|
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 ... |
5323-5593 |
1.54e-145 |
|
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: 454.50 E-value: 1.54e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5323 LSQRLCEELRLILEPTQAAKLKGDYRTGKRLNIRKVIPYIASQFRKDKIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5402
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5403 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQKKTKIAQFLESVANMFaaaQQLSQ 5482
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIF---EDART 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5483 NISSETA-QLLLVVSDGRGLFLEGKERVLaaVQAARNANIFVIFVVLDNPSSRDSILDIKVPIFKGPGeMPEIRSYMEEF 5561
Cdd:cd01460 158 QSSSGSLwQLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEF 234
|
250 260 270
....*....|....*....|....*....|..
gi 24415404 5562 PFPYYIILRDVNALPETLSDALRQWFELVTAS 5593
Cdd:cd01460 235 PFPYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
915-1017 |
4.77e-41 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 407722 Cd Length: 104 Bit Score: 148.11 E-value: 4.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 915 DLQVLIVDYLKGLSVNKNTVQGIINFYTALRKESGTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGNIQRSLYEGFCLG 993
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 24415404 994 FLTQLDRASHPIVQKLICQHIVPG 1017
Cdd:pfam17865 81 FLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1385-1540 |
2.53e-27 |
|
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: 110.07 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1385 PVLLVGDTGCGKTTICQVFA-ALANQKLYSVSCHLHMETSDFLGGLrpvrqkpndkeEIDTsRLFEWHDGPLVQAMKEDG 1463
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDP-GGASWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24415404 1464 FFLLDEISLADDSVLERLNSVLEvEKSLVLAEKGSPEDKdseielltAGKKFRILATMNPgGDFGKKELSPALRNRF 1540
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKA--------APDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1900-1999 |
1.66e-24 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 465540 Cd Length: 106 Bit Score: 101.22 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1900 DMEFIASTLFPaIEKNIVKKMVAFNNQIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*
gi 24415404 1975 LVYGERMRTEEDKKKVIAVFKDVFG 1999
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1227-1328 |
8.63e-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: 96.22 E-value: 8.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1227 ELETILHKRCSLPPSYCSKLVKVMLDLQSYRRSSSVFA--GKQGFITLRDLFRWAERYRLAEPTEKEYDWLQHLANDGYM 1304
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 24415404 1305 LLAGRVRKQEEIDVIQEVLEKHFK 1328
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1079-1215 |
8.73e-23 |
|
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: 97.36 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1079 PVLIQGETSVGKTSLIQWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDSSGKlVFKEGVLIDAMRKGYWIILDELNLAP 1157
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 24415404 1158 TDVLEALNRLLDDNRELLVTETQEVVKAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 1215
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 ... |
480-604 |
7.63e-19 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 465540 Cd Length: 106 Bit Score: 85.05 E-value: 7.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 480 ELNEVLQSRYPSLLAVVDHLLDIYIQLTGEKHHSWSDSSVGceqapeevsearrenkrptlEGRELSLRDLLNWCNRIAH 559
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSG--------------------SPREFNLRDLLRWCRRLSS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24415404 560 SFDSSSLSASL-NIFQEALDCFTAMLSEHTSKLKMAEVIGSKLNIS 604
Cdd:pfam17867 61 LLPTLLSPTVReEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
325-453 |
1.54e-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: 85.04 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 325 VLLEGPIGCGKTSLVEYLAAVTGRTKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATMGHWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 24415404 405 YAPLDVVSVLIPLLENGELLIP-GRGDCLKVAPGFQFFATRRLLSCGGNW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1748-1888 |
2.31e-16 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 78.87 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1748 PILLEGSPGVGKTSLVGALAKA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWRDGPLLAALKAGHWVVLDELN 1826
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24415404 1827 LASQSVLEGLNACFDHRgEIYVPELGMSFQVQHEKTKIFGCQNPfrQGGGRKGLPRSFLNRF 1888
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4687-5321 |
1.21e-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: 65.42 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4687 KDVSDQIGNEEQV-EDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDfdgkmHDGELEEQEEDDEKSDSEGGDLDkhmGD 4765
Cdd:COG5271 408 SPTSDTDEEEEEAdEDASAGETEDESTDVTSAEDDIATDEEADSLAD-----EEEEAEAELDTEEDTESAEEDAD---GD 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4766 LNGEEADKLDERLwgdddeeedeEEEDNKTEETGPGMDEEDSELVAKDDNLDSgNSNKDKSQQDKKEEkeeaeaddggqg 4845
Cdd:COG5271 480 EATDEDDASDDGD----------EEEAEEDAEAEADSDELTAEETSADDGADT-DAAADPEDSDEDAL------------ 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4846 EDKINEQIDERDYDEN---EVDPYHGNQEKVPEPEALDLPDDLNLDSEDKNggedtdneEGEEENPLEIKEKPEEAGHEA 4922
Cdd:COG5271 537 EDETEGEENAPGSDQDadeTDEPEATAEEDEPDEAEAETEDATENADADET--------EESADESEEAEASEDEAAEEE 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4923 EERGE-TETDQNESQSPQEPEEGPSEDDKAEGEEEmDTGADDQDGDAAQHPEEHSEEQQQSVEEKDKEADEEGGENGPAD 5001
Cdd:COG5271 609 EADDDeADADADGAADEEETEEEAAEDEAAEPETD-ASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAA 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5002 QGFQPQEEEEREDSDTE-EQVPEALERKEhascgqtgVENMQNTQAMELAGAAPEKEQGKEEHGSGAADANQAEghESNF 5080
Cdd:COG5271 688 AAEASDDEEETEEADEDaETASEEADAEE--------ADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEE--EAEE 757
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5081 IAQLASqkhtrkntqsfkrkpGQADNERsmgDHNERVHKRLRTVDTDshAEQGPAQQPQAQVEDADAFEHIKQGSDAYDA 5160
Cdd:COG5271 758 AEEAEE---------------DDADGLE---EALEEEKADAEEAATD--EEAEAAAEEKEKVADEDQDTDEDALLDEAEA 817
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5161 Q---TYDVASKEQQQSAKDSGKDQEEEEIEDTLMDTEEQEefKAADVEQLKPEEIKSGTTAPLGFDEMEVEIQTVKTEED 5237
Cdd:COG5271 818 DeeeDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKD--VDADLDLDADLAADEHEAEEAQEAETDADADADAGEAD 895
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5238 QDPRTDKAHKETENEKPERSRESTIHTAHQFLMDTIFQPFLKDVNELRQELERQLEMwqprESGNPEEEKVAAEMWQSYL 5317
Cdd:COG5271 896 SSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALAL----DEAGDEESDDAAADDAGDD 971
|
....
gi 24415404 5318 ILTA 5321
Cdd:COG5271 972 SLAD 975
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
672-902 |
2.62e-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: 58.46 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 672 PVLLVGETGTGKTSTIQYLAH-ITGHRLRVVNMNQQSDTADLLGGYKPvdhkliwlplreafeelfaqtfskkqnftflg 750
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 751 hiqtcyrqkrwhdllrlmqhvhksavnkdgkdsetgllikekweafglrlnhaqqqmkmteNTLLFAFVEGTLAQAVKKG 830
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24415404 831 EWILLDEINLAAPEILECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 902
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 ... |
2220-2306 |
2.51e-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: 55.76 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 2220 GTFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPGgvltisERGMIDGSTPTITPNPNFRLFLSMDPVHGD- 2298
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER------RLLLPDGGELVKAAPDGFRLIATMNPLDRGl 124
|
90
....*....|
gi 24415404 2299 --ISRAMRNR 2306
Cdd:pfam07728 125 neLSPALRSR 134
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
659-780 |
1.93e-03 |
|
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 cd00009:
Pssm-ID: 476819 [Multi-domain] Cd Length: 151 Bit Score: 42.13 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 659 LIEQL--AVCVSKGEPVLLVGETGTGKTSTIQYLAHITGHR-LRVVNMNqqsdTADLLGGYkpVDHKLIWLPLREAFEEL 735
Cdd:cd00009 6 AIEALreALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgAPFLYLN----ASDLLEGL--VVAELFGHFLVRLLFEL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24415404 736 FAqtfsKKQNFT-FLGHIQTCYRQKRWHdLLRLMQHVHKSAVNKDG 780
Cdd:cd00009 80 AE----KAKPGVlFIDEIDSLSRGAQNA-LLRVLETLNDLRIDREN 120
|
|
| |
|
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 ... |
5323-5593 |
1.54e-145 |
|
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: 454.50 E-value: 1.54e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5323 LSQRLCEELRLILEPTQAAKLKGDYRTGKRLNIRKVIPYIASQFRKDKIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5402
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5403 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQKKTKIAQFLESVANMFaaaQQLSQ 5482
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIF---EDART 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5483 NISSETA-QLLLVVSDGRGLFLEGKERVLaaVQAARNANIFVIFVVLDNPSSRDSILDIKVPIFKGPGeMPEIRSYMEEF 5561
Cdd:cd01460 158 QSSSGSLwQLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEF 234
|
250 260 270
....*....|....*....|....*....|..
