|
Name |
Accession |
Description |
Interval |
E-value |
| Ape1-like_AP-endo |
cd09087 |
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ... |
427-677 |
2.32e-155 |
|
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This subfamily includes human Ape1 (also known as Apex, Hap1, or Ref-1) and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Ape1 and Ape2 in humans. Ape1 is found in this subfamily, it exhibits strong AP-endonuclease activity but shows weak 3'-5' exonuclease and 3'-phosphodiesterase activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes exonuclease III (ExoIII) and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.
Pssm-ID: 197321 [Multi-domain] Cd Length: 253 Bit Score: 448.54 E-value: 2.32e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 427 LKICSWNVAGLRAWLKKDGLQLIDLEEPDIFCLQETKCANDQLPEEVTR-LPGYHPYWLCMP-GGYAGVAIYSKIMPIHV 504
Cdd:cd09087 1 LKIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKELKElLKGYHQYWNAAEkKGYSGTAILSKKKPLSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 505 EYGIGNEEFDDVGRMITAEYEKFYLINVYVPNSGRKLVNLEPRMRWEKLFQAYVKKLDALKPVVICGDMNVSHMPIDLEN 584
Cdd:cd09087 81 TYGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 585 PKNNTKNAGFTQEERDKMTELLGLGFVDTFRHLYPDRKGAYTFWTYMANARARNVGWRLDYCLVSERFVPKVVEHEIRSQ 664
Cdd:cd09087 161 PKTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSD 240
|
250
....*....|...
gi 7295875 665 CLGSDHCPITIFF 677
Cdd:cd09087 241 IMGSDHCPIGLEL 253
|
|
| xth |
TIGR00633 |
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are ... |
427-678 |
6.14e-147 |
|
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are 5' AP endonucleases that funciton in base excision repair and the repair of abasic sites in DNA.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273186 [Multi-domain] Cd Length: 254 Bit Score: 427.08 E-value: 6.14e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 427 LKICSWNVAGLRAWLKKDGLQLIDLEEPDIFCLQETKCANDQLPEEVTRLPGYHPYWLCMPGGYAGVAIYSKIMPIHVEY 506
Cdd:TIGR00633 1 MKIISWNVNGLRARLHKLFLDWLKEEQPDVLCLQETKVADEQFPAELFEELGYHVFFHGAKKGYSGVAILSKVEPLDVRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 507 GIGNEEFDDVGRMITAEYEKFYLINVYVPNSG-RKLVNLEPRM-RWEKLFQAYVKKLDALKPVVICGDMNVSHMPIDLEN 584
Cdd:TIGR00633 81 GFGGEPHDEEGRVITAEFDGFTVVNVYVPNGGsRDLERLEYKLqFWDALFQYLEKELDAGKPVVICGDMNVAHTEIDLGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 585 PKNNTKNAGFTQEERDKMTELLGLGFVDTFRHLYPDRKGAYTFWTYMANARARNVGWRLDYCLVSERFVPKVVEHEIRSQ 664
Cdd:TIGR00633 161 PKENKGNAGFTPEEREWFDELLEAGFVDTFRHFNPDTGDAYTWWDYRSGARDRNRGWRIDYFLVSEPLAERVVDSYIDSE 240
|
250
....*....|....
gi 7295875 665 CLGSDHCPITIFFN 678
Cdd:TIGR00633 241 IRGSDHCPIVLELD 254
|
|
| ExoIII_AP-endo |
cd09073 |
Escherichia coli exonuclease III (ExoIII)-like apurinic/apyrimidinic (AP) endonucleases; The ... |
428-677 |
4.48e-118 |
|
Escherichia coli exonuclease III (ExoIII)-like apurinic/apyrimidinic (AP) endonucleases; The ExoIII family AP endonucleases belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, which is then followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, which have both mutagenic and cytotoxic effects. AP endonucleases can carry out a wide range of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two functional AP endonucleases, for example, APE1/Ref-1 and Ape2 in humans, Apn1 and Apn2 in bakers yeast, Nape and NExo in Neisseria meningitides, and exonuclease III (ExoIII) and endonuclease IV (EndoIV) in Escherichia coli. Usually, one of the two is the dominant AP endonuclease, the other has weak AP endonuclease activity, but exhibits strong 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, and 3'-phosphatase activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes. This family contains the ExoIII family; the EndoIV family belongs to a different superfamily.
Pssm-ID: 197307 [Multi-domain] Cd Length: 251 Bit Score: 353.13 E-value: 4.48e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 428 KICSWNVAGLRAWLKKDGLQLIDLEEPDIFCLQETKCANDQLPEEVTRLPGYHPYWLCMPG-GYAGVAIYSKIMPIHVEY 506
Cdd:cd09073 1 KIISWNVNGLRARLKKGVLKWLKEEKPDILCLQETKADEDKLPEELQHVEGYHSYWSPARKkGYSGVATLSKEEPLDVSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 507 GIGNEEFDDVGRMITAEYEKFYLINVYVPNSGRKLVNLEPRMRWEKLFQAYVKKL-DALKPVVICGDMNVSHMPIDLENP 585
Cdd:cd09073 81 GIGGEEFDSEGRVITAEFDDFYLINVYFPNGGRGLERLDYKLRFYEAFLEFLEKLrKRGKPVVICGDFNVAHEEIDLARP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 586 KNNTKNAGFTQEERDKMTELLGLGFVDTFRHLYPDrKGAYTFWTYMANARARNVGWRLDYCLVSERFVPKVVEHEIRSQC 665
Cdd:cd09073 161 KKNEKNAGFTPEERAWFDKLLSLGYVDTFRHFHPE-PGAYTWWSYRGNARERNVGWRIDYFLVSEELAEKVKDSGILSKV 239
|
250
....*....|..
