|
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 ... |
4643-4910 |
5.12e-139 |
|
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: 435.63 E-value: 5.12e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4643 LVSRLGEQLRLILEPTLATKLKGDYKTGKRLNMKRIIPYIASQFRKDKIWLRRTKPSKRQYQIMIALDDSKSMSESKCVK 4722
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4723 LAFDSLCLVSKTLTQLEAGGLSIVKFGENIKEVHSFDQQFSNESGARAFQWFGFQETKTDVKKLVAESTKIFERARAMVH 4802
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4803 NDQ-WQLEIVISDGICEDHETIQKL-VRRARENKIMLVFVIIDGITSNESILDMSQVNYIPDQYGnpqlKITKYLDTFPF 4880
Cdd:cd01460 161 SGSlWQLLLIISDGRGEFSEGAQKVrLREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDKSG----VITPYLDEFPF 236
|
250 260 270
....*....|....*....|....*....|
gi 6323135 4881 EFYVVVHDISELPEMLSLILRQYFTDLASS 4910
Cdd:cd01460 237 PYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
910-1015 |
4.87e-32 |
|
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: 122.31 E-value: 4.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 910 DLLSIIDKYIGKYSVSDEWVgNDIAELYLEAKKLSdNNTIVDGSNQKPHFSIRTLTRTLLYVTDIIHIYGLRRSLYDGFC 989
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLV-RDIVKFYLEAKKLA-EKSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90 100
....*....|....*....|....*.
gi 6323135 990 MSFLTLLDQKSEAILKPVIEKFTLGR 1015
Cdd:pfam17865 79 MSFLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4046-4671 |
7.81e-24 |
|
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: 111.65 E-value: 7.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4046 PQPPSEEVDDKNLQEGTGLGDGEGAQNNNKDVEQDEDLTEDAQNENKEQQDKDERDDENEDDAVEMEGDMAGELEDLSNG 4125
Cdd:COG5271 335 DEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4126 EENDDEDTDSEEEELDEEiddlNEDDPNAIDDKMWDDKASD--NSKEKDTDQNLDGKNQEEDVQAAENDEQ---QRDNKE 4200
Cdd:COG5271 415 EEEEEADEDASAGETEDE----STDVTSAEDDIATDEEADSlaDEEEEAEAELDTEEDTESAEEDADGDEAtdeDDASDD 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4201 GGDEDPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEGEDLEANVPEIETLDlpEDMNLDSEHEESDEDVDMSDGMPD 4280
Cdd:COG5271 491 GDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEE--NAPGSDQDADETDEPEATAEEDEP 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4281 DLNKEEVGNEDEEVkqesgiESDNENDEPGPEEDAGETETALDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQ 4360
Cdd:COG5271 569 DEAEAETEDATENA------DADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPET 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4361 DAAMEENKEKGGEQNTEG-----LDGVEEKADTEDIDQEAAvqQDSGSKGAGADATDTQEQDDVGGSGTTQNTYEE---D 4432
Cdd:COG5271 643 DASEAADEDADAETEAEAsadesEEEAEDESETSSEDAEED--ADAAAAEASDDEEETEEADEDAETASEEADAEEadtE 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4433 QEDVTKNNEESREEATAALKQLGDSMKEYHRRRQDIKEAQTNGEEDENLEKNNERPDEFEHVEGANTETDTQALGSATQ- 4511
Cdd:COG5271 721 ADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVa 800
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4512 DQLQTIDEDMAIDDDREEQEVD-QKELVEDADDEKMDIDEE--EMLSDIDAHDANNDVDSKKSGFIGKRK----SEEDFE 4584
Cdd:COG5271 801 DEDQDTDEDALLDEAEADEEEDlDGEDEETADEALEDIEAGiaEDDEEDDDAAAAKDVDADLDLDADLAAdeheAEEAQE 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4585 NELSNEHFSADQEDDSEIQSLiENIEDNPPDASASLTPERSLEESRELWHKSEISTADLVSRLGEQLRLILEPTLATKLK 4664
Cdd:COG5271 881 AETDADADADAGEADSSGESS-AAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEE 959
|
....*..
gi 6323135 4665 GDYKTGK 4671
Cdd:COG5271 960 SDDAAAD 966
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1078-1214 |
9.33e-24 |
|
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: 99.67 E-value: 9.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1078 PVLIQGPTSSGKTSMIKYLAD-ITGHKFVRINNHEHTDLQEYLGTYVTDDTGKlSFKEGVLVEALRKGYWIVLDELNLAP 1156
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323135 1157 TDVLEALNRLLDDNRELFIPETQEVVHPHPDFLLFATQNPPgiYGGRKILSRAFRNRF 1214
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 ... |
1891-1990 |
2.57e-22 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins. :
Pssm-ID: 465540 Cd Length: 106 Bit Score: 94.68 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1891 DLLLIAKHLYPsIEPDIIAKMIKLMSTLEDQVCKRKLWGNSGSPWEFNLRDTLRWLKLLN---QYSICEDV--DVFDFVD 1965
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSsllPTLLSPTVreEIFLEAV 79
|
90 100
....*....|....*....|....*
gi 6323135 1966 IIVKQRFRTISDKNKAQLLIEDIFG 1990
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLG 104
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1363-1558 |
7.68e-22 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families. The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 94.28 E-value: 7.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1363 PVLLVGETGCGKTTICQLLAQ-FMGRELITLNAHQNTETGDILGAqrpvrnrseiqyklikslktalniandqdvdlkel 1441
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGR----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1442 lqlysksdnkniaedvqleiqklRDSLNVLFEWSDGPLIQAMRTGNFFLLDEISLADDSVLERLNSVLEpERSLLLAEQG 1521
Cdd:pfam07728 46 -----------------------RNIDPGGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGG 101
|
170 180 190
....*....|....*....|....*....|....*..
gi 6323135 1522 SSDSLvtASENFQFFATMNPgGDYGKKELSPALRNRF 1558
Cdd:pfam07728 102 ELVKA--APDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
465-579 |
6.54e-21 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins. :
Pssm-ID: 465540 Cd Length: 106 Bit Score: 90.44 E-value: 6.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 465 DLTHILAQKFPILTNLIPKLIDSYKNVKSIYMNTKFISLnkGAHTRVVSVRDLIKLCERLDILFKNnginkpdqLIQSSV 544
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGS--SGSPREFNLRDLLRWCRRLSSLLPT--------LLSPTV 70
|
90 100 110
....*....|....*....|....*....|....*
gi 6323135 545 YDSIFSEAADCFAGAIGEFKALEPIIQAIGESLDI 579
Cdd:pfam17867 71 REEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGI 105
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
310-427 |
1.17e-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: 85.42 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 310 PIMLIGKAGSGKTFLINELSKYMgCHDSIVKIHLGEQTDAKLLIGTYTSgdKPGTFEWRAGVLATAVKEGRWVLIEDIDK 389
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL-SNRPVFYVQLTRDTTEEDLFGRRNI--DPGGASWVDGPLVRAAREGEIAVLDEINR 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 6323135 390 APTDVLSILLSLLEKRELTIPSRGETVKAAN-GFQLIST 427
Cdd:pfam07728 78 ANPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIAT 116
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1742-1879 |
1.29e-16 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families. The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 79.26 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1742 PILLEGSPGVGKTSLITALAN-ITGNKLTRINLSEQTDLVDLFGADAPGERSGEflWHDAPFLRAMKKGEWVLLDEMNLA 1820
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNIDPGGAS--WVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323135 1821 SQSVLEGLNACLDHRgeaYIPELDISFSCH---PNFLVFAAQNPQYQGGgrKGLPKSFVNRF 1879
Cdd:pfam07728 79 NPDVLNSLLSLLDER---RLLLPDGGELVKaapDGFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1226-1320 |
4.82e-16 |
|
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: 76.57 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1226 ELEIILRERCQIAPSYAKKIVEVYRQLSIERSASRLFEQKNS--FATLRDLFRWALR---------DAVGYEQLAASGYM 1294
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCRRlssllptllSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 6323135 1295 LLAERCRTPQEKVTVKKTLEKVMKVK 1320
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
2190-2276 |
1.12e-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: 56.53 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 2190 VKFEWFDGMLVKAVEKGHWLILDNANLCSPSVLDRLNSLLEiDGSLLInecsqEDGQPRVLKPHPNFRLFLTMDPKYG-- 2267
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLD-ERRLLL-----PDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 6323135 2268 -ELSRAMRNR 2276
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
648-703 |
2.15e-06 |
|
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: 49.98 E-value: 2.15e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323135 648 PVLLVGETGTGKTTVVQQLAKMLA-KKLTVINVSQQTETGDLLGGYKPVNSKTVAVP 703
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVD 57
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
811-896 |
1.07e-05 |
|
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: 48.06 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 811 FVEGSLVKTIRAGEWLLLDEVNLATADTLESISDLLtepDSRSILLSEKGdaEPIKAHPD-FRIFACMNPAtDVGKRDLP 889
Cdd:pfam07728 55 WVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLL---DERRLLLPDGG--ELVKAAPDgFRLIATMNPL-DRGLNELS 128
|
....*..
gi 6323135 890 MGIRSRF 896
Cdd:pfam07728 129 PALRSRF 135
|
|
|
|
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 ... |
4643-4910 |
5.12e-139 |
|
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: 435.63 E-value: 5.12e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4643 LVSRLGEQLRLILEPTLATKLKGDYKTGKRLNMKRIIPYIASQFRKDKIWLRRTKPSKRQYQIMIALDDSKSMSESKCVK 4722
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4723 LAFDSLCLVSKTLTQLEAGGLSIVKFGENIKEVHSFDQQFSNESGARAFQWFGFQETKTDVKKLVAESTKIFERARAMVH 4802
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4803 NDQ-WQLEIVISDGICEDHETIQKL-VRRARENKIMLVFVIIDGITSNESILDMSQVNYIPDQYGnpqlKITKYLDTFPF 4880
Cdd:cd01460 161 SGSlWQLLLIISDGRGEFSEGAQKVrLREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDKSG----VITPYLDEFPF 236
|
250 260 270
....*....|....*....|....*....|
gi 6323135 4881 EFYVVVHDISELPEMLSLILRQYFTDLASS 4910
Cdd:cd01460 237 PYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
910-1015 |
4.87e-32 |
|
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: 122.31 E-value: 4.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 910 DLLSIIDKYIGKYSVSDEWVgNDIAELYLEAKKLSdNNTIVDGSNQKPHFSIRTLTRTLLYVTDIIHIYGLRRSLYDGFC 989
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLV-RDIVKFYLEAKKLA-EKSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90 100
....*....|....*....|....*.
gi 6323135 990 MSFLTLLDQKSEAILKPVIEKFTLGR 1015
Cdd:pfam17865 79 MSFLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4046-4671 |
7.81e-24 |
|
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: 111.65 E-value: 7.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4046 PQPPSEEVDDKNLQEGTGLGDGEGAQNNNKDVEQDEDLTEDAQNENKEQQDKDERDDENEDDAVEMEGDMAGELEDLSNG 4125
Cdd:COG5271 335 DEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4126 EENDDEDTDSEEEELDEEiddlNEDDPNAIDDKMWDDKASD--NSKEKDTDQNLDGKNQEEDVQAAENDEQ---QRDNKE 4200
Cdd:COG5271 415 EEEEEADEDASAGETEDE----STDVTSAEDDIATDEEADSlaDEEEEAEAELDTEEDTESAEEDADGDEAtdeDDASDD 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4201 GGDEDPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEGEDLEANVPEIETLDlpEDMNLDSEHEESDEDVDMSDGMPD 4280
Cdd:COG5271 491 GDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEE--NAPGSDQDADETDEPEATAEEDEP 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4281 DLNKEEVGNEDEEVkqesgiESDNENDEPGPEEDAGETETALDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQ 4360
Cdd:COG5271 569 DEAEAETEDATENA------DADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPET 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4361 DAAMEENKEKGGEQNTEG-----LDGVEEKADTEDIDQEAAvqQDSGSKGAGADATDTQEQDDVGGSGTTQNTYEE---D 4432
Cdd:COG5271 643 DASEAADEDADAETEAEAsadesEEEAEDESETSSEDAEED--ADAAAAEASDDEEETEEADEDAETASEEADAEEadtE 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4433 QEDVTKNNEESREEATAALKQLGDSMKEYHRRRQDIKEAQTNGEEDENLEKNNERPDEFEHVEGANTETDTQALGSATQ- 4511
Cdd:COG5271 721 ADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVa 800
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4512 DQLQTIDEDMAIDDDREEQEVD-QKELVEDADDEKMDIDEE--EMLSDIDAHDANNDVDSKKSGFIGKRK----SEEDFE 4584
Cdd:COG5271 801 DEDQDTDEDALLDEAEADEEEDlDGEDEETADEALEDIEAGiaEDDEEDDDAAAAKDVDADLDLDADLAAdeheAEEAQE 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4585 NELSNEHFSADQEDDSEIQSLiENIEDNPPDASASLTPERSLEESRELWHKSEISTADLVSRLGEQLRLILEPTLATKLK 4664
Cdd:COG5271 881 AETDADADADAGEADSSGESS-AAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEE 959
|
....*..
gi 6323135 4665 GDYKTGK 4671
Cdd:COG5271 960 SDDAAAD 966
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1078-1214 |
9.33e-24 |
|
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: 99.67 E-value: 9.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1078 PVLIQGPTSSGKTSMIKYLAD-ITGHKFVRINNHEHTDLQEYLGTYVTDDTGKlSFKEGVLVEALRKGYWIVLDELNLAP 1156
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323135 1157 TDVLEALNRLLDDNRELFIPETQEVVHPHPDFLLFATQNPPgiYGGRKILSRAFRNRF 1214
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 ... |
1891-1990 |
2.57e-22 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 94.68 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1891 DLLLIAKHLYPsIEPDIIAKMIKLMSTLEDQVCKRKLWGNSGSPWEFNLRDTLRWLKLLN---QYSICEDV--DVFDFVD 1965
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSsllPTLLSPTVreEIFLEAV 79
|
90 100
....*....|....*....|....*
gi 6323135 1966 IIVKQRFRTISDKNKAQLLIEDIFG 1990
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1363-1558 |
7.68e-22 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 94.28 E-value: 7.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1363 PVLLVGETGCGKTTICQLLAQ-FMGRELITLNAHQNTETGDILGAqrpvrnrseiqyklikslktalniandqdvdlkel 1441
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGR----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1442 lqlysksdnkniaedvqleiqklRDSLNVLFEWSDGPLIQAMRTGNFFLLDEISLADDSVLERLNSVLEpERSLLLAEQG 1521
Cdd:pfam07728 46 -----------------------RNIDPGGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGG 101
|
170 180 190
....*....|....*....|....*....|....*..
gi 6323135 1522 SSDSLvtASENFQFFATMNPgGDYGKKELSPALRNRF 1558
Cdd:pfam07728 102 ELVKA--APDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
465-579 |
6.54e-21 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 90.44 E-value: 6.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 465 DLTHILAQKFPILTNLIPKLIDSYKNVKSIYMNTKFISLnkGAHTRVVSVRDLIKLCERLDILFKNnginkpdqLIQSSV 544
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGS--SGSPREFNLRDLLRWCRRLSSLLPT--------LLSPTV 70
|
90 100 110
....*....|....*....|....*....|....*
gi 6323135 545 YDSIFSEAADCFAGAIGEFKALEPIIQAIGESLDI 579
Cdd:pfam17867 71 REEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGI 105
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
310-427 |
1.17e-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: 85.42 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 310 PIMLIGKAGSGKTFLINELSKYMgCHDSIVKIHLGEQTDAKLLIGTYTSgdKPGTFEWRAGVLATAVKEGRWVLIEDIDK 389
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL-SNRPVFYVQLTRDTTEEDLFGRRNI--DPGGASWVDGPLVRAAREGEIAVLDEINR 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 6323135 390 APTDVLSILLSLLEKRELTIPSRGETVKAAN-GFQLIST 427
Cdd:pfam07728 78 ANPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIAT 116
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1742-1879 |
1.29e-16 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 79.26 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1742 PILLEGSPGVGKTSLITALAN-ITGNKLTRINLSEQTDLVDLFGADAPGERSGEflWHDAPFLRAMKKGEWVLLDEMNLA 1820
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNIDPGGAS--WVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323135 1821 SQSVLEGLNACLDHRgeaYIPELDISFSCH---PNFLVFAAQNPQYQGGgrKGLPKSFVNRF 1879
Cdd:pfam07728 79 NPDVLNSLLSLLDER---RLLLPDGGELVKaapDGFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1226-1320 |
4.82e-16 |
|
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: 76.57 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1226 ELEIILRERCQIAPSYAKKIVEVYRQLSIERSASRLFEQKNS--FATLRDLFRWALR---------DAVGYEQLAASGYM 1294
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCRRlssllptllSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 6323135 1295 LLAERCRTPQEKVTVKKTLEKVMKVK 1320
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1078-1281 |
1.09e-14 |
|
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: 77.90 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1078 PVLIQGPTSSGKTSMIKYLADITGHKFVRINNHEHTDLQEYLGTYVTD-DTGKLSFKEGVLVEAlrkgywIVL-DELNLA 1155
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDqQTGEFEFRPGPLFAN------VLLaDEINRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1156 PTDV----LEALnrlldDNRELFIPEtQEVVHPHPdFLLFATQNPPGIYGGRKiLSRAFRNRFL-ELHFdDIPQDELEI- 1229
Cdd:COG0714 107 PPKTqsalLEAM-----EERQVTIPG-GTYKLPEP-FLVIATQNPIEQEGTYP-LPEAQLDRFLlKLYI-GYPDAEEERe 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6323135 1230 ILRERCQIAPSYAKKIVEVYRQLSIERSASRLFEQKNSFATLRDLFRwALRD 1281
Cdd:COG0714 178 ILRRHTGRHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVR-ATRE 228
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1732-1922 |
1.26e-14 |
|
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: 77.90 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1732 RVVRAMQV----HKPILLEGSPGVGKTSLITALANITGNKLTRINLSEQTDLVDLFGADAPGERSGEFLWHDAPFLRAMk 1807
Cdd:COG0714 19 ELIELVLIallaGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTGEFEFRPGPLFANV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1808 kgewVLLDEMNLAS---QSVLegLNAcLDHRgEAYIPELDISFScHPnFLVFAAQNPQYQGGGRKgLPKSFVNRFSV-VF 1883
Cdd:COG0714 98 ----LLADEINRAPpktQSAL--LEA-MEER-QVTIPGGTYKLP-EP-FLVIATQNPIEQEGTYP-LPEAQLDRFLLkLY 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6323135 1884 IDMLTSDDLLLI----AKHLYPSIEPDIIAKMIKLMSTLEDQV 1922
Cdd:COG0714 167 IGYPDAEEEREIlrrhTGRHLAEVEPVLSPEELLALQELVRQV 209
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4183-4451 |
1.56e-12 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 74.65 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4183 EEDVQAAENDEQQRDNkEGGDEDPNAPEDGDEEIENDENAEEENDVGEQEDEvKDEEGEDLEANVPEIETLDLPEDMNLD 4262
Cdd:TIGR00927 632 KGDVAEAEHTGERTGE-EGERPTEAEGENGEESGGEAEQEGETETKGENESE-GEIPAERKGEQEGEGEIEAKEADHKGE 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4263 SEHEESDEDVDMSDGMPDDLNKEEVGNEDEEVKQE------SGIESDNENDEPGPEEDAG-ETETALDEEEG---AEEDV 4332
Cdd:TIGR00927 710 TEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEgegeaeGKHEVETEGDRKETEHEGEtEAEGKEDEDEGeiqAGEDG 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4333 DMTNDEGkedeengpEEQAMSDEEELKQDAAMEENKEKGGEQNTEGLDGVEEKADTEDIDQEAAVQQDSGSKG-AGADAT 4411
Cdd:TIGR00927 790 EMKGDEG--------AEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGgGGSDGG 861
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6323135 4412 DTQEQDDvggsgttQNTYEEDQEDVTKNNEESREEATAAL 4451
Cdd:TIGR00927 862 DSEEEEE-------EEEEEEEEEEEEEEEEEEEEENEEPL 894
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4148-4457 |
1.28e-11 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 71.48 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4148 NEDDPNAidDKMWDDKASDNSKEKDTDQNLD-GKNQEEDVQAAENDEQQRDNKEGGDEDPNAPEDGDEEIENDENAEEEN 4226
Cdd:NF033609 561 SDSDPGS--DSGSDSSNSDSGSDSGSDSTSDsGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSAS 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4227 DVGEQEDEvkdeegeDLEANVPEIETLDLPEDMNLDSEHE-ESDEDVDMSDGMPDDLNKEEVGNEDEEVKQESGIESDNE 4305
Cdd:NF033609 639 DSDSDSDS-------DSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4306 NDEPGPEEDAGETETALDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEENKEKGGEQNTEGLDGVEEK 4385
Cdd:NF033609 712 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 791
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323135 4386 ADTE-DIDQEAAVQQDSGSKGAGADATDTQEQDDVGGSGTTQNTYEEDQEDVTKNNEESREEATAALKQLGDS 4457
Cdd:NF033609 792 SDSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDS 864
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4162-4460 |
2.76e-11 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 70.32 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4162 DKASDNSKEKDTDQNLDGKNQEEDVQAAENDEqqrdnkeggDEDPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEGE 4241
Cdd:NF033609 605 DSASDSDSASDSDSASDSDSASDSDSASDSDS---------ASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4242 -DLEANVPEIETLDLPEDMNLDSEHE-ESDEDVDMSDGMPDDLNKEEVGNEDEEVKQESGIESDNENDEPGPEEDAGETE 4319
Cdd:NF033609 676 sDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4320 TALDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEENKEKGGEQNTEGLDGVEEKADTE-DIDQEAAVQ 4398
Cdd:NF033609 756 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSD 835
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323135 4399 QDSGSKGAGADATDTQEQDDVGGSGTTQNTYEEDQEDVTKN------NEESREEATAALKQLGDSMKE 4460
Cdd:NF033609 836 SDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNspkngtNASNKNEAKDSKEPLPDTGSE 903
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4178-4376 |
3.32e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 68.84 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4178 DGKNQEEDVQAAENDEQQR-DNKEGGDEDPNAPEDgdeeiendENAEEENDVGEQEDEVKDEEGEDLEANVPEIETLDLP 4256
Cdd:PHA03169 50 APTTSGPQVRAVAEQGHRQtESDTETAEESRHGEK--------EERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4257 EDMNLDSEHEESDEDV--DMSDGMPDDLNKEEVGNEDEEVKQESGIESDNEN-DEPG------PEEDA---GETETALDE 4324
Cdd:PHA03169 122 NTSGSSPESPASHSPPpsPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDsPEEPepptsePEPDSpgpPQSETPTSS 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6323135 4325 EEGAEEdvdmtNDEGKEDEENGPEEQAMSDE-EELKQDAAMEENKEKGGEQNT 4376
Cdd:PHA03169 202 PPPQSP-----PDEPGEPQSPTPQQAPSPNTqQAVEHEDEPTEPEREGPPFPG 249
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4255-4631 |
1.98e-10 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 67.63 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4255 LPEDMNLDSEHEESDEDVDM---SDGMPDDLNKEEVGNEDEEVKQESGIESDNENDEPGPEEDAGETETALDEEEGAEED 4331
Cdd:NF033609 544 VPEQPDEPGEIEPIPEDSDSdpgSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSD 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4332 VDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEENKEKGGEQNTEGlDGVEEKADTEDIDQEAAVQQDSGSKGAGADAT 4411
Cdd:NF033609 624 SASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4412 DTQEQDDVGGSGTTQNTYEEDQEDVTKNNEESREEATAALKQLGDSmkeyhrrrqdikEAQTNGEEDENLEKNNErpdef 4491
Cdd:NF033609 703 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS------------DSDSDSDSDSDSDSDSD----- 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4492 ehvegANTETDTQALGSATQDQLQTIDEDMAIDDDREEQEVDQKELVEDAD-DEKMDIDeeemlSDIDAhDANNDVDSKK 4570
Cdd:NF033609 766 -----SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSD-----SDSDS-DSDSDSDSDS 834
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323135 4571 SGFIGKRKSEEDFENELSNEHFSADQEDDSEIQSLIENIEDNPPDASASLTPERSLEESRE 4631
Cdd:NF033609 835 DSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASNKNEAKDSKE 895
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4046-4393 |
3.57e-10 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 66.86 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4046 PQPPSEEVDDKNLQEGT----GLGDGEGAQNNNKDVEQDEDLTEDAQNENKEQQDKDERDDENEDDAVEMEGDMAGELED 4121
Cdd:NF033609 545 PEQPDEPGEIEPIPEDSdsdpGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDS 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4122 LSNGEENDDEDTDSEEEELDEEIDDLNEDDPNAIDDKMWDDKASDNSKEKDTDQNLDGKNQEEDVQAAENDEqqrDNKEG 4201
Cdd:NF033609 625 ASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS---DSDSD 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4202 GDEDPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEGE-DLEANVPEIETLDLPEDMNLDSEhEESDEDVDMSDGMPD 4280
Cdd:NF033609 702 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDS 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4281 DLNKEEVGNEDEEVKQESGIESDNENDEPGPEEDAGETETALDEEEGAEEDVDMTNDEGKE---------DEENGPEEQA 4351
Cdd:NF033609 781 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsdsdsdsdsDSDSDSESDS 860
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 6323135 4352 MSDEEELKQDAAMEENKEKGG---EQNTEGLDGVEEKADTEDIDQ 4393
Cdd:NF033609 861 NSDSESGSNNNVVPPNSPKNGtnaSNKNEAKDSKEPLPDTGSEDE 905
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2190-2276 |
1.12e-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: 56.53 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 2190 VKFEWFDGMLVKAVEKGHWLILDNANLCSPSVLDRLNSLLEiDGSLLInecsqEDGQPRVLKPHPNFRLFLTMDPKYG-- 2267
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLD-ERRLLL-----PDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 6323135 2268 -ELSRAMRNR 2276
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
4162-4562 |
2.20e-08 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 60.43 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4162 DKASDNSKEKDTDQNLDGKNQEEDVQAAENDEQqrdnkeggdEDPNAPEDGDeeiendenaeeenDVGEQEDEVKDEEGE 4241
Cdd:pfam01271 184 DTPSKQKREKSDEREKSSQESGEDTYRQENIPQ---------EDQVGPEDQE-------------PSEEGEEDATQEEVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4242 DLEANVPEIETLdlPEDMNLDSEHEESDEDVDMSDG---MPDDLNKEEVGNEDEEVKQESGIESDNENDEPGPEEDAGEt 4318
Cdd:pfam01271 242 RSRPRTHHGRSL--PDESSRGGQLGLEEEASEEEEEygeESRGLSAVQTYLLRLVNARGRGRSEKRAERERSEESEEEE- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4319 etalDEEEGAEEDVDMTNDEgkedeeNGPEeqamSDEEELKQDAAMEENKEKGGEQNTEGLDGVEEKADTEDidQEAAVQ 4398
Cdd:pfam01271 319 ----LKRASPYEELEITANL------QIPP----SEEERMLKKAGRSPRGRVDEAGALEALEALEEKRKLDL--DHSRVF 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4399 QDSGSKGAGADATDTQEQD----DVGGSGTTQNTyeeDQEDVTKNNEESREEATAALKQ-LGDSMKEYHRRRQ---DIKE 4470
Cdd:pfam01271 383 ESSEDGAPRAPQGAWVEALrnylSYGEEGMEGKW---NQQGPYFPNEENREEARFRLPQyLGELSNPWEDPKQwkpSDFE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4471 AQTN-------GEEDENL---------EKNNERPdEFEhVEGANTETDTQALGSATQDQLQTIDEDMAIDDDREEQEVdQ 4534
Cdd:pfam01271 460 RKELtadkfleGEEENEYtlsmknsfpEYNYDGY-EKR-VPSPGLDLKRQYDPVAREDQLLHYRKKSSEFPDFYDSEE-K 536
|
410 420 430
....*....|....*....|....*....|...
gi 6323135 4535 KELVEDADDEK-----MDIDEEEMLSDIDAHDA 4562
Cdd:pfam01271 537 KEPPVGAEKEEdsanrQTRDEDKELENLAAMDL 569
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
310-427 |
2.60e-08 |
|
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: 58.64 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 310 PIMLIGKAGSGKTFLINELSKYMGCHDSIVKIHlgEQTDAKLLIGTYTSGDKPGTFEWRAGVLATAVkegrwVLIEDIDK 389
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFT--PDLLPSDILGTYIYDQQTGEFEFRPGPLFANV-----LLADEINR 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 6323135 390 APTDVLSILLSLLEKRELTIPsrGETVKAANGFQLIST 427
Cdd:COG0714 106 APPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIAT 141
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
648-703 |
2.15e-06 |
|
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: 49.98 E-value: 2.15e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323135 648 PVLLVGETGTGKTTVVQQLAKMLA-KKLTVINVSQQTETGDLLGGYKPVNSKTVAVP 703
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVD 57
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1729-1881 |
4.05e-06 |
|
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: 49.84 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1729 NLVRVVRAMQVHKPILLEGSPGVGKTSLITALANITGNKLTRINlseQTDLVDLFGADAPGERSGEFLWHDAPFLRAMKK 1808
Cdd:cd00009 8 EALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFL---YLNASDLLEGLVVAELFGHFLVRLLFELAEKAK 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323135 1809 GEWVLLDEMNLASQSVLEGLNACLDhrgeayipELDISFSCHPNFLVFAAQNPQYQGGGRKGLPKSFVNRFSV 1881
Cdd:cd00009 85 PGVLFIDEIDSLSRGAQNALLRVLE--------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVI 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1361-1558 |
4.42e-06 |
|
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: 49.68 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1361 KEPVLLVGETGCGKTTICQLLAQFMGRE---LITLNAhQNTETGDILGAQRPVRNRSEIQYKLIKSLKTALNIANDQDVD 1437
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDG-EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1438 LkellqlysksdnkniaedvqleiqklrdslnvlfewsdgpliqamrtgnfFLLDEISLADDSVLERLNSVLEPERSLLL 1517
Cdd:smart00382 81 V--------------------------------------------------LILDEITSLLDAEQEALLLLLEELRLLLL 110
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6323135 1518 AEQgssdslvtaSENFQFFATMNPGGDYGKKELSPALRNRF 1558
Cdd:smart00382 111 LKS---------EKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4329-4618 |
6.67e-06 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 52.60 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4329 EEDVDMTNDEGKEDEENGPEEQAMSDE----EELKQDAAMEENKEKGGEQNTEGLDGVEEKADTEDIDQEAAVQQDSGSK 4404
Cdd:NF033609 524 DNEVAFNNGSGSGDGIDKPVVPEQPDEpgeiEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASD 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4405 GAGADATDTQEQDDVGGSGTTQNTYEEDQEDVTKNNEESREEATAALKQLGDSMKEYHRRRQDIKEAQTNGEEDENLEKN 4484
Cdd:NF033609 604 SDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4485 NERPDEFEHVEGANTETDTQALGSATQDQLQTIDEDMAIDDDREEQEVDQKELVEDADDEKMDIDEEEMLSDIDA-HDAN 4563
Cdd:NF033609 684 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSD 763
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323135 4564 NDVDS-KKSGFIGKRKSEEDFENElSNEHFSADQEDDSEIQSLIENIEDNPPDASA 4618
Cdd:NF033609 764 SDSDSdSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 818
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1078-1229 |
1.03e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 51.27 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1078 PVLIQGPTSSGKTSMIKYLADITGHKFVRINnhehTDLQEYLGTYVTDDTGKlsFKEGVLVEALRKGYWIVLDELNLAPT 1157
Cdd:PHA02244 121 PVFLKGGAGSGKNHIAEQIAEALDLDFYFMN----AIMDEFELKGFIDANGK--FHETPFYEAFKKGGLFFIDEIDASIP 194
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323135 1158 DVLEALNRLLDDNRELFIPETqevVHPHPDFLLFATQNPPG-----IYGGRKILSRAFRNRFLELHFDDIPQDELEI 1229
Cdd:PHA02244 195 EALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFDYDEKIEHLI 268
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
811-896 |
1.07e-05 |
|
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: 48.06 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 811 FVEGSLVKTIRAGEWLLLDEVNLATADTLESISDLLtepDSRSILLSEKGdaEPIKAHPD-FRIFACMNPAtDVGKRDLP 889
Cdd:pfam07728 55 WVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLL---DERRLLLPDGG--ELVKAAPDgFRLIATMNPL-DRGLNELS 128
|
....*..
gi 6323135 890 MGIRSRF 896
Cdd:pfam07728 129 PALRSRF 135
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
4705-4879 |
1.29e-05 |
|
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: 48.99 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4705 IMIALDDSKSMSESK--CVKLAfdslclVSKTLTQLEAGG----LSIVKFGENIKEVHSFDQQFSNE---SGARAFQWFG 4775
Cdd:smart00327 2 VVFLLDGSGSMGGNRfeLAKEF------VLKLVEQLDIGPdgdrVGLVTFSDDARVLFPLNDSRSKDallEALASLSYKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4776 FQETKTD--VKKLVAESTKIFERARAMVHndqwQLEIVISDGICEDHET-IQKLVRRARENKIMLVFViidGITSNESIL 4852
Cdd:smart00327 76 GGGTNLGaaLQYALENLFSKSAGSRRGAP----KVVILITDGESNDGPKdLLKAAKELKRSGVKVFVV---GVGNDVDEE 148
|
170 180
....*....|....*....|....*..
gi 6323135 4853 DMSQVNYIPDQYGNPQLKITKYLDTFP 4879
Cdd:smart00327 149 ELKKLASAPGGVYVFLPELLDLLIDLL 175
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1075-1214 |
1.80e-05 |
|
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: 47.75 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1075 KRFPVLIQGPTSSGKTSMIKYLA---DITGHKFVRIN--NHEHTDLQEYLGTYVTDDTGKLSFKEGV--LVEALRKGYW- 1146
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALArelGPPGGGVIYIDgeDILEEVLDQLLLIIVGGKKASGSGELRLrlALALARKLKPd 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323135 1147 -IVLDELNLAPTDVLEALNRLLDDNRELFIPETQEVVHphpdfLLFATQNPPGIygGRKILSRAFRNRF 1214
Cdd:smart00382 81 vLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLT-----VILTTNDEKDL--GPALLRRRFDRRI 142
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1724-1894 |
2.42e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 50.12 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1724 PTTASNLVRVVRAMQVHKPILLEGSPGVGKTSLITALAnitgnKLTRINLSEQTDLVDLFGADAPGERSGEFlwHDAPFL 1803
Cdd:PHA02244 103 PTFHYETADIAKIVNANIPVFLKGGAGSGKNHIAEQIA-----EALDLDFYFMNAIMDEFELKGFIDANGKF--HETPFY 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1804 RAMKKGEWVLLDEMNLASQSVLEGLNACLDHRgeaYIPELDISFSCHPNFLVFAAQNPQYQGG-----GRKGLPKSFVNR 1878
Cdd:PHA02244 176 EAFKKGGLFFIDEIDASIPEALIIINSAIANK---FFDFADERVTAHEDFRVISAGNTLGKGAdhiyvARNKIDGATLDR 252
|
170
....*....|....*.
gi 6323135 1879 FSVVFIDMLTSDDLLL 1894
Cdd:PHA02244 253 FAPIEFDYDEKIEHLI 268
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1352-1426 |
5.19e-05 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 46.37 E-value: 5.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323135 1352 VLVSSCLKNKEPVLLVGETGCGKTTICQLLAQ---FMGRELITLNAHQNTETGDILGAQRPVRNRSEIQYKLIKSLKT 1426
Cdd:cd00009 10 LREALELPPPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPGV 87
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4045-4376 |
1.36e-04 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 48.37 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4045 SPQPPSEEVDDKNLQEGTGLGDGEGAQNNNKDVEQDEDLTEDAQNENKEQQDKDERDDENEDDAVEMEGDMAGELEDLSN 4124
Cdd:NF033609 624 SASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4125 GEENDDEdtdseeeeldeeiddlnedDPNAIDDKmwdDKASDNSKEKDTDQNLDgKNQEEDVQAAENDEQQRDNKEGGDE 4204
Cdd:NF033609 704 SDSDSDS-------------------DSDSDSDS---DSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDS 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4205 DPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEGedleanvpeietlDLPEDMNLDSeheESDEDVDMSDGMPDDLNK 4284
Cdd:NF033609 761 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-------------DSDSDSDSDS---DSDSDSDSDSDSDSDSDS 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4285 EEVGNEDEEVKQESGIESDNENDEPGPEEDAGETETALDEEEGAEEDVDMTNDegKEDEENGPEEQAMSDEEELKQDAAM 4364
Cdd:NF033609 825 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNS--PKNGTNASNKNEAKDSKEPLPDTGS 902
|
330
....*....|..
gi 6323135 4365 EenkekgGEQNT 4376
Cdd:NF033609 903 E------DEANT 908
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1068-1214 |
2.34e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 44.83 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1068 LVRATSGKRFPVLIQGPTSSGKTSMIKYLADIT---GHKFVRINNHEhtdlqEYLGTYVTDDTGKLSFKEGVLVEALRKG 1144
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASD-----LLEGLVVAELFGHFLVRLLFELAEKAKP 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1145 YWIVLDELNLAPTDVLEALNRLLDDnrelfipETQEVVHPHPDFLLFATQNPPGIyggrkILSRAFRNRF 1214
Cdd:cd00009 86 GVLFIDEIDSLSRGAQNALLRVLET-------LNDLRIDRENVRVIGATNRPLLG-----DLDRALYDRL 143
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1342-1394 |
1.46e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 44.91 E-value: 1.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 6323135 1342 TWTKGmrrlsvlvssclKNKEPVLLVGETGCGKTTICQLLAQFMGRELITLNA 1394
Cdd:PRK04195 32 SWLKG------------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNA 72
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
310-420 |
3.11e-03 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 43.89 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 310 PI---MLIGKAGSGKTFLINELSKYM-GCHDSIVKIHLGE----QTDAKLLigtytsGDKPGTFEW-RAGVLATAVKEGR 380
Cdd:CHL00095 538 PIasfLFSGPTGVGKTELTKALASYFfGSEDAMIRLDMSEymekHTVSKLI------GSPPGYVGYnEGGQLTEAVRKKP 611
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 6323135 381 W--VLIEDIDKAPTDVLSILLSLLEKRELTiPSRGETVKAAN 420
Cdd:CHL00095 612 YtvVLFDEIEKAHPDIFNLLLQILDDGRLT-DSKGRTIDFKN 652
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
312-416 |
6.54e-03 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 41.01 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 312 MLIGKAGSGKTFLINELSKYM-GCHDSIVKIHLGEQT---DAKLLIGT------YTSGdkpgtfewraGVLATAVKEGRW 381
Cdd:cd19499 45 LFLGPTGVGKTELAKALAELLfGDEDNLIRIDMSEYMekhSVSRLIGAppgyvgYTEG----------GQLTEAVRRKPY 114
|
90 100 110
....*....|....*....|....*....|....*..
gi 6323135 382 --VLIEDIDKAPTDVLSILLSLLEKRELTiPSRGETV 416
Cdd:cd19499 115 svVLLDEIEKAHPDVQNLLLQVLDDGRLT-DSHGRTV 150
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
310-415 |
6.97e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 310 PIMLIGKAGSGKTFLINELSKYMGCHDSIVKI----HLGEQTDAKLLIGTYTSGDKPGTFEWRAGVLATAVKEGRW--VL 383
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIYidgeDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110
....*....|....*....|....*....|..
gi 6323135 384 IEDIDKAPTDVLSILLSLLEKRELTIPSRGET 415
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLKSEK 115
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
630-686 |
7.48e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX 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: 410905 [Multi-domain] Cd Length: 251 Bit Score: 41.43 E-value: 7.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323135 630 NHSLRLMEQISVCIQMTE----PVLLVGETGTGKTTVVQQLAKMLAKKLTVINVSQQTETG 686
Cdd:cd19497 30 NHYKRIRNNLKQKDDDVEleksNILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAG 90
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
647-712 |
8.12e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 8.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323135 647 EPVLLVGETGTGKTTVVQQLAKMLAKKLT---VINVSQQTETGDLLGGYKPVNSKTVAVPIQENFETLF 712
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGgviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL 71
|
|
|
|
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 ... |
4643-4910 |
5.12e-139 |
|
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: 435.63 E-value: 5.12e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4643 LVSRLGEQLRLILEPTLATKLKGDYKTGKRLNMKRIIPYIASQFRKDKIWLRRTKPSKRQYQIMIALDDSKSMSESKCVK 4722
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4723 LAFDSLCLVSKTLTQLEAGGLSIVKFGENIKEVHSFDQQFSNESGARAFQWFGFQETKTDVKKLVAESTKIFERARAMVH 4802
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4803 NDQ-WQLEIVISDGICEDHETIQKL-VRRARENKIMLVFVIIDGITSNESILDMSQVNYIPDQYGnpqlKITKYLDTFPF 4880
Cdd:cd01460 161 SGSlWQLLLIISDGRGEFSEGAQKVrLREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDKSG----VITPYLDEFPF 236
|
250 260 270
....*....|....*....|....*....|
gi 6323135 4881 EFYVVVHDISELPEMLSLILRQYFTDLASS 4910
Cdd:cd01460 237 PYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
910-1015 |
4.87e-32 |
|
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: 122.31 E-value: 4.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 910 DLLSIIDKYIGKYSVSDEWVgNDIAELYLEAKKLSdNNTIVDGSNQKPHFSIRTLTRTLLYVTDIIHIYGLRRSLYDGFC 989
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLV-RDIVKFYLEAKKLA-EKSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90 100
....*....|....*....|....*.
gi 6323135 990 MSFLTLLDQKSEAILKPVIEKFTLGR 1015
Cdd:pfam17865 79 MSFLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4046-4671 |
7.81e-24 |
|
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: 111.65 E-value: 7.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4046 PQPPSEEVDDKNLQEGTGLGDGEGAQNNNKDVEQDEDLTEDAQNENKEQQDKDERDDENEDDAVEMEGDMAGELEDLSNG 4125
Cdd:COG5271 335 DEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4126 EENDDEDTDSEEEELDEEiddlNEDDPNAIDDKMWDDKASD--NSKEKDTDQNLDGKNQEEDVQAAENDEQ---QRDNKE 4200
Cdd:COG5271 415 EEEEEADEDASAGETEDE----STDVTSAEDDIATDEEADSlaDEEEEAEAELDTEEDTESAEEDADGDEAtdeDDASDD 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4201 GGDEDPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEGEDLEANVPEIETLDlpEDMNLDSEHEESDEDVDMSDGMPD 4280
Cdd:COG5271 491 GDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEE--NAPGSDQDADETDEPEATAEEDEP 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4281 DLNKEEVGNEDEEVkqesgiESDNENDEPGPEEDAGETETALDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQ 4360
Cdd:COG5271 569 DEAEAETEDATENA------DADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPET 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4361 DAAMEENKEKGGEQNTEG-----LDGVEEKADTEDIDQEAAvqQDSGSKGAGADATDTQEQDDVGGSGTTQNTYEE---D 4432
Cdd:COG5271 643 DASEAADEDADAETEAEAsadesEEEAEDESETSSEDAEED--ADAAAAEASDDEEETEEADEDAETASEEADAEEadtE 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4433 QEDVTKNNEESREEATAALKQLGDSMKEYHRRRQDIKEAQTNGEEDENLEKNNERPDEFEHVEGANTETDTQALGSATQ- 4511
Cdd:COG5271 721 ADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVa 800
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4512 DQLQTIDEDMAIDDDREEQEVD-QKELVEDADDEKMDIDEE--EMLSDIDAHDANNDVDSKKSGFIGKRK----SEEDFE 4584
Cdd:COG5271 801 DEDQDTDEDALLDEAEADEEEDlDGEDEETADEALEDIEAGiaEDDEEDDDAAAAKDVDADLDLDADLAAdeheAEEAQE 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4585 NELSNEHFSADQEDDSEIQSLiENIEDNPPDASASLTPERSLEESRELWHKSEISTADLVSRLGEQLRLILEPTLATKLK 4664
Cdd:COG5271 881 AETDADADADAGEADSSGESS-AAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEE 959
|
....*..
gi 6323135 4665 GDYKTGK 4671
Cdd:COG5271 960 SDDAAAD 966
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1078-1214 |
9.33e-24 |
|
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: 99.67 E-value: 9.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1078 PVLIQGPTSSGKTSMIKYLAD-ITGHKFVRINNHEHTDLQEYLGTYVTDDTGKlSFKEGVLVEALRKGYWIVLDELNLAP 1156
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323135 1157 TDVLEALNRLLDDNRELFIPETQEVVHPHPDFLLFATQNPPgiYGGRKILSRAFRNRF 1214
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 ... |
1891-1990 |
2.57e-22 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 94.68 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1891 DLLLIAKHLYPsIEPDIIAKMIKLMSTLEDQVCKRKLWGNSGSPWEFNLRDTLRWLKLLN---QYSICEDV--DVFDFVD 1965
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSsllPTLLSPTVreEIFLEAV 79
|
90 100
....*....|....*....|....*
gi 6323135 1966 IIVKQRFRTISDKNKAQLLIEDIFG 1990
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1363-1558 |
7.68e-22 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 94.28 E-value: 7.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1363 PVLLVGETGCGKTTICQLLAQ-FMGRELITLNAHQNTETGDILGAqrpvrnrseiqyklikslktalniandqdvdlkel 1441
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGR----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1442 lqlysksdnkniaedvqleiqklRDSLNVLFEWSDGPLIQAMRTGNFFLLDEISLADDSVLERLNSVLEpERSLLLAEQG 1521
Cdd:pfam07728 46 -----------------------RNIDPGGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGG 101
|
170 180 190
....*....|....*....|....*....|....*..
gi 6323135 1522 SSDSLvtASENFQFFATMNPgGDYGKKELSPALRNRF 1558
Cdd:pfam07728 102 ELVKA--APDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
465-579 |
6.54e-21 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 90.44 E-value: 6.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 465 DLTHILAQKFPILTNLIPKLIDSYKNVKSIYMNTKFISLnkGAHTRVVSVRDLIKLCERLDILFKNnginkpdqLIQSSV 544
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGS--SGSPREFNLRDLLRWCRRLSSLLPT--------LLSPTV 70
|
90 100 110
....*....|....*....|....*....|....*
gi 6323135 545 YDSIFSEAADCFAGAIGEFKALEPIIQAIGESLDI 579
Cdd:pfam17867 71 REEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGI 105
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4049-4637 |
2.04e-19 |
|
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: 97.01 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4049 PSEEVDDKNLQEGTGLGDGEGAQNNNKDVEQDEDLTEDAQNENKEQqdKDERDDENEDDAVEMEGDMAGELEDLSNGEEN 4128
Cdd:COG5271 187 IEATPGGTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASAVVE--EEDASEDAVAAADETLLADDDDTESAGATAEV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4129 DDEDTDSEEEELDEEIDDLNEDDPNAIDDKMWDDKASDNSKEKDTDQNLDGKNQEEDVQAAENDEQQRDNKEGGDEDPNA 4208
Cdd:COG5271 265 GGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4209 PEDGDEEIENDENAEEENDVGEQEDEVKDEEGEDLEANVPEIETLDLPEDMNLDSEH-------EESDEDVDMSDGMPDD 4281
Cdd:COG5271 345 DAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEAsadggtsPTSDTDEEEEEADEDA 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4282 LNKEEVGNEDEEVKQESGIESDNE-------------NDEPGPEEDAGETETALDE---EEGAEEDVDMTNDEGKEDEEN 4345
Cdd:COG5271 425 SAGETEDESTDVTSAEDDIATDEEadsladeeeeaeaELDTEEDTESAEEDADGDEatdEDDASDDGDEEEAEEDAEAEA 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4346 GPEEqamSDEEELKQDAAMEENKEKGGEQNTEG--LDGVEEKADTEDIDQEAAVQQDsgskgagADATDTQEQDDVGGSG 4423
Cdd:COG5271 505 DSDE---LTAEETSADDGADTDAAADPEDSDEDalEDETEGEENAPGSDQDADETDE-------PEATAEEDEPDEAEAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4424 TTQNTYEEDQEDVTKNNEESREEATAALKQLGDSMKEYHRRRQDIKEAQTNGEEDENLEKNNERPDEFEHVEGANTETDT 4503
Cdd:COG5271 575 TEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4504 QALGSATQD-QLQTIDEDMAIDDDREEQEVDQKELVEDADDEKM---DIDEEEMLSDIDAHDANNDVDSKKSGFIGKRKS 4579
Cdd:COG5271 655 ETEAEASADeSEEEAEDESETSSEDAEEDADAAAAEASDDEEETeeaDEDAETASEEADAEEADTEADGTAEEAEEAAEE 734
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323135 4580 EEDFENELSNEHFSADQEDD---------SEIQSLIENIEDNPPDASASLTPERSLEESRELWHKSE 4637
Cdd:COG5271 735 AESADEEAASLPDEADAEEEaeeaeeaeeDDADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVAD 801
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4051-4619 |
2.96e-19 |
|
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: 96.62 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4051 EEVDDKNLQEGTGLGDGEGAQNNNKDvEQDEDLTEDAQNENKEQQDKDeRDDENEDDAVEMEGDMAGELEDLSNGEENDD 4130
Cdd:COG5271 418 EEADEDASAGETEDESTDVTSAEDDI-ATDEEADSLADEEEEAEAELD-TEEDTESAEEDADGDEATDEDDASDDGDEEE 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4131 EDTDS-------EEEELDEEIDDLNEDDPNAIDDKMWDDKASDNSKEKDTDQNLDGKNQEEDVQAAENDEQQRDNKEGGD 4203
Cdd:COG5271 496 AEEDAeaeadsdELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAET 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4204 EDPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEGEDLEA---NVPEIETLDLPEDMNLDSEHE-----ESDEDVDMS 4275
Cdd:COG5271 576 EDATENADADETEESADESEEAEASEDEAAEEEEADDDEADAdadGAADEEETEEEAAEDEAAEPEtdaseAADEDADAE 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4276 DGMPDDLNKEEVGNEDEEVKQESGIESDNE---------NDEPGPEEDAGETETALDEEEGAEEDVDMTNDEGKE----- 4341
Cdd:COG5271 656 TEAEASADESEEEAEDESETSSEDAEEDADaaaaeasddEEETEEADEDAETASEEADAEEADTEADGTAEEAEEaaeea 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4342 ---DEENGPEEQAmSDEEELKQDAAMEENKEkgGEQNTEGLDGVEEKADTEDIDQEAAVQQDSGSKGA--------GADA 4410
Cdd:COG5271 736 esaDEEAASLPDE-ADAEEEAEEAEEAEEDD--ADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVAdedqdtdeDALL 812
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4411 TDTQEQDDVGGSGTTQNTYEEDQEDVTKNNEESREEATAALKQLGDSMKEYHRRRQDIKEAQT--NGEEDENLEKNNERP 4488
Cdd:COG5271 813 DEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAeeAQEAETDADADADAG 892
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4489 DEFEHVEGANTETDTQALGSATQDQLQTIDEDMAIDDDREEQEVDQKELVEDADDEKMDIDEEEMLSDIDAHDANNDVDS 4568
Cdd:COG5271 893 EADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEESDDAAADDAGDDS 972
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 6323135 4569 KKSGF-IGKRKSEEDFENELSNEHFSADQEDDSEIQSLIENIEDNPPDASAS 4619
Cdd:COG5271 973 LADDDeALADAADDAEADDSELDASESTGEAEGDEDDDELEDGEAAAGEATA 1024
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
310-427 |
1.17e-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: 85.42 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 310 PIMLIGKAGSGKTFLINELSKYMgCHDSIVKIHLGEQTDAKLLIGTYTSgdKPGTFEWRAGVLATAVKEGRWVLIEDIDK 389
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL-SNRPVFYVQLTRDTTEEDLFGRRNI--DPGGASWVDGPLVRAAREGEIAVLDEINR 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 6323135 390 APTDVLSILLSLLEKRELTIPSRGETVKAAN-GFQLIST 427
Cdd:pfam07728 78 ANPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIAT 116
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4069-4631 |
3.97e-18 |
|
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: 93.16 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4069 GAQNNNKDVEQDEDLTEDAQN-ENKEQQDKDERDDENEDDAVEMEGDMAGELEDLSNGEENDDEDTDSEEEELDEEIDDL 4147
Cdd:COG5271 142 GGDLDLATKDGDELLPSLADNdEAAADEGDELAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDSVAADDDL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4148 NEDDPNAIDDKMWDDKASDNSKEKDTDQNLDGKNQEEDVQAAENDEQQRDNKEGGDEDPNAPEDGDEEIENDENAEEEND 4227
Cdd:COG5271 222 AAEEGASAVVEEEDASEDAVAAADETLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADP 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4228 VGEQEDEVKDEEGEDLEANVPEIETLDLPEDMNLDSEHEESDEDVDMSDGMPDDLNKEE-VGNEDEEVKQESGIESDNEN 4306
Cdd:COG5271 302 ESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDtQDAEDEAAGEAADESEGADT 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4307 DEPGPEEDAGETETALDEE-------------EGAEEDVDMTNDEGKEDEENG----PEEQAMSDEEElkQDAAMEENKE 4369
Cdd:COG5271 382 DAAADEADAAADDSADDEEasadggtsptsdtDEEEEEADEDASAGETEDESTdvtsAEDDIATDEEA--DSLADEEEEA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4370 KGGEQNTEGLDGVEEKADTEDIDQEAAVQQDSGSKGAGADATDTQEQDDVGGSGTTQNtyEEDQEDVTKNNEESREEATA 4449
Cdd:COG5271 460 EAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSAD--DGADTDAAADPEDSDEDALE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4450 ALKQLGDSMKEYHRRRQDIKEAQTNGEEDENLEKNNERPDEFEHVEGANTETDTQALGSATQDQLQTIDEDMAIDDDREE 4529
Cdd:COG5271 538 DETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADA 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4530 QEVDQKELVEDADDEKMDIDEEEMLSDIDAHDANNDVDSKKSGFIGKRKSEEDFENELSNEhfSADQEDDSEIQS-LIEN 4608
Cdd:COG5271 618 DADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDESETSSE--DAEEDADAAAAEaSDDE 695
|
570 580
....*....|....*....|...
gi 6323135 4609 IEDNPPDASASLTPERSLEESRE 4631
Cdd:COG5271 696 EETEEADEDAETASEEADAEEAD 718
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4047-4590 |
6.26e-18 |
|
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: 92.39 E-value: 6.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4047 QPPSEEVDDKNLQEGTGLGDGEGAQNNNKDVE---QDEDLTEDAQNENKEQQDKDERDDENEDDAVEMEGDMAGELEDLS 4123
Cdd:COG5271 481 ATDEDDASDDGDEEEAEEDAEAEADSDELTAEetsADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPE 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4124 NGEENDDEDTDSEEEELDEEIDDLNED----DPNAIDDKMWDDKASDNSKEKDTDQNlDGKNQEEDVQAAENDEQQRDNK 4199
Cdd:COG5271 561 ATAEEDEPDEAEAETEDATENADADETeesaDESEEAEASEDEAAEEEEADDDEADA-DADGAADEEETEEEAAEDEAAE 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4200 EGGDEDPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEGEDLEANVPEIETLDLPEDMNLDSEHEESDEDVDMSDgmp 4279
Cdd:COG5271 640 PETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADAEE--- 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4280 DDLNKEEVGNEDEEVKQESGiESDNENDEPGPEEDAGETEtaLDEEEGAEEDVDmTNDEGKEDEENGPEEQAmSDEEELK 4359
Cdd:COG5271 717 ADTEADGTAEEAEEAAEEAE-SADEEAASLPDEADAEEEA--EEAEEAEEDDAD-GLEEALEEEKADAEEAA-TDEEAEA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4360 QDAAMEENKEKGGEQNTEGLDGVEEKADTEDIDQEAAVQQDSGSKGAGADATDTQEQDDVGGSGTTQNTYEEDQEDVTKN 4439
Cdd:COG5271 792 AAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAAD 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4440 NEESREEATAALKQLGD----SMKEYHRRRQDIKEAQTNGEEDENLEKNNERPDEFEHVEGANTETDTQAlGSATQDQLQ 4515
Cdd:COG5271 872 EHEAEEAQEAETDADADadagEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELG-AAEDDLDAL 950
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323135 4516 TIDEDMAIDDDREEQEVDQKELVEDADDEKMDIDEEEMLSDIDAHDANNDVDSKKSGFIGKRKSEEDFENELSNE 4590
Cdd:COG5271 951 ALDEAGDEESDDAAADDAGDDSLADDDEALADAADDAEADDSELDASESTGEAEGDEDDDELEDGEAAAGEATAD 1025
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4050-4633 |
7.71e-17 |
|
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: 88.92 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4050 SEEVDDKNLQEGTGLGDGEGAQNNNKDVEQDEDLTEDAQNENKEQQDKDERDDENEDDAVEMEGDMAGELEDLSNGEEND 4129
Cdd:COG5271 79 SAESDAGASLITAANLEEGDIAGNAADDSADEESDANAKEDATDDADSSGDAQGDPLATDTLGGGDLDLATKDGDELLPS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4130 DEDTDSEEEELDEEIDDLNEDDPNAIDDKMWDDKASDNSKEKDTDQNLDGKNQEEDVQAAENDEQQRDNKEGGDEDPNaP 4209
Cdd:COG5271 159 LADNDEAAADEGDELAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASAVVEEEDA-S 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4210 EDGDEEIENDENAEEENDVGEQEDEVKDEEGEDLEANVPEIETLDLPEDMNLDSE-HEESDEDVDMSDGMPDDLNKEEVG 4288
Cdd:COG5271 238 EDAVAAADETLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAElTAAQAADPESDDDADDSTLAALEG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4289 NEDEEVKQESGIESDNENDEPGPEEDAGETETALDEEEGAEEDVDmTNDEGKEDEENGPEEQAMSDEEELK-QDAAMEEN 4367
Cdd:COG5271 318 AAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQ-DAEDEAAGEAADESEGADTDAAADEaDAAADDSA 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4368 KEKGGEQNTEGLDGVEEKADTEDIDQEAAVQQD--------SGSKGAGADATDTQEQDDVGGSGTTQNTYEEDQEDVTK- 4438
Cdd:COG5271 397 DDEEASADGGTSPTSDTDEEEEEADEDASAGETedestdvtSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDa 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4439 NNEESREEATAALKQLGDSMKEYHRRRQDIKEAQTNGEEDENLEKNNERPDEFEHVEGANTETDTQALGSATQDQLQTID 4518
Cdd:COG5271 477 DGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDADET 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4519 EDmaIDDDREEQEVDQKELVEDADDEKMDIDEEEMLSDIDAhDANNDVDSKKSGFI-GKRKSEEDFENELSNEHFSADQE 4597
Cdd:COG5271 557 DE--PEATAEEDEPDEAEAETEDATENADADETEESADESE-EAEASEDEAAEEEEaDDDEADADADGAADEEETEEEAA 633
|
570 580 590
....*....|....*....|....*....|....*.
gi 6323135 4598 DDSEIQSLIENIEDNPPDASASLTPERSLEESRELW 4633
Cdd:COG5271 634 EDEAAEPETDASEAADEDADAETEAEASADESEEEA 669
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1742-1879 |
1.29e-16 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 79.26 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1742 PILLEGSPGVGKTSLITALAN-ITGNKLTRINLSEQTDLVDLFGADAPGERSGEflWHDAPFLRAMKKGEWVLLDEMNLA 1820
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNIDPGGAS--WVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323135 1821 SQSVLEGLNACLDHRgeaYIPELDISFSCH---PNFLVFAAQNPQYQGGgrKGLPKSFVNRF 1879
Cdd:pfam07728 79 NPDVLNSLLSLLDER---RLLLPDGGELVKaapDGFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1226-1320 |
4.82e-16 |
|
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: 76.57 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1226 ELEIILRERCQIAPSYAKKIVEVYRQLSIERSASRLFEQKNS--FATLRDLFRWALR---------DAVGYEQLAASGYM 1294
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCRRlssllptllSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 6323135 1295 LLAERCRTPQEKVTVKKTLEKVMKVK 1320
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1078-1281 |
1.09e-14 |
|
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: 77.90 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1078 PVLIQGPTSSGKTSMIKYLADITGHKFVRINNHEHTDLQEYLGTYVTD-DTGKLSFKEGVLVEAlrkgywIVL-DELNLA 1155
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDqQTGEFEFRPGPLFAN------VLLaDEINRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1156 PTDV----LEALnrlldDNRELFIPEtQEVVHPHPdFLLFATQNPPGIYGGRKiLSRAFRNRFL-ELHFdDIPQDELEI- 1229
Cdd:COG0714 107 PPKTqsalLEAM-----EERQVTIPG-GTYKLPEP-FLVIATQNPIEQEGTYP-LPEAQLDRFLlKLYI-GYPDAEEERe 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6323135 1230 ILRERCQIAPSYAKKIVEVYRQLSIERSASRLFEQKNSFATLRDLFRwALRD 1281
Cdd:COG0714 178 ILRRHTGRHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVR-ATRE 228
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1732-1922 |
1.26e-14 |
|
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: 77.90 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1732 RVVRAMQV----HKPILLEGSPGVGKTSLITALANITGNKLTRINLSEQTDLVDLFGADAPGERSGEFLWHDAPFLRAMk 1807
Cdd:COG0714 19 ELIELVLIallaGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTGEFEFRPGPLFANV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1808 kgewVLLDEMNLAS---QSVLegLNAcLDHRgEAYIPELDISFScHPnFLVFAAQNPQYQGGGRKgLPKSFVNRFSV-VF 1883
Cdd:COG0714 98 ----LLADEINRAPpktQSAL--LEA-MEER-QVTIPGGTYKLP-EP-FLVIATQNPIEQEGTYP-LPEAQLDRFLLkLY 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6323135 1884 IDMLTSDDLLLI----AKHLYPSIEPDIIAKMIKLMSTLEDQV 1922
Cdd:COG0714 167 IGYPDAEEEREIlrrhTGRHLAEVEPVLSPEELLALQELVRQV 209
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4183-4451 |
1.56e-12 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 74.65 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4183 EEDVQAAENDEQQRDNkEGGDEDPNAPEDGDEEIENDENAEEENDVGEQEDEvKDEEGEDLEANVPEIETLDLPEDMNLD 4262
Cdd:TIGR00927 632 KGDVAEAEHTGERTGE-EGERPTEAEGENGEESGGEAEQEGETETKGENESE-GEIPAERKGEQEGEGEIEAKEADHKGE 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4263 SEHEESDEDVDMSDGMPDDLNKEEVGNEDEEVKQE------SGIESDNENDEPGPEEDAG-ETETALDEEEG---AEEDV 4332
Cdd:TIGR00927 710 TEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEgegeaeGKHEVETEGDRKETEHEGEtEAEGKEDEDEGeiqAGEDG 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4333 DMTNDEGkedeengpEEQAMSDEEELKQDAAMEENKEKGGEQNTEGLDGVEEKADTEDIDQEAAVQQDSGSKG-AGADAT 4411
Cdd:TIGR00927 790 EMKGDEG--------AEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGgGGSDGG 861
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6323135 4412 DTQEQDDvggsgttQNTYEEDQEDVTKNNEESREEATAAL 4451
Cdd:TIGR00927 862 DSEEEEE-------EEEEEEEEEEEEEEEEEEEEENEEPL 894
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4147-4631 |
1.16e-11 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 71.58 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4147 LNEDDPNAIDDKMWDDKASDNSKEKDTDQNLDGKNQEEDVQAAENDEQQRDNKEGGDEDPNAPEDGDEEIENDENAEEEN 4226
Cdd:COG5271 66 KLLDLKSADGAALSAESDAGASLITAANLEEGDIAGNAADDSADEESDANAKEDATDDADSSGDAQGDPLATDTLGGGDL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4227 DVGEQEDEVKDEEGEDLEANVPEIETLDLPEDMNLDSEHEESDEDvdmsdgmPDDLNKEEVGNEDEEVKQESGIESDNEN 4306
Cdd:COG5271 146 DLATKDGDELLPSLADNDEAAADEGDELAADGDDTLAVADAIEAT-------PGGTDAVELTATLGATVTTDPGDSVAAD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4307 DEPGPEEDAGETETALDEEEGAEEDVDMTNDEGKEDEENGPEEqamsDEEELKQDAAMEENKEKGGEQNTEGLDGVEEKA 4386
Cdd:COG5271 219 DDLAAEEGASAVVEEEDASEDAVAAADETLLADDDDTESAGAT----AEVGGTPDTDDEATDDADGLEAAEDDALDAELT 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4387 DTEDIDQEAAVQQDSGSKGAGADATDTQEqddvggsGTTQNTYEEDQEDVTKNNEESREEATAALKQLGDSMKEYHRRRQ 4466
Cdd:COG5271 295 AAQAADPESDDDADDSTLAALEGAAEDTE-------IATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4467 DIKEAQTNGE--EDENLEKNNERPDEFEHVEGANTETDTQALGSATQDQLQTIDED---MAIDDDREEQEVDQKELVEDA 4541
Cdd:COG5271 368 AAGEAADESEgaDTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDasaGETEDESTDVTSAEDDIATDE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4542 DDEKMDIDEEEMLSDIDAHDANNDVDSKKSGfiGKRKSEEDFENELSNEHFSADQEDDSEIQSLIENI--EDNPPDASAS 4619
Cdd:COG5271 448 EADSLADEEEEAEAELDTEEDTESAEEDADG--DEATDEDDASDDGDEEEAEEDAEAEADSDELTAEEtsADDGADTDAA 525
|
490
....*....|..
gi 6323135 4620 LTPERSLEESRE 4631
Cdd:COG5271 526 ADPEDSDEDALE 537
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4148-4457 |
1.28e-11 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 71.48 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4148 NEDDPNAidDKMWDDKASDNSKEKDTDQNLD-GKNQEEDVQAAENDEQQRDNKEGGDEDPNAPEDGDEEIENDENAEEEN 4226
Cdd:NF033609 561 SDSDPGS--DSGSDSSNSDSGSDSGSDSTSDsGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSAS 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4227 DVGEQEDEvkdeegeDLEANVPEIETLDLPEDMNLDSEHE-ESDEDVDMSDGMPDDLNKEEVGNEDEEVKQESGIESDNE 4305
Cdd:NF033609 639 DSDSDSDS-------DSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4306 NDEPGPEEDAGETETALDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEENKEKGGEQNTEGLDGVEEK 4385
Cdd:NF033609 712 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 791
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323135 4386 ADTE-DIDQEAAVQQDSGSKGAGADATDTQEQDDVGGSGTTQNTYEEDQEDVTKNNEESREEATAALKQLGDS 4457
Cdd:NF033609 792 SDSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDS 864
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4045-4447 |
1.64e-11 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 71.20 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4045 SPQPPSEEVDDKNLQEGTglGDGEgaqnnNKDVEQDEDLTEDAQNENKEQQDKDERDDENEDDAVEMEGDMAGELEDLSN 4124
Cdd:COG5271 644 ASEAADEDADAETEAEAS--ADES-----EEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADAEE 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4125 GEENDDEDTDSEEEELDEEiddlNEDDPNAIDDKMWDDKASDNSKEKDtdqnldgKNQEEDVQAAENDEQQRDNKEGGDE 4204
Cdd:COG5271 717 ADTEADGTAEEAEEAAEEA----ESADEEAASLPDEADAEEEAEEAEE-------AEEDDADGLEEALEEEKADAEEAAT 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4205 DPNAPEDGDEEIEND-ENAEEENDVGEQEDEVKDEEGEDLEANVPEIETLDLPEDMNlDSEHEESDEDVDMSDGMPDDLN 4283
Cdd:COG5271 786 DEEAEAAAEEKEKVAdEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGI-AEDDEEDDDAAAAKDVDADLDL 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4284 KEEVGNEDEEVKQESGIESDNENDEPGPEEDAGETETALDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAA 4363
Cdd:COG5271 865 DADLAADEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAE 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4364 MEENKEKGGEQNTEGLDGVEEKADTEDIDQEAAVQQDSGSKGAGADATDTQEQDDVGGSGTTQNTYEEDQEDVTKNNEES 4443
Cdd:COG5271 945 DDLDALALDEAGDEESDDAAADDAGDDSLADDDEALADAADDAEADDSELDASESTGEAEGDEDDDELEDGEAAAGEATA 1024
|
....
gi 6323135 4444 REEA 4447
Cdd:COG5271 1025 DLAA 1028
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4162-4460 |
2.76e-11 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 70.32 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4162 DKASDNSKEKDTDQNLDGKNQEEDVQAAENDEqqrdnkeggDEDPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEGE 4241
Cdd:NF033609 605 DSASDSDSASDSDSASDSDSASDSDSASDSDS---------ASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4242 -DLEANVPEIETLDLPEDMNLDSEHE-ESDEDVDMSDGMPDDLNKEEVGNEDEEVKQESGIESDNENDEPGPEEDAGETE 4319
Cdd:NF033609 676 sDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4320 TALDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEENKEKGGEQNTEGLDGVEEKADTE-DIDQEAAVQ 4398
Cdd:NF033609 756 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSD 835
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323135 4399 QDSGSKGAGADATDTQEQDDVGGSGTTQNTYEEDQEDVTKN------NEESREEATAALKQLGDSMKE 4460
Cdd:NF033609 836 SDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNspkngtNASNKNEAKDSKEPLPDTGSE 903
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4178-4376 |
3.32e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 68.84 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4178 DGKNQEEDVQAAENDEQQR-DNKEGGDEDPNAPEDgdeeiendENAEEENDVGEQEDEVKDEEGEDLEANVPEIETLDLP 4256
Cdd:PHA03169 50 APTTSGPQVRAVAEQGHRQtESDTETAEESRHGEK--------EERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4257 EDMNLDSEHEESDEDV--DMSDGMPDDLNKEEVGNEDEEVKQESGIESDNEN-DEPG------PEEDA---GETETALDE 4324
Cdd:PHA03169 122 NTSGSSPESPASHSPPpsPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDsPEEPepptsePEPDSpgpPQSETPTSS 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6323135 4325 EEGAEEdvdmtNDEGKEDEENGPEEQAMSDE-EELKQDAAMEENKEKGGEQNT 4376
Cdd:PHA03169 202 PPPQSP-----PDEPGEPQSPTPQQAPSPNTqQAVEHEDEPTEPEREGPPFPG 249
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
1743-1879 |
5.25e-11 |
|
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: 63.35 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1743 ILLEGSPGVGKTSLITALANITGNKLTRINLSeqTDLV--DLFGADAPGERSGEFLWHDAPFLramkkGEWVLLDEMNLA 1820
Cdd:pfam07726 2 VLLEGVPGLAKTLLVRTLARSLGLDFRRIQFT--PDLLpsDITGTEVFDQKTREFEFRPGPVF-----ANVLLADEINRA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323135 1821 S---QSVLegLNACLDHR----GEAY-IPELdisfschpnFLVFAAQNPQYQGGGRKgLPKSFVNRF 1879
Cdd:pfam07726 75 PpktQSAL--LEAMQERQvtidGETHpLPEP---------FFVLATQNPIEQEGTYP-LPEAQLDRF 129
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4247-4555 |
5.53e-11 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 69.64 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4247 VPEIETL-DLPEDMNLDSEH--EESDEDVDMSDGMPDDLNKEEVGNEDEEVKQESGIESDNENDEPGPEEDAGETETald 4323
Cdd:TIGR00927 621 VAKVMALgDLSKGDVAEAEHtgERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEG--- 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4324 EEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEEnKEKGGEQNTEGLDGVEEKADTEDIDQEAavqQDSGS 4403
Cdd:TIGR00927 698 EIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEE-VEDEGEGEAEGKHEVETEGDRKETEHEG---ETEAE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4404 KGAGADATDTQEQDDVGGSGTTQNTYEEDQEDVTKNNEESREEATAALKQLGDSMKEyhrrrqdikeaqTNGEEDENLEK 4483
Cdd:TIGR00927 774 GKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKD------------ETGEQELNAEN 841
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323135 4484 NNERPDEFEHVEGANtetdtqalGSATQDQlqtidedmaiDDDREEQEVDQKELVEDADDEKMDIDEEEMLS 4555
Cdd:TIGR00927 842 QGEAKQDEKGVDGGG--------GSDGGDS----------EEEEEEEEEEEEEEEEEEEEEEEEEENEEPLS 895
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4198-4495 |
1.32e-10 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 68.48 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4198 NKEGGDEDPNAPEDGDEEIENDEnaeeendVGEQEdevKDEEGEDleanvpeietldlpedmnlDSEHEESDEDVDMSDG 4277
Cdd:TIGR00927 631 SKGDVAEAEHTGERTGEEGERPT-------EAEGE---NGEESGG-------------------EAEQEGETETKGENES 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4278 MPDDLNKEEVGNEDE-EVKQESGIESDNENDEPGPEEDAGETETALDEEEG-AEEDVDMTNDEGKEDEENGPEEQAMSDE 4355
Cdd:TIGR00927 682 EGEIPAERKGEQEGEgEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIeTGEEGEEVEDEGEGEAEGKHEVETEGDR 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4356 EELKQDAAME-ENKEKGGEQNTEGLDGVEEKADTEDIDQ-EAAVQQDSGSKGAGADATDTQEQDDVGGSGTTQNTYEEDQ 4433
Cdd:TIGR00927 762 KETEHEGETEaEGKEDEDEGEIQAGEDGEMKGDEGAEGKvEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAEN 841
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323135 4434 EDVTKNNEESREEATAAlkQLGDSMKEYHRRRQDIKEAQTNGEEDENlEKNNERPDEFEHVE 4495
Cdd:TIGR00927 842 QGEAKQDEKGVDGGGGS--DGGDSEEEEEEEEEEEEEEEEEEEEEEE-EEENEEPLSLEWPE 900
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4255-4631 |
1.98e-10 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 67.63 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4255 LPEDMNLDSEHEESDEDVDM---SDGMPDDLNKEEVGNEDEEVKQESGIESDNENDEPGPEEDAGETETALDEEEGAEED 4331
Cdd:NF033609 544 VPEQPDEPGEIEPIPEDSDSdpgSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSD 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4332 VDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEENKEKGGEQNTEGlDGVEEKADTEDIDQEAAVQQDSGSKGAGADAT 4411
Cdd:NF033609 624 SASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4412 DTQEQDDVGGSGTTQNTYEEDQEDVTKNNEESREEATAALKQLGDSmkeyhrrrqdikEAQTNGEEDENLEKNNErpdef 4491
Cdd:NF033609 703 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS------------DSDSDSDSDSDSDSDSD----- 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4492 ehvegANTETDTQALGSATQDQLQTIDEDMAIDDDREEQEVDQKELVEDAD-DEKMDIDeeemlSDIDAhDANNDVDSKK 4570
Cdd:NF033609 766 -----SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSD-----SDSDS-DSDSDSDSDS 834
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323135 4571 SGFIGKRKSEEDFENELSNEHFSADQEDDSEIQSLIENIEDNPPDASASLTPERSLEESRE 4631
Cdd:NF033609 835 DSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASNKNEAKDSKE 895
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4229-4450 |
3.14e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 65.76 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4229 GEQEDEVKDEEGEDLEANvpeietldlpEDMNLDSEHEESDEDvdmSDGMPDDLNKEEVGNEDeevkqesgiesdnende 4308
Cdd:PHA03169 55 GPQVRAVAEQGHRQTESD----------TETAEESRHGEKEER---GQGGPSGSGSESVGSPT----------------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4309 PGPEEDAGETETALDEEEGAEEdvdmtNDEGKEDEENGPEEQAmsdEEELKQDAAMEENKEKGGEQNTEGLDGVEEKADT 4388
Cdd:PHA03169 105 PSPSGSAEELASGLSPENTSGS-----SPESPASHSPPPSPPS---HPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323135 4389 EDIDQEAAVQQDSGSKGAGADATDTQEQDDVGGSGTTQNTYEEDQEDVTKNNEESREEATAA 4450
Cdd:PHA03169 177 EPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPT 238
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4046-4393 |
3.57e-10 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 66.86 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4046 PQPPSEEVDDKNLQEGT----GLGDGEGAQNNNKDVEQDEDLTEDAQNENKEQQDKDERDDENEDDAVEMEGDMAGELED 4121
Cdd:NF033609 545 PEQPDEPGEIEPIPEDSdsdpGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDS 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4122 LSNGEENDDEDTDSEEEELDEEIDDLNEDDPNAIDDKMWDDKASDNSKEKDTDQNLDGKNQEEDVQAAENDEqqrDNKEG 4201
Cdd:NF033609 625 ASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS---DSDSD 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4202 GDEDPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEGE-DLEANVPEIETLDLPEDMNLDSEhEESDEDVDMSDGMPD 4280
Cdd:NF033609 702 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDS 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4281 DLNKEEVGNEDEEVKQESGIESDNENDEPGPEEDAGETETALDEEEGAEEDVDMTNDEGKE---------DEENGPEEQA 4351
Cdd:NF033609 781 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsdsdsdsdsDSDSDSESDS 860
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 6323135 4352 MSDEEELKQDAAMEENKEKGG---EQNTEGLDGVEEKADTEDIDQ 4393
Cdd:NF033609 861 NSDSESGSNNNVVPPNSPKNGtnaSNKNEAKDSKEPLPDTGSEDE 905
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
4153-4393 |
4.63e-10 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 66.35 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4153 NAIDDKMWDDKASDNSKEKDTdQNLDGK--------NQEEDVQAAENDEQQRDNKEGgdedpNAPEDGDEEIENDENAEE 4224
Cdd:PTZ00341 890 NAIEKYAGGGKKDKKAKKKDA-KDLSGNiaheinliNKELKNQNENVPEHLKEHAEA-----NIEEDAEENVEEDAEENV 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4225 ENDVGEQ-EDEVKDEEGEDLEANVPEIETLDLPEDM--NLDSEHEES-DEDVDMSDGMPDDLNKEEVGNEDEEVKQESgI 4300
Cdd:PTZ00341 964 EENVEENvEENVEENVEENVEENVEENVEENVEENVeeNIEENVEENvEENIEENVEEYDEENVEEVEENVEEYDEEN-V 1042
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4301 ESDNENDEPGPEEDAGETETALDEE--EGAEEDVDMTNDEGKED--EENgPEEQAMSDEEELKQDAamEENKEKGGEQNT 4376
Cdd:PTZ00341 1043 EEIEENAEENVEENIEENIEEYDEEnvEEIEENIEENIEENVEEnvEEN-VEEIEENVEENVEENA--EENAEENAEENA 1119
|
250
....*....|....*..
gi 6323135 4377 EGLDGVEEKADTEDIDQ 4393
Cdd:PTZ00341 1120 EEYDDENPEEHNEEYDE 1136
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
4282-4490 |
1.01e-09 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 65.58 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4282 LNKE---EVGNEDEEVKQ--ESGIESD-NENDEPGPEEDAGET-ETALDE--EEGAEEDVDMTNDEGKED--EENGPEEQ 4350
Cdd:PTZ00341 924 INKElknQNENVPEHLKEhaEANIEEDaEENVEEDAEENVEENvEENVEEnvEENVEENVEENVEENVEEnvEENVEENI 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4351 AMSDEEELKQDaaMEENKEKGGEQNTEGLDGVEEKADTEDIDQ-EAAVQQDSgskgagadATDTQEQDDVGGSGTTQNTY 4429
Cdd:PTZ00341 1004 EENVEENVEEN--IEENVEEYDEENVEEVEENVEEYDEENVEEiEENAEENV--------EENIEENIEEYDEENVEEIE 1073
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323135 4430 EEDQEDVTKNNEESREEATAALKQLGDSMKEYHRRRQDIKEAQTNGEE--DENLEKNNERPDE 4490
Cdd:PTZ00341 1074 ENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEydDENPEEHNEEYDE 1136
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4270-4552 |
1.68e-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: 64.63 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4270 EDVDMSDGMPDDLNKEEVGNEDE-------EVKQESGIESDN--ENDEPGPEEDAGETETAL-----DEEEGAEEDVDMT 4335
Cdd:TIGR00927 628 GDLSKGDVAEAEHTGERTGEEGErpteaegENGEESGGEAEQegETETKGENESEGEIPAERkgeqeGEGEIEAKEADHK 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4336 NDEGKEDEENGPEEQAMSDEEElKQDAAMEENKEKGGEQNTE--GLDGVEEKADTEDIDQEAavqQDSGSKGAGADATDT 4413
Cdd:TIGR00927 708 GETEAEEVEHEGETEAEGTEDE-GEIETGEEGEEVEDEGEGEaeGKHEVETEGDRKETEHEG---ETEAEGKEDEDEGEI 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4414 QEQDDVGGSGTTQNTYEEDQEDVTKNNEESREEATAALKQLGDSMKEyhrrrqdikeaqTNGEEDENLEKNNERPDEFEH 4493
Cdd:TIGR00927 784 QAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKD------------ETGEQELNAENQGEAKQDEKG 851
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323135 4494 VEGANtetdtqalGSATQDQLQTIDEDMAIDDDREEQEVDQKElvEDADDEKMDIDEEE 4552
Cdd:TIGR00927 852 VDGGG--------GSDGGDSEEEEEEEEEEEEEEEEEEEEEEE--EEENEEPLSLEWPE 900
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
4703-4855 |
2.50e-09 |
|
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: 59.50 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4703 YQIMIALDDSKSMSESKcVKLAFDSLCLVSKTLTQLEAGG-LSIVKFGENIKEVHSFDQQFSNESGARAFQWFGFQ-ETK 4780
Cdd:cd00198 1 ADIVFLLDVSGSMGGEK-LDKAKEALKALVSSLSASPPGDrVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323135 4781 TDVKKLVAESTKIFERARamvHNDQWQLEIVISDGICEDH-ETIQKLVRRARENKIMLVFVIIDGITSNESILDMS 4855
Cdd:cd00198 80 TNIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDGpELLAEAARELRKLGITVYTIGIGDDANEDELKEIA 152
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4163-4569 |
2.65e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4163 KASDNSKEKDTDQNLDGKNQEEDVQAAENDEQQRDNKEGGDEDPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEGED 4242
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4243 LEANVPEIETLDLPEDMNLDSEHEESDEDVDMSDGmpDDLNKEEVGN----------EDEEVKQESGIESDNENDEPGPE 4312
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA--EELKKAEEENkikaaeeakkAEEDKKKAEEAKKAEEDEKKAAE 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4313 EDAGETETALDEEE---GAEEDVDMTNDEGKEDEENGPE-EQAMSDEEELKQDAamEENKEKGGEQN-TEGLDGVEEKAD 4387
Cdd:PTZ00121 1693 ALKKEAEEAKKAEElkkKEAEEKKKAEELKKAEEENKIKaEEAKKEAEEDKKKA--EEAKKDEEEKKkIAHLKKEEEKKA 1770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4388 TEDIDQEAAVQQDsgskgaGADATDTQEQDDVGGS-GTTQNTYEEDQEDVTKNN---EESREEATAALKQLGDSmKEYHR 4463
Cdd:PTZ00121 1771 EEIRKEKEAVIEE------ELDEEDEKRRMEVDKKiKDIFDNFANIIEGGKEGNlviNDSKEMEDSAIKEVADS-KNMQL 1843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4464 RRQDIKEAQTNGEEDENLEKNNERPDefehvegANTETDtqaLGSATQDQLQTIDEDMAIDDDREEQEVDQKELV---ED 4540
Cdd:PTZ00121 1844 EEADAFEKHKFNKNNENGEDGNKEAD-------FNKEKD---LKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAgknND 1913
|
410 420 430
....*....|....*....|....*....|....*....
gi 6323135 4541 ADDEKMDIDE----------EEMLSDIDAHDANNDVDSK 4569
Cdd:PTZ00121 1914 IIDDKLDKDEyikrdaeetrEEIIKISKKDMCINDFSSK 1952
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4161-4347 |
4.26e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 62.30 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4161 DDKASDNSKEKDTDQNLDGKNQEEDvQAAENDEQQRDNKEGGDEDPNAPEDgdeeiendenaeEENDVGEQEDEVKDEEG 4240
Cdd:PHA03169 84 KEERGQGGPSGSGSESVGSPTPSPS-GSAEELASGLSPENTSGSSPESPAS------------HSPPPSPPSHPGPHEPA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4241 EDLEANVPEIETldlpEDMNLDSEHEESDEDVDMSDGMPDDlnkEEVGNEDEEVKQESGIESDnENDEPGPE-EDAGETE 4319
Cdd:PHA03169 151 PPESHNPSPNQQ----PSSFLQPSHEDSPEEPEPPTSEPEP---DSPGPPQSETPTSSPPPQS-PPDEPGEPqSPTPQQA 222
|
170 180
....*....|....*....|....*...
gi 6323135 4320 TALDEEEGAEEDVDMTNDEGKEDEENGP 4347
Cdd:PHA03169 223 PSPNTQQAVEHEDEPTEPEREGPPFPGH 250
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4328-4601 |
4.39e-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: 63.48 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4328 AEEDVDMTNDEGKEdeengPEEQAMSDEEELKQDAAMEENKEKGGEQNTEGLDGVEEKADTEDidqEAAVQQDSGSKGAG 4407
Cdd:TIGR00927 638 AEHTGERTGEEGER-----PTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEG---EGEIEAKEADHKGE 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4408 ADATDTQEQDDVGGSGTTQNTYEEDQEDVTKNNEESREEATAalkqlgdsmKEYHRRRQDIKEAQTNGEEdENLEKNNER 4487
Cdd:TIGR00927 710 TEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEG---------KHEVETEGDRKETEHEGET-EAEGKEDED 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4488 PDEFEHVEGANTETDTQALGSATQDQLQTIDEDMAIDDDREEQEVDQKELVEDAddekmdidEEEMLSDI--DAHDANND 4565
Cdd:TIGR00927 780 EGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG--------EQELNAENqgEAKQDEKG 851
|
250 260 270
....*....|....*....|....*....|....*.
gi 6323135 4566 VDSKKSGFIGKRKSEEDFENELSNEHFSADQEDDSE 4601
Cdd:TIGR00927 852 VDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEE 887
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4065-4364 |
4.86e-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: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4065 GDGEGAQNNNKDVEQDEDLTEDAQNENKEQQDKDERDDENEDDAVE--MEGDMAGELEDlsngeenddedtdseeeelde 4142
Cdd:TIGR00927 633 GDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGEneSEGEIPAERKG--------------------- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4143 eiddlNEDDPNAIDDKMWDDKASDNSKEKDTDQNL--DGKNQEEDVQAAENDEQQRDNKEGGDEDPNAPEDGDEEIENDE 4220
Cdd:TIGR00927 692 -----EQEGEGEIEAKEADHKGETEAEEVEHEGETeaEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEH 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4221 NAEEENDVGEQEDEVKDEEGEDLEANVPEIEtldlpEDMNLDSEHEESDEDVDMSDGMPDDLNKEEVGNEDEEVKQESGI 4300
Cdd:TIGR00927 767 EGETEAEGKEDEDEGEIQAGEDGEMKGDEGA-----EGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAEN 841
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323135 4301 ESDNENDEPGPEE----DAGETEtalDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDE-EELKQDAAM 4364
Cdd:TIGR00927 842 QGEAKQDEKGVDGgggsDGGDSE---EEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEwPETRQKQAI 907
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2190-2276 |
1.12e-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: 56.53 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 2190 VKFEWFDGMLVKAVEKGHWLILDNANLCSPSVLDRLNSLLEiDGSLLInecsqEDGQPRVLKPHPNFRLFLTMDPKYG-- 2267
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLD-ERRLLL-----PDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 6323135 2268 -ELSRAMRNR 2276
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4156-4369 |
1.53e-08 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 61.55 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4156 DDKMWDDKASDNSKEKDTDQNLDGKNQEEDVQAAENDEQQRDNKEGGDEDPNAPEDGDEEIENdeNAEEENDVGEQEDEV 4235
Cdd:TIGR00927 674 ETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGE--EGEEVEDEGEGEAEG 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4236 KDEEGEDLEANVPEIETLDLPEDMNLDSEHE-ESDEDVDMSDGMPDDLNKEEVGNEDEEVKQESGIESDNENDEPGPEED 4314
Cdd:TIGR00927 752 KHEVETEGDRKETEHEGETEAEGKEDEDEGEiQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDE 831
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323135 4315 AGETETALDEEEGAEEDVDMTNDEG------KEDEENGPEEQAMSDEEELKQDAAMEENKE 4369
Cdd:TIGR00927 832 TGEQELNAENQGEAKQDEKGVDGGGgsdggdSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
4162-4562 |
2.20e-08 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 60.43 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4162 DKASDNSKEKDTDQNLDGKNQEEDVQAAENDEQqrdnkeggdEDPNAPEDGDeeiendenaeeenDVGEQEDEVKDEEGE 4241
Cdd:pfam01271 184 DTPSKQKREKSDEREKSSQESGEDTYRQENIPQ---------EDQVGPEDQE-------------PSEEGEEDATQEEVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4242 DLEANVPEIETLdlPEDMNLDSEHEESDEDVDMSDG---MPDDLNKEEVGNEDEEVKQESGIESDNENDEPGPEEDAGEt 4318
Cdd:pfam01271 242 RSRPRTHHGRSL--PDESSRGGQLGLEEEASEEEEEygeESRGLSAVQTYLLRLVNARGRGRSEKRAERERSEESEEEE- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4319 etalDEEEGAEEDVDMTNDEgkedeeNGPEeqamSDEEELKQDAAMEENKEKGGEQNTEGLDGVEEKADTEDidQEAAVQ 4398
Cdd:pfam01271 319 ----LKRASPYEELEITANL------QIPP----SEEERMLKKAGRSPRGRVDEAGALEALEALEEKRKLDL--DHSRVF 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4399 QDSGSKGAGADATDTQEQD----DVGGSGTTQNTyeeDQEDVTKNNEESREEATAALKQ-LGDSMKEYHRRRQ---DIKE 4470
Cdd:pfam01271 383 ESSEDGAPRAPQGAWVEALrnylSYGEEGMEGKW---NQQGPYFPNEENREEARFRLPQyLGELSNPWEDPKQwkpSDFE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4471 AQTN-------GEEDENL---------EKNNERPdEFEhVEGANTETDTQALGSATQDQLQTIDEDMAIDDDREEQEVdQ 4534
Cdd:pfam01271 460 RKELtadkfleGEEENEYtlsmknsfpEYNYDGY-EKR-VPSPGLDLKRQYDPVAREDQLLHYRKKSSEFPDFYDSEE-K 536
|
410 420 430
....*....|....*....|....*....|...
gi 6323135 4535 KELVEDADDEK-----MDIDEEEMLSDIDAHDA 4562
Cdd:pfam01271 537 KEPPVGAEKEEdsanrQTRDEDKELENLAAMDL 569
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
310-427 |
2.60e-08 |
|
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: 58.64 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 310 PIMLIGKAGSGKTFLINELSKYMGCHDSIVKIHlgEQTDAKLLIGTYTSGDKPGTFEWRAGVLATAVkegrwVLIEDIDK 389
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFT--PDLLPSDILGTYIYDQQTGEFEFRPGPLFANV-----LLADEINR 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 6323135 390 APTDVLSILLSLLEKRELTIPsrGETVKAANGFQLIST 427
Cdd:COG0714 106 APPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIAT 141
|
|
| DMP1 |
pfam07263 |
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ... |
4285-4630 |
5.15e-08 |
|
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.
Pssm-ID: 462128 [Multi-domain] Cd Length: 519 Bit Score: 59.17 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4285 EEVGNED--EEVKQESGIESDNENDEPGPeeDAGETETALDEEEGAEEDVDMTNDEGKEDEENGPeeqamsdeeelkqda 4362
Cdd:pfam07263 58 EEQANEDpsDSTESEEDLGSDDGQYVYRP--AGGLSRSGGKEGDDKDDDEDDSGDDTFGDEDNGP--------------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4363 ameenkekGGEQNTEGldGVEEKADTEDidqeaavqqdsgskgaGADATDTQEQDDVGGSGTTQNTYEEDQEdvtKNNEE 4442
Cdd:pfam07263 121 --------GPEERQEG--GNSRLGSDED----------------SADTTQSREDSASQGEDSAQDTTSESRD---LDNED 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4443 SREEATAALKQLGDSMKEYHRR--RQDIKEAQTNGEEDENLEKNNERPDEFEHvEGANTETDTQALGSatqDQLQTIDED 4520
Cdd:pfam07263 172 EVSSRPESGDSTQDSESEEHWVggGSEGDSSHGDGSEFDDEGMQSDDPDSIRS-ERGNSRMSSASVKS---KESKGDSEQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4521 MAIDDDREEQEVDQKelvEDADDEKMDIDEEEMLSDIDAHDANNDVDS-----KKSGFIGKRKSEEDFENElSNE--HFS 4593
Cdd:pfam07263 248 ASTQDSGDSQSVEYP---SRKFFRKSRISEEDDRGELDDSNTMEEVKSdstesTSSKEAGLSQSREDSKSE-SQEdsEES 323
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 6323135 4594 ADQEDDSEIQSLIENI---EDNPPDASASLTPERSLEESR 4630
Cdd:pfam07263 324 QSQEDSQNSQDPSSESsqeADLPSQESSSESQEEVVSESR 363
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4323-4590 |
7.03e-08 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 59.24 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4323 DEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEENKEKGGEQNTEGlDGVEEKADTEDIDQEAavqqdsg 4402
Cdd:TIGR00927 646 GEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEA-KEADHKGETEAEEVEH------- 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4403 SKGAGADATDTQEQDDVGGSGTtqntyEEDQEDVTKNNEESREEATAALKQLGDSMKEYHRRRQDIKEAQTNGEEDENLE 4482
Cdd:TIGR00927 718 EGETEAEGTEDEGEIETGEEGE-----EVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMK 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4483 KNNERPDEFEHveGANTETDTQALGsatQDQLQTIDEDMAIDDDREEQEVDQKELVEDADDEKmDIDEEEMLSDIDAHDA 4562
Cdd:TIGR00927 793 GDEGAEGKVEH--EGETEAGEKDEH---EGQSETQADDTEVKDETGEQELNAENQGEAKQDEK-GVDGGGGSDGGDSEEE 866
|
250 260
....*....|....*....|....*...
gi 6323135 4563 NNDVDSKKSgfigkrKSEEDFENELSNE 4590
Cdd:TIGR00927 867 EEEEEEEEE------EEEEEEEEEEEEE 888
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4158-4631 |
9.44e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 9.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4158 KMWDDKASDNSKEKDTDQNLDGKNQEEDVQAAENDEQQRDNKEGGDEDPNAPEDGDeeiendenaeeendvgEQEDEVKD 4237
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK----------------KKADELKK 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4238 EEGEDLEANVPEIETLDLPEDMNLDSEHEESDEDVDMSDGMPDDLNKEEVGNEDEEVKQESGIESDNENDEPGPE--EDA 4315
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakKKA 1492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4316 GETETALDEEEGAEEDvDMTNDEGKEDEENGPEEQAMSDEEELKQDAAME-ENKEKGGE-QNTEGLDGVEEKADTEDIDQ 4393
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaEEKKKADElKKAEELKKAEEKKKAEEAKK 1571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4394 EAAVQQDSGSKGAGADATDTQEQDDVGGSGTTQNTYEEDQ----EDVTKNNEESR--EEATAALKQLGDSMKEYHRRRQD 4467
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEE 1651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4468 IKEAqtngEEDENLEKNNERPDEFEHVEGANTETDTQALGSATQDQLQTIDEDMaidddREEQEVDQKELVEDADDEKMD 4547
Cdd:PTZ00121 1652 LKKA----EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELKKKEAEEKKKAEELK 1722
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4548 IDEEEMLSDIDAHDANNDVDSKKSGFIGKRKSEEDFENELSNEHFSADQEDDSEIQSLIENiEDNPPDASASLTPERSLE 4627
Cdd:PTZ00121 1723 KAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE-ELDEEDEKRRMEVDKKIK 1801
|
....
gi 6323135 4628 ESRE 4631
Cdd:PTZ00121 1802 DIFD 1805
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
4331-4552 |
1.38e-07 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 58.26 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4331 DVDMTNDEGKEDEENGPEEQAMSDEEELKQDAamEENKEKGGEQNTEglDGVEEKADtEDIDQ--EAAVQQDSgskgaga 4408
Cdd:PTZ00341 920 EINLINKELKNQNENVPEHLKEHAEANIEEDA--EENVEEDAEENVE--ENVEENVE-ENVEEnvEENVEENV------- 987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4409 datdtqeQDDVggsgtTQNTYEEDQEDVTKNNEESREE---------ATAALKQLGDSMKEYHrrRQDIKEAQTNGEE-- 4477
Cdd:PTZ00341 988 -------EENV-----EENVEENVEENIEENVEENVEEnieenveeyDEENVEEVEENVEEYD--EENVEEIEENAEEnv 1053
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4478 DENLEKNNERPDE--FEHVEGANTETDTQALGSATQDQLQTIDEDMA--IDDDREEQ-EVDQKELVEDADDEKMDIDEEE 4552
Cdd:PTZ00341 1054 EENIEENIEEYDEenVEEIEENIEENIEENVEENVEENVEEIEENVEenVEENAEENaEENAEENAEEYDDENPEEHNEE 1133
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
2198-2264 |
4.82e-07 |
|
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: 51.29 E-value: 4.82e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323135 2198 MLVKAVEKGHWLILDNANLcSPSVLDRLNSLLEIDGSLlinecsqedgqprvlKPHPNFRLFLTMDP 2264
Cdd:pfam03028 49 LIEEAAKEGGWVLLQNCHL-ALSWMPELEKILEELPEE---------------TLHPDFRLWLTSEP 99
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
4230-4553 |
1.21e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.87 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4230 EQEDEVKDEEGEDLEANVPEIETldlPEDMNLDSEHEES--------DEDVDMSD-----------GMPDDLNKEEvgNE 4290
Cdd:pfam02029 15 AREERRRQKEEEEPSGQVTESVE---PNEHNSYEEDSELkpsgqgglDEEEAFLDrtakreerrqkRLQEALERQK--EF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4291 DEEVKQES-GIESDNENDEPGPEEDAGETETALDEEEGAEEDVDMTNDegKEDEENGPEEQAMSDEEELKQDAAMEENKE 4369
Cdd:pfam02029 90 DPTIADEKeSVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIRE--KEYQENKWSTEVRQAEEEGEEEEDKSEEAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4370 KGGEQNTEGLDGVEEKADTED---IDQEAAVQQDSG-SKGAGADATDTqeqddvggsgTTQNTYEEDQEDVTKNNEESRE 4445
Cdd:pfam02029 168 EVPTENFAKEEVKDEKIKKEKkvkYESKVFLDQKRGhPEVKSQNGEEE----------VTKLKVTTKRRQGGLSQSQERE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4446 EATAALKQLGDSMKEYHRRRQDIKEaqtngEEDENL-EKNNERPDEFEHvegantetdtqaLGSATQDQLQTIDEdmaiD 4524
Cdd:pfam02029 238 EEAEVFLEAEQKLEELRRRRQEKES-----EEFEKLrQKQQEAELELEE------------LKKKREERRKLLEE----E 296
|
330 340
....*....|....*....|....*....
gi 6323135 4525 DDREEQEVDQKELVEDADDEKMdidEEEM 4553
Cdd:pfam02029 297 EQRRKQEEAERKLREEEEKRRM---KEEI 322
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
648-703 |
2.15e-06 |
|
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: 49.98 E-value: 2.15e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323135 648 PVLLVGETGTGKTTVVQQLAKMLA-KKLTVINVSQQTETGDLLGGYKPVNSKTVAVP 703
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVD 57
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4280-4396 |
3.47e-06 |
|
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: 53.26 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4280 DDLNKEEVGNEDEEVKQEsgiESDNENDEPGPEEDAGETETALDEEEGAEEDvdmtNDEGKEDEENGPEEQAMSDEEELK 4359
Cdd:COG4547 203 RDLDLAEELGEDEDEEDE---DDEDDSGEQEEDEEDGEDEDEESDEGAEAED----AEASGDDAEEGESEAAEAESDEMA 275
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 6323135 4360 QDAAMEENKEKGG--EQNTEGLDGVEE---KADTEDIDQEAA 4396
Cdd:COG4547 276 EEAEGEDSEEPGEpwRPNAPPPDDPADpdyKVFTTAFDEVVA 317
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1729-1881 |
4.05e-06 |
|
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: 49.84 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1729 NLVRVVRAMQVHKPILLEGSPGVGKTSLITALANITGNKLTRINlseQTDLVDLFGADAPGERSGEFLWHDAPFLRAMKK 1808
Cdd:cd00009 8 EALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFL---YLNASDLLEGLVVAELFGHFLVRLLFELAEKAK 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323135 1809 GEWVLLDEMNLASQSVLEGLNACLDhrgeayipELDISFSCHPNFLVFAAQNPQYQGGGRKGLPKSFVNRFSV 1881
Cdd:cd00009 85 PGVLFIDEIDSLSRGAQNALLRVLE--------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVI 149
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
629-683 |
4.39e-06 |
|
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: 50.08 E-value: 4.39e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323135 629 TNHSLRLMEQISVCIQMTEPVLLVGETGTGKTTVVQQLAKMLAKK---LTVINVSQQT 683
Cdd:pfam12775 14 TVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEkylPLFINFSAQT 71
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1361-1558 |
4.42e-06 |
|
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: 49.68 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1361 KEPVLLVGETGCGKTTICQLLAQFMGRE---LITLNAhQNTETGDILGAQRPVRNRSEIQYKLIKSLKTALNIANDQDVD 1437
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDG-EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1438 LkellqlysksdnkniaedvqleiqklrdslnvlfewsdgpliqamrtgnfFLLDEISLADDSVLERLNSVLEPERSLLL 1517
Cdd:smart00382 81 V--------------------------------------------------LILDEITSLLDAEQEALLLLLEELRLLLL 110
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6323135 1518 AEQgssdslvtaSENFQFFATMNPGGDYGKKELSPALRNRF 1558
Cdd:smart00382 111 LKS---------EKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
4161-4397 |
5.26e-06 |
|
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) or RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II.
Pssm-ID: 310411 [Multi-domain] Cd Length: 528 Bit Score: 52.64 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4161 DDKASDNSKEKDTDQNLDGKNQEEDVQAAENDEQqrdnkEGGDEDPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEG 4240
Cdd:pfam05793 189 PAAFGEHDEETEGEKGGGGRGKDLKIKDLEGDDE-----DDGDESDKGGEDGDEEKKKKKKKKLAKNKKKLDDDKKKKRG 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4241 EDLEANVPEIEtldlpedmnlDSEHEESDEDVdMSDGmpddlnkEEVGNEDEEvkqesgiesdnENDEPgpeedagetet 4320
Cdd:pfam05793 264 GDDDAFEYDSD----------DGDDEGREEDY-ISDS-------SASGNDPEE-----------REDKL----------- 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323135 4321 alDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEE-ELKQDaameeNKEKGGEQNTEGLDGveEKADTEDIDQEAAV 4397
Cdd:pfam05793 304 --SPEEPAKGEIEQSDDSEESEEEKNEEEGKLSKKGkKAKKL-----KGKKNGKDKSESSDG--DDSDDSDIDDEDSV 372
|
|
| COG5137 |
COG5137 |
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ... |
4263-4447 |
5.78e-06 |
|
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];
Pssm-ID: 227466 [Multi-domain] Cd Length: 279 Bit Score: 51.54 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4263 SEHEESDEDVDMSDgmpddlNKEEVGNEDEEVKQESGIE-SDNENDEPGPE-EDAGETETALDEEEGAEEDvdmtndegK 4340
Cdd:COG5137 126 SDVEEPSEKVDEED------VEREILAEKPRVTRFNIVWdNDEDNDEAPPAqPDVDNEEEERLEESDGREE--------E 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4341 EDEENGPEEQAMSDEEELKQdaamEENKEKGGEQNTEGLDGVEEKADTEDIDQEaavqqdsgskgagadatdtQEQDDVG 4420
Cdd:COG5137 192 EDEEVGSDSYGEGNRELNEE----EEEEAEGSDDGEDVVDYEGERIDKKQGEEE-------------------EMEEEVI 248
|
170 180
....*....|....*....|....*..
gi 6323135 4421 GSGTTQNTYEEDQEDVTKNNEESREEA 4447
Cdd:COG5137 249 NLFEIEWEEESPSEEVPRNNEESPAKK 275
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
4155-4413 |
6.40e-06 |
|
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) or RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II.
Pssm-ID: 310411 [Multi-domain] Cd Length: 528 Bit Score: 52.64 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4155 IDDKMWDDKASDNSKEKDTDQNLDGKNQEEDVQAAENDEQQRDNKE---GGDEDPNAPE--DGDeeiendenaeeenDVG 4229
Cdd:pfam05793 214 IKDLEGDDEDDGDESDKGGEDGDEEKKKKKKKKLAKNKKKLDDDKKkkrGGDDDAFEYDsdDGD-------------DEG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4230 EQEDEVKDEEGEdleanvpeietldlpedmnlDSEHEEsdedvdmsdgmpddlnKEEVGNEDEEVKQESGI-ESDNENDE 4308
Cdd:pfam05793 281 REEDYISDSSAS--------------------GNDPEE----------------REDKLSPEEPAKGEIEQsDDSEESEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4309 PGPEEDAGETEtaldEEEGAEEDVDMTNDEGKEDEENGpEEQAMSDEEELKQDAAMEENKEKggeqntegldgveEKADT 4388
Cdd:pfam05793 325 EKNEEEGKLSK----KGKKAKKLKGKKNGKDKSESSDG-DDSDDSDIDDEDSVPLFTAKKKK-------------EPKKE 386
|
250 260
....*....|....*....|....*
gi 6323135 4389 EDIDQEAAVQQDSGSKGAGADATDT 4413
Cdd:pfam05793 387 EPVDSGPSSPGNSGPARPSPESGST 411
|
|
| DMP1 |
pfam07263 |
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ... |
4169-4545 |
6.43e-06 |
|
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.
Pssm-ID: 462128 [Multi-domain] Cd Length: 519 Bit Score: 52.62 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4169 KEKDTDQNLDGKNQEEDvqaaeNDEQQRDNKEGGDEDPNAPEDGDEEIENDENAEEENDVGEQ--EDEVKDEEGEDLEAN 4246
Cdd:pfam07263 101 KDDDEDDSGDDTFGDED-----NGPGPEERQEGGNSRLGSDEDSADTTQSREDSASQGEDSAQdtTSESRDLDNEDEVSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4247 VPEietldlPEDMNLDSEHEE------SDEDVDMSDGMPDDlnKEEVGNED-EEVKQESG---IESD-------NENDEP 4309
Cdd:pfam07263 176 RPE------SGDSTQDSESEEhwvgggSEGDSSHGDGSEFD--DEGMQSDDpDSIRSERGnsrMSSAsvkskesKGDSEQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4310 GPEEDAGETETA------------LDEEEG--------AEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEENKE 4369
Cdd:pfam07263 248 ASTQDSGDSQSVeypsrkffrksrISEEDDrgelddsnTMEEVKSDSTESTSSKEAGLSQSREDSKSESQEDSEESQSQE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4370 KG-GEQNTEGLDGVEEKADTEDIDQEAAVQQDSGSKGAGADAT----------DTQEQDDVGGSGTTQNTYEEDQEDVTK 4438
Cdd:pfam07263 328 DSqNSQDPSSESSQEADLPSQESSSESQEEVVSESRGDNPDNTssseedqedsDSSEEDSLSTFSSSESESREEQADSES 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4439 N-----NEESREeataalkqlgdSMKEYHRRRQDIKEAQTNGEEDENLEKNNERPDEFEHvegaNTETDTQALGSATQDQ 4513
Cdd:pfam07263 408 NeslrsSEESPE-----------SSEDENSSSQEGLQSHSASTESQSEESQSEQDSQSEE----DDESDSQDSSRSKEDS 472
|
410 420 430
....*....|....*....|....*....|....*
gi 6323135 4514 LQTidEDMA-IDDDREEQ--EVDQKELVEDADDEK 4545
Cdd:pfam07263 473 NST--ESTSsSEEDGQSKnmEIESRKLTVDAYHNK 505
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4329-4618 |
6.67e-06 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 52.60 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4329 EEDVDMTNDEGKEDEENGPEEQAMSDE----EELKQDAAMEENKEKGGEQNTEGLDGVEEKADTEDIDQEAAVQQDSGSK 4404
Cdd:NF033609 524 DNEVAFNNGSGSGDGIDKPVVPEQPDEpgeiEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASD 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4405 GAGADATDTQEQDDVGGSGTTQNTYEEDQEDVTKNNEESREEATAALKQLGDSMKEYHRRRQDIKEAQTNGEEDENLEKN 4484
Cdd:NF033609 604 SDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4485 NERPDEFEHVEGANTETDTQALGSATQDQLQTIDEDMAIDDDREEQEVDQKELVEDADDEKMDIDEEEMLSDIDA-HDAN 4563
Cdd:NF033609 684 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSD 763
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323135 4564 NDVDS-KKSGFIGKRKSEEDFENElSNEHFSADQEDDSEIQSLIENIEDNPPDASA 4618
Cdd:NF033609 764 SDSDSdSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 818
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
4162-4553 |
6.75e-06 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 52.78 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4162 DKASDNSKEKDTDQNldGKNQEEDVQAAEN-DEQQRDNKEGGDEDPNAPEDGdeeiendenaeeendvgeqedevKDEEG 4240
Cdd:COG5644 32 DSEELEDNDEQGYSF--GVNSEDDEEIDSDeAFDEEDEKRFADWSFNASKSG-----------------------KSNKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4241 EDLEANVPEIETLDLPEDMNLDSEHEE-SDEDVDMSDGMPDDlnkeEVGNEDEEVKQESGIESDNENDEPGPEEDAGETE 4319
Cdd:COG5644 87 HKNLNNTKEISLNDSDDSVNSDKLENEgSVSSIDENELVDLD----TLLDNDQPEKNESGNNDHATDKENLLESDASSSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4320 TALDEEEGAEEDVDmtndegkeDEENGPEEQAMSDEEELKQDAAMEENKEKGGEQNTEGLDgveekadteDIDQEAAVQQ 4399
Cdd:COG5644 163 DSESEESDSESEIE--------SSDSDHDDENSDSKLDNLRNYIVSLKKDEADAESVLSSD---------DNDSIEEIKY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4400 DSGSKGAGADATDTQEQDDVGGSgttqntyeEDQEDVTKNNEESREEATAALKQLGDSMKEYHRRRQDIKEAQTNGEEDE 4479
Cdd:COG5644 226 DPHETNKESGSSETIDITDLLDS--------IPMEQLKVSLKPLVSESSKLDAPLAKSIQDRLERQAAYEQTKNDLEKWK 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323135 4480 NLEKNNERPDEFEHVEGANTETDTQALGSATQDQLQTidedmaidddREEQEVDQKELVEDADDEKMDIDEEEM 4553
Cdd:COG5644 298 PIVADNRKSDQLIFPMNETARPVPSNNGLASSFEPRT----------ESERKMHQALLDAGLENESALKKQEEL 361
|
|
| Mpp10 |
COG5384 |
U3 small nucleolar ribonucleoprotein component [Translation, ribosomal structure and ... |
4232-4564 |
1.00e-05 |
|
U3 small nucleolar ribonucleoprotein component [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227674 [Multi-domain] Cd Length: 569 Bit Score: 52.00 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4232 EDEVKDEEGEDLEANVPEIETLDlPEDMNLDSEHEESDEDVDMSDGMPDDLNKEEVGNED----EEVKQESGIES----- 4302
Cdd:COG5384 89 SSSGEESELEEAESVFKEKQMLS-ADVSEIEEQSNDSLSENDEEPSMDDEKTSAEAAREEfaeeKRIPDPYGINDkffdl 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4303 DNENDEPGPEEDAGETETAlDEEEGAEEDVDMtnDEGKEDEEN-------GPEEQAmsDEEELKQDAAMEENKEKGGEQN 4375
Cdd:COG5384 168 EKFNRDTLAAEDSNEASEG-SEDEDIDYFQDM--PSDDEEEEAiyyedffDKPTKE--PVKKHSDVKDPKEDEELDEEEH 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4376 TEGLDGVEEKADTEDIDQEAAvqqdsgskgagadatdtQEQDDVggSGTTQNTYEEDQEDVTKNNEESREEATAAlkqlg 4455
Cdd:COG5384 243 DSAMDKVKLDLFADEEDEPNA-----------------EGVGEA--SDKNLSSFEKQQIEMDEQIEELEKELVAP----- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4456 dsmKEYHRRRQ-DIKEAQTNGEEDENLE-KNNERPDEFEHVEGANTETDT--QALGSATQDQLQ-TIDEDMAIDDDREEQ 4530
Cdd:COG5384 299 ---KEWKYAGEvSAKKRPKNSLLAEELEfKQGAKPVPVSTKEDTESLEDIilQRIREGTFDDHAyRIREEVTIADEIPEF 375
|
330 340 350
....*....|....*....|....*....|....*...
gi 6323135 4531 EV----DQKELVEDADDEKMDIDEEEMLSDIDAHDANN 4564
Cdd:COG5384 376 ELleskSILSLAEEYEGDLMQIVDESALSEELDKGHNE 413
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1078-1229 |
1.03e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 51.27 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1078 PVLIQGPTSSGKTSMIKYLADITGHKFVRINnhehTDLQEYLGTYVTDDTGKlsFKEGVLVEALRKGYWIVLDELNLAPT 1157
Cdd:PHA02244 121 PVFLKGGAGSGKNHIAEQIAEALDLDFYFMN----AIMDEFELKGFIDANGK--FHETPFYEAFKKGGLFFIDEIDASIP 194
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323135 1158 DVLEALNRLLDDNRELFIPETqevVHPHPDFLLFATQNPPG-----IYGGRKILSRAFRNRFLELHFDDIPQDELEI 1229
Cdd:PHA02244 195 EALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFDYDEKIEHLI 268
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
811-896 |
1.07e-05 |
|
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: 48.06 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 811 FVEGSLVKTIRAGEWLLLDEVNLATADTLESISDLLtepDSRSILLSEKGdaEPIKAHPD-FRIFACMNPAtDVGKRDLP 889
Cdd:pfam07728 55 WVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLL---DERRLLLPDGG--ELVKAAPDgFRLIATMNPL-DRGLNELS 128
|
....*..
gi 6323135 890 MGIRSRF 896
Cdd:pfam07728 129 PALRSRF 135
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
4705-4879 |
1.29e-05 |
|
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: 48.99 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4705 IMIALDDSKSMSESK--CVKLAfdslclVSKTLTQLEAGG----LSIVKFGENIKEVHSFDQQFSNE---SGARAFQWFG 4775
Cdd:smart00327 2 VVFLLDGSGSMGGNRfeLAKEF------VLKLVEQLDIGPdgdrVGLVTFSDDARVLFPLNDSRSKDallEALASLSYKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4776 FQETKTD--VKKLVAESTKIFERARAMVHndqwQLEIVISDGICEDHET-IQKLVRRARENKIMLVFViidGITSNESIL 4852
Cdd:smart00327 76 GGGTNLGaaLQYALENLFSKSAGSRRGAP----KVVILITDGESNDGPKdLLKAAKELKRSGVKVFVV---GVGNDVDEE 148
|
170 180
....*....|....*....|....*..
gi 6323135 4853 DMSQVNYIPDQYGNPQLKITKYLDTFP 4879
Cdd:smart00327 149 ELKKLASAPGGVYVFLPELLDLLIDLL 175
|
|
| COG5137 |
COG5137 |
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ... |
4227-4367 |
1.61e-05 |
|
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];
Pssm-ID: 227466 [Multi-domain] Cd Length: 279 Bit Score: 49.99 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4227 DVGEQEDEVKDEEGEDLEANV----PEIETLDLPEDMNLDSEHEESDEDvdmSDGMPDDlnkeevgnEDEEVKQESGIES 4302
Cdd:COG5137 136 DEEDVEREILAEKPRVTRFNIvwdnDEDNDEAPPAQPDVDNEEEERLEE---SDGREEE--------EDEEVGSDSYGEG 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323135 4303 DNENDEPGPEEDAGeTETALDEEEGAEEDVdmtnDEGKEDEENGPEEQAMSDEEELKQDAAMEEN 4367
Cdd:COG5137 205 NRELNEEEEEEAEG-SDDGEDVVDYEGERI----DKKQGEEEEMEEEVINLFEIEWEEESPSEEV 264
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1075-1214 |
1.80e-05 |
|
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: 47.75 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1075 KRFPVLIQGPTSSGKTSMIKYLA---DITGHKFVRIN--NHEHTDLQEYLGTYVTDDTGKLSFKEGV--LVEALRKGYW- 1146
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALArelGPPGGGVIYIDgeDILEEVLDQLLLIIVGGKKASGSGELRLrlALALARKLKPd 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323135 1147 -IVLDELNLAPTDVLEALNRLLDDNRELFIPETQEVVHphpdfLLFATQNPPGIygGRKILSRAFRNRF 1214
Cdd:smart00382 81 vLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLT-----VILTTNDEKDL--GPALLRRRFDRRI 142
|
|
| Mpp10 |
pfam04006 |
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The ... |
4162-4370 |
1.83e-05 |
|
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The U3 small nucleolar ribonucleoprotein (snoRNP) is required for three cleavage events that generate the mature 18S rRNA from the pre-rRNA. In Saccharomyces cerevisiae, depletion of Mpp10, a U3 snoRNP-specific protein, halts 18S rRNA production and impairs cleavage at the three U3 snoRNP-dependent sites.
Pssm-ID: 461128 [Multi-domain] Cd Length: 506 Bit Score: 51.12 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4162 DKASDNSKEKDtDQNLDGKNQEEDVQAAENDEQQRDNKEGGDEDPNAPEDGDEEIEndenaeeenDVGEQEDEV--KDEE 4239
Cdd:pfam04006 70 KKIGSLLKDEK-ELRLLLDSEQDDEEDEDEEEDEEDEEDEEEDEDEEEEEEEEEED---------DEDEDSDDEglEEED 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4240 GEDLEANVPEIETLDLP----------EDMN--LDSE---------HEESDEDVDMSDGMPDDLNKEEVGNE-------- 4290
Cdd:pfam04006 140 VKELEQKTKKDAKKGRKsvvddkffklDEMEkfLEDEekkeerkdkGKEDEDDIDYFEDDDSEDDEDDGARNlkyedffd 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4291 --DEEVKQESGIESDNENDEPGPEEDAGEtetalDEEEGAEEDVDMTNDEGKEDEENGPEEqaMSDEEELKQDAAMEENK 4368
Cdd:pfam04006 220 ppEEEDEKETKKKKDKKKEEDEKDDEEEE-----DEEDDAMEEEKEDEFAEDEDEEEDDDE--DSDDEEEEASPEELSSF 292
|
..
gi 6323135 4369 EK 4370
Cdd:pfam04006 293 EK 294
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1711-1846 |
1.93e-05 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 50.92 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1711 FPDAQSSSFNLTAPTTASNLVRVVRAMQVHKPILLEGSPGVGKTSLITALAN-ITGNKLTRINL----SEQTDLVDLFGA 1785
Cdd:COG1401 192 LESEDDYLKDLLREKFEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEaLGGEDNGRIEFvqfhPSWSYEDFLLGY 271
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323135 1786 dAPGERSGEFLWHDAPFLRAMKKGE-------WVLLDEMNLA--SQ------SVLEglnacLDHRGEAYIPELDIS 1846
Cdd:COG1401 272 -RPSLDEGKYEPTPGIFLRFCLKAEknpdkpyVLIIDEINRAnvEKyfgellSLLE-----SDKRGEELSIELPYS 341
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
4348-4652 |
1.95e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4348 EEQAMSDEeeLKQDAAMEENKEKGGEQNTegldGVEekaDTEDIDQEAAVQQDSgsKGAGADATDTQEqddvggsgtTQN 4427
Cdd:PRK02224 150 DRQDMIDD--LLQLGKLEEYRERASDARL----GVE---RVLSDQRGSLDQLKA--QIEEKEEKDLHE---------RLN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4428 TYEEDQEDVT---KNNEESREEATAALKQLGDSMKEYHRRRQDIKE------------AQTNGEEDENLEKNNERPDEFE 4492
Cdd:PRK02224 210 GLESELAELDeeiERYEEQREQARETRDEADEVLEEHEERREELETleaeiedlretiAETEREREELAEEVRDLRERLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4493 HVEGANTET-DTQALGSATQ----DQLQTID-EDMAIDDDREEQEVDQKELVEDADDEKMDIDEEEMLSDiDAHDANNDV 4566
Cdd:PRK02224 290 ELEEERDDLlAEAGLDDADAeaveARREELEdRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE-ELREEAAEL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4567 DSKksgfIGKRKSE-EDFENELSnehfsadqEDDSEIQSLIENIEDNP------PDASASLTPERSLEESRELWHKSEIS 4639
Cdd:PRK02224 369 ESE----LEEAREAvEDRREEIE--------ELEEEIEELRERFGDAPvdlgnaEDFLEELREERDELREREAELEATLR 436
|
330
....*....|...
gi 6323135 4640 TADLVSRLGEQLR 4652
Cdd:PRK02224 437 TARERVEEAEALL 449
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4250-4352 |
1.98e-05 |
|
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: 50.95 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4250 IETLDLPEDmnLDSEHEESDEDVDmsdgmpddlnkeevgnEDEEVKQESGIESDNENDEPGPEEDAGETETALDE-EEGA 4328
Cdd:COG4547 202 LRDLDLAEE--LGEDEDEEDEDDE----------------DDSGEQEEDEEDGEDEDEESDEGAEAEDAEASGDDaEEGE 263
|
90 100
....*....|....*....|....
gi 6323135 4329 EEDVDMTNDEGKEDEENGPEEQAM 4352
Cdd:COG4547 264 SEAAEAESDEMAEEAEGEDSEEPG 287
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4338-4552 |
2.37e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 50.35 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4338 EGKEDEENGPEEQAMSDEEELKQDAAMEEN-KEKGGEQNTEGlDGVEEKADTEDIDQEAAvqQDSGSKGAGADATDTQEQ 4416
Cdd:PHA03169 47 APPAPTTSGPQVRAVAEQGHRQTESDTETAeESRHGEKEERG-QGGPSGSGSESVGSPTP--SPSGSAEELASGLSPENT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4417 DDVGGSGTTQNT-YEEDQEDVTKNNEESREEATAALKQLGDSmkeyhrrrqdikEAQTNGEE--DENLEKNNERPDEFEH 4493
Cdd:PHA03169 124 SGSSPESPASHSpPPSPPSHPGPHEPAPPESHNPSPNQQPSS------------FLQPSHEDspEEPEPPTSEPEPDSPG 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323135 4494 VEGANTETDTQALGSATqdqlqtiDEDmAIDDDREEQEVDQKELVEDADDEKMDIDEEE 4552
Cdd:PHA03169 192 PPQSETPTSSPPPQSPP-------DEP-GEPQSPTPQQAPSPNTQQAVEHEDEPTEPER 242
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1724-1894 |
2.42e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 50.12 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1724 PTTASNLVRVVRAMQVHKPILLEGSPGVGKTSLITALAnitgnKLTRINLSEQTDLVDLFGADAPGERSGEFlwHDAPFL 1803
Cdd:PHA02244 103 PTFHYETADIAKIVNANIPVFLKGGAGSGKNHIAEQIA-----EALDLDFYFMNAIMDEFELKGFIDANGKF--HETPFY 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1804 RAMKKGEWVLLDEMNLASQSVLEGLNACLDHRgeaYIPELDISFSCHPNFLVFAAQNPQYQGG-----GRKGLPKSFVNR 1878
Cdd:PHA02244 176 EAFKKGGLFFIDEIDASIPEALIIINSAIANK---FFDFADERVTAHEDFRVISAGNTLGKGAdhiyvARNKIDGATLDR 252
|
170
....*....|....*.
gi 6323135 1879 FSVVFIDMLTSDDLLL 1894
Cdd:PHA02244 253 FAPIEFDYDEKIEHLI 268
|
|
| PLN03021 |
PLN03021 |
Low-temperature-induced protein; Provisional |
4184-4483 |
2.64e-05 |
|
Low-temperature-induced protein; Provisional
Pssm-ID: 178593 [Multi-domain] Cd Length: 619 Bit Score: 50.74 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4184 EDVQAAENDEQQRDNKEGGDEDPNAPEDGDEEIEndenaeeenDVGEQEDEVKDEEGEDLEANVPEIEtldlpedmnlds 4263
Cdd:PLN03021 211 EDDYLGGQRKVNVETPKRLEEDPAAPGGGSDYLS---------GVSNYQSKVTDPTHKGGEAGVPEIA------------ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4264 eheESDEDVDMSDGMPDDLNKEEVGNEDEEVKQESGIESDNENDEPGPEEDAGETETALDEEEGAEEDVDMTNDEGKE-- 4341
Cdd:PLN03021 270 ---ESLGRMKVTDESPDQKSRQGREEDFPTRSHEFDLKKESDINKNSPARFGGESKAGMEEDFPTRGDVKVESGLGRDlp 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4342 --------DEENGPEEQamSDEEELKQDAAMEENKEKGGEQNTEGLDGVEEKAdtedIDQEAAVQQDSGSKG-AGADATD 4412
Cdd:PLN03021 347 tgthdqfsPELSRPKER--DDSEETKDESTHETKPSTYTEQLASATSAITNKA----IAAKNVVASKLGYTGeNGGGQSE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4413 TQEQDDVGGSGTT--QNTYEEDQEDVTKNNEESREEATAALKQL-----GDSMKEYHR-------RRQDIKEAQTNGEED 4478
Cdd:PLN03021 421 SPVKDETPRSVTAygQKVAGTVAEKLTPVYEKVKETGSTVMTKLplsggGSGVKETQQgeekgvtAKNYISEKLKPGEED 500
|
....*
gi 6323135 4479 ENLEK 4483
Cdd:PLN03021 501 KALSE 505
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1740-1775 |
4.74e-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: 46.89 E-value: 4.74e-05
10 20 30
....*....|....*....|....*....|....*.
gi 6323135 1740 HKPILLEGSPGVGKTSLITALANITGNKLTRINLSE 1775
Cdd:cd19481 26 PKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| COG5137 |
COG5137 |
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ... |
4236-4363 |
5.16e-05 |
|
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];
Pssm-ID: 227466 [Multi-domain] Cd Length: 279 Bit Score: 48.45 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4236 KDEEGEDLEANVPEIETldlpEDMNLDSEHEESDEDVDMSDGMPDDLNKEEVGNEDEEVKQESgiESDNENDEPGPEEDA 4315
Cdd:COG5137 160 NDEDNDEAPPAQPDVDN----EEEERLEESDGREEEEDEEVGSDSYGEGNRELNEEEEEEAEG--SDDGEDVVDYEGERI 233
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 6323135 4316 GETEtaLDEEEGaEEDVDmtNDEGKEDEENGPEEQAMSDEEELKQDAA 4363
Cdd:COG5137 234 DKKQ--GEEEEM-EEEVI--NLFEIEWEEESPSEEVPRNNEESPAKKQ 276
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1352-1426 |
5.19e-05 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 46.37 E-value: 5.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323135 1352 VLVSSCLKNKEPVLLVGETGCGKTTICQLLAQ---FMGRELITLNAHQNTETGDILGAQRPVRNRSEIQYKLIKSLKT 1426
Cdd:cd00009 10 LREALELPPPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPGV 87
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
4229-4376 |
5.26e-05 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 49.93 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4229 GEQEDEVKDEEGEDleanvPEIETLDLPEDMNLDseHEESDEDVDMSDGMPDDLNKEEVGNEDEEvkqESGIESDNENDE 4308
Cdd:pfam04147 280 GEEDEEEEDGKKKK-----KHKSADDLDDDFVVD--DDDDDEEFGLGKGIKERPTATELGDEDED---DFIIDDDLVESE 349
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323135 4309 PGPEEDAGETetalDEEEGAEEDVDMTNDEGKEDEENGPEEQaMSDEEELKQDAAMEENKEKGGEQNT 4376
Cdd:pfam04147 350 SDLELDEEEE----DEEEEDDEDEDEEEEEDDDDLSDLESEE-DEEDDEFEEEKKKKKKKDEEGAKEE 412
|
|
| Mpp10 |
pfam04006 |
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The ... |
4329-4573 |
5.55e-05 |
|
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The U3 small nucleolar ribonucleoprotein (snoRNP) is required for three cleavage events that generate the mature 18S rRNA from the pre-rRNA. In Saccharomyces cerevisiae, depletion of Mpp10, a U3 snoRNP-specific protein, halts 18S rRNA production and impairs cleavage at the three U3 snoRNP-dependent sites.
Pssm-ID: 461128 [Multi-domain] Cd Length: 506 Bit Score: 49.19 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4329 EEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEENKEKGGEQNTEGLDGVEEKADtEDIDQEAAvQQDSGSKGAGA 4408
Cdd:pfam04006 79 EKELRLLLDSEQDDEEDEDEEEDEEDEEDEEEDEDEEEEEEEEEEDDEDEDSDDEGLEE-EDVKELEQ-KTKKDAKKGRK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4409 DATDTQ--EQDDVggsgttqNTYEEDQEDvtknNEESREEATAalkqlGDSMKEYHrrrQDIkeaqtNGEEDENLEKNNE 4486
Cdd:pfam04006 157 SVVDDKffKLDEM-------EKFLEDEEK----KEERKDKGKE-----DEDDIDYF---EDD-----DSEDDEDDGARNL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4487 RPDEFEHVEGANTETDTQALGSATQDQLQTIDEDmaiDDDREEQEVDQKELVEDADDekmdIDEEEMLSDIDAHDANNDV 4566
Cdd:pfam04006 213 KYEDFFDPPEEEDEKETKKKKDKKKEEDEKDDEE---EEDEEDDAMEEEKEDEFAED----EDEEEDDDEDSDDEEEEAS 285
|
....*..
gi 6323135 4567 DSKKSGF 4573
Cdd:pfam04006 286 PEELSSF 292
|
|
| COG5137 |
COG5137 |
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ... |
4167-4315 |
6.11e-05 |
|
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];
Pssm-ID: 227466 [Multi-domain] Cd Length: 279 Bit Score: 48.45 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4167 NSKEKDTDQNLDGKNQEEDVQAAENDEQQR--------DNKEGGDEDPNAPEDGDEEIENDENAEEENDVGEQEDEVKDE 4238
Cdd:COG5137 121 TKLEKSDVEEPSEKVDEEDVEREILAEKPRvtrfnivwDNDEDNDEAPPAQPDVDNEEEERLEESDGREEEEDEEVGSDS 200
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323135 4239 EGE-DLEANVPEIETLDLPEDMNLDSEHEEsdEDVDMSDGmPDDLNKEEVGNEDE-EVKQESGIESDNENDEPGPEEDA 4315
Cdd:COG5137 201 YGEgNRELNEEEEEEAEGSDDGEDVVDYEG--ERIDKKQG-EEEEMEEEVINLFEiEWEEESPSEEVPRNNEESPAKKQ 276
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
311-417 |
6.18e-05 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 46.80 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 311 IMLIGKAGSGKTFLINELSKYM-GCHDSIVKIHLGEQTDAKL---LIGTytsgdKPG--TFEwRAGVLATAVKEGRW--V 382
Cdd:pfam07724 6 FLFLGPTGVGKTELAKALAELLfGDERALIRIDMSEYMEEHSvsrLIGA-----PPGyvGYE-EGGQLTEAVRRKPYsiV 79
|
90 100 110
....*....|....*....|....*....|....*
gi 6323135 383 LIEDIDKAPTDVLSILLSLLEKRELTiPSRGETVK 417
Cdd:pfam07724 80 LIDEIEKAHPGVQNDLLQILEGGTLT-DKQGRTVD 113
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
4231-4553 |
7.32e-05 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 49.35 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4231 QEDEVKDEEGEDLEANVPEIETLDlPEDMNLDSEHEES----------DEDVDMsDGMPDDLNKEEVGNEDEEVKQESGI 4300
Cdd:COG5192 373 EQDPGVDGVGLQLFSNSDAIDTVD-RESSEIDNVGRKTrrqptgkaiaEETSRE-DELSFDDSDVSTSDENEDVDFTGKK 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4301 ESDNENDEPGPEEDAGETETALDEEEGaeedvdmtndegkedeengpeeqAMSDEEELKQDAAMEENKEKGGEqntegld 4380
Cdd:COG5192 451 GAINNEDESDNEEVAFDSDSQFDESEG-----------------------NLRWKEGLASKLAYSQSGKRGRN------- 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4381 gVEEKADTEDIDQEAAVQQDSGSKGAGADATDTQEQDDVGGSGTTQntyeEDQEDVTKNNEESREEATAALKQLGDSMKE 4460
Cdd:COG5192 501 -IQKIFYDESLSPEECIEEYKGESAKSSESDLVVQDEPEDFFDVSK----VANESISSNHEKLMESEFEELKKKWSSLAQ 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4461 YHRRRQD--IKEAQTNGEE-DENLEKNNERPDEFEHVEGANTETDTQalGSATQDQLQTIDEDMAIDDDREEQEVDQK-- 4535
Cdd:COG5192 576 LKSRFQKdaTLDSIEGEEElIQDDEKGNFEDLEDEENSSDNEMEESR--GSSVTAENEESADEVDYETEREENARKKEel 653
|
330 340
....*....|....*....|..
gi 6323135 4536 ----ELVEDADDEKMDIDEEEM 4553
Cdd:COG5192 654 rgnfELEERGDPEKKDVDWYTE 675
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4320-4426 |
1.33e-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: 48.25 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4320 TALD--EEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEENkEKGGEQNTEGLDGVEEKADTEDIDQEAAv 4397
Cdd:COG4547 203 RDLDlaEELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAEDA-EASGDDAEEGESEAAEAESDEMAEEAEG- 280
|
90 100 110
....*....|....*....|....*....|...
gi 6323135 4398 qqDSGSKGAGADATDTQEQDDVGGSG----TTQ 4426
Cdd:COG4547 281 --EDSEEPGEPWRPNAPPPDDPADPDykvfTTA 311
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4045-4376 |
1.36e-04 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 48.37 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4045 SPQPPSEEVDDKNLQEGTGLGDGEGAQNNNKDVEQDEDLTEDAQNENKEQQDKDERDDENEDDAVEMEGDMAGELEDLSN 4124
Cdd:NF033609 624 SASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4125 GEENDDEdtdseeeeldeeiddlnedDPNAIDDKmwdDKASDNSKEKDTDQNLDgKNQEEDVQAAENDEQQRDNKEGGDE 4204
Cdd:NF033609 704 SDSDSDS-------------------DSDSDSDS---DSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDS 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4205 DPNAPEDGDEEIENDENAEEENDVGEQEDEVKDEEGedleanvpeietlDLPEDMNLDSeheESDEDVDMSDGMPDDLNK 4284
Cdd:NF033609 761 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-------------DSDSDSDSDS---DSDSDSDSDSDSDSDSDS 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4285 EEVGNEDEEVKQESGIESDNENDEPGPEEDAGETETALDEEEGAEEDVDMTNDegKEDEENGPEEQAMSDEEELKQDAAM 4364
Cdd:NF033609 825 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNS--PKNGTNASNKNEAKDSKEPLPDTGS 902
|
330
....*....|..
gi 6323135 4365 EenkekgGEQNT 4376
Cdd:NF033609 903 E------DEANT 908
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1743-1778 |
1.40e-04 |
|
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: 44.89 E-value: 1.40e-04
10 20 30
....*....|....*....|....*....|....*.
gi 6323135 1743 ILLEGSPGVGKTSLITALANITGNKLTRINLSEQTD 1778
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS 36
|
|
| PTZ00441 |
PTZ00441 |
sporozoite surface protein 2 (SSP2); Provisional |
4238-4542 |
2.03e-04 |
|
sporozoite surface protein 2 (SSP2); Provisional
Pssm-ID: 240420 [Multi-domain] Cd Length: 576 Bit Score: 47.65 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4238 EEGEDLeanvPEIETLDLPEDMnldseheesdedvdmsDGMPDDLNKEEVGNEDEEVKQESGIESDNENDEPGPEEDAGE 4317
Cdd:PTZ00441 278 EEEECP----VEPEPLPVPAPV----------------PPTPEDDNPRPTDDEFAVPNFNEGLDVPDNPQDPVPPPNEGK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4318 TETALdeeegaEEDVDMTNDEGKEDEENG---PEEQAMSDEEELKQDAAMEENKEK-GGEQNTEGLDGVEEKADTEDIDQ 4393
Cdd:PTZ00441 338 DGNPN------EENLFPPGDDEVPDESNVppnPPNVPGGSNSEFSSDVENPPNPPNpDIPEQEPNIPEDSNKEVPEDVPM 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4394 EAAVQQDsgskgagaDATDTQEQDDVGGSGTTQNTY------EEDQED----VTKNNEESREEATAALKQLGDSMKEYHR 4463
Cdd:PTZ00441 412 EPEDDRD--------NNFNEPKKPENKGDGQNEPVIpkpldnERDQSNknkqVNPGNRHNSEDRYTRPHGRNNENRNYNN 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4464 RRQDIKEAQTNGEEDENLEKNNERPDEFEHVEG-----------ANTETDTQALGSAT--QDQLQTIDEDMAiDDDREEQ 4530
Cdd:PTZ00441 484 KNSDIPKHPERSEHEQPEDKKKKSSNNGYKIAGgviaglalvgcVGFAYNFVVPGGAAgmAGEPAPFDEAMA-EDEKDLD 562
|
330
....*....|..
gi 6323135 4531 EVDQKELVEDAD 4542
Cdd:PTZ00441 563 EADQFKLPEDND 574
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1068-1214 |
2.34e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 44.83 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1068 LVRATSGKRFPVLIQGPTSSGKTSMIKYLADIT---GHKFVRINNHEhtdlqEYLGTYVTDDTGKLSFKEGVLVEALRKG 1144
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASD-----LLEGLVVAELFGHFLVRLLFELAEKAKP 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1145 YWIVLDELNLAPTDVLEALNRLLDDnrelfipETQEVVHPHPDFLLFATQNPPGIyggrkILSRAFRNRF 1214
Cdd:cd00009 86 GVLFIDEIDSLSRGAQNALLRVLET-------LNDLRIDRENVRVIGATNRPLLG-----DLDRALYDRL 143
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
1349-1393 |
2.99e-04 |
|
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).
Pssm-ID: 463698 [Multi-domain] Cd Length: 179 Bit Score: 44.69 E-value: 2.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6323135 1349 RLSVLVSSCLKNKEPVLLVGETGCGKTTICQ-LLAQFMGRELITLN 1393
Cdd:pfam12775 19 RYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQnLLRKLDKEKYLPLF 64
|
|
| PHA02664 |
PHA02664 |
hypothetical protein; Provisional |
4306-4456 |
5.63e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 177447 Cd Length: 534 Bit Score: 46.15 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4306 NDEPGPEEDAGE--TETALDEEEGAEEDVDMTNDEGKE-DEENG-PEEQAMSDEEELKQDAAMEENKEKGGEQNTEGLDG 4381
Cdd:PHA02664 399 NGARGSPMAAPEegRAAAAAAAANAPADQDVEAEAHDEfDQDPGaPAHADRADSDEDDMDEQESGDERADGEDDSDSSYS 478
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323135 4382 VEEKADTEDidqeaavqQDSGSKGAGaDATDTQEQDDVGGSGttQNTYEEDqedvtknnEESREEATAALKQLGD 4456
Cdd:PHA02664 479 YSTTSSEDE--------SDSADDSWG-DESDSGIEHDDGGVG--QAIEEEE--------EEERAVLGAVAEMLGD 534
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4141-4599 |
6.20e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4141 DEEIDDLNEDDPNAIDDKMWDDKA-----SDNSKEKDTDQNLDGKNQEEDVQAAENDEQQRDNKEGGDEDPNAPEDG--- 4212
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAeearkADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkk 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4213 -DEEIENDENAEEENDVGEQEDEVKDEEGEDLEANvPEIETLDLPEDMNLDSEHEESDEDVDMSdgmpDDLNK--EEVGN 4289
Cdd:PTZ00121 1331 aDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKKKA----DEAKKkaEEDKK 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4290 EDEEVKQESGIESDNENDEPGPEE---------DAGETETALDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQ 4360
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEkkkadeakkKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4361 DAA---MEENKEKGGE--------QNTEGLDGVEEKADTEDIDQ-EAAVQQDSGSKgagadATDTQEQDDVGGSGTTQNT 4428
Cdd:PTZ00121 1486 DEAkkkAEEAKKKADEakkaaeakKKADEAKKAEEAKKADEAKKaEEAKKADEAKK-----AEEKKKADELKKAEELKKA 1560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4429 YEEDQEDVTKNNEESR-------EEATAALKQLGDSMKEYHRRRQDIKEAQTNGEED-----ENLEKNNERPDEFEHVEG 4496
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKnmalrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaEELKKAEEEKKKVEQLKK 1640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4497 ANTETDTQAlgsatqDQLQTIDEDMAIDDDRE-EQEVDQKELVEDADDEKMDIDEEEMLSDIDAHDANNDVDSKKSGFIG 4575
Cdd:PTZ00121 1641 KEAEEKKKA------EELKKAEEENKIKAAEEaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
|
490 500
....*....|....*....|....*...
gi 6323135 4576 KRKSEE----DFENELSNEHFSADQEDD 4599
Cdd:PTZ00121 1715 KKKAEElkkaEEENKIKAEEAKKEAEED 1742
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1735-1910 |
6.66e-04 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 46.09 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1735 RAMQVHKPIL-LEGSPGVGKTSLITALANITGNKLTRINLSEQTDLVDLFGADAP--GERSGEFLWHDApflRAMKKGEW 1811
Cdd:PRK10787 343 RVNKIKGPILcLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTyiGSMPGKLIQKMA---KVGVKNPL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1812 VLLDEMNLASQsvleglnaclDHRG-------EAYIPELDISFSCH--------PNFLVFAAQNPQyqgggrkGLPKSFV 1876
Cdd:PRK10787 420 FLLDEIDKMSS----------DMRGdpasallEVLDPEQNVAFSDHylevdydlSDVMFVATSNSM-------NIPAPLL 482
|
170 180 190
....*....|....*....|....*....|....*.
gi 6323135 1877 NRFSVVFIDMLTSDDLLLIAK-HLYP-SIEPDIIAK 1910
Cdd:PRK10787 483 DRMEVIRLSGYTEDEKLNIAKrHLLPkQIERNALKK 518
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
4323-4602 |
1.17e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 45.31 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4323 DEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAA--MEE------------NKEKggeqntegldgvEEKAD- 4387
Cdd:pfam04147 125 DDDDSEEEEDGQLDLKRVRRAHFGGGEDDEEEEPERKKSKKevMEEviaksklhkyerQKAK------------EEDEEl 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4388 TEDIDQE-AAVQQD-SGSKGAGADATDTQEqddvggsgTTQNTYEEDQE-----------------DVTKNNEESREEAT 4448
Cdd:pfam04147 193 REELDKElKDLRSLlSGSKRPKPEQAKKPE--------EKPDRKKPDDDydklvrelafdkrakpsDRTKTEEELAEEEK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4449 AALKQLgdsmkEyhRRRQdikeAQTNGEEDENLEKNNERP---------DEFEHVEGANTETDTQALGSATQDQ----LQ 4515
Cdd:pfam04147 265 ERLEKL-----E--EERL----RRMRGEEDEEEEDGKKKKkhksaddldDDFVVDDDDDDEEFGLGKGIKERPTatelGD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4516 TIDEDMAIDDDREEQEVDQKELVEDADDEKMDIDEEEMLSDIDAHDANNDVDSKKSgfigkrkSEEDFENELSNEHFSAD 4595
Cdd:pfam04147 334 EDEDDFIIDDDLVESESDLELDEEEEDEEEEDDEDEDEEEEEDDDDLSDLESEEDE-------EDDEFEEEKKKKKKKDE 406
|
....*..
gi 6323135 4596 QEDDSEI 4602
Cdd:pfam04147 407 EGAKEEL 413
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1342-1394 |
1.46e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 44.91 E-value: 1.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 6323135 1342 TWTKGmrrlsvlvssclKNKEPVLLVGETGCGKTTICQLLAQFMGRELITLNA 1394
Cdd:PRK04195 32 SWLKG------------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNA 72
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1740-1762 |
1.68e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 44.53 E-value: 1.68e-03
10 20
....*....|....*....|...
gi 6323135 1740 HKPILLEGSPGVGKTSLITALAN 1762
Cdd:PRK04195 39 KKALLLYGPPGVGKTSLAHALAN 61
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1083-1171 |
1.94e-03 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 42.55 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 1083 GPTSSGKTSMIKYLADI---TGHKFVRIN------NHEHTDLQEYLGTYVTDDTGklsfkeGVLVEAL-RKGYWIVL-DE 1151
Cdd:cd19499 48 GPTGVGKTELAKALAELlfgDEDNLIRIDmseymeKHSVSRLIGAPPGYVGYTEG------GQLTEAVrRKPYSVVLlDE 121
|
90 100
....*....|....*....|
gi 6323135 1152 LNLAPTDVLEALNRLLDDNR 1171
Cdd:cd19499 122 IEKAHPDVQNLLLQVLDDGR 141
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
4154-4556 |
2.32e-03 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 44.22 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4154 AIDDKMWDDKASDNSKEKDTDQNLDGKNQEEDVQAAENDEQQRDNKEGGDEDPNAPEDGDEEIendenaeeendVGEQED 4233
Cdd:COG5281 47 AAAAAAASLAAAAAAAALAAAAAAAAAAAAADALAAALAEDAAAAAAAAEAALAALAAAALAL-----------AAAALA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4234 EVKDEEGEDLEANVPEIETLDLPEDMNLDSEHEESDEDvdmsdgmpDDLNKEEVGNEDEEVKQESGIESDNENDEPGPEE 4313
Cdd:COG5281 116 EAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAA--------AAAAALAAAAAAAAAAAAAAAAAAALAAASAAAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4314 DAGETETALDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEENKEKG---GEQNTEGLDGVEEKADTED 4390
Cdd:COG5281 188 AAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAASAAAQalaALAAAAAAAALALAAAAEL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4391 IDQEAAVQQdsgSKGAGADATDTQEQDDVGGSGTTQNTYEEDQEDVTKNNEESREEATAALKQLGDSMKEYHRRRQDIKE 4470
Cdd:COG5281 268 ALTAQAEAA---AAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALRAAAQALAALAQRALAAAAL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4471 AQTNGEEDENLEKnnerpdefehvEGANTETDTQALGSATQDQLQtidEDMAIDDDREEQEVDQKELVEDADDEKMDIDE 4550
Cdd:COG5281 345 AAAAQEAALAAAA-----------AALQAALEAAAAAAAAELAAA---GDWAAGAKAALAEYADSATNVAAQVAQAATSA 410
|
....*.
gi 6323135 4551 EEMLSD 4556
Cdd:COG5281 411 FSGLTD 416
|
|
| COG5593 |
COG5593 |
Nucleic-acid-binding protein possibly involved in ribosomal biogenesis [Translation, ribosomal ... |
4229-4370 |
2.43e-03 |
|
Nucleic-acid-binding protein possibly involved in ribosomal biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227880 [Multi-domain] Cd Length: 821 Bit Score: 44.26 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4229 GEQEDEVKDEEGEDLEANVPEI--ETLDLPEDMNLDSEHEESD-EDVDMSDGMPDDLNKEEvGNEDEEVKQESGIESDNE 4305
Cdd:COG5593 669 GKGKKSNKASFDSDDEMDENEIwsALVKSRPDVEDDSDDSELDfAEDDFSDSTSDDEPKLD-AIDDEDAKSEGSQESDQE 747
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323135 4306 ndepgpeEDAGETETALDEEEgaeEDVDMTNDEGKEDEENGPEEQamsdEEELKQDAAMEENKEK 4370
Cdd:COG5593 748 -------EGLDEIFYSFDGEQ---DNSDSFAESSEEDESSEEEKE----EEENKEVSAKRAKKKQ 798
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4197-4330 |
3.09e-03 |
|
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443611 [Multi-domain] Cd Length: 608 Bit Score: 44.01 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 4197 DNKEGGDEDPNAPEDGDeeiendenaeeendvgEQEDEVKDEEGEDLEANVPEIETLDLPEDMNLDSEHEEsDEDVDMSD 4276
Cdd:COG4547 206 DLAEELGEDEDEEDEDD----------------EDDSGEQEEDEEDGEDEDEESDEGAEAEDAEASGDDAE-EGESEAAE 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323135 4277 GMPDDLNKEEVGNEDEEVKQESgiesdnENDEPGPEEDAGET----ETALDEEEGAEE 4330
Cdd:COG4547 269 AESDEMAEEAEGEDSEEPGEPW------RPNAPPPDDPADPDykvfTTAFDEVVAAED 320
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
310-420 |
3.11e-03 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 43.89 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 310 PI---MLIGKAGSGKTFLINELSKYM-GCHDSIVKIHLGE----QTDAKLLigtytsGDKPGTFEW-RAGVLATAVKEGR 380
Cdd:CHL00095 538 PIasfLFSGPTGVGKTELTKALASYFfGSEDAMIRLDMSEymekHTVSKLI------GSPPGYVGYnEGGQLTEAVRKKP 611
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 6323135 381 W--VLIEDIDKAPTDVLSILLSLLEKRELTiPSRGETVKAAN 420
Cdd:CHL00095 612 YtvVLFDEIEKAHPDIFNLLLQILDDGRLT-DSKGRTIDFKN 652
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1364-1408 |
3.66e-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: 40.65 E-value: 3.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 6323135 1364 VLLVGETGCGKTTICQLLAQFMGRELITLNAHQNTETGDILGAQR 1408
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKR 45
|
|
| Merozoite_SPAM |
pfam07133 |
Merozoite surface protein (SPAM); This family consists of several Plasmodium falciparum SPAM ... |
4312-4389 |
3.94e-03 |
|
Merozoite surface protein (SPAM); This family consists of several Plasmodium falciparum SPAM (secreted polymorphic antigen associated with merozoites) proteins. Variation among SPAM alleles is the result of deletions and amino acid substitutions in non-repetitive sequences within and flanking the alanine heptad-repeat domain. Heptad repeats in which the a and d position contain hydrophobic residues generate amphipathic alpha-helices which give rise to helical bundles or coiled-coil structures in proteins. SPAM is an example of a P. falciparum antigen in which a repetitive sequence has features characteriztic of a well-defined structural element.
Pssm-ID: 429310 [Multi-domain] Cd Length: 176 Bit Score: 41.50 E-value: 3.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323135 4312 EEDAGETETALDEEEGAEEDVDMTNDEGKEDEENGPEEQAMSDEEELKQDAAMEENKEKGGEQNTEGLDGVEEKADTE 4389
Cdd:pfam07133 34 EDIAKENEDVEDEKEDEEEETEDEETEEKNEEETEEETEDEEDEEEVEEEEEKEENEDKKKELEEEQINKNTDTSDLE 111
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
312-416 |
6.54e-03 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 41.01 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 312 MLIGKAGSGKTFLINELSKYM-GCHDSIVKIHLGEQT---DAKLLIGT------YTSGdkpgtfewraGVLATAVKEGRW 381
Cdd:cd19499 45 LFLGPTGVGKTELAKALAELLfGDEDNLIRIDMSEYMekhSVSRLIGAppgyvgYTEG----------GQLTEAVRRKPY 114
|
90 100 110
....*....|....*....|....*....|....*..
gi 6323135 382 --VLIEDIDKAPTDVLSILLSLLEKRELTiPSRGETV 416
Cdd:cd19499 115 svVLLDEIEKAHPDVQNLLLQVLDDGRLT-DSHGRTV 150
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
310-415 |
6.97e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323135 310 PIMLIGKAGSGKTFLINELSKYMGCHDSIVKI----HLGEQTDAKLLIGTYTSGDKPGTFEWRAGVLATAVKEGRW--VL 383
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIYidgeDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110
....*....|....*....|....*....|..
gi 6323135 384 IEDIDKAPTDVLSILLSLLEKRELTIPSRGET 415
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLKSEK 115
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
630-686 |
7.48e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX 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: 410905 [Multi-domain] Cd Length: 251 Bit Score: 41.43 E-value: 7.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323135 630 NHSLRLMEQISVCIQMTE----PVLLVGETGTGKTTVVQQLAKMLAKKLTVINVSQQTETG 686
Cdd:cd19497 30 NHYKRIRNNLKQKDDDVEleksNILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAG 90
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
647-712 |
8.12e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 8.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323135 647 EPVLLVGETGTGKTTVVQQLAKMLAKKLT---VINVSQQTETGDLLGGYKPVNSKTVAVPIQENFETLF 712
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGgviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL 71
|
|
|