGEGEESMDTGADDQ----DKDTASHAEEQEEEE----EGEEGEEEEEEEDRAATDGSGE 4987
Cdd:COG5271 711 EADAEEADTEADGTAEEAEEAAEEAESADEEAASLpdeaDAEEEAEEAEEAEEDdadgLEEALEEEKADAEEAATDEEAE 790
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4988 sgvsPVDKDLQPQKEEEEGEKSDAEEQVPEATERKEHDSCGQTGVDNVQSAQAVELAGAAPEKEQGKEEHGSGAADANQa 5067
Cdd:COG5271 791 ----AAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLD- 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5068 EGHESNFIARLSSQQHTNkntqsfkrrPGQADNERSIGDPNEHVRKRLRTVDTDRKTEQEPAQPQAQVEDADTFEHIQQG 5147
Cdd:COG5271 866 ADLAADEHEAEEAQEAET---------DADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAE 936
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5148 SD-----AYDAQTYDVAS---SEQQQTTKASGEDQEEEEKEDILMDTEEELIRAEDTEQLKPEAVRSETATASGSSEMEV 5219
Cdd:COG5271 937 EDelgaaEDDLDALALDEagdEESDDAAADDAGDDSLADDDEALADAADDAEADDSELDASESTGEAEGDEDDDELEDGE 1016
|
570
....*....|..
gi 1958779119 5220 DMQTLKTKEDED 5231
Cdd:COG5271 1017 AAAGEATADLAA 1028
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
670-900 |
6.19e-09 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 57.69 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 670 PVLLVGETGTGKTSAVQHLAHAT-GQHLRVVNMNQQSDTADLLGGFKPvdhkliwlplretfeelfvqtfskkqnftflg 748
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 749 hiqtcyrqkrwhdllklmqhvqksaitkegkesqpglllkekweafglrlnhaqqqmkmteNALLFAFVEGTLAQAIKKG 828
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779119 829 EWILLDEINLAAPETLECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 900
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2217-2303 |
4.70e-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: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 2217 GSFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPggvltiNERGMVDGSTCTVTPNPNFRLFLSMDPVHG-- 2294
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 1958779119 2295 -EISRAMRNR 2303
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4692-5235 |
7.30e-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: 59.64 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4692 ENEEQVEDTFQKGQEKDKEDLDSKPDTKGEDSAVEMSEDFDGKMHDGELEQEDDEKSDSEDGDLDKQMGNLNGEEADKLD 4771
Cdd:COG5271 381 TDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4772 ERLWGDDEEEDEDDDGKGEEAGPGMDEEDSELVAKD----------DNLDAGNLNKNKKHQGEEEDSEPEDVEQGQE-KI 4840
Cdd:COG5271 461 AELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAeedaeaeadsDELTAEETSADDGADTDAAADPEDSDEDALEdET 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4841 NEQMDEREYDES---EVDPYHGSQEQLPEPEALDLPDDLKLDSEDRSAgedtdneeaEEENPLEIKEKTVDmEEIDREVE 4917
Cdd:COG5271 541 EGEENAPGSDQDadeTDEPEATAEEDEPDEAEAETEDATENADADETE---------ESADESEEAEASED-EAAEEEEA 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4918 EPDAAQSEGERppAPDEGPGEGEESMDTGA-DDQDKDTAShaeeqeeeeegeegeeeeeeedRAATDGSGESGVSPvDKD 4996
Cdd:COG5271 611 DDDEADADADG--AADEEETEEEAAEDEAAePETDASEAA----------------------DEDADAETEAEASA-DES 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4997 LQPQKEEEEGEKSDAEEQVPEATERKEHDSCGQTGVDNVQSAQAVELAGAAPEKEQ-GKEEHGSGAADANQAEGHESNFI 5075
Cdd:COG5271 666 EEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADAEEADTEAdGTAEEAEEAAEEAESADEEAASL 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5076 ARLSSQQHTNKNTQSfkRRPGQADNERSiGDPNEHVRKRLRTVDTDRKTEQEPAQPQA---QVEDADTFEHIQQGSDAYD 5152
Cdd:COG5271 746 PDEADAEEEAEEAEE--AEEDDADGLEE-ALEEEKADAEEAATDEEAEAAAEEKEKVAdedQDTDEDALLDEAEADEEED 822
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5153 AQTYDVASSEQQQTTKASGEDQEEEEKEDILMDTEEELIRAEDTEQLKPEAVRSETATASGSSEMEVDMQTLKTKEDEDP 5232
Cdd:COG5271 823 LDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSA 902
|
...
gi 1958779119 5233 RTT 5235
Cdd:COG5271 903 AAE 905
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4685-5247 |
1.01e-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: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4685 KDVSDRIENEEQVEDTFQKGQEKDKEDLDSKPDTKGEDSAVEMSEDFDGKMHDGELEQ--EDDEKSDSEDGDLDKQMGNL 4762
Cdd:COG5271 133 DPLATDTLGGGDLDLATKDGDELLPSLADNDEAAADEGDELAADGDDTLAVADAIEATpgGTDAVELTATLGATVTTDPG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4763 NGEEADKLDERLWGDDEEEDEDDDGKGEEAGPGMDEEDSELvakDDNLDAGNLNKNKKHQGEEEDSEP----EDVEQGQE 4838
Cdd:COG5271 213 DSVAADDDLAAEEGASAVVEEEDASEDAVAAADETLLADDD---DTESAGATAEVGGTPDTDDEATDDadglEAAEDDAL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4839 KINEQMDEREYDESEVDPYH-GSQEQLPEPEALDLPDDLKLDSEDRSAgedtdneeaeeenPLEIKEKTVDMEEIDREVE 4917
Cdd:COG5271 290 DAELTAAQAADPESDDDADDsTLAALEGAAEDTEIATADELAAADDED-------------DDDSAAEDAAEEAATAEDS 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4918 epDAAQSEGERPPAPDEGPGEGEESMDTGADDQDKDTAShaeeqeeeeegeEGEEEEEEEDRAATDGSGESGVSPVDKDL 4997
Cdd:COG5271 357 --AAEDTQDAEDEAAGEAADESEGADTDAAADEADAAAD------------DSADDEEASADGGTSPTSDTDEEEEEADE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4998 QPQKEEEEGEKSDAEeqvpEATERKEHDSCGQTGVDNVQSAQAVELAGAAPEKEQGKEEhGSGAADANQAEGHESNFIAR 5077
Cdd:COG5271 423 DASAGETEDESTDVT----SAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDAD-GDEATDEDDASDDGDEEEAE 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5078 LSSQQHT---NKNTQSFKRRPGQADNERSIGDPNE--------HVRKRLRTVDTDRKTEQEPA--QPQAQVEDADTFEHI 5144
Cdd:COG5271 498 EDAEAEAdsdELTAEETSADDGADTDAAADPEDSDedaledetEGEENAPGSDQDADETDEPEatAEEDEPDEAEAETED 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5145 QQGSDAYDAQTYDVASSEQQQTTKASGEDQEEEEKEDILMDTEEELIRAEDTEQLKPEAVRSETATASGSSEMEVDMQTL 5224
Cdd:COG5271 578 ATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETE 657
|
570 580
....*....|....*....|....