gi 7295875 666 LGSDHCPITIFF 677
Cdd:cd09073 240 KGSDHAPVTLEL 251
|
|
| XthA |
COG0708 |
Exonuclease III [Replication, recombination and repair]; |
427-678 |
7.40e-112 |
|
Exonuclease III [Replication, recombination and repair];
Pssm-ID: 440472 [Multi-domain] Cd Length: 256 Bit Score: 337.43 E-value: 7.40e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 427 LKICSWNVAGLRAWLKKDgLQLIDLEEPDIFCLQETKCANDQLPEEVTRLPGYHPYWLCMPGgYAGVAIYSKIMPIHVEY 506
Cdd:COG0708 1 MKIASWNVNGIRARLPKL-LDWLAEEDPDVLCLQETKAQDEQFPLEAFEAAGYHVYFHGQKG-YNGVAILSRLPPEDVRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 507 GIGNEEFDDVGRMITAEYEKFYLINVYVPNSG-RKLVNLEPRMRWEKLFQAYVKKLDAL-KPVVICGDMNVSHMPIDLEN 584
Cdd:COG0708 79 GLGGDEFDAEGRYIEADFGGVRVVSLYVPNGGsVGSEKFDYKLRFLDALRAYLAELLAPgRPLILCGDFNIAPTEIDVKN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 585 PKNNTKNAGFTQEERDKMTELLGLGFVDTFRHLYPDRKGAYTFWTYMANARARNVGWRLDYCLVSERFVPKVVEHEI--- 661
Cdd:COG0708 159 PKANLKNAGFLPEERAWFDRLLELGLVDAFRALHPDVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGIdre 238
|
250
....*....|....*...
gi 7295875 662 -RSQCLGSDHCPITIFFN 678
Cdd:COG0708 239 pRGDERPSDHAPVVVELD 256
|
|
| Mth212-like_AP-endo |
cd09085 |
Methanothermobacter thermautotrophicus Mth212-like subfamily of the ExoIII family purinic ... |
427-675 |
4.82e-103 |
|
Methanothermobacter thermautotrophicus Mth212-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes the thermophilic archaeon Methanothermobacter thermautotrophicus Mth212and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Mth212 is an AP endonuclease, and a DNA uridine endonuclease (U-endo) that nicks double-stranded DNA at the 5'-side of a 2'-d-uridine residue. After incision at the 5'-side of a 2'-d-uridine residue by Mth212, DNA polymerase B takes over the 3'-OH terminus and carries out repair synthesis, generating a 5'-flap structure that is resolved by a 5'-flap endonuclease. Finally, DNA ligase seals the resulting nick. This U-endo activity shares the same catalytic center as its AP-endo activity, and is absent from other AP endonuclease homologues.
Pssm-ID: 197319 [Multi-domain] Cd Length: 252 Bit Score: 314.60 E-value: 4.82e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 427 LKICSWNVAGLRAWLKKDGLQLIDLEEPDIFCLQETKCANDQLPEEVTRLPGYHPYWL-CMPGGYAGVAIYSKIMPIHVE 505
Cdd:cd09085 1 MKIISWNVNGLRAVHKKGFLDWFKEEKPDILCLQETKAQPEQLPEDLRNIEGYHSYFNsAERKGYSGVALYSKIEPDSVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 506 YGIGNEEFDDVGRMITAEYEKFYLINVYVPNSGRKLVNLEPRMRWEKLFQAYVKKLDAL-KPVVICGDMNVSHMPIDLEN 584
Cdd:cd09085 81 EGLGVEEFDNEGRILIADFDDFTLFNIYFPNGQMSEERLDYKLEFYDAFLEYLNELRDSgKNVIICGDFNTAHKEIDLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 585 PKNNTKNAGFTQEERDKMTELLGLGFVDTFRHLYPDRkGAYTFWTYMANARARNVGWRLDYCLVSERFVPKVVEHEIRSQ 664
Cdd:cd09085 161 PKENEKVSGFLPEERAWMDKFIENGYVDTFRMFNKEP-GQYTWWSYRTRARERNVGWRIDYFFVNEEFKPKVKDAGILPD 239
|
250
....*....|.
gi 7295875 665 CLGSDHCPITI 675
Cdd:cd09085 240 VMGSDHCPVSL 250
|
|
| exoDNase_III |
TIGR00195 |
exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model ... |
427-673 |
3.26e-97 |
|
exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model also contains eukaryotic apurinic/apyrimidinic endonucleases which group in the same family [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 272954 [Multi-domain] Cd Length: 254 Bit Score: 299.30 E-value: 3.26e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 427 LKICSWNVAGLRAWLKKdGLQLIDLEEPDIFCLQETKCANDQLPEEVTRLPGYHPYWLCMPGgYAGVAIYSKIMPIHVEY 506
Cdd:TIGR00195 1 MKIISWNVNGLRARPHK-GLAWLKENQPDVLCLQETKVQDEQFPLEPFHKEGYHVFFSGQKG-YSGVAIFSKEEPISVRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 507 GIGNEEFDDVGRMITAEYEKFYLINVYVPNSGRK-LVNLEPRMRWEKLFQAYVKKL-DALKPVVICGDMNVSHMPIDLEN 584
Cdd:TIGR00195 79 GFGVEEEDAEGRIIMAEFDSFLVINGYFPNGSRDdSEKLPYKLQWLEALQNYLEKLvDKDKPVLICGDMNIAPTEIDLHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 585 PKNNTKNAGFTQEERDKMTELLGLGFVDTFRHLYPDrKGAYTFWTYMANARARNVGWRLDYCLVSERFVPKVVE----HE 660
Cdd:TIGR00195 159 PDENRNHTGFLPEEREWLDRLLEAGLVDTFRKFNPD-EGAYSWWDYRTKARDRNRGWRIDYFLVSEPLKERCVDcgidYD 237
|
250
....*....|...