gi 24415404 5562 PFPYYIILRDVNALPETLSDALRQWFELVTAS 5593
Cdd:cd01460 235 PFPYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
915-1017 |
4.77e-41 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 407722 Cd Length: 104 Bit Score: 148.11 E-value: 4.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 915 DLQVLIVDYLKGLSVNKNTVQGIINFYTALRKESGTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGNIQRSLYEGFCLG 993
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 24415404 994 FLTQLDRASHPIVQKLICQHIVPG 1017
Cdd:pfam17865 81 FLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1385-1540 |
2.53e-27 |
|
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: 110.07 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1385 PVLLVGDTGCGKTTICQVFA-ALANQKLYSVSCHLHMETSDFLGGLrpvrqkpndkeEIDTsRLFEWHDGPLVQAMKEDG 1463
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDP-GGASWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24415404 1464 FFLLDEISLADDSVLERLNSVLEvEKSLVLAEKGSPEDKdseielltAGKKFRILATMNPgGDFGKKELSPALRNRF 1540
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKA--------APDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1900-1999 |
1.66e-24 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 101.22 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1900 DMEFIASTLFPaIEKNIVKKMVAFNNQIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*
gi 24415404 1975 LVYGERMRTEEDKKKVIAVFKDVFG 1999
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1227-1328 |
8.63e-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: 96.22 E-value: 8.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1227 ELETILHKRCSLPPSYCSKLVKVMLDLQSYRRSSSVFA--GKQGFITLRDLFRWAERYRLAEPTEKEYDWLQHLANDGYM 1304
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 24415404 1305 LLAGRVRKQEEIDVIQEVLEKHFK 1328
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1079-1215 |
8.73e-23 |
|
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: 97.36 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1079 PVLIQGETSVGKTSLIQWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDSSGKlVFKEGVLIDAMRKGYWIILDELNLAP 1157
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 24415404 1158 TDVLEALNRLLDDNRELLVTETQEVVKAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 1215
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 ... |
480-604 |
7.63e-19 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 85.05 E-value: 7.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 480 ELNEVLQSRYPSLLAVVDHLLDIYIQLTGEKHHSWSDSSVGceqapeevsearrenkrptlEGRELSLRDLLNWCNRIAH 559
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSG--------------------SPREFNLRDLLRWCRRLSS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24415404 560 SFDSSSLSASL-NIFQEALDCFTAMLSEHTSKLKMAEVIGSKLNIS 604
Cdd:pfam17867 61 LLPTLLSPTVReEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
325-453 |
1.54e-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: 85.04 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 325 VLLEGPIGCGKTSLVEYLAAVTGRTKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATMGHWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 24415404 405 YAPLDVVSVLIPLLENGELLIP-GRGDCLKVAPGFQFFATRRLLSCGGNW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1748-1888 |
2.31e-16 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 78.87 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1748 PILLEGSPGVGKTSLVGALAKA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWRDGPLLAALKAGHWVVLDELN 1826
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24415404 1827 LASQSVLEGLNACFDHRgEIYVPELGMSFQVQHEKTKIFGCQNPfrQGGGRKGLPRSFLNRF 1888
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1736-1888 |
3.39e-10 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 64.80 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1736 AQRLLRATKLKKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWRDGPLLAAlk 1815
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQ--QTGEFEFRPGPLFAN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1816 aghwVVL-DELNLAS---QS----VLEglnacfdhRGEIYVP----ELGMSFQVqhektkiFGCQNPFRQGGGRKgLPRS 1883
Cdd:COG0714 97 ----VLLaDEINRAPpktQSalleAME--------ERQVTIPggtyKLPEPFLV-------IATQNPIEQEGTYP-LPEA 156
|
....*
gi 24415404 1884 FLNRF 1888
Cdd:COG0714 157 QLDRF 161
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1079-1235 |
3.96e-10 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 64.42 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1079 PVLIQGETSVGKTSLIQWLAAATGNHCVRINNHEHTDIQEyiGCYTSD---SSGKLVFKEG------VLIdamrkgywii 1149
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSD--ILGTYIydqQTGEFEFRPGplfanvLLA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1150 lDELNLAPTDVLEALNRLLDDNRellVTETQEVVKAHPRFMLFATQNPPGLYGGRkVLSRAFRNRF-VELHFDeLPSSEL 1228
Cdd:COG0714 101 -DEINRAPPKTQSALLEAMEERQ---VTIPGGTYKLPEPFLVIATQNPIEQEGTY-PLPEAQLDRFlLKLYIG-YPDAEE 174
|
....*...
gi 24415404 1229 ET-ILHKR 1235
Cdd:COG0714 175 EReILRRH 182
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4687-5321 |
1.21e-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: 65.42 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4687 KDVSDQIGNEEQV-EDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDfdgkmHDGELEEQEEDDEKSDSEGGDLDkhmGD 4765
Cdd:COG5271 408 SPTSDTDEEEEEAdEDASAGETEDESTDVTSAEDDIATDEEADSLAD-----EEEEAEAELDTEEDTESAEEDAD---GD 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4766 LNGEEADKLDERLwgdddeeedeEEEDNKTEETGPGMDEEDSELVAKDDNLDSgNSNKDKSQQDKKEEkeeaeaddggqg 4845
Cdd:COG5271 480 EATDEDDASDDGD----------EEEAEEDAEAEADSDELTAEETSADDGADT-DAAADPEDSDEDAL------------ 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4846 EDKINEQIDERDYDEN---EVDPYHGNQEKVPEPEALDLPDDLNLDSEDKNggedtdneEGEEENPLEIKEKPEEAGHEA 4922
Cdd:COG5271 537 EDETEGEENAPGSDQDadeTDEPEATAEEDEPDEAEAETEDATENADADET--------EESADESEEAEASEDEAAEEE 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4923 EERGE-TETDQNESQSPQEPEEGPSEDDKAEGEEEmDTGADDQDGDAAQHPEEHSEEQQQSVEEKDKEADEEGGENGPAD 5001
Cdd:COG5271 609 EADDDeADADADGAADEEETEEEAAEDEAAEPETD-ASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAA 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5002 QGFQPQEEEEREDSDTE-EQVPEALERKEhascgqtgVENMQNTQAMELAGAAPEKEQGKEEHGSGAADANQAEghESNF 5080
Cdd:COG5271 688 AAEASDDEEETEEADEDaETASEEADAEE--------ADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEE--EAEE 757
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5081 IAQLASqkhtrkntqsfkrkpGQADNERsmgDHNERVHKRLRTVDTDshAEQGPAQQPQAQVEDADAFEHIKQGSDAYDA 5160
Cdd:COG5271 758 AEEAEE---------------DDADGLE---EALEEEKADAEEAATD--EEAEAAAEEKEKVADEDQDTDEDALLDEAEA 817
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5161 Q---TYDVASKEQQQSAKDSGKDQEEEEIEDTLMDTEEQEefKAADVEQLKPEEIKSGTTAPLGFDEMEVEIQTVKTEED 5237
Cdd:COG5271 818 DeeeDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKD--VDADLDLDADLAADEHEAEEAQEAETDADADADAGEAD 895
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5238 QDPRTDKAHKETENEKPERSRESTIHTAHQFLMDTIFQPFLKDVNELRQELERQLEMwqprESGNPEEEKVAAEMWQSYL 5317
Cdd:COG5271 896 SSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALAL----DEAGDEESDDAAADDAGDD 971
|
....
gi 24415404 5318 ILTA 5321
Cdd:COG5271 972 SLAD 975
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
672-902 |
2.62e-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: 58.46 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 672 PVLLVGETGTGKTSTIQYLAH-ITGHRLRVVNMNQQSDTADLLGGYKPvdhkliwlplreafeelfaqtfskkqnftflg 750
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 751 hiqtcyrqkrwhdllrlmqhvhksavnkdgkdsetgllikekweafglrlnhaqqqmkmteNTLLFAFVEGTLAQAVKKG 830
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24415404 831 EWILLDEINLAAPEILECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 902
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4912-5253 |
4.11e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4912 KEKPEEAGHEAEERGETETDQNESQSPQEPEEGPSEDDKAEGEEEMDTGAD------------------DQDGDAAQHPE 4973
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeakkadeakkkaeeakkaDEAKKKAEEAK 1496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4974 EHSEEQQQSVEEKDKEADEEGGENG-PADQGFQPQEEEEREDSDTEEQVPEALERKEhascgqtgVENMQNTQAMELAGA 5052
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAkKADEAKKAEEAKKADEAKKAEEKKKADELKK--------AEELKKAEEKKKAEE 1568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5053 APEKEQGKEEHGSGAADANQAEGHESNFIAQLASQKHTRKNTQSFKrkpgqADNERSMGDHNERVHKRLRTVDTDSHAEQ 5132
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5133 gpaqqpqaqvEDADAFEHIKQGSDAYDAQTYDVASK--EQQQSAKDSGKDQEEEEIEDTLMDTEEQEEFKAADVEQLKPE 5210
Cdd:PTZ00121 1644 ----------EEKKKAEELKKAEEENKIKAAEEAKKaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24415404 5211 EIKSGTTAPLGFDEMEVEIQTVKTEEDQDPRTDKAHKETENEK 5253
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4757-5029 |
5.87e-09 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 63.09 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4757 GDLDK-------HMGDLNGEEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDSELVAKDDNLDSGNSNKDKSQQD 4829
Cdd:TIGR00927 628 GDLSKgdvaeaeHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHK 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4830 KKEEKEEAEADDGGQgedkineqiDERDYDENEVDPYHGNQEKVPEPEALDLPDDLNLDSEDKNGGEDTDNEEGEEENPL 4909
Cdd:TIGR00927 708 GETEAEEVEHEGETE---------AEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDE 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4910 EikEKPEEAGHEAEERGETETDQNESQSPQEPEEGPSEDDKAEGEEEMDTGADDQDGDAAQHPEEHSEEQQQSveekdke 4989
Cdd:TIGR00927 779 D--EGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDE------- 849
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 24415404 4990 adeEGGENGPADQGFQPQEEEEREDSDTEEQVPEALERKE 5029
Cdd:TIGR00927 850 ---KGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEE 886
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5385-5535 |
1.05e-08 |
|
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: 57.85 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5385 ICLAIDDSSSMVDNhTKQLAFESLAVIGNALTLLEVG-QIAVCSFGESVKLLHPFHeqfSDYSGSQILRLCKFQQKK--- 5460
Cdd:smart00327 2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgg 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24415404 5461 -TKIAQFLESVANMFAAAQQLSQnisSETAQLLLVVSDGRGLFleGKERVLAAVQAARNANIFVIFVVLDNPSSRD 5535
Cdd:smart00327 78 gTNLGAALQYALENLFSKSAGSR---RGAPKVVILITDGESND--GPKDLLKAAKELKRSGVKVFVVGVGNDVDEE 148
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2220-2306 |
2.51e-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: 55.76 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 2220 GTFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPGgvltisERGMIDGSTPTITPNPNFRLFLSMDPVHGD- 2298
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER------RLLLPDGGELVKAAPDGFRLIATMNPLDRGl 124
|
90
....*....|
gi 24415404 2299 --ISRAMRNR 2306
Cdd:pfam07728 125 neLSPALRSR 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1383-1540 |
1.03e-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: 54.30 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1383 GEPVLLVGDTGCGKTTICQVFAALANQKLYSVschLHMETSDFLGGLRPVRQKPNDKEEIDTSRLFEWHDGPLVQAMKED 1462
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV---IYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24415404 1463 -GFFLLDEISLADDSVLERLNSVLEVEKSLVLAEKgspedkdseielltaGKKFRILATMNPGGDFGKKELSPALRNRF 1540
Cdd:smart00382 79 pDVLILDEITSLLDAEQEALLLLLEELRLLLLLKS---------------EKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1372-1540 |
2.98e-07 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 55.56 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1372 LAMLVGRalefgePVLLVGDTGCGKTTICQVFAALANQKLYSVSCHLHMETSDFLGglrpvrqkpndkEEI---DTSRlF 1448
Cdd:COG0714 26 IALLAGG------HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILG------------TYIydqQTGE-F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1449 EWHDGPLVQamkedGFFLLDEISLADDSVLerlNSVLEV--EKSLVLAEkgspedkdseiELLTAGKKFRILATMNPGGD 1526
Cdd:COG0714 87 EFRPGPLFA-----NVLLADEINRAPPKTQ---SALLEAmeERQVTIPG-----------GTYKLPEPFLVIATQNPIEQ 147
|
170
....*....|....
gi 24415404 1527 FGKKELSPALRNRF 1540
Cdd:COG0714 148 EGTYPLPEAQLDRF 161
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1746-1896 |
6.74e-07 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 52.15 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1746 KKPILLEGSPGVGKTSLVGALAKAS---GNTLVRINLSeqtditDLFGADlpVEGGKGGEFAWRDGPLLAALKAGHWVVL 1822
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFI 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24415404 1823 DELNLASQSVLEGLNACFdhrgeiyvpELGMSFQVQHEKTKIFG-CQNPFRQgggrkGLPRSFLNRFTQVFVDPL 1896
Cdd:cd00009 91 DEIDSLSRGAQNALLRVL---------ETLNDLRIDRENVRVIGaTNRPLLG-----DLDRALYDRLDIRIVIPL 151
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1301-1618 |
1.42e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 54.35 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1301 DGYMLLAGRVRKQEEIDVIQEVLEKHFKKKLcpqSLFSKENVLKLLGKLSTQISTLECNFGHIVWTEGMR--RLAMLVGR 1378
Cdd:PHA02244 42 DAIREKAETEGKEIAIDDIKKEIEDSPEEQF---FELPVKIELQQEGKPAGDISGIDTTKIASNPTFHYEtaDIAKIVNA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1379 ALefgePVLLVGDTGCGKTTICQVFAALANQKLYSvschlhmetsdflggLRPVRQKPNDKEEIDTSRLFewHDGPLVQA 1458
Cdd:PHA02244 119 NI----PVFLKGGAGSGKNHIAEQIAEALDLDFYF---------------MNAIMDEFELKGFIDANGKF--HETPFYEA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1459 MKEDGFFLLDEISLADDSVLERLNSVLevekslvlaekgSPEDKDSEIELLTAGKKFRILA---TMNPGGD---FGKKEL 1532
Cdd:PHA02244 178 FKKGGLFFIDEIDASIPEALIIINSAI------------ANKFFDFADERVTAHEDFRVISagnTLGKGADhiyVARNKI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1533 SPALRNRFTEIWCPQSTSREDLIqiishnlrpglclgridpkgSDIPEVMLDFIDWLTHQ--EFGRKCVVSIRDILSWVN 1610
Cdd:PHA02244 246 DGATLDRFAPIEFDYDEKIEHLI--------------------SNGDEDLVNFVALLRHEmaEKGLDHVFSMRAIIHGKK 305
|
....*...
gi 24415404 1611 FMNKMGEE 1618
Cdd:PHA02244 306 FDGVFEAD 313
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1068-1221 |
3.83e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 49.73 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1068 DIVRVVSAGTyPVLIQGETSVGKTSLIQWLAAAtgnhcVRINNHEHTDI-QEYIGCYTSDSSGKlvFKEGVLIDAMRKGY 1146
Cdd:PHA02244 111 DIAKIVNANI-PVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAImDEFELKGFIDANGK--FHETPFYEAFKKGG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1147 WIILDELNLAPTDVLEALNRLLDDNRELLVTETqevVKAHPRFMLFATQNPPG-----LYGGRKVLSRAFRNRFVELHFD 1221
Cdd:PHA02244 183 LFFIDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1368-1543 |
1.49e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 45.21 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1368 GMRRLAMLVGRALEFGEP--VLLVGDTGCGKTTICQVFAALANQKLYSVschLHMETSDFLGGLRpvrqkpndKEEIDTS 1445
Cdd:cd00009 2 GQEEAIEALREALELPPPknLLLYGPPGTGKTTLARAIANELFRPGAPF---LYLNASDLLEGLV--------VAELFGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1446 RLFEWHDGPLVQAMKedGFFLLDEISLADDSVLERLNSVLEVekslvlaekgspedkdsEIELLTAGKKFRILATMNPGG 1525
Cdd:cd00009 71 FLVRLLFELAEKAKP--GVLFIDEIDSLSRGAQNALLRVLET-----------------LNDLRIDRENVRVIGATNRPL 131
|
170
....*....|....*...
gi 24415404 1526 DFgkkELSPALRNRFTEI 1543
Cdd:cd00009 132 LG---DLDRALYDRLDIR 146
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1746-1782 |
2.23e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 47.61 E-value: 2.23e-04
10 20 30
....*....|....*....|....*....|....*..
gi 24415404 1746 KKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQ 1782
Cdd:PRK04195 39 KKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1079-1221 |
4.29e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1079 PVLIQGETSVGKTSLIQ---WLAAATGNHCVRIN----NHEHTDIQEYIGCYTSDSSGKLVFKEGVLIDAMRKGYW--II 1149
Cdd:smart00382 4 VILIVGPPGSGKTTLARalaRELGPPGGGVIYIDgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24415404 1150 LDELNLAPTDVLEALNRLLDDNRELLVTEtqevvKAHPRFMLFATQNPPGLygGRKVLSRAFRNRFVELHFD 1221
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLK-----SEKNLTVILTTNDEKDL--GPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
669-737 |
6.23e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.52 E-value: 6.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24415404 669 KGEPVLLVGETGTGKTSTIQYLAHI---TGHRLRVVNMNQQSDTADLLGGYKPVDHKLIWLPLREAFEELFA 737
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA 72
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1079-1215 |
1.19e-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: 42.90 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1079 PVLIQGETSVGKTSLIQ---WLAAATGNHCVRINNHEHTDIqeyigcyTSDSSGKLVFKEGVLIDAMRKGYW--IILDEL 1153
Cdd:cd00009 21 NLLLYGPPGTGKTTLARaiaNELFRPGAPFLYLNASDLLEG-------LVVAELFGHFLVRLLFELAEKAKPgvLFIDEI 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24415404 1154 NLAPTDVLEALNRLLDDnRELLVTETQEVvkahpRFMLFATQNPPGLyggrkvLSRAFRNRF 1215
Cdd:cd00009 94 DSLSRGAQNALLRVLET-LNDLRIDRENV-----RVIGATNRPLLGD------LDRALYDRL 143
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
659-780 |
1.93e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 42.13 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 659 LIEQL--AVCVSKGEPVLLVGETGTGKTSTIQYLAHITGHR-LRVVNMNqqsdTADLLGGYkpVDHKLIWLPLREAFEEL 735
Cdd:cd00009 6 AIEALreALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgAPFLYLN----ASDLLEGL--VVAELFGHFLVRLLFEL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24415404 736 FAqtfsKKQNFT-FLGHIQTCYRQKRWHdLLRLMQHVHKSAVNKDG 780
Cdd:cd00009 80 AE----KAKPGVlFIDEIDSLSRGAQNA-LLRVLETLNDLRIDREN 120
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
4916-5063 |
1.97e-03 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 44.64 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4916 EEAGHEAEERGETETDQNESQ--SPQEPEEGP-SEDDKAEGEEEMDTGADDQDGDAAQHPEEHSEEQQQS---------- 4982
Cdd:pfam01271 191 REKSDEREKSSQESGEDTYRQenIPQEDQVGPeDQEPSEEGEEDATQEEVKRSRPRTHHGRSLPDESSRGgqlgleeeas 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4983 ---------------VEEKDKEADEEGGENGPADQGFQPQEEEEREDSDTEE------------QVPEALERKEHASCGQ 5035
Cdd:pfam01271 271 eeeeeygeesrglsaVQTYLLRLVNARGRGRSEKRAERERSEESEEEELKRAspyeeleitanlQIPPSEEERMLKKAGR 350
|
170 180
....*....|....*....|....*...
gi 24415404 5036 TGVENMQNTQAMELAGAAPEKEQGKEEH 5063
Cdd:pfam01271 351 SPRGRVDEAGALEALEALEEKRKLDLDH 378
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
320-432 |
2.75e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 41.75 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 320 ASQNAVLLEGPIGCGKTSLVEYLAAVTGRTKPPqLLKVQLGDqtdskMLLGMYRCTDVpGEFVWQPGTLTQAATMGHWIL 399
Cdd:cd00009 17 PPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNASD-----LLEGLVVAELF-GHFLVRLLFELAEKAKPGVLF 89
|
90 100 110
....*....|....*....|....*....|...
gi 24415404 400 LEDIDYAPLDVVSVLIPLLENGELLIPGRGDCL 432
Cdd:cd00009 90 IDEIDSLSRGAQNALLRVLETLNDLRIDRENVR 122
|
|
| |
|
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 ... |
5323-5593 |
1.54e-145 |
|
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: 454.50 E-value: 1.54e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5323 LSQRLCEELRLILEPTQAAKLKGDYRTGKRLNIRKVIPYIASQFRKDKIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5402
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5403 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQKKTKIAQFLESVANMFaaaQQLSQ 5482
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIF---EDART 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5483 NISSETA-QLLLVVSDGRGLFLEGKERVLaaVQAARNANIFVIFVVLDNPSSRDSILDIKVPIFKGPGeMPEIRSYMEEF 5561
Cdd:cd01460 158 QSSSGSLwQLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEF 234
|
250 260 270
....*....|....*....|....*....|..
gi 24415404 5562 PFPYYIILRDVNALPETLSDALRQWFELVTAS 5593
Cdd:cd01460 235 PFPYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
915-1017 |
4.77e-41 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 407722 Cd Length: 104 Bit Score: 148.11 E-value: 4.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 915 DLQVLIVDYLKGLSVNKNTVQGIINFYTALRKESGTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGNIQRSLYEGFCLG 993
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 24415404 994 FLTQLDRASHPIVQKLICQHIVPG 1017
Cdd:pfam17865 81 FLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1385-1540 |
2.53e-27 |
|
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: 110.07 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1385 PVLLVGDTGCGKTTICQVFA-ALANQKLYSVSCHLHMETSDFLGGLrpvrqkpndkeEIDTsRLFEWHDGPLVQAMKEDG 1463
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDP-GGASWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24415404 1464 FFLLDEISLADDSVLERLNSVLEvEKSLVLAEKGSPEDKdseielltAGKKFRILATMNPgGDFGKKELSPALRNRF 1540
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKA--------APDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1900-1999 |
1.66e-24 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 101.22 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1900 DMEFIASTLFPaIEKNIVKKMVAFNNQIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*
gi 24415404 1975 LVYGERMRTEEDKKKVIAVFKDVFG 1999
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1227-1328 |
8.63e-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: 96.22 E-value: 8.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1227 ELETILHKRCSLPPSYCSKLVKVMLDLQSYRRSSSVFA--GKQGFITLRDLFRWAERYRLAEPTEKEYDWLQHLANDGYM 1304
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 24415404 1305 LLAGRVRKQEEIDVIQEVLEKHFK 1328
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1079-1215 |
8.73e-23 |
|
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: 97.36 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1079 PVLIQGETSVGKTSLIQWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDSSGKlVFKEGVLIDAMRKGYWIILDELNLAP 1157
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 24415404 1158 TDVLEALNRLLDDNRELLVTETQEVVKAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 1215
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 ... |
480-604 |
7.63e-19 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 85.05 E-value: 7.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 480 ELNEVLQSRYPSLLAVVDHLLDIYIQLTGEKHHSWSDSSVGceqapeevsearrenkrptlEGRELSLRDLLNWCNRIAH 559
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSG--------------------SPREFNLRDLLRWCRRLSS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24415404 560 SFDSSSLSASL-NIFQEALDCFTAMLSEHTSKLKMAEVIGSKLNIS 604
Cdd:pfam17867 61 LLPTLLSPTVReEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
325-453 |
1.54e-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: 85.04 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 325 VLLEGPIGCGKTSLVEYLAAVTGRTKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATMGHWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 24415404 405 YAPLDVVSVLIPLLENGELLIP-GRGDCLKVAPGFQFFATRRLLSCGGNW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1748-1888 |
2.31e-16 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 78.87 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1748 PILLEGSPGVGKTSLVGALAKA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWRDGPLLAALKAGHWVVLDELN 1826
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24415404 1827 LASQSVLEGLNACFDHRgEIYVPELGMSFQVQHEKTKIFGCQNPfrQGGGRKGLPRSFLNRF 1888
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1736-1888 |
3.39e-10 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 64.80 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1736 AQRLLRATKLKKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWRDGPLLAAlk 1815
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQ--QTGEFEFRPGPLFAN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1816 aghwVVL-DELNLAS---QS----VLEglnacfdhRGEIYVP----ELGMSFQVqhektkiFGCQNPFRQGGGRKgLPRS 1883
Cdd:COG0714 97 ----VLLaDEINRAPpktQSalleAME--------ERQVTIPggtyKLPEPFLV-------IATQNPIEQEGTYP-LPEA 156
|
....*
gi 24415404 1884 FLNRF 1888
Cdd:COG0714 157 QLDRF 161
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1079-1235 |
3.96e-10 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 64.42 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1079 PVLIQGETSVGKTSLIQWLAAATGNHCVRINNHEHTDIQEyiGCYTSD---SSGKLVFKEG------VLIdamrkgywii 1149
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSD--ILGTYIydqQTGEFEFRPGplfanvLLA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1150 lDELNLAPTDVLEALNRLLDDNRellVTETQEVVKAHPRFMLFATQNPPGLYGGRkVLSRAFRNRF-VELHFDeLPSSEL 1228
Cdd:COG0714 101 -DEINRAPPKTQSALLEAMEERQ---VTIPGGTYKLPEPFLVIATQNPIEQEGTY-PLPEAQLDRFlLKLYIG-YPDAEE 174
|
....*...
gi 24415404 1229 ET-ILHKR 1235
Cdd:COG0714 175 EReILRRH 182
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4687-5321 |
1.21e-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: 65.42 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4687 KDVSDQIGNEEQV-EDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDfdgkmHDGELEEQEEDDEKSDSEGGDLDkhmGD 4765
Cdd:COG5271 408 SPTSDTDEEEEEAdEDASAGETEDESTDVTSAEDDIATDEEADSLAD-----EEEEAEAELDTEEDTESAEEDAD---GD 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4766 LNGEEADKLDERLwgdddeeedeEEEDNKTEETGPGMDEEDSELVAKDDNLDSgNSNKDKSQQDKKEEkeeaeaddggqg 4845
Cdd:COG5271 480 EATDEDDASDDGD----------EEEAEEDAEAEADSDELTAEETSADDGADT-DAAADPEDSDEDAL------------ 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4846 EDKINEQIDERDYDEN---EVDPYHGNQEKVPEPEALDLPDDLNLDSEDKNggedtdneEGEEENPLEIKEKPEEAGHEA 4922
Cdd:COG5271 537 EDETEGEENAPGSDQDadeTDEPEATAEEDEPDEAEAETEDATENADADET--------EESADESEEAEASEDEAAEEE 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4923 EERGE-TETDQNESQSPQEPEEGPSEDDKAEGEEEmDTGADDQDGDAAQHPEEHSEEQQQSVEEKDKEADEEGGENGPAD 5001
Cdd:COG5271 609 EADDDeADADADGAADEEETEEEAAEDEAAEPETD-ASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAA 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5002 QGFQPQEEEEREDSDTE-EQVPEALERKEhascgqtgVENMQNTQAMELAGAAPEKEQGKEEHGSGAADANQAEghESNF 5080
Cdd:COG5271 688 AAEASDDEEETEEADEDaETASEEADAEE--------ADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEE--EAEE 757
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5081 IAQLASqkhtrkntqsfkrkpGQADNERsmgDHNERVHKRLRTVDTDshAEQGPAQQPQAQVEDADAFEHIKQGSDAYDA 5160
Cdd:COG5271 758 AEEAEE---------------DDADGLE---EALEEEKADAEEAATD--EEAEAAAEEKEKVADEDQDTDEDALLDEAEA 817
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5161 Q---TYDVASKEQQQSAKDSGKDQEEEEIEDTLMDTEEQEefKAADVEQLKPEEIKSGTTAPLGFDEMEVEIQTVKTEED 5237
Cdd:COG5271 818 DeeeDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKD--VDADLDLDADLAADEHEAEEAQEAETDADADADAGEAD 895
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5238 QDPRTDKAHKETENEKPERSRESTIHTAHQFLMDTIFQPFLKDVNELRQELERQLEMwqprESGNPEEEKVAAEMWQSYL 5317
Cdd:COG5271 896 SSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALAL----DEAGDEESDDAAADDAGDD 971
|
....
gi 24415404 5318 ILTA 5321
Cdd:COG5271 972 SLAD 975
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
672-902 |
2.62e-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: 58.46 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 672 PVLLVGETGTGKTSTIQYLAH-ITGHRLRVVNMNQQSDTADLLGGYKPvdhkliwlplreafeelfaqtfskkqnftflg 750
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 751 hiqtcyrqkrwhdllrlmqhvhksavnkdgkdsetgllikekweafglrlnhaqqqmkmteNTLLFAFVEGTLAQAVKKG 830
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24415404 831 EWILLDEINLAAPEILECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 902
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4912-5253 |
4.11e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4912 KEKPEEAGHEAEERGETETDQNESQSPQEPEEGPSEDDKAEGEEEMDTGAD------------------DQDGDAAQHPE 4973
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeakkadeakkkaeeakkaDEAKKKAEEAK 1496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4974 EHSEEQQQSVEEKDKEADEEGGENG-PADQGFQPQEEEEREDSDTEEQVPEALERKEhascgqtgVENMQNTQAMELAGA 5052
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAkKADEAKKAEEAKKADEAKKAEEKKKADELKK--------AEELKKAEEKKKAEE 1568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5053 APEKEQGKEEHGSGAADANQAEGHESNFIAQLASQKHTRKNTQSFKrkpgqADNERSMGDHNERVHKRLRTVDTDSHAEQ 5132
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5133 gpaqqpqaqvEDADAFEHIKQGSDAYDAQTYDVASK--EQQQSAKDSGKDQEEEEIEDTLMDTEEQEEFKAADVEQLKPE 5210
Cdd:PTZ00121 1644 ----------EEKKKAEELKKAEEENKIKAAEEAKKaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24415404 5211 EIKSGTTAPLGFDEMEVEIQTVKTEEDQDPRTDKAHKETENEK 5253
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4757-5029 |
5.87e-09 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 63.09 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4757 GDLDK-------HMGDLNGEEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDSELVAKDDNLDSGNSNKDKSQQD 4829
Cdd:TIGR00927 628 GDLSKgdvaeaeHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHK 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4830 KKEEKEEAEADDGGQgedkineqiDERDYDENEVDPYHGNQEKVPEPEALDLPDDLNLDSEDKNGGEDTDNEEGEEENPL 4909
Cdd:TIGR00927 708 GETEAEEVEHEGETE---------AEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDE 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4910 EikEKPEEAGHEAEERGETETDQNESQSPQEPEEGPSEDDKAEGEEEMDTGADDQDGDAAQHPEEHSEEQQQSveekdke 4989
Cdd:TIGR00927 779 D--EGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDE------- 849
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 24415404 4990 adeEGGENGPADQGFQPQEEEEREDSDTEEQVPEALERKE 5029
Cdd:TIGR00927 850 ---KGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEE 886
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4659-5261 |
9.04e-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: 62.34 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4659 EFMEDSAGEGATEFH-DYEGGGIGEGEGMKDVSDQIGNEEQVEDTFQKGQEKDKEDPDSksdikGEDNAIEMSEDFDGKM 4737
Cdd:COG5271 219 DDLAAEEGASAVVEEeDASEDAVAAADETLLADDDDTESAGATAEVGGTPDTDDEATDD-----ADGLEAAEDDALDAEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4738 HDGELEEQEEDDEKSDSEGGDLDKHMGDLNGEEADKLDERLwGDDDEEEDEEEEDNKTEETGPGMDEEDSELV---AKDD 4814
Cdd:COG5271 294 TAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAAD-DEDDDDSAAEDAAEEAATAEDSAAEDTQDAEdeaAGEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4815 NLDSGNSNKDKSQQDKKEEKEEAEADDGGQGEDKINEQIDErDYDENEVDPyhGNQEKVPEPEALDLPDDLNLDSEDKNG 4894
Cdd:COG5271 373 ADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDT-DEEEEEADE--DASAGETEDESTDVTSAEDDIATDEEA 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4895 GEDTDNEEGEEENPLEIKEKPEEAGHEAEERGETETDQNESQSPQEPEEGPSEDDKAEGEEEMDTGADDQ-DGDAAQHPE 4973
Cdd:COG5271 450 DSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGaDTDAAADPE 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4974 EHSEEqqqSVEEKDKEADEEGGENGPADQGFQPQEEEEREDSDTEEQvpEALERKEHASCGQTGVENMQNTQAMELAGAA 5053
Cdd:COG5271 530 DSDED---ALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEA--ETEDATENADADETEESADESEEAEASEDEA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5054 PEKEQGKEEH----GSGAAD---ANQAEGHESNFIAQLASQKHTRKNTQSFKRKPGQADNERSMG-DHNErvhkrlrTVD 5125
Cdd:COG5271 605 AEEEEADDDEadadADGAADeeeTEEEAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAeDESE-------TSS 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5126 TDSHaeqgpaqqpqaqvEDADAFEhikqGSDAYDAQTYDVASKEQQQSAKDSGKDQEEEEIEDT-LMDTEEQEEFKAADv 5204
Cdd:COG5271 678 EDAE-------------EDADAAA----AEASDDEEETEEADEDAETASEEADAEEADTEADGTaEEAEEAAEEAESAD- 739
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 24415404 5205 eqlkpeeiKSGTTAPLGFDEMEVEIQTVKTEEDQDprtDKAHKETENEKPERSREST 5261
Cdd:COG5271 740 --------EEAASLPDEADAEEEAEEAEEAEEDDA---DGLEEALEEEKADAEEAAT 785
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5385-5535 |
1.05e-08 |
|
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: 57.85 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5385 ICLAIDDSSSMVDNhTKQLAFESLAVIGNALTLLEVG-QIAVCSFGESVKLLHPFHeqfSDYSGSQILRLCKFQQKK--- 5460
Cdd:smart00327 2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgg 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24415404 5461 -TKIAQFLESVANMFAAAQQLSQnisSETAQLLLVVSDGRGLFleGKERVLAAVQAARNANIFVIFVVLDNPSSRD 5535
Cdd:smart00327 78 gTNLGAALQYALENLFSKSAGSR---RGAPKVVILITDGESND--GPKDLLKAAKELKRSGVKVFVVGVGNDVDEE 148
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2220-2306 |
2.51e-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: 55.76 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 2220 GTFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPGgvltisERGMIDGSTPTITPNPNFRLFLSMDPVHGD- 2298
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER------RLLLPDGGELVKAAPDGFRLIATMNPLDRGl 124
|
90
....*....|
gi 24415404 2299 --ISRAMRNR 2306
Cdd:pfam07728 125 neLSPALRSR 134
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4912-5312 |
6.60e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4912 KEKPEEAGHEAEERGETETDQNESQSPQEPEEGPSEDDKAEGEEEMDTGADD--QDGDAAQHPEEHSEEQQQSveekdke 4989
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEakKKADEAKKAAEAKKKADEA------- 1515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4990 adEEGGENGPADQGFQPQEEEEREDSDTEEQVPEALERKEhascgqtgVENMQNTQAMELAGAAPEKEQGKEEHGSGAAD 5069
Cdd:PTZ00121 1516 --KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK--------AEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5070 ANQAEGHESNFIAQLASQKHTRKNTQSFKrkpgqADNERSMGdhnERVHKrlrtvdtdshAEQGPAQQPQAQVEDAdafE 5149
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKA---EELKK----------AEEEKKKVEQLKKKEA---E 1644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5150 HIKQGSDAYDAQTYDVASKEQQQSAKDSGKDQEEEeiedtlMDTEEQEEFKAADVEQLKPEEIKSGTTAPLGFDEMEVEI 5229
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE------AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5230 QTV-KTEEDQDPRTDKAHKETENEKpERSRESTIHTAHQFLMDTIFQPFLKDVNELRQELERQLEmwqprESGNPEEEKV 5308
Cdd:PTZ00121 1719 EELkKAEEENKIKAEEAKKEAEEDK-KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE-----EELDEEDEKR 1792
|
....
gi 24415404 5309 AAEM 5312
Cdd:PTZ00121 1793 RMEV 1796
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1383-1540 |
1.03e-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: 54.30 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1383 GEPVLLVGDTGCGKTTICQVFAALANQKLYSVschLHMETSDFLGGLRPVRQKPNDKEEIDTSRLFEWHDGPLVQAMKED 1462
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV---IYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24415404 1463 -GFFLLDEISLADDSVLERLNSVLEVEKSLVLAEKgspedkdseielltaGKKFRILATMNPGGDFGKKELSPALRNRF 1540
Cdd:smart00382 79 pDVLILDEITSLLDAEQEALLLLLEELRLLLLLKS---------------EKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4658-5315 |
1.13e-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: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4658 KEFMEDSAGEGATEFHDYEGGGIGEGEGMKDVSDQIGNEEQVEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDFDGKM 4737
Cdd:COG5271 61 ASDEGKLLDLKSADGAALSAESDAGASLITAANLEEGDIAGNAADDSADEESDANAKEDATDDADSSGDAQGDPLATDTL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4738 HDGELEEQEEDDEKSDSEGGDLDKH---MGDLNGEEADKLDER-------LWGDDDEEEDEEEEDNKTEETGPGMDEEDS 4807
Cdd:COG5271 141 GGGDLDLATKDGDELLPSLADNDEAaadEGDELAADGDDTLAVadaieatPGGTDAVELTATLGATVTTDPGDSVAADDD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4808 ELVAKDDNLDSGNS------NKDKSQQDKKEEKEEAEADDGGQG---EDKINEQIDERDYDENEVDPYHGNQEKVPEP-- 4876
Cdd:COG5271 221 LAAEEGASAVVEEEdasedaVAAADETLLADDDDTESAGATAEVggtPDTDDEATDDADGLEAAEDDALDAELTAAQAad 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4877 -EALDLPDDLNLDSEDKNGGEDTDNEEGEEENPLEIKEKPEEAGHEAEERGETETDQNESQSPQEPEEGPSEDDKAEGEE 4955
Cdd:COG5271 301 pESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGAD 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4956 EMDTGADDQ-DGDAAQHPEEHSEEQQQSVEEKDKEADE------EGGENGPADQGFQPQEEEEREDS------DTEEQVP 5022
Cdd:COG5271 381 TDAAADEADaAADDSADDEEASADGGTSPTSDTDEEEEeadedaSAGETEDESTDVTSAEDDIATDEeadslaDEEEEAE 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5023 EALERKEHASCGQTGVENMQNTQAMELAGAAPEKEQGKEEHGSGAADANQAEGHESNFIAQlasqkhtrknTQSFKRKPG 5102
Cdd:COG5271 461 AELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGAD----------TDAAADPED 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5103 QAdnERSMGDHNErVHKRLRTVDTDSHAEQGPAQQPQAQVEDADAFE-HIKQGSDAYDAQTYDVASKEQQQSAKDSGKDQ 5181
Cdd:COG5271 531 SD--EDALEDETE-GEENAPGSDQDADETDEPEATAEEDEPDEAEAEtEDATENADADETEESADESEEAEASEDEAAEE 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5182 EEEEIEDTLMDTEEQEEFKAADVEQLKPEEIKSGTTAPLGFDEMEVEIQTVKTEEDQDPRTDKAHKETENEKPERSREST 5261
Cdd:COG5271 608 EEADDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAA 687
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 24415404 5262 IHTAhqfLMDTIfQPFLKDVNELRQELERQLEMWQPRESGNPEEEKVAAEMWQS 5315
Cdd:COG5271 688 AAEA---SDDEE-ETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAES 737
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4688-5255 |
2.38e-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: 57.72 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4688 DVSDQIGNEEQVEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDFDGKmhDGELEEQEEDDEKSDSEGGDLDKHMGDL- 4766
Cdd:COG5271 360 DTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTS--PTSDTDEEEEEADEDASAGETEDESTDVt 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4767 NGEEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDSELVAKDDNLDSGNSNKDKSqqdkkeekeeaEADDGGQGE 4846
Cdd:COG5271 438 SAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAE-----------EDAEAEADS 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4847 DKINEQIDERDyDENEVDPYHGNQEKVPEPEALDLPDDLNLDSEDKNGGEDTDNEEGEEENPLEIKEKPEEAGHEAEERG 4926
Cdd:COG5271 507 DELTAEETSAD-DGADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADAD 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4927 ETETDQNESQSPQEPEEGPSEDDKAEGEE---EMDTGADDQDGDAAQHPEEHSEEQQqsveekdkeadeegGENGPADQG 5003
Cdd:COG5271 586 ETEESADESEEAEASEDEAAEEEEADDDEadaDADGAADEEETEEEAAEDEAAEPET--------------DASEAADED 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5004 FQPQEEEEREDSDTEEQVPEALERKEhascgqtgveNMQNTQAMELAGAAPEKEQGKEEHGSGAADANQAEGHESNFIAQ 5083
Cdd:COG5271 652 ADAETEAEASADESEEEAEDESETSS----------EDAEEDADAAAAEASDDEEETEEADEDAETASEEADAEEADTEA 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5084 LASQKHTRKNTQsfkrKPGQADNERSmgdhnervhkrLRTVDTDshAEQGPAQQPQAQVEDADAF-EHIKQGSDAYDAQT 5162
Cdd:COG5271 722 DGTAEEAEEAAE----EAESADEEAA-----------SLPDEAD--AEEEAEEAEEAEEDDADGLeEALEEEKADAEEAA 784
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5163 YDvASKEQQQSAKDSGKDQEEEEIEDTLMDTEEQEEFKAADVEQlkpeeiksgttaplgfdemeveiqtvKTEEDQDPRT 5242
Cdd:COG5271 785 TD-EEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGED--------------------------EETADEALED 837
|
570
....*....|...
gi 24415404 5243 DKAHKETENEKPE 5255
Cdd:COG5271 838 IEAGIAEDDEEDD 850
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1372-1540 |
2.98e-07 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 55.56 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1372 LAMLVGRalefgePVLLVGDTGCGKTTICQVFAALANQKLYSVSCHLHMETSDFLGglrpvrqkpndkEEI---DTSRlF 1448
Cdd:COG0714 26 IALLAGG------HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILG------------TYIydqQTGE-F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1449 EWHDGPLVQamkedGFFLLDEISLADDSVLerlNSVLEV--EKSLVLAEkgspedkdseiELLTAGKKFRILATMNPGGD 1526
Cdd:COG0714 87 EFRPGPLFA-----NVLLADEINRAPPKTQ---SALLEAmeERQVTIPG-----------GTYKLPEPFLVIATQNPIEQ 147
|
170
....*....|....
gi 24415404 1527 FGKKELSPALRNRF 1540
Cdd:COG0714 148 EGTYPLPEAQLDRF 161
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
1749-1888 |
3.64e-07 |
|
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: 52.17 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1749 ILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWRDGPLLAALkaghwVVLDELNLA 1828
Cdd:pfam07726 2 VLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQ--KTREFEFRPGPVFANV-----LLADEINRA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24415404 1829 S---QSVLegLNACFDHR----GEIY-VPELGMsfqvqhektkIFGCQNPFRQGGGRKgLPRSFLNRF 1888
Cdd:pfam07726 75 PpktQSAL--LEAMQERQvtidGETHpLPEPFF----------VLATQNPIEQEGTYP-LPEAQLDRF 129
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4913-5198 |
6.57e-07 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 56.16 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4913 EKPEEAGHEAEERGETETDQNESQSPQEPEEGPSEDdkaEGEEEMDTGADDQDGDAAQHPEEHSEEQQqsveekdkeade 4992
Cdd:TIGR00927 658 ENGEESGGEAEQEGETETKGENESEGEIPAERKGEQ---EGEGEIEAKEADHKGETEAEEVEHEGETE------------ 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4993 eggENGPADQG-FQPQEE-EEREDSD-TEEQVPEALERKehascGQTGVENMQNTQAMELAGAAPEKEQGKEEHGSGAAD 5069
Cdd:TIGR00927 723 ---AEGTEDEGeIETGEEgEEVEDEGeGEAEGKHEVETE-----GDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGD 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5070 anqaEGHEsnfiaqlasqkhtrkntqsfkrkpGQADNERSMGDHNERVHKRLRTVDTDSHAEQGPAQQPQAQVEDADAFE 5149
Cdd:TIGR00927 795 ----EGAE------------------------GKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAK 846
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 24415404 5150 HIKQGSDayDAQTYDVASKEQQQSAKDSGKDQEEEEIEdtlmdtEEQEE 5198
Cdd:TIGR00927 847 QDEKGVD--GGGGSDGGDSEEEEEEEEEEEEEEEEEEE------EEEEE 887
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1746-1896 |
6.74e-07 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 52.15 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1746 KKPILLEGSPGVGKTSLVGALAKAS---GNTLVRINLSeqtditDLFGADlpVEGGKGGEFAWRDGPLLAALKAGHWVVL 1822
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFI 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24415404 1823 DELNLASQSVLEGLNACFdhrgeiyvpELGMSFQVQHEKTKIFG-CQNPFRQgggrkGLPRSFLNRFTQVFVDPL 1896
Cdd:cd00009 91 DEIDSLSRGAQNALLRVL---------ETLNDLRIDRENVRVIGaTNRPLLG-----DLDRALYDRLDIRIVIPL 151
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4796-5311 |
9.33e-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: 55.79 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4796 EETGPGMDEEDSELVAKDDNLDSGNSNKDKSQQDKKEEKEEAEADDGGQGEDKINEQIDERDYDENEVDPYHGNQEKVPE 4875
Cdd:COG5271 311 TLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4876 PEALDLPDDLNLDSEDKNGGEDTDNEEGEEENPLEIKEKPEEAGHEAEERGETETDQNESQSPQEPEEGPSEDDKAEGEE 4955
Cdd:COG5271 391 AADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4956 EMDTGAD-DQDGDAAQHPEEHSEEQQQSVEEKDKEADEEGGENGPADQGFQPQEEEEREDSDtEEQVPEALERKEHASCG 5034
Cdd:COG5271 471 SAEEDADgDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSD-EDALEDETEGEENAPGS 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5035 QTgvenmqntqamelagAAPEKEQGKEEHGSGAADANQAEghesnfiaqlASQKHTRKNTQSFKRKPGQADNERSMGDhn 5114
Cdd:COG5271 550 DQ---------------DADETDEPEATAEEDEPDEAEAE----------TEDATENADADETEESADESEEAEASED-- 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5115 ervhKRLRTVDTDSHAEqgpaqqpqaqveDADAfEHIKQGSDAYDAQTYDVASKEQQQSAKDSGKDQEEEEIEDTLMDTE 5194
Cdd:COG5271 603 ----EAAEEEEADDDEA------------DADA-DGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASADES 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5195 EQEEFKAADVEQLKPEEIKSGTTAPLGFDEMEVEiqtvktEEDQDPRT---DKAHKETENEKPERSRESTIHTAHQFLMD 5271
Cdd:COG5271 666 EEEAEDESETSSEDAEEDADAAAAEASDDEEETE------EADEDAETaseEADAEEADTEADGTAEEAEEAAEEAESAD 739
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24415404 5272 --TIFQPFLKDVNELRQELERQLEMWQPRESGNPEEEKVAAE 5311
Cdd:COG5271 740 eeAASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAE 781
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4912-5249 |
1.20e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4912 KEKPEEAGHEAEERGETETDQNESQSPQEPEEGP--SEDDKAEGEEEMDTGADDQDGDAAQHPEE--HSEEQQQSVEEKD 4987
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKkkAEEAKKKADEAKKAAEAKKKADEAKKAEEakKADEAKKAEEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4988 KEADEEGGENGPADQGFQPQEEEEREDSDTEEQVPEALERKEHASCGQTGVENMQNTQAMELAGAAPEKEQGKEEHGSGA 5067
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5068 ADAN-QAEghesnfiaQLASQKHTRKNTQSFKRKPGQ------------------ADNERSMGDHNERVHKRLRTVDTDs 5128
Cdd:PTZ00121 1616 EEAKiKAE--------ELKKAEEEKKKVEQLKKKEAEekkkaeelkkaeeenkikAAEEAKKAEEDKKKAEEAKKAEED- 1686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5129 haEQGPAQQPQAQVEDADAFEHIKQGS--DAYDAQTYDVASKEQQQSAKDSGKDQEEEEIEDTLMDTEEQEEFKaadVEQ 5206
Cdd:PTZ00121 1687 --EKKAAEALKKEAEEAKKAEELKKKEaeEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK---IAH 1761
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 24415404 5207 LKPEEIKSgttAPLGFDEMEVEIQTVKTEEDQDPR--TDKAHKET 5249
Cdd:PTZ00121 1762 LKKEEEKK---AEEIRKEKEAVIEEELDEEDEKRRmeVDKKIKDI 1803
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1301-1618 |
1.42e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 54.35 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1301 DGYMLLAGRVRKQEEIDVIQEVLEKHFKKKLcpqSLFSKENVLKLLGKLSTQISTLECNFGHIVWTEGMR--RLAMLVGR 1378
Cdd:PHA02244 42 DAIREKAETEGKEIAIDDIKKEIEDSPEEQF---FELPVKIELQQEGKPAGDISGIDTTKIASNPTFHYEtaDIAKIVNA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1379 ALefgePVLLVGDTGCGKTTICQVFAALANQKLYSvschlhmetsdflggLRPVRQKPNDKEEIDTSRLFewHDGPLVQA 1458
Cdd:PHA02244 119 NI----PVFLKGGAGSGKNHIAEQIAEALDLDFYF---------------MNAIMDEFELKGFIDANGKF--HETPFYEA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1459 MKEDGFFLLDEISLADDSVLERLNSVLevekslvlaekgSPEDKDSEIELLTAGKKFRILA---TMNPGGD---FGKKEL 1532
Cdd:PHA02244 178 FKKGGLFFIDEIDASIPEALIIINSAI------------ANKFFDFADERVTAHEDFRVISagnTLGKGADhiyVARNKI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1533 SPALRNRFTEIWCPQSTSREDLIqiishnlrpglclgridpkgSDIPEVMLDFIDWLTHQ--EFGRKCVVSIRDILSWVN 1610
Cdd:PHA02244 246 DGATLDRFAPIEFDYDEKIEHLI--------------------SNGDEDLVNFVALLRHEmaEKGLDHVFSMRAIIHGKK 305
|
....*...
gi 24415404 1611 FMNKMGEE 1618
Cdd:PHA02244 306 FDGVFEAD 313
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1016-1234 |
1.69e-06 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 54.39 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1016 PGNVKSLLKQPIPEPKGGRLIQVEGYWIAVGDKEPTIDETYILTSSVKLNLRDIVRVVSAGTYP--VLIQGETSVGKTSL 1093
Cdd:COG1401 158 LEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKTKknVILAGPPGTGKTYL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1094 IQWLAAATG---NHCVRI-----NNHEHTDIQEYigcYTSDSSGKLVFKEGVLIDAMRKG-------YWIILDELNLAPT 1158
Cdd:COG1401 238 ARRLAEALGgedNGRIEFvqfhpSWSYEDFLLGY---RPSLDEGKYEPTPGIFLRFCLKAeknpdkpYVLIIDEINRANV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1159 D--------VLEALNRLLDDNRELLVTETQEVVKAHPRFMLFATQNPP--GLYGGRKVLSRAFRNRFVELHFDELPSSEL 1228
Cdd:COG1401 315 EkyfgellsLLESDKRGEELSIELPYSGEGEEFSIPPNLYIIGTMNTDdrSLALSDKALRRRFTFEFLDPDLDKLSNEEV 394
|
....*.
gi 24415404 1229 ETILHK 1234
Cdd:COG1401 395 VDLLEE 400
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4916-5210 |
1.77e-06 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 55.00 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4916 EEAGHEAEERGETETDQNESQSPQEPEEGP-SEDDKAEGEEEMDTGADDQDGDAAQHPEEHSEEQQQSveekdkeADEEG 4994
Cdd:TIGR00927 632 KGDVAEAEHTGERTGEEGERPTEAEGENGEeSGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEI-------EAKEA 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4995 GENGPADQGFQPQEEEEREDSDTEEQVPEALERKEhaSCGQTGVENMQNTQAMELAGAAPEKEQGKEEHGSGAADANQAE 5074
Cdd:TIGR00927 705 DHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGE--EVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGE 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5075 GHesnfiaqlASQKHTRKNTQSfkrKPGQADNERSMGDHNERVHKRLRTVDTDSHAEQGPAQQPQAQVEDADAFEHIKQG 5154
Cdd:TIGR00927 783 IQ--------AGEDGEMKGDEG---AEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKG 851
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 24415404 5155 SDayDAQTYDVASKEQQQsakdsgkdQEEEEIEDTLMDTEEQEEFKAADVEQLKPE 5210
Cdd:TIGR00927 852 VD--GGGGSDGGDSEEEE--------EEEEEEEEEEEEEEEEEEEEEENEEPLSLE 897
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4913-5074 |
1.78e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 54.21 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4913 EKPEEAGHEA-------EERGETETDQNESQSPQEPEEGPSEDDKAEGEEEMDTGADDQDGDAAQHPEEHSEEQQQSvee 4985
Cdd:PHA03169 136 PPPSPPSHPGphepappESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPG--- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4986 kdkEADEEGGENGPADQGfqpQEEEEREDSDTEEQVPEAlERKEHASCGQTGVENMQNTQamelAGAAPE---KEQGKEE 5062
Cdd:PHA03169 213 ---EPQSPTPQQAPSPNT---QQAVEHEDEPTEPEREGP-PFPGHRSHSYTVVGWKPSTR----PGGVPKlclRCTSHPS 281
|
170
....*....|..
gi 24415404 5063 HGSGAADANQAE 5074
Cdd:PHA03169 282 HRSRLPEGQQSE 293
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1738-1828 |
4.30e-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: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1738 RLLRATKLKKPILLEGSPGVGKTSLVGALAKA-SGNTLVRINLseqtdIT---DLFGADLpVEG----GKGGEFAWRDGP 1809
Cdd:COG1401 213 AFLAALKTKKNVILAGPPGTGKTYLARRLAEAlGGEDNGRIEF-----VQfhpSWSYEDF-LLGyrpsLDEGKYEPTPGI 286
|
90 100
....*....|....*....|....*.
gi 24415404 1810 LL-AALKAG------HWVVLDELNLA 1828
Cdd:COG1401 287 FLrFCLKAEknpdkpYVLIIDEINRA 312
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4916-5077 |
4.74e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 52.67 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4916 EEAGHEAEERGETETDQNESQSPQEPEEGPSEDDKAEGEEEMDtGADDQDGDAAQhPEEH--SEEQQQSveekdkeaDEE 4993
Cdd:PHA03169 98 ESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSP-PSHPGPHEPAP-PESHnpSPNQQPS--------SFL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4994 GGENGPADQGFQPQEEEEREDSDTEEQVPEALERKEHASCGQTGVENMQNTqamelAGAAPEKEQGKEEHGSGAADANQA 5073
Cdd:PHA03169 168 QPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPT-----PQQAPSPNTQQAVEHEDEPTEPER 242
|
....
gi 24415404 5074 EGHE 5077
Cdd:PHA03169 243 EGPP 246
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1749-1784 |
7.20e-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: 48.74 E-value: 7.20e-06
10 20 30
....*....|....*....|....*....|....*.
gi 24415404 1749 ILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTD 1784
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS 36
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
5383-5540 |
1.38e-05 |
|
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.
Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 48.72 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5383 YQICLAIDDSSSMVD---NHTKQLAfesLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQK 5459
Cdd:cd00198 1 ADIVFLLDVSGSMGGeklDKAKEAL---KALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5460 -KTKIAQFLEsvanmfAAAQQLSQNISSETAQLLLVVSDGRglFLEGKERVLAAVQAARNANIFVIFVVLDNPSSRDSIL 5538
Cdd:cd00198 78 gGTNIGAALR------LALELLKSAKRPNARRVIILLTDGE--PNDGPELLAEAARELRKLGITVYTIGIGDDANEDELK 149
|
..
gi 24415404 5539 DI 5540
Cdd:cd00198 150 EI 151
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1744-1781 |
1.50e-05 |
|
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: 48.43 E-value: 1.50e-05
10 20 30
....*....|....*....|....*....|....*...
gi 24415404 1744 KLKKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSE 1781
Cdd:cd19481 24 GLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4913-5078 |
3.04e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 50.35 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4913 EKPEEAGH-EAEERGE--TETDQNESQSPQEPEEGPSEDDKAEGEEEMDTGADDQDGDAAQ--------HPEEHSEEQQQ 4981
Cdd:PHA03169 74 ETAEESRHgEKEERGQggPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHspppsppsHPGPHEPAPPE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4982 SveekdkeadEEGGENGPADQGFQPQEE---EERE--DSDTEEQVPEALERKEHASCGQtgvenmqntqamelaGAAPEK 5056
Cdd:PHA03169 154 S---------HNPSPNQQPSSFLQPSHEdspEEPEppTSEPEPDSPGPPQSETPTSSPP---------------PQSPPD 209
|
170 180
....*....|....*....|....
gi 24415404 5057 EQGKE--EHGSGAADANQAEGHES 5078
Cdd:PHA03169 210 EPGEPqsPTPQQAPSPNTQQAVEH 233
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1068-1221 |
3.83e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 49.73 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1068 DIVRVVSAGTyPVLIQGETSVGKTSLIQWLAAAtgnhcVRINNHEHTDI-QEYIGCYTSDSSGKlvFKEGVLIDAMRKGY 1146
Cdd:PHA02244 111 DIAKIVNANI-PVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAImDEFELKGFIDANGK--FHETPFYEAFKKGG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1147 WIILDELNLAPTDVLEALNRLLDDNRELLVTETqevVKAHPRFMLFATQNPPG-----LYGGRKVLSRAFRNRFVELHFD 1221
Cdd:PHA02244 183 LFFIDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4910-5316 |
3.94e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4910 EIKEKPEEAGHEAEERGETETDQNESQSPQEPEEGPSEDDKAEGEEEMDTGADDQDGDAAQHPEEhSEEQQQSVEEKDKE 4989
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK-ADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4990 ADEEGGENGPADQGFQPQEEEERedsdTEEQVPEALERKEHASCGQTGVEnmQNTQAMELAGAAPEKEQGKEEHGSGAAD 5069
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKK----ADEAKKKAEEAKKKADAAKKKAE--EAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5070 ANQAEGHESNFIAQLASQKHTRKNTQSFKRKPGQADNERSmgdhnERVHKRlrtvdtdsHAEQGPAQQPQAQVEDADAFE 5149
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA-----DELKKA--------AAAKKKADEAKKKAEEKKKAD 1434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5150 HIKQgsDAYDAQTYDVASK--EQQQSAKDSGKDQEEEEIEDTLMDTEEQ-----EEFKAADVEQLKPEEIKSGTTAPLGF 5222
Cdd:PTZ00121 1435 EAKK--KAEEAKKADEAKKkaEEAKKAEEAKKKAEEAKKADEAKKKAEEakkadEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5223 DEMEVEIQTVKTEE----DQDPRTDKAHKETENEKPERSRES-TIHTAHQflmdtifqpfLKDVNELRQELERQLEMWQP 5297
Cdd:PTZ00121 1513 DEAKKAEEAKKADEakkaEEAKKADEAKKAEEKKKADELKKAeELKKAEE----------KKKAEEAKKAEEDKNMALRK 1582
|
410
....*....|....*....
gi 24415404 5298 RESGNPEEEKVAAEMWQSY 5316
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLY 1601
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
4913-5020 |
5.47e-05 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 49.31 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4913 EKPEEAGHEAEERGETETD------QNESQSPQEPEEGPSED-DKAEGEEEMDTGADDQDGDAAQhPEEHSEEQQQSVEE 4985
Cdd:COG5414 217 MKAESVSVVLKDEKELARQervsswENFKEEPGEPLSRPALKkEKQGAEEEGEEGMSEEDLDVGA-AEIENKEVSEGDKE 295
|
90 100 110
....*....|....*....|....*....|....*
gi 24415404 4986 KDKEADEEGGENGPADQGFQPQEEEEREDSDTEEQ 5020
Cdd:COG5414 296 QQQEEVENAEAHKEEVQSDRPDEIGEEKEEDDENE 330
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1368-1543 |
1.49e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 45.21 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1368 GMRRLAMLVGRALEFGEP--VLLVGDTGCGKTTICQVFAALANQKLYSVschLHMETSDFLGGLRpvrqkpndKEEIDTS 1445
Cdd:cd00009 2 GQEEAIEALREALELPPPknLLLYGPPGTGKTTLARAIANELFRPGAPF---LYLNASDLLEGLV--------VAELFGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1446 RLFEWHDGPLVQAMKedGFFLLDEISLADDSVLERLNSVLEVekslvlaekgspedkdsEIELLTAGKKFRILATMNPGG 1525
Cdd:cd00009 71 FLVRLLFELAEKAKP--GVLFIDEIDSLSRGAQNALLRVLET-----------------LNDLRIDRENVRVIGATNRPL 131
|
170
....*....|....*...
gi 24415404 1526 DFgkkELSPALRNRFTEI 1543
Cdd:cd00009 132 LG---DLDRALYDRLDIR 146
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
663-712 |
2.10e-04 |
|
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).
Pssm-ID: 463698 [Multi-domain] Cd Length: 179 Bit Score: 45.46 E-value: 2.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 24415404 663 LAVCVSKGEPVLLVGETGTGKTSTIQ-YLAHI--TGHRLRVVNMNQQSDTADL 712
Cdd:pfam12775 24 LDLLLKNGKPVLLVGPTGTGKTVIIQnLLRKLdkEKYLPLFINFSAQTTSNQT 76
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1746-1782 |
2.23e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 47.61 E-value: 2.23e-04
10 20 30
....*....|....*....|....*....|....*..
gi 24415404 1746 KKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQ 1782
Cdd:PRK04195 39 KKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4912-5074 |
2.35e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 47.27 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4912 KEKPEEAGHEAEERGETETDQNESQSPQEPEE--GPSED-----DKAEGEEEMDTGADDQDGDAAQHPEEHSEEQQQSve 4984
Cdd:PHA03169 48 PPAPTTSGPQVRAVAEQGHRQTESDTETAEESrhGEKEErgqggPSGSGSESVGSPTPSPSGSAEELASGLSPENTSG-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4985 ekdkeadeeGGENGPADQGfqPQEEEEREDSDTEEQVPEalerkEHASCGQTGVENMQNTQAMELAGAAPEKEQGKEEHG 5064
Cdd:PHA03169 126 ---------SSPESPASHS--PPPSPPSHPGPHEPAPPE-----SHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDS 189
|
170
....*....|
gi 24415404 5065 SGAADANQAE 5074
Cdd:PHA03169 190 PGPPQSETPT 199
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
1736-1790 |
3.52e-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: 44.86 E-value: 3.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 24415404 1736 AQRLLRAtKLKKPIL-LEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFG 1790
Cdd:cd19500 27 AVRKLKG-SMKGPILcLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRG 81
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1079-1221 |
4.29e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1079 PVLIQGETSVGKTSLIQ---WLAAATGNHCVRIN----NHEHTDIQEYIGCYTSDSSGKLVFKEGVLIDAMRKGYW--II 1149
Cdd:smart00382 4 VILIVGPPGSGKTTLARalaRELGPPGGGVIYIDgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24415404 1150 LDELNLAPTDVLEALNRLLDDNRELLVTEtqevvKAHPRFMLFATQNPPGLygGRKVLSRAFRNRFVELHFD 1221
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLK-----SEKNLTVILTTNDEKDL--GPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
669-737 |
6.23e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.52 E-value: 6.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24415404 669 KGEPVLLVGETGTGKTSTIQYLAHI---TGHRLRVVNMNQQSDTADLLGGYKPVDHKLIWLPLREAFEELFA 737
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA 72
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4690-5189 |
6.40e-04 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 46.55 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4690 SDQIGNEEQVEDTFQKGQEKDK-----------EDPDSKSDIKGEDNAIEMSEDFDGKMHDGELEEQEEDDEKSDSEGGD 4758
Cdd:COG5271 549 SDQDADETDEPEATAEEDEPDEaeaetedatenADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEET 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4759 LDKHMGDLN-----------GEEADKLDErlwgDDDEEEDEEEEDNKTEETGPGMDEEDSELVAKDDNLDSGNSNkdKSQ 4827
Cdd:COG5271 629 EEEAAEDEAaepetdaseaaDEDADAETE----AEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETE--EAD 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4828 QDKKEEKEEAEADDGGQGEDKINEQIDERDYDENEVDPYHGNQEKVPEPEALDLPDDLNLDSEDKNggedtdneegeeen 4907
Cdd:COG5271 703 EDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADG-------------- 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4908 pleIKEKPEEAGHEAEergETETDQNESQSPQEPEEGPSEDDKAEGEEEMDTGADDQDGDAAQHPEEHSEEQQQSVeekd 4987
Cdd:COG5271 769 ---LEEALEEEKADAE---EAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDI---- 838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4988 keadeeggENGPADQGFQPQEEEEREDSDTEEQVPEALERKEHASCGQTGVENMQNTQAMELAGAAPEKEQGKEEHGSGA 5067
Cdd:COG5271 839 --------EAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAA 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5068 ADANQAEGhESNFIAQLASQKHTRKNTQSFKRKPGQADNERSMGDHNErvhkrlrTVDTDSHAEQGPAQQPQAQVEDADA 5147
Cdd:COG5271 911 EDADSDDG-ANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGD-------EESDDAAADDAGDDSLADDDEALAD 982
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24415404 5148 FEHIKQGsdayDAQTYDVASKEQQQSAKDSGKDQEEEEIEDT 5189
Cdd:COG5271 983 AADDAEA----DDSELDASESTGEAEGDEDDDELEDGEAAAG 1020
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4911-5077 |
7.25e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 46.14 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4911 IKEKPEEAGHEAEERGETETDQNESQSpQEPEEGPSEDDKAEGEEEmdtGADDQDGDAAQHPEEHSEEQQQSVEEKDKEA 4990
Cdd:TIGR00927 706 HKGETEAEEVEHEGETEAEGTEDEGEI-ETGEEGEEVEDEGEGEAE---GKHEVETEGDRKETEHEGETEAEGKEDEDEG 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4991 DEEGGENG--PADQGFQPQEEEEREDSDTEEQVPEALERKEHASCGQTGVENMQNTQAmELAGAAPEKEQGKEehGSGAA 5068
Cdd:TIGR00927 782 EIQAGEDGemKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNA-ENQGEAKQDEKGVD--GGGGS 858
|
....*....
gi 24415404 5069 DANQAEGHE 5077
Cdd:TIGR00927 859 DGGDSEEEE 867
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4933-5032 |
7.93e-04 |
|
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443611 [Multi-domain] Cd Length: 608 Bit Score: 45.94 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4933 NESQSPQEPEEGPSEDDKAEGEEEMDTGADDQDGDAAQHPEEHSEEQQQSveekdkeadEEGGENGPADQGfqPQEEEER 5012
Cdd:COG4547 209 EELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAEDAEASGDD---------AEEGESEAAEAE--SDEMAEE 277
|
90 100
....*....|....*....|
gi 24415404 5013 EDSDTEEQVPEALERKEHAS 5032
Cdd:COG4547 278 AEGEDSEEPGEPWRPNAPPP 297
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1741-1790 |
9.82e-04 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 45.70 E-value: 9.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 24415404 1741 RATKLKKPIL-LEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFG 1790
Cdd:PRK10787 343 RVNKIKGPILcLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRG 393
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1079-1215 |
1.19e-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: 42.90 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1079 PVLIQGETSVGKTSLIQ---WLAAATGNHCVRINNHEHTDIqeyigcyTSDSSGKLVFKEGVLIDAMRKGYW--IILDEL 1153
Cdd:cd00009 21 NLLLYGPPGTGKTTLARaiaNELFRPGAPFLYLNASDLLEG-------LVVAELFGHFLVRLLFELAEKAKPgvLFIDEI 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24415404 1154 NLAPTDVLEALNRLLDDnRELLVTETQEVvkahpRFMLFATQNPPGLyggrkvLSRAFRNRF 1215
Cdd:cd00009 94 DSLSRGAQNALLRVLET-LNDLRIDRENV-----RVIGATNRPLLGD------LDRALYDRL 143
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1724-1800 |
1.21e-03 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 43.32 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1724 DYALSAGTTAMNAQRLLRATKLKKPI--LLEGSPGVGKTSLVGALAKA---SGNTLVRINLSEQT---DITDLFGADlPV 1795
Cdd:cd19499 17 DEAVKAVSDAIRRARAGLSDPNRPIGsfLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMekhSVSRLIGAP-PG 95
|
....*
gi 24415404 1796 EGGKG 1800
Cdd:cd19499 96 YVGYT 100
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
659-780 |
1.93e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 42.13 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 659 LIEQL--AVCVSKGEPVLLVGETGTGKTSTIQYLAHITGHR-LRVVNMNqqsdTADLLGGYkpVDHKLIWLPLREAFEEL 735
Cdd:cd00009 6 AIEALreALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgAPFLYLN----ASDLLEGL--VVAELFGHFLVRLLFEL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24415404 736 FAqtfsKKQNFT-FLGHIQTCYRQKRWHdLLRLMQHVHKSAVNKDG 780
Cdd:cd00009 80 AE----KAKPGVlFIDEIDSLSRGAQNA-LLRVLETLNDLRIDREN 120
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
4916-5063 |
1.97e-03 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 44.64 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4916 EEAGHEAEERGETETDQNESQ--SPQEPEEGP-SEDDKAEGEEEMDTGADDQDGDAAQHPEEHSEEQQQS---------- 4982
Cdd:pfam01271 191 REKSDEREKSSQESGEDTYRQenIPQEDQVGPeDQEPSEEGEEDATQEEVKRSRPRTHHGRSLPDESSRGgqlgleeeas 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4983 ---------------VEEKDKEADEEGGENGPADQGFQPQEEEEREDSDTEE------------QVPEALERKEHASCGQ 5035
Cdd:pfam01271 271 eeeeeygeesrglsaVQTYLLRLVNARGRGRSEKRAERERSEESEEEELKRAspyeeleitanlQIPPSEEERMLKKAGR 350
|
170 180
....*....|....*....|....*...
gi 24415404 5036 TGVENMQNTQAMELAGAAPEKEQGKEEH 5063
Cdd:pfam01271 351 SPRGRVDEAGALEALEALEEKRKLDLDH 378
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
5166-5294 |
2.42e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 43.92 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5166 ASKEQQQSAKDSGKDQEEEEIEDTLMDTEEQEEFKAADVEQLKPEEIKSGTTAPLGFDEMEVEIQtvkTEEDQDPRTDKA 5245
Cdd:COG5414 256 ALKKEKQGAEEEGEEGMSEEDLDVGAAEIENKEVSEGDKEQQQEEVENAEAHKEEVQSDRPDEIG---EEKEEDDENEEN 332
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 24415404 5246 HKETENEKPERSR-ESTI-HTAHQflMDTIFQP-----FLKDVNELRQELE---RQLEM 5294
Cdd:COG5414 333 ERHTELLADELNElEKGIeEKRRQ--MESATNPilqkrFESQLNVLLKELElkrKQLEM 389
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
320-432 |
2.75e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 41.75 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 320 ASQNAVLLEGPIGCGKTSLVEYLAAVTGRTKPPqLLKVQLGDqtdskMLLGMYRCTDVpGEFVWQPGTLTQAATMGHWIL 399
Cdd:cd00009 17 PPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNASD-----LLEGLVVAELF-GHFLVRLLFELAEKAKPGVLF 89
|
90 100 110
....*....|....*....|....*....|...
gi 24415404 400 LEDIDYAPLDVVSVLIPLLENGELLIPGRGDCL 432
Cdd:cd00009 90 IDEIDSLSRGAQNALLRVLETLNDLRIDRENVR 122
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1080-1215 |
3.10e-03 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 41.04 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 1080 VLIQGETSVGKTSLIQWLAAATGNHCVRINNHEHTDiqEYIGcytsDSSGKLvfkEGVLIDAMRKGYWII-LDELNLAPT 1158
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS--KYVG----ESEKRL---RELFEAAKKLAPCVIfIDEIDALAG 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24415404 1159 DVLEALNRLLDDNRELLVTETQEVVKAHPRFMLFATQNPPGLyggrkvLSRAFRNRF 1215
Cdd:pfam00004 72 SRGSGGDSESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDK------LDPALLGRF 122
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
2228-2294 |
4.69e-03 |
|
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of dynein heavy chain. The chain also contains ATPase activity and microtubule binding ability and acts as a motor for the movement of organelles and vesicles along microtubules. Dynein is also involved in cilia and flagella movement. The dynein subunit consists of at least two heavy chains and a number of intermediate and light chains. The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This C-terminal domain carries the D6 region of the dynein motor where the P-loop has been lost in evolution but the general structure of a potential ATP binding site appears to be retained.
Pssm-ID: 460782 Cd Length: 115 Bit Score: 40.12 E-value: 4.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24415404 2228 MLVQALKSGDWLLMDNVNFCnPSVLDRLNALLEpggvltisergmidgSTPTITPNPNFRLFLSMDP 2294
Cdd:pfam03028 49 LIEEAAKEGGWVLLQNCHLA-LSWMPELEKILE---------------ELPEETLHPDFRLWLTSEP 99
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
1738-1784 |
6.10e-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: 40.87 E-value: 6.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 24415404 1738 RLLRATKlkkPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTD 1784
Cdd:cd19520 30 RLLQPPK---GVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTD 73
|
|
| Sigma54_activ_2 |
pfam14532 |
Sigma-54 interaction domain; |
650-708 |
6.54e-03 |
|
Sigma-54 interaction domain;
Pssm-ID: 434021 [Multi-domain] Cd Length: 138 Bit Score: 40.40 E-value: 6.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 24415404 650 FAATRPSSVLIEQLAVCVSKGEPVLLVGETGTGKTSTIQYLAHITGHRLRVVNMNQQSD 708
Cdd:pfam14532 1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAH 59
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4911-5228 |
6.89e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4911 IKEKPEEAGHEAEE--RGETETDQNESQSPQEPEEGPSEDDKAEGEEEMDTGADDQDGDAAQHPEEHSEEQQQSVEEKDK 4988
Cdd:PTZ00121 1638 LKKKEAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 4989 EADEEGGENGPADQGFQPQEEEEREDSDTEEQVPEALERKEHAscgQTGVENMQNTQAMELAGAAPEKEQGKEEHGSGAA 5068
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA---HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5069 DANQaeghesnfiaqlaSQKHTRKNTQSFKRkpGQADNERSMGDHNERVHKRLRTVDTDSHAEQgpaqqpqaqvEDADAF 5148
Cdd:PTZ00121 1795 EVDK-------------KIKDIFDNFANIIE--GGKEGNLVINDSKEMEDSAIKEVADSKNMQL----------EEADAF 1849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24415404 5149 EHIKQGSDAYDAQTydvASKEQQQSAKDSGKDQEEEEIEdtlmDTEEQEEFKAADVEQLKPEEIKSGTTAPLGFDEMEVE 5228
Cdd:PTZ00121 1850 EKHKFNKNNENGED---GNKEADFNKEKDLKEDDEEEIE----EADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
|
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
1741-1779 |
7.33e-03 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 43.08 E-value: 7.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 24415404 1741 RATKLKKPIL-LEGSPGVGKTSLVGALAKASGNTLVRINL 1779
Cdd:COG0466 346 LKKKLKGPILcLVGPPGVGKTSLGKSIARALGRKFVRISL 385
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4912-4978 |
8.12e-03 |
|
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443611 [Multi-domain] Cd Length: 608 Bit Score: 42.47 E-value: 8.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24415404 4912 KEKPEEAGHEAEERGETETDQNESQSPQEPEEG-PSEDDKAEGEEEMDTGADDQDGDAAqhPEEHSEE 4978
Cdd:COG4547 220 EDDEDDSGEQEEDEEDGEDEDEESDEGAEAEDAeASGDDAEEGESEAAEAESDEMAEEA--EGEDSEE 285
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
646-693 |
9.66e-03 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 40.21 E-value: 9.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 24415404 646 EKFTFAaTRPSSVLIEQLAVCVSKGEPVLLVGETGTGKTSTIQYLAHI 693
Cdd:cd03223 4 ENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL 50
|
|
| |