gi 1958779119 5225 -KTKEDEDPRTTTSHQEIESERPE 5247
Cdd:COG5271 658 aEASADESEEEAEDESETSSEDAE 681
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4708-5251 |
1.82e-07 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 58.10 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4708 DKEDLDSKPDTKGEDSAVEMSEDFDGKMHDGELEQEDDEKSDSEDGDLDKQMGNLNGEE--ADKLDERLWGDDEEEDEDD 4785
Cdd:COG5271 221 LAAEEGASAVVEEEDASEDAVAAADETLLADDDDTESAGATAEVGGTPDTDDEATDDADglEAAEDDALDAELTAAQAAD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4786 DGKGEEAGPGMDEEDSELVAKDDNLDAGNLNKNKKHQGEEEDSEPEDVEQGQEKINeqMDEREYDESEVDPYHGSQEQLP 4865
Cdd:COG5271 301 PESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDS--AAEDTQDAEDEAAGEAADESEG 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4866 EPEALDLPDDLKLDSEDRSAGEDTDNEEAEEENPLEIKEKTVD--MEEIDREVEEPDAAQSEGERP------PAPDEGP- 4936
Cdd:COG5271 379 ADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADedASAGETEDESTDVTSAEDDIAtdeeadSLADEEEe 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4937 ----GEGEESMDTGADDQDKDTAShaeeqEEEEEGEEGEEEEEEEDRAATDGSGESGVSPVDKDLQPQKEEEEGEKSDAE 5012
Cdd:COG5271 459 aeaeLDTEEDTESAEEDADGDEAT-----DEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5013 EQVPEATERKEHDSCGQTGVDNVQSAQA------VELAGAAPEKEQGKEEHGSGAADANQAEGHESNFIARLSSQQHTNK 5086
Cdd:COG5271 534 DALEDETEGEENAPGSDQDADETDEPEAtaeedePDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDD 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5087 NTqsfkrrpgQADNERSIGDPNEHVrkrlrTVDTDRKTEQEPAQPQAQVEDADTF--------EHIQQGSDAYDAQTyDV 5158
Cdd:COG5271 614 EA--------DADADGAADEEETEE-----EAAEDEAAEPETDASEAADEDADAEteaeasadESEEEAEDESETSS-ED 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5159 ASSEQQQTTKASGE--DQEEEEKEDILMDTEEELIRAEDTEQlkPEAVRSETATASGSSEMEVDMQTLKTKEDEDPRTTT 5236
Cdd:COG5271 680 AEEDADAAAAEASDdeEETEEADEDAETASEEADAEEADTEA--DGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEE 757
|
570
....*....|....*
gi 1958779119 5237 SHQEIESERPERSRE 5251
Cdd:COG5271 758 AEEAEEDDADGLEEA 772
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1381-1537 |
3.90e-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: 52.76 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1381 GEPVLLVGDTGCGKTTVCQLFSALSNQKLYSVnCHLNMETSdFLGGLRPVRQKPNDKEEPDTRLFEWHDGPLVLAMKED- 1459
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-IYIDGEDI-LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKp 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779119 1460 SFFLLDEISLADDSVLERLNSVLEVEKclvlaekgspeskdtEVELLTAGKHFRILATMNPGGDFGKKELSPALRNRF 1537
Cdd:smart00382 80 DVLILDEITSLLDAEQEALLLLLEELR---------------LLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1734-1893 |
8.08e-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: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1734 QRLLRAAKLN--KPILLEGSPGVGKTSLVAALAKAS---GNTLVRINLSeqtditDLFGADlpVEGGKGGEFAWCDGPLL 1808
Cdd:cd00009 8 EALREALELPppKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1809 AALKAGHWVVLDELNLASQSILEGLNACFdhrgeiyvpELGMSFQVQHEKTRIFG-CQNPFRQgggrkGLPKSFLNRFTQ 1887
Cdd:cd00009 80 AEKAKPGVLFIDEIDSLSRGAQNALLRVL---------ETLNDLRIDRENVRVIGaTNRPLLG-----DLDRALYDRLDI 145
|
....*.
gi 1958779119 1888 VFVDPL 1893
Cdd:cd00009 146 RIVIPL 151
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1370-1606 |
1.15e-06 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 54.02 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1370 LAVLVGRalefgePVLLVGDTGCGKTTVCQLFSALSNQKLYSVNCHLNMETSDFLGglrpvRQKPNdkeePDTRLFEWHD 1449
Cdd:COG0714 26 IALLAGG------HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILG-----TYIYD----QQTGEFEFRP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1450 GPlVLAmkedSFFLLDEISLADDSVLerlNSVLEVekclvLAEKgspeskdtEV----ELLTAGKHFRILATMNPGGDFG 1525
Cdd:COG0714 91 GP-LFA----NVLLADEINRAPPKTQ---SALLEA-----MEER--------QVtipgGTYKLPEPFLVIATQNPIEQEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1526 KKELSPALRNRFT-EIWC--PQstkREDLVQIIN-------HNLRPGLS---------LARAGHKGADIAEVMLDFITWL 1586
Cdd:COG0714 150 TYPLPEAQLDRFLlKLYIgyPD---AEEEREILRrhtgrhlAEVEPVLSpeellalqeLVRQVHVSEAVLDYIVDLVRAT 226
|
250 260
....*....|....*....|.
gi 1958779119 1587 -THQEFGRKcvVSIRDILSWV 1606
Cdd:COG0714 227 rEHPDLRKG--PSPRASIALL 245
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1746-1781 |
2.96e-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: 2.96e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1958779119 1746 ILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQTD 1781
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS 36
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
1746-1885 |
3.62e-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: 49.48 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1746 ILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWCDGPLLAALkaghwVVLDELNLA 1825
Cdd:pfam07726 2 VLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQ--KTREFEFRPGPVFANV-----LLADEINRA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779119 1826 S---QSILegLNACFDHR----GEIY-VPELGMsfqvqhektrIFGCQNPFRQGGGRKgLPKSFLNRF 1885
Cdd:pfam07726 75 PpktQSAL--LEAMQERQvtidGETHpLPEPFF----------VLATQNPIEQEGTYP-LPEAQLDRF 129
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1014-1315 |
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 1958779119 1014 SGNVKSLLKQPIPEPKGGRLIQVEGYWISVGDKEPKIDETYVLTPSVKLNLRDIARVVSAGTYP--VLIQGETSVGKTSL 1091
Cdd:COG1401 158 LEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKTKknVILAGPPGTGKTYL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1092 IRWLAAATG---NHCVRI-----NNHEHTDIQEYigcYTSDTSGKLVFNEGVLIDAMRKG-------YWIVLDELNLAPT 1156
Cdd:COG1401 238 ARRLAEALGgedNGRIEFvqfhpSWSYEDFLLGY---RPSLDEGKYEPTPGIFLRFCLKAeknpdkpYVLIIDEINRANV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1157 D--------VLEALNRLLDDNRELLITETQEVVRAHPRFMLFATQNPP--GLYGGRKVLSRAFRNRFVELHFDELPSSEL 1226
Cdd:COG1401 315 EkyfgellsLLESDKRGEELSIELPYSGEGEEFSIPPNLYIIGTMNTDdrSLALSDKALRRRFTFEFLDPDLDKLSNEEV 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1227 ETILHKrcslppsycsklVKVMLELQSYRRRSSVFAGKQGFIALRDLFRWAERYRLAEQTEKDYDWLQHLANDGFMLLAG 1306
Cdd:COG1401 395 VDLLEE------------LNEILEKRDFQIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLLDKLDLLGMAEFEDRLE 462
|
....*....
gi 1958779119 1307 RVRKQEEAD 1315
Cdd:COG1401 463 LSEYLPLLL 471
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1741-1778 |
8.37e-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: 8.37e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1958779119 1741 KLNKPILLEGSPGVGKTSLVAALAKASGNTLVRINLSE 1778
Cdd:cd19481 24 GLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4825-5245 |
3.77e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4825 EEDSEPEDVEQGQEKINEQMDEREYDESEVDPYHGSQEQLPEPEALDLPDDLKLDSEDRSAGEDTDNEEAEEENPLEIKE 4904
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4905 KTVDMEEIDREVEEPDAAQSEGERPPAPDEGPGEGEESMDTGADDQDKDTASHAEEQEEEEEGEEGEEEEEEEDRAATDG 4984
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK 1498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4985 SGES-GVSPVDKDLQPQKEEEEGEKSD----AEE-----QVPEATERKEHDSCGQTgvDNVQSAQAVELAGAAPEKEQGK 5054
Cdd:PTZ00121 1499 ADEAkKAAEAKKKADEAKKAEEAKKADeakkAEEakkadEAKKAEEKKKADELKKA--EELKKAEEKKKAEEAKKAEEDK 1576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5055 EEHGSGAADANQAEGHESNFIARLSSQQHTNKNTQSFKRRPGQADNERSigDPNEHVRKRlrtVDTDRKTEQEPAQPQAQ 5134
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL--KKAEEEKKK---VEQLKKKEAEEKKKAEE 1651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5135 VEDADTFEHIQQGSDAYDAQtydvasSEQQQTTKASGEDQEEEEKEDILMDTEEELIRAEDTEQLKPEAVRSETATASGS 5214
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAE------EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
410 420 430
....*....|....*....|....*....|.
gi 1958779119 5215 SEMEVDMQTLKTKEDEDPRTTTSHQEIESER 5245
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4686-5252 |
4.89e-05 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 50.01 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4686 DVSDRIENEEQVEDTFQKGQEKDKEDLDSKPDTKGEDSAVEmseDFDGKMHDGELEQEDDEKSDSEDGDLDKQMGNLNGE 4765
Cdd:COG5271 70 LKSADGAALSAESDAGASLITAANLEEGDIAGNAADDSADE---ESDANAKEDATDDADSSGDAQGDPLATDTLGGGDLD 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4766 EADKLDERLWGDDEEEDEdddgkgeeAGPGMDEEDSELVAKDD-NLDAGNLNKNKKHQGEEEDSEPEDVEQGQEKINEQM 4844
Cdd:COG5271 147 LATKDGDELLPSLADNDE--------AAADEGDELAADGDDTLaVADAIEATPGGTDAVELTATLGATVTTDPGDSVAAD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4845 DEREYDESEV-DPYHGSQEQLPEPEALDLPDDLKLDSEDRSAGEDTDNEEAEEENPLEIKEKTVDmEEIDREVEEPDAAQ 4923
Cdd:COG5271 219 DDLAAEEGASaVVEEEDASEDAVAAADETLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEA-AEDDALDAELTAAQ 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4924 SEGerPPAPDEGPGEGEESMDTGADDQDKDTAshaeeQEEEEEGEEGEEEEEEEDRAATDGSGESGVSPVDKDLQPQKEE 5003
Cdd:COG5271 298 AAD--PESDDDADDSTLAALEGAAEDTEIATA-----DELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAG 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5004 EEGEKSDAEEQVPEATErkehdscgqTGVDNVQSAQAVELAGAAPEKEQGKEEHGSGAADANQAEGHESNFIARLSSQQH 5083
Cdd:COG5271 371 EAADESEGADTDAAADE---------ADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAED 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5084 TNKNTQSFKRRPGQADNERSIGDPNEHVRKRLRTVDTDRKTEQEPAQPQAQVEDADTFEHIQQGSDAYDAQTY------- 5156
Cdd:COG5271 442 DIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETsaddgad 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5157 -DVASSEQQQTTKASGEDQEEEEKEDILMDTEEELIRAEDTEQLKPEAvRSETATASGSSEMEVDMQTLKTKEDEDPRTT 5235
Cdd:COG5271 522 tDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPD-EAEAETEDATENADADETEESADESEEAEAS 600
|
570
....*....|....*..
gi 1958779119 5236 TSHQEIESERPERSRES 5252
Cdd:COG5271 601 EDEAAEEEEADDDEADA 617
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1383-1540 |
8.03e-05 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 45.99 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1383 PVLLVGDTGCGKTTVCQLF---SALSNQKLYSVNCHLNMEtsdflgglrpvrqkpNDKEEPDTRLFEWHDGPLVLAMKED 1459
Cdd:cd00009 21 NLLLYGPPGTGKTTLARAIaneLFRPGAPFLYLNASDLLE---------------GLVVAELFGHFLVRLLFELAEKAKP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1460 SFFLLDEISLADDSVLERLNSVLEvekclvlaekgspeskdTEVELLTAGKHFRILATMNPGGDFgkkELSPALRNRFTE 1539
Cdd:cd00009 86 GVLFIDEIDSLSRGAQNALLRVLE-----------------TLNDLRIDRENVRVIGATNRPLLG---DLDRALYDRLDI 145
|
.
gi 1958779119 1540 I 1540
Cdd:cd00009 146 R 146
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1735-1825 |
8.20e-05 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 49.00 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1735 RLLRAAKLNKPILLEGSPGVGKTSLVAALAKA-SGNTLVRINLseqtdIT---DLFGADLpVEG----GKGGEFAWCDGP 1806
Cdd:COG1401 213 AFLAALKTKKNVILAGPPGTGKTYLARRLAEAlGGEDNGRIEF-----VQfhpSWSYEDF-LLGyrpsLDEGKYEPTPGI 286
|
90 100
....*....|....*....|....*.
gi 1958779119 1807 LL-AALKAG------HWVVLDELNLA 1825
Cdd:COG1401 287 FLrFCLKAEknpdkpYVLIIDEINRA 312
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1050-1219 |
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 1958779119 1050 IDETYVLT-PSVKLNLRDIARVVSAGTyPVLIQGETSVGKTSLIRWLAAAtgnhcVRINNHEHTDI-QEYIGCYTSDTSG 1127
Cdd:PHA02244 94 IDTTKIASnPTFHYETADIAKIVNANI-PVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAImDEFELKGFIDANG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1128 KlvFNEGVLIDAMRKGYWIVLDELNLAPTDVLEALNRLLDDNRELLITETqevVRAHPRFMLFATQNPPG-----LYGGR 1202
Cdd:PHA02244 168 K--FHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVAR 242
|
170
....*....|....*..
gi 1958779119 1203 KVLSRAFRNRFVELHFD 1219
Cdd:PHA02244 243 NKIDGATLDRFAPIEFD 259
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5377-5523 |
1.44e-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: 45.91 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5377 ICLAIDDSSSMVDNhTKQLAFESLAVIGNALTLLEVG-QIAVCSFGESVKLLHPFHeqfNDSSGSQILRLCKFQQRK--- 5452
Cdd:smart00327 2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgg 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779119 5453 -TKIAQFLESVAIMFAAAqklSQNTSPETAQLLLIVSDGRGLFLEGKDRVLAAVQAAQNANIFVIFVVLDNP 5523
Cdd:smart00327 78 gTNLGAALQYALENLFSK---SAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVD 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4692-5254 |
2.17e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4692 ENEEQVEDTFQKGQEKDKEDLDSKPDTKGEDSAVEMSEDFDGKMHDGELEQEDDEKSDSEDgdLDKQmgnlnGEEADKLD 4771
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE--AKKK-----AEEAKKAD 1447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4772 ERLWGDDEEEDEDDDGKGEEAGPGMDE--EDSELVAKDDNLDAGNLNKNKK----HQGEEEDSEPEDVEQGQEK-----I 4840
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEakKKAEEAKKADEAKKKAEEAKKKadeaKKAAEAKKKADEAKKAEEAkkadeA 1527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4841 NEQMDEREYDESEVDPYHGSQEQLPEPEALDLPDDLKLDSEDRSAGEDTDNEEAEEENPLEIKEKTVdmEEIDREVEEPD 4920
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI--EEVMKLYEEEK 1605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4921 AAQSEGERPpapdegpgegEESMDTGADDQDKDTASHAEEQEEEEEGEEGEeeeeeedRAATDGSGESGVSPVDKDLQPQ 5000
Cdd:PTZ00121 1606 KMKAEEAKK----------AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK-------KKAEELKKAEEENKIKAAEEAK 1668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5001 KEEEEGEKSD----AEEQVPEATERKEHDSCGQTGVDNVQSAQAVELAgAAPEKEQGKEEHGSGAADANQAEGHESNFIA 5076
Cdd:PTZ00121 1669 KAEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5077 RLSSQQHTNKNTQSFKRRPGQADNErsIGDPNEHVRKRlrtvDTDRKTEQEPAQPQAQVEDA-DTFEHIQQGS------- 5148
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEE--IRKEKEAVIEE----ELDEEDEKRRMEVDKKIKDIfDNFANIIEGGkegnlvi 1821
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 5149 ----DAYDAQTYDVASSEQQQ-----------------TTKASGEDQEEEEKEDILMDTEEELIRAEDTEQLKPEAVRSE 5207
Cdd:PTZ00121 1822 ndskEMEDSAIKEVADSKNMQleeadafekhkfnknneNGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIERE 1901
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1958779119 5208 TATASgssemevdmqtLKTKEDEDPRTTTSHQEIESERPERSRESTI 5254
Cdd:PTZ00121 1902 IPNNN-----------MAGKNNDIIDDKLDKDEYIKRDAEETREEII 1937
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1721-1797 |
4.47e-04 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 44.48 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1721 DYALSAGTTAMNAQRLLrAAKLNKPI---LLEGSPGVGKTSLVAALAKA---SGNTLVRINLSEQT---DITDLFGADlP 1791
Cdd:cd19499 17 DEAVKAVSDAIRRARAG-LSDPNRPIgsfLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMekhSVSRLIGAP-P 94
|
....*.
gi 1958779119 1792 VEGGKG 1797
Cdd:cd19499 95 GYVGYT 100
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1744-1779 |
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 1958779119 1744 KPILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQ 1779
Cdd:PRK04195 40 KALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
1736-1787 |
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 1958779119 1736 LLRAAKLNKPIL-LEGSPGVGKTSLVAALAKASGNTLVRINLSEQTDITDLFG 1787
Cdd:cd19500 29 RKLKGSMKGPILcLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRG 81
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1383-1559 |
9.81e-04 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 45.11 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1383 PVLLVGDTGCGKTTVCQLFSALSNQKLYSvnchLNMETSDF-LGGLRPVRQKpndkeepdtrlfeWHDGPLVLAMKEDSF 1461
Cdd:PHA02244 121 PVFLKGGAGSGKNHIAEQIAEALDLDFYF----MNAIMDEFeLKGFIDANGK-------------FHETPFYEAFKKGGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1462 FLLDEISLADDSVLERLNSVLevekclvlaekgSPESKDTEVELLTAGKHFRILA---TMNPGGD---FGKKELSPALRN 1535
Cdd:PHA02244 184 FFIDEIDASIPEALIIINSAI------------ANKFFDFADERVTAHEDFRVISagnTLGKGADhiyVARNKIDGATLD 251
|
170 180
....*....|....*....|....
gi 1958779119 1536 RFTEIWCPQSTKREDLVQIINHNL 1559
Cdd:PHA02244 252 RFAPIEFDYDEKIEHLISNGDEDL 275
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1078-1213 |
1.29e-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: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1078 VLIQGETSVGKTSLIRWLAAATGNHCVRINNHEHTDiqEYIGcytsDTSGKLvfnEGVLIDAMRKGYWIV-LDELNLAPT 1156
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS--KYVG----ESEKRL---RELFEAAKKLAPCVIfIDEIDALAG 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958779119 1157 DVLEALNRLLDDNRELLITETQEVVRAHPRFMLFATQNPPGLyggrkvLSRAFRNRF 1213
Cdd:pfam00004 72 SRGSGGDSESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDK------LDPALLGRF 122
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
317-433 |
1.55e-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: 42.52 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 317 AVAVASQNAVLLEGPIGSGKTSLVEHLAAVTGRTKPPqLLKVQLGDqtdskMLLGMYRCTDVpGEFVWQPGTLTQAATKG 396
Cdd:cd00009 13 ALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNASD-----LLEGLVVAELF-GHFLVRLLFELAEKAKP 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958779119 397 HWILLEDIDYAPLDVVSVLIPLLENGELLIPGQGDCL 433
Cdd:cd00009 86 GVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVR 122
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1077-1219 |
1.60e-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: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1077 PVLIQGETSVGKTSLIR---WLAAATGNHCVRIN----NHEHTDIQEYIGCYTSDTSGKLVFNEGVLIDAMRKGYW--IV 1147
Cdd:smart00382 4 VILIVGPPGSGKTTLARalaRELGPPGGGVIYIDgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779119 1148 LDELNLAPTDVLEALNRLLDDNRELLITETQEVVRAhprfmLFATQNPPGLygGRKVLSRAFRNRFVELHFD 1219
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV-----ILTTNDEKDL--GPALLRRRFDRRIVLLLIL 148
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
657-688 |
1.60e-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: 42.76 E-value: 1.60e-03
10 20 30
....*....|....*....|....*....|..
gi 1958779119 657 LLEQLavcVSQGEPVLLVGETGTGKTSAVQHL 688
Cdd:pfam12775 23 LLDLL---LKNGKPVLLVGPTGTGKTVIIQNL 51
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
4692-4942 |
3.23e-03 |
|
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) or RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II.
Pssm-ID: 310411 [Multi-domain] Cd Length: 528 Bit Score: 43.78 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4692 ENEEQVEDTFQKGQEK-----DKEDLDSKPDTKGEDSAVEMSEDFDGKMHDGELEQE-DDEKSDSEDGD--LDKQMGNLN 4763
Cdd:pfam05793 168 ERRKKTANGFSLMMMKaakngPAAFGEHDEETEGEKGGGGRGKDLKIKDLEGDDEDDgDESDKGGEDGDeeKKKKKKKKL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4764 GEEADKLDERlwgDDEEEDEDDDGKGEEAGPGmDEEDSELVAKDDNLDAGNlnknkKHQGEEEDSEPEDVEQGQEKINEQ 4843
Cdd:pfam05793 248 AKNKKKLDDD---KKKKRGGDDDAFEYDSDDG-DDEGREEDYISDSSASGN-----DPEEREDKLSPEEPAKGEIEQSDD 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4844 MDEREYDESEvdpyHGSQEQLPEPEALDLPDDLKLDSEDRSAgedtdneeaeeenpleiKEKTVDMEEIDREVEEPDAAQ 4923
Cdd:pfam05793 319 SEESEEEKNE----EEGKLSKKGKKAKKLKGKKNGKDKSESS-----------------DGDDSDDSDIDDEDSVPLFTA 377
|
250
....*....|....*....
gi 1958779119 4924 SEgERPPAPDEGPGEGEES 4942
Cdd:pfam05793 378 KK-KKEPKKEEPVDSGPSS 395
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1738-1787 |
3.82e-03 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 43.77 E-value: 3.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958779119 1738 RAAKLNKPIL-LEGSPGVGKTSLVAALAKASGNTLVRINLSEQTDITDLFG 1787
Cdd:PRK10787 343 RVNKIKGPILcLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRG 393
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1077-1213 |
4.58e-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: 40.98 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1077 PVLIQGETSVGKTSLIR---WLAAATGNHCVRINNHEHTDIQEYIGCYTSDTSGKLVFnegvlIDAMRKGYWIVLDELNL 1153
Cdd:cd00009 21 NLLLYGPPGTGKTTLARaiaNELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFE-----LAEKAKPGVLFIDEIDS 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 1154 APTDVLEALNRLLDDnRELLITETQEVvrahpRFMLFATQNPPGLyggrkvLSRAFRNRF 1213
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 ... |
657-712 |
6.19e-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: 42.46 E-value: 6.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779119 657 LLEQLAVCVSQGEPVLLVGETGTGKTSAVQHLAHATGQHLRVVNMNqqSDT--ADLLG 712
Cdd:COG0714 20 LIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFT--PDLlpSDILG 75
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4826-5071 |
7.45e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.06 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4826 EDSEPEDVEQGQ---EKINEQMDEREYDESEVDPYHGSQEQLPEpealdlpdDLKLDSEDRSAGEDTDNEEAEEENPLEI 4902
Cdd:TIGR00927 628 GDLSKGDVAEAEhtgERTGEEGERPTEAEGENGEESGGEAEQEG--------ETETKGENESEGEIPAERKGEQEGEGEI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4903 KEKTVDM--EEIDREVEEPDAAQSEGERPPAPDEGPGEGEESMDTGADDQDKDTASHAEEQEEEEEGEEGEEEEEEEDRA 4980
Cdd:TIGR00927 700 EAKEADHkgETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDED 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779119 4981 ATDGSGESGVSPVDKDLQPQKEEEEGEKSDAEEQVPEATERKEHDSCGQTGVDNVQSAQAvELAGAAPEKEQGKEehGSG 5060
Cdd:TIGR00927 780 EGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNA-ENQGEAKQDEKGVD--GGG 856
|
250
....*....|.
gi 1958779119 5061 AADANQAEGHE 5071
Cdd:TIGR00927 857 GSDGGDSEEEE 867
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
1735-1778 |
8.97e-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: 8.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958779119 1735 RLLRAAKLNKP--ILLEGSPGVGKTSLVAALAKASGNTLVRINLSE 1778
Cdd:COG0464 181 ELREEYGLPPPrgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSD 226
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
1744-1781 |
9.92e-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: 9.92e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1958779119 1744 KPILLEGSPGVGKTSLVAALAKASGNTLVRINLSEQTD 1781
Cdd:cd19520 36 KGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTD 73
|
|
| |