gi 7295875 661 IRSQCLGSDHCPI 673
Cdd:TIGR00195 238 IRGSEKPSDHCPV 250
|
|
| PRK13911 |
PRK13911 |
exodeoxyribonuclease III; Provisional |
427-673 |
1.73e-82 |
|
exodeoxyribonuclease III; Provisional
Pssm-ID: 139971 [Multi-domain] Cd Length: 250 Bit Score: 261.17 E-value: 1.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 427 LKICSWNVAGLRAWLKKDGLQLIDLEEPDIFCLQETKCANDQlpeEVTRLPGYHPYWLC-MPGGYAGVAIYSKIMPIHVE 505
Cdd:PRK13911 1 MKLISWNVNGLRACMTKGFMDFFNSVDADVFCIQESKMQQEQ---NTFEFKGYFDFWNCaIKKGYSGVVTFTKKEPLSVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 506 YGIGNEEFDDVGRMITAEYEKFYLINVYVPNSGRKLVNLEPRMRWEKLFQAYVKKLDALKPVVICGDMNVSHMPIDLENP 585
Cdd:PRK13911 78 YGINIEEHDKEGRVITCEFESFYLVNVYTPNSQQALSRLSYRMSWEVEFKKFLKALELKKPVIVCGDLNVAHNEIDLENP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 586 KNNTKNAGFTQEERDKMTELLGLGFVDTFRHLYPDRKGAYTFWTYMANARARNVGWRLDYCLVSERFVPKVVEHEIRSQC 665
Cdd:PRK13911 158 KTNRKNAGFSDEERGKFSELLNAGFIDTFRYFYPNKEKAYTWWSYMQQARDKNIGWRIDYFLCSNPLKTRLKDALIYKDI 237
|
....*...
gi 7295875 666 LGSDHCPI 673
Cdd:PRK13911 238 LGSDHCPV 245
|
|
| Nape_like_AP-endo |
cd10281 |
Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) ... |
427-675 |
1.27e-80 |
|
Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes Neisseria meningitides Nape and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Neisseria meningitides Nape and NExo. Nape, found in this subfamily, is the dominant AP endonuclease. It exhibits strong AP endonuclease activity, and also exhibits 3'-5'exonuclease and 3'-deoxyribose phosphodiesterase activities.
Pssm-ID: 197336 [Multi-domain] Cd Length: 253 Bit Score: 256.39 E-value: 1.27e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 427 LKICSWNVAGLRAWLKKDGLQLIDLEEPDIFCLQETKCANDQLPEEVTRLPGYHPYWL-CMPGGYAGVAIYSKIMPIHVE 505
Cdd:cd10281 1 MRVISVNVNGIRAAAKKGFLEWLAAQDADVVCLQEVRAQEEQLDDDFFEPEGYNAYFFdAEKKGYAGVAIYSRTQPKAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 506 YGIGNEEFDDVGRMITAEYEKFYLINVYVPNSGRKLVNLEPRMRWEKLFQAYVKKLDALKP-VVICGDMNVSHMPIDLEN 584
Cdd:cd10281 81 YGLGFEEFDDEGRYIEADFDNVSVASLYVPSGSSGDERQEAKMAFLDAFLEHLKELRRKRReFIVCGDFNIAHTEIDIKN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 585 PKNNTKNAGFTQEERDKMTELLG-LGFVDTFRHLYPDrKGAYTFWTYMANARARNVGWRLDYCLVSERFVPKVVEHEIRS 663
Cdd:cd10281 161 WKANQKNSGFLPEERAWLDQVFGeLGYVDAFRELNPD-EGQYTWWSNRGQARANNVGWRIDYQIATPGLASKVVSAWIYR 239
|
250
....*....|..
gi 7295875 664 QCLGSDHCPITI 675
Cdd:cd10281 240 EERFSDHAPLIV 251
|
|
| ExoIII-like_AP-endo |
cd09086 |
Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of ... |
427-677 |
2.61e-73 |
|
Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes Escherichia coli ExoIII, Neisseria meningitides NExo,and related proteins. These are ExoIII family AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiencies. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity. For example, Neisseria meningitides Nape and NExo, and exonuclease III (ExoIII) and endonuclease IV (EndoIV) in Escherichia coli. NExo and ExoIII are found in this subfamily. NExo is the non-dominant AP endonuclease. It exhibits strong 3'-5' exonuclease and 3'-deoxyribose phosphodiesterase activities. Escherichia coli ExoIII is an active AP endonuclease, and in addition, it exhibits double strand (ds)-specific 3'-5' exonuclease, exonucleolytic RNase H, 3'-phosphomonoesterase and 3'-phosphodiesterase activities, all catalyzed by a single active site. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes ExoIII and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.
Pssm-ID: 197320 [Multi-domain] Cd Length: 254 Bit Score: 237.03 E-value: 2.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 427 LKICSWNVAGLRA-------WLKKdglqlidlEEPDIFCLQETKCANDQLPEEVTRLPGYHPYWLCMPGgYAGVAIYSKI 499
Cdd:cd09086 1 MKIATWNVNSIRArleqvldWLKE--------EDPDVLCLQETKVEDDQFPADAFEALGYHVAVHGQKA-YNGVAILSRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 500 MPIHVEYGIGNEEFDDVGRMITAEYEKFYLINVYVPNsGRKLVNlePR----MRWEKLFQAYVKK-LDALKPVVICGDMN 574
Cdd:cd09086 72 PLEDVRTGFPGDPDDDQARLIAARVGGVRVINLYVPN-GGDIGS--PKfaykLDWLDRLIRYLQKlLKPDDPLVLVGDFN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 575 VSHMPIDLENPKNNTKNAGFTQEERDKMTELLGLGFVDTFRHLYPDrKGAYTFWTYMANARARNVGWRLDYCLVSERFVP 654
Cdd:cd09086 149 IAPEDIDVWDPKQLLGKVLFTPEEREALRALLDLGFVDAFRALHPD-EKLFTWWDYRAGAFERNRGLRIDHILASPALAD 227
|
250 260
....*....|....*....|....*..
gi 7295875 655 KVVEHEIRSQCLG----SDHCPITIFF 677
Cdd:cd09086 228 RLKDVGIDREPRGwekpSDHAPVVAEL 254
|
|
| Ape2-like_AP-endo |
cd09088 |
Human Ape2-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This ... |
428-677 |
2.80e-54 |
|
Human Ape2-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes human APE2, Saccharomyces cerevisiae Apn2/Eth1, and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity. For examples, Ape1 and Ape2 in humans, and Apn1 and Apn2 in bakers yeast. Ape2 and Apn2/Eth1 are both found in this subfamily, and have the weaker AP endonuclease activity. Ape2 shows strong 3'-5' exonuclease and 3'-phosphodiesterase activities; it can reduce the mutagenic consequences of attack by reactive oxygen species by removing 3'-end adenine opposite from 8-oxoG, in addition to repairing 3'-damaged termini. Apn2/Eth1 exhibits AP endonuclease activity, but has 30-40 fold more active 3'-phosphodiesterase and 3'-5' exonuclease activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes exonuclease III (ExoIII) and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.
Pssm-ID: 197322 [Multi-domain] Cd Length: 309 Bit Score: 188.29 E-value: 2.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 428 KICSWNVAGLRA------WLKKDGL-QLIDLEEPDIFCLQETKCANDQLPEEVTRLPGYHPYWLCMPG--GYAGVAIYSK 498
Cdd:cd09088 1 RIVTWNVNGIRTrlqyqpWNKENSLkSFLDSLDADIICLQETKLTRDELDEPSAIVEGYDSFFSFSRGrkGYSGVATYCR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 499 I---MPIHVE------------------------YGIGNEEFDDV--------GRMITAEYEKFYLINVYVP-NSGRKLV 542
Cdd:cd09088 81 DsaaTPVAAEegltgvlsspnqknelsenddigcYGEMLEFTDSKelleldseGRCVLTDHGTFVLINVYCPrADPEKEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 543 NLEPRMRWEKLFQAYVKKL-DALKPVVICGDMNVSHMPIDLENPKNNTKNAGFTQEE---RDKMTELLGLG--------- 609
Cdd:cd09088 161 RLEFKLDFYRLLEERVEALlKAGRRVILVGDVNVSHRPIDHCDPDDSEDFGGESFEDnpsRQWLDQLLGDSgegggspgg 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7295875 610 -FVDTFRHLYPDRKGAYTFWTYMANARARNVGWRLDYCLVSERFVPKVVEHEIRSQCLGSDHCPITIFF 677
Cdd:cd09088 241 lLIDSFRYFHPTRKGAYTCWNTLTGARPTNYGTRIDYILADRGLLPWVKAADILPEVEGSDHCPVYADL 309
|
|
| PRK11756 |
PRK11756 |
exonuclease III; Provisional |
427-679 |
2.71e-41 |
|
exonuclease III; Provisional
Pssm-ID: 236970 [Multi-domain] Cd Length: 268 Bit Score: 151.20 E-value: 2.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 427 LKICSWNVAGLRAWLKKdgLQ-LIDLEEPDIFCLQETKCANDQLP-EEVTRLpGYHPYWLCMPGGYaGVAIYSKIMPIHV 504
Cdd:PRK11756 1 MKFVSFNINGLRARPHQ--LEaIIEKHQPDVIGLQETKVHDEMFPlEEVEAL-GYHVFYHGQKGHY-GVALLSKQTPIAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 505 EYGIGNEEFDDVGRMITAEYE----KFYLINVYVPN--SGRKLVNLEPRMRWEKLFQAYVKK-LDALKPVVICGDMNVSH 577
Cdd:PRK11756 77 RKGFPTDDEEAQRRIIMATIPtpngNLTVINGYFPQgeSRDHPTKFPAKRQFYQDLQNYLETeLSPDNPLLIMGDMNISP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 578 MPIDL----ENPKN--NTKNAGFTQEERDKMTELLGLGFVDTFRHLYPDRKGAYTFWTYMANARARNVGWRLDYCLVSER 651
Cdd:PRK11756 157 TDLDIgigeENRKRwlRTGKCSFLPEEREWLDRLMDWGLVDTFRQLNPDVNDRFSWFDYRSKGFDDNRGLRIDLILATQP 236
|
250 260 270
....*....|....*....|....*....|..
gi 7295875 652 FVPKVVE----HEIRSQCLGSDHCPITIFFNI 679
Cdd:PRK11756 237 LAERCVEtgidYDIRGMEKPSDHAPIWATFKL 268
|
|
| EEP |
cd08372 |
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ... |
429-675 |
1.85e-38 |
|
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.
Pssm-ID: 197306 [Multi-domain] Cd Length: 241 Bit Score: 142.62 E-value: 1.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 429 ICSWNVAGLRA-WLKKDGLQLIDLEEPDIFCLQETKCANDQLPEEVTRLPGYHPYWLCMP---GGYAGVAIYSK---IMP 501
Cdd:cd08372 1 VASYNVNGLNAaTRASGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLPEGYHQYQSGPsrkEGYEGVAILSKtpkFKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 502 IHVEYGIGNEEFDDVGRMITAEYEK----FYLINVYVPNSGRklvNLEPRMRWEKLFQAYVKKL--DALKPVVICGDMNV 575
Cdd:cd08372 81 VEKHQYKFGEGDSGERRAVVVKFDVhdkeLCVVNAHLQAGGT---RADVRDAQLKEVLEFLKRLrqPNSAPVVICGDFNV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 576 SHMPIDLENPknntknagftQEERDKmteLLGLGFVDTFRHLypdrKGAYTFWTYManaraRNVGWRLDYCLVSERFVPK 655
Cdd:cd08372 158 RPSEVDSENP----------SSMLRL---FVALNLVDSFETL----PHAYTFDTYM-----HNVKSRLDYIFVSKSLLPS 215
|
250 260
....*....|....*....|....
gi 7295875 656 VVEHEIRS----QCLGSDHCPITI 675
Cdd:cd08372 216 VKSSKILSdaarARIPSDHYPIEV 239
|
|
| L1-EN |
cd09076 |
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; ... |
429-675 |
1.11e-23 |
|
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; This family contains the endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains, including the endonuclease of Xenopus laevis Tx1. These retrotranspons belong to the subtype 2, L1-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. LINE-1/L1 elements (full length and truncated) comprise about 17% of the human genome. This endonuclease nicks the genomic DNA at the consensus target sequence 5'TTTT-AA3' producing a ribose 3'-hydroxyl end as a primer for reverse transcription of associated template RNA. This subgroup also includes the endonuclease of Xenopus laevis Tx1, another member of the L1-clade. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.
Pssm-ID: 197310 [Multi-domain] Cd Length: 236 Bit Score: 100.12 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 429 ICSWNVAGLRAWLKKDGL-QLIDLEEPDIFCLQETKC-ANDQLPEEVTrlpGYHPYWLCMPGGY-AGVAI-YSK-IMPIH 503
Cdd:cd09076 1 IGTLNVRGLRSPGKRAQLlEELKRKKLDILGLQETHWtGEGELKKKRE---GGTILYSGSDSGKsRGVAIlLSKtAANKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 504 VEYgigneEFDDVGRMITA----EYEKFYLINVYVPNSGrklvnlEPRMR---WEKLfQAYVKKLDALKPVVICGDMNVs 576
Cdd:cd09076 78 LEY-----TKVVSGRIIMVrfkiKGKRLTIINVYAPTAR------DEEEKeefYDQL-QDVLDKVPRHDTLIIGGDFNA- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 577 hmpidLENPKNNTKNAGFTQ---EERDKMTELLGLGFVDTFRHLYPDRKGaytfWTYMANAR-ARNvgwRLDYCLVSERF 652
Cdd:cd09076 145 -----VLGPKDDGRKGLDKRnenGERALSALIEEHDLVDVWRENNPKTRE----YTWRSPDHgSRS---RIDRILVSKRL 212
|
250 260
....*....|....*....|...
gi 7295875 653 VPKVVEHEIRSqCLGSDHCPITI 675
Cdd:cd09076 213 RVKVKKTKITP-GAGSDHRLVTL 234
|
|
| Exo_endo_phos |
pfam03372 |
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ... |
430-578 |
1.98e-18 |
|
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.
Pssm-ID: 460902 [Multi-domain] Cd Length: 183 Bit Score: 83.43 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 430 CSWNVAGLRAWLKKDGLQLIDLEE------PDIFCLQETKCANDQLPEEVTRLPGYHPYWLC--MPGGYAGVAIYSKIMP 501
Cdd:pfam03372 1 LTWNVNGGNADAAGDDRKLDALAAliraydPDVVALQETDDDDASRLLLALLAYGGFLSYGGpgGGGGGGGVAILSRYPL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7295875 502 IHVEYGIGNEEFDDVGRMITAEYEKFYLINVYVPNSGRKLVNLEPRM-RWEKLFQAYVKKLDALKPVVICGDMNVSHM 578
Cdd:pfam03372 81 SSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEqRADLLLLLLALLAPRSEPVILAGDFNADYI 158
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-392 |
7.99e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 8 KKQAEALASEPTDPTPNANGNGVDENADSAAEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARGKKKQPKDT 87
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 88 DENGQMEVVAKPKGRAKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPDEvtssppkGRAKAEKPTNAQAKGRKRKELP 167
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE-------AKKKADEAKKAEEAKKADEAKK 1529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 168 AEANGGAEEAAEPPKQRARKEavptLKEQAEpgTISKEKVQKAETAAK-RARGTKRLADSEIAAALDEPEVDEVPPKAAS 246
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADE----LKKAEE--LKKAEEKKKAEEAKKaEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 247 KRAKKGKMVEPSPETVGDFQSVQEEVESPPKTAAAPKKRAKKTTNGETAVELEPKTKAKpTKQRAKKEGKEPAPGKKQKK 326
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK-AAEEAKKAEEDKKKAEEAKK 1682
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7295875 327 SADKENGVVEEEAKPSTETKPAKGRKKAPV----KAEDVEDIEEA----AEESKpaRGRKKAAAKAEEPDVDEE 392
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAeekkKAEELKKAEEEnkikAEEAK--KEAEEDKKKAEEAKKDEE 1754
|
|
| YafD |
COG3021 |
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ... |
427-673 |
2.35e-12 |
|
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily [General function prediction only];
Pssm-ID: 442257 [Multi-domain] Cd Length: 310 Bit Score: 68.48 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 427 LKICSWNVAGLRAwlkkDGLQLIDL---EEPDIFCLQETkcaNDQLPEEVTRLPGYHPYWLCMP-GGYAGVAIYSKiMPI 502
Cdd:COG3021 95 LRVLTANVLFGNA----DAEALAALvreEDPDVLVLQET---TPAWEEALAALEADYPYRVLCPlDNAYGMALLSR-LPL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 503 hVEYGIgNEEFDDVGRMITAEYEkfylinvyVPNSGRKLVNLEPRM------RWEKLFQAYVKKLDALK-PVVICGDMNV 575
Cdd:COG3021 167 -TEAEV-VYLVGDDIPSIRATVE--------LPGGPVRLVAVHPAPpvggsaERDAELAALAKAVAALDgPVIVAGDFNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 576 S--HMPIDLenpknntknagFTQEerdkmtellgLGFVDTfrhlypdRKGAYTFWTYmaNARARNVGWRLDYCLVSERFV 653
Cdd:COG3021 237 TpwSPTLRR-----------LLRA----------SGLRDA-------RAGRGLGPTW--PANLPFLRLPIDHVLVSRGLT 286
|
250 260
....*....|....*....|
gi 7295875 654 PKVVEheiRSQCLGSDHCPI 673
Cdd:COG3021 287 VVDVR---VLPVIGSDHRPL 303
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
32-393 |
8.78e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 8.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 32 ENADSAAEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARGKKKQPKDTDENGQMEVVAKPKGRAKKATAEA- 110
Cdd:PTZ00121 1269 QAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAa 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 111 --EPEPKVDlpagKATKPRAKKEptpaPDEVTSSPPKGRAKAEKPTNAQAkgRKRKELPAEANGGAEEAAEPPKQRARKE 188
Cdd:PTZ00121 1349 kaEAEAAAD----EAEAAEEKAE----AAEKKKEEAKKKADAAKKKAEEK--KKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 189 AVPTLKEQAepgtiskEKVQKAETAAKRARgTKRLADSEIAAALDEPEVDEVPPKAasKRAKKGKMVEPSPETVGDFQSV 268
Cdd:PTZ00121 1419 KADEAKKKA-------EEKKKADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKA--EEAKKADEAKKKAEEAKKADEA 1488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 269 QEEVESPPKTAAAPKKRAKKTTNGETAVELEPKTKAKPTKQRAKKEGKEPAPGKKQKKSADKENGVVE----EEAKPSTE 344
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaEEKKKAEE 1568
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 7295875 345 TKPAKGRKKAPV-KAEDVEDIEEAAEESKPARGRKKAAAKAEEPDVDEES 393
Cdd:PTZ00121 1569 AKKAEEDKNMALrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
38-393 |
2.78e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 38 AEELKVPAKGKPRARKATKtAVSAENSEEVEPQKAPTAAARGKKKQPKDTDENGQMEVVAKPKGRAKKATA-EAEPEPKV 116
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKK-AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 117 DLPAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQAKGRKRKELPAEANGGAEEAAEPPKQRARKEavptlKEQ 196
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-----KKK 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 197 AEPGTISKEKVQKAETAAKRARGTKRLADSEIAAALDEPEVDEVPPKAASKRakkgkmvepspetvgdfqsvqeevespp 276
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK---------------------------- 1431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 277 ktaaapkkrakkttngeTAVELEPKTKAKPTKQRAKKEGKEPAPGKKQKKSADKENGVVEEEAKPSTETKPAKGRKKAPV 356
Cdd:PTZ00121 1432 -----------------KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
|
330 340 350
....*....|....*....|....*....|....*....
gi 7295875 357 KAEDVEDIEEAAEESKPARGRKKA--AAKAEEPDVDEES 393
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAeeAKKADEAKKAEEA 1533
|
|
| EEP-2 |
cd09084 |
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ... |
431-673 |
5.37e-10 |
|
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps, proteins.
Pssm-ID: 197318 [Multi-domain] Cd Length: 246 Bit Score: 60.39 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 431 SWNVAGLR----AWLKKDGLQLIDLEEPDIFCLQETKCANDQLPEEVTRL-PGYhPYW---LCMPGGYAGVAIYSKiMPI 502
Cdd:cd09084 3 SYNVRSFNrykwKDDPDKILDFIKKQDPDILCLQEYYGSEGDKDDDLRLLlKGY-PYYyvvYKSDSGGTGLAIFSK-YPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 503 H----VEYGIGNEEF---D-DVG--------------RMITAEYEKFYLINVYVPNSGRKLVNLEPRMRWEklfQAYVKK 560
Cdd:cd09084 81 LnsgsIDFPNTNNNAifaDiRVGgdtirvynvhlesfRITPSDKELYKEEKKAKELSRNLLRKLAEAFKRR---AAQADL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 561 LDALK-----PVVICGDMnvshmpidlenpkNNTKnAGFTqeeRDKMTEllglGFVDTFRhlypdRKGAYTFWTYMANAR 635
Cdd:cd09084 158 LAADIaaspyPVIVCGDF-------------NDTP-ASYV---YRTLKK----GLTDAFV-----EAGSGFGYTFNGLFF 211
|
250 260 270
....*....|....*....|....*....|....*...
gi 7295875 636 arnvGWRLDYCLVSERFvpKVVEHEIRSQcLGSDHCPI 673
Cdd:cd09084 212 ----PLRIDYILTSKGF--KVLRYRVDPG-KYSDHYPI 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
32-391 |
5.38e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 32 ENADSAAEELKVPAKGKP-RARKATKTAVSAENSEEVEPQKAPTA---------AARGKKKQPKDTDENGQMEVVAKPKG 101
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAAdEAEAAEEKAEAAEKKKEEAKKKADAAkkkaeekkkADEAKKKAEEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 102 RAKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQAKGRKRKELPAEANGGAEEAAEPP 181
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK 1498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 182 KQRARKEAvpTLKEQAEPGTISKEKvQKAETAAKRARgtKRLADsEIAAALDEPEVDEVPPKAASKRAKKGKMVEPSPET 261
Cdd:PTZ00121 1499 ADEAKKAA--EAKKKADEAKKAEEA-KKADEAKKAEE--AKKAD-EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA 1572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 262 VGDFQSVQEEVESPPKTAAAPKKRAKKTTNGETAVELEPKTKAKPTKQRAKKEGKEPAPGKKQKKSADKEngvvEEEAKP 341
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE----AEEKKK 1648
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 7295875 342 STETKPAK--GRKKAPVKAEDVEDIEEAAEESKPARGRKKAAAKAEEPDVDE 391
Cdd:PTZ00121 1649 AEELKKAEeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-415 |
1.09e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 3 RVKAVKKQAEALASEPTDPTPNANGNGVDENADSAAEELKVPAK-GKPRARKATKTAVSAENSEEVEPQKAPTAAARGKK 81
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEeDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 82 KQPKDTDENGQMEVVAKPKGRAKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQAKGR 161
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 162 KRKELPAEANGGAEEA--AEPPKQRARKEAVPTLKEQAEpgTISKEKVQKAETAAK-RARGTKRLADSEIAAALDEPEVD 238
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAkkADEAKKAEEKKKADELKKAEE--LKKAEEKKKAEEAKKaEEDKNMALRKAEEAKKAEEARIE 1595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 239 EVPPKAASKRAKKGKMVEPSPETVGDFQSVQEEVESPPKTAAAPKKRAKKTTNGETAVELEPKTKAKpTKQRAKKEGKEP 318
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK-AAEEAKKAEEDK 1674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 319 APGKKQKKSADKENGVVEEEAKPSTETKPAKGRKKApvKAEDVEDIEEAAEESKPARGRKKAAAKAEEpdvdeesgsktt 398
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK--EAEEKKKAEELKKAEEENKIKAEEAKKEAE------------ 1740
|
410
....*....|....*..
gi 7295875 399 kkakkAETKTTVTLDKD 415
Cdd:PTZ00121 1741 -----EDKKKAEEAKKD 1752
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1-227 |
4.17e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 1 MPRVKAVKKQAEALASEPTDPTPnangngvDENADSAAEELKVPAKgkpRARKATKTAVSAENseevePQKAPTAAARGK 80
Cdd:PRK05035 492 LARVKAKKAAATQPIVIKAGARP-------DNSAVIAAREARKAQA---RARQAEKQAAAAAD-----PKKAAVAAAIAR 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 81 kkqpkdtdengqmevvAKPKgRAKKATAEAEPEPKVDL--PAGKATKPRAK-KEPTPAPDEVTSSPPKGRAKAEKPTNAQ 157
Cdd:PRK05035 557 ----------------AKAK-KAAQQAANAEAEEEVDPkkAAVAAAIARAKaKKAAQQAASAEPEEQVAEVDPKKAAVAA 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7295875 158 AKGRKRKELPAEANGGAEEAAEPPKQRARKEAVPTLK------EQAEPGTISKEKVQKAETAAKRARGTKRLADSE 227
Cdd:PRK05035 620 AIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKarkaaqQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-395 |
1.47e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 8 KKQAEALASEPTDPTPNANGNGVDENADSAAEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARGKKKQPKDT 87
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 88 DENGQMEVVAKPKGRAKKATAEAEPEPKvDLPAGKATKPRaKKEPTPAPDEVTSSPPKGRAKAEkptnaQAKGRKRKELP 167
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDK-NMALRKAEEAK-KAEEARIEEVMKLYEEEKKMKAE-----EAKKAEEAKIK 1621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 168 AEANGGAEEAAEPPKQRARKEAVPTLKEQAEPGTISKEKVQKAETAaKRARGTKRLADSEIAAALDEPEVDEVPPKAASK 247
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 248 RAKKGKMVEPSPETVGDFQSVQ--EEVESPPKTAAAPKKRAKKTTNGETAVELEPKTKAkptkQRAKKEGKEPAPGKKQK 325
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKkaEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI----AHLKKEEEKKAEEIRKE 1776
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 326 KSAdkengVVEEEAKPSTETKPAKGRKKAPVKAEDVEDIEEAAEESKPARGRKKAAAKAEEPDVDEESGS 395
Cdd:PTZ00121 1777 KEA-----VIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNM 1841
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
23-392 |
3.05e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 23 PNANGNGVDENADSAAEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARG----------KKKQPKDTDENGQ 92
Cdd:PTZ00121 1074 PSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAeearkaedarKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 93 MEVVAKPKGRAKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKgraKAEKPTNAQAKGRKRKELPAEANG 172
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAAR---KAEEERKAEEARKAEDAKKAEAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 173 GAEEAA--EPPKQRARKEAVPTLKEQAEPGTISKEKVQKAETAAKRARGTKRLADSEIAAALDEPEVDEVPPKA--ASKR 248
Cdd:PTZ00121 1231 KAEEAKkdAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAdeAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 249 AKKGKMVEPSPETVGDFQSVQEEV-----------ESPPKTAAAPKKRAKKTTNGETAVEL---EPKTKAKPTKQRAKKE 314
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAkkkaeeakkaaEAAKAEAEAAADEAEAAEEKAEAAEKkkeEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7295875 315 GKepapGKKQKKSADKENGVVEEEAKPSTETKPAKGRKKapvKAEDVEDIEEAAEESKPARGRKKAAAKAEEPDVDEE 392
Cdd:PTZ00121 1391 KK----ADEAKKKAEEDKKKADELKKAAAAKKKADEAKK---KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
45-245 |
5.16e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.03 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 45 AKGKPRARKAT-KTAVSAENSEEVEPQKAPTAAARGKKKQPKDTDENGQMEVVAKPKGRAKKA--TAEAEPEPKVDLPAG 121
Cdd:PRK05035 473 HKKAAEARAAKdKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAekQAAAAADPKKAAVAA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 122 KATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQAKGRKRKELPAEANGGAEEAAEPPKQRARKEAV---PTLKEQAE 198
Cdd:PRK05035 553 AIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIaraKAKKAEQQ 632
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 7295875 199 PGTISKEKVQ--KAETAAKRARGTKRLAdsEIAAALDEPEVDEVPPKAA 245
Cdd:PRK05035 633 ANAEPEEPVDprKAAVAAAIARAKARKA--AQQQANAEPEEAEDPKKAA 679
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-375 |
7.83e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 8 KKQAEALASEPTDPTPNANGNGVDENADSAAEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARGKKKQPKDT 87
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 88 DENGQMEVVAKPKGRAKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKGRA----KAEKPTNAQAKG--- 160
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeeakKADEAKKAEEKKkad 1549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 161 --RKRKEL-PAEANGGAEEA-------------AEPPKQ--RARKEAVPTLKE-----------QAEPGTISKEKVQKAE 211
Cdd:PTZ00121 1550 elKKAEELkKAEEKKKAEEAkkaeedknmalrkAEEAKKaeEARIEEVMKLYEeekkmkaeeakKAEEAKIKAEELKKAE 1629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 212 TAAKRARGTKRLADSEIAAAldepevDEVPPKAASKRAKKGKMVEPSPETVGDFQSVQEEVESPPKTAAAPKKRAKKTTN 291
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKA------EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 292 GETAVELEPKTKAKPTK-QRAKKEGKEPAPGKKQKKSADK----ENGVVEEEAKPSTETKPAKGRKKAPVKAEDVEDIEE 366
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEElKKAEEENKIKAEEAKKEAEEDKkkaeEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
....*....
gi 7295875 367 AAEESKPAR 375
Cdd:PTZ00121 1784 ELDEEDEKR 1792
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
71-392 |
3.00e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 71 KAPTAAARGKKKQPKDTDENgqmevvAKPKGRAKKATAEAEP--EPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKGRA 148
Cdd:PTZ00121 1063 KAHVGQDEGLKPSYKDFDFD------AKEDNRADEATEEAFGkaEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 149 ----KAEKPTNAQAKGRKRKELPAEANGGAEEAAEPPKQRARKEAVPTLKEQAEPGTISKEKVQKAETAAK-----RARG 219
Cdd:PTZ00121 1137 edarKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKaeeerKAEE 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 220 TKRLADSEIAAAL---DEPEVDEVPPKAASKRAKKGKMVEPSPETVGDFQSVQEEVESPPKTAAAPKKRAKKTTNGETAV 296
Cdd:PTZ00121 1217 ARKAEDAKKAEAVkkaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 297 ELEPKTKAkptkQRAKKEGKEPAPGKKQKKSADKENGVVEEEAKPSTETKPAK--GRKKAPVKAEDVEDIEEAAE--ESK 372
Cdd:PTZ00121 1297 KAEEKKKA----DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAeaAKAEAEAAADEAEAAEEKAEaaEKK 1372
|
330 340
....*....|....*....|...
gi 7295875 373 PARGRKKAAA---KAEEPDVDEE 392
Cdd:PTZ00121 1373 KEEAKKKADAakkKAEEKKKADE 1395
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
102-253 |
1.58e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.02 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 102 RAKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAekptnAQAKGRKRKELPAEANGGAEEAAEPP 181
Cdd:PRK05035 472 RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVI-----AAREARKAQARARQAEKQAAAAADPK 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 182 KQ-----RARKEAVPTLKEQAEPGTISKEKVQKAETAAKRARGTKRLADSEIAAALDEPEVDEVPPK-----AASKRAKK 251
Cdd:PRK05035 547 KAavaaaIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKkaavaAAIARAKA 626
|
..
gi 7295875 252 GK 253
Cdd:PRK05035 627 KK 628
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
33-315 |
2.01e-05 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 47.93 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 33 NADSAAEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAptaaargkkkqpkdTDENGQMEVVaKPKGRAkkataeaep 112
Cdd:PLN03237 1189 GESGAAKKVSRQAPKKPAPKKTTKKASESETTEETYGSSA--------------METENVAEVV-KPKGRA--------- 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 113 epkvdlpaGKATKPRAKKEPTPAPDEVTS-----------SPPKGRAKAEKPTNAQAKGRKRKELPAEANGGAEEAAEPP 181
Cdd:PLN03237 1245 --------GAKKKAPAAAKEKEEEDEILDlkdrlaaynldSAPAQSAKMEETVKAVPARRAAARKKPLASVSVISDSDDD 1316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 182 KQRARKE--AVPTLKEQAEPGTISKEKVQKAETAAKRARG--TKRLADSEIAAALDEPEVDEVPPKAASKRAKKGKMVEP 257
Cdd:PLN03237 1317 DDDFAVEvsLAERLKKKGGRKPAAANKKAAKPPAAAKKRGpaTVQSGQKLLTEMLKPAEAIGISPEKKVRKMRASPFNKK 1396
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 7295875 258 SPETVGDFQSVQEEVESPPktaaapkkraKKTTNGETAVELEPKTKAKPtkQRAKKEG 315
Cdd:PLN03237 1397 SGSVLGRAATNKETESSEN----------VSGSSSSEKDEIDVSAKPRP--QRANRKQ 1442
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
45-233 |
3.93e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 47.15 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 45 AKGKPRARKATKTAVSAENSEEvEPQKAPTAAARGKKKQPKDTdengqmEVVAKPKGRAKKATAEAEPEPKVDLPAGKAT 124
Cdd:PRK07003 379 AVPAPGARAAAAVGASAVPAVT-AVTGAAGAALAPKAAAAAAA------TRAEAPPAAPAPPATADRGDDAADGDAPVPA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 125 KPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAqAKGRKRKELPAEANGGAEEAAEPPKQRARKEAVPTLKE---QAEPGT 201
Cdd:PRK07003 452 KANARASADSRCDERDAQPPADSGSASAPASD-APPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDApaaAAPPAP 530
|
170 180 190
....*....|....*....|....*....|..
gi 7295875 202 ISKEKVQKAETAAKRARGTkrladseiAAALD 233
Cdd:PRK07003 531 EARPPTPAAAAPAARAGGA--------AAALD 554
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
141-388 |
6.07e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.13 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 141 SSPPKGRAKAEKPTNAQAKGRKRKELPAEAngGAEEAAEPPKQRARKEAVPTLK----EQAEPGTISKEKVQKAETAAKR 216
Cdd:PRK07735 1 MDPEKDLEDLKKEAARRAKEEARKRLVAKH--GAEISKLEEENREKEKALPKNDdmtiEEAKRRAAAAAKAKAAALAKQK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 217 ARGTKRLADSEIAAAlDEPEVDEVPPKAASKRAKKGKMVEPSPETVGDFQSVQEEVESPPKTAAAPKKRAKKTTNGETAV 296
Cdd:PRK07735 79 REGTEEVTEEEKAKA-KAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 297 ELEPKTKAKpTKQRAKKEGKEPAPGKKQKKSADKENGVVEEEAKPSTETKP---AKGRKKAPVKAEDVEDIEEAAEESKP 373
Cdd:PRK07735 158 EETDKEKAK-AKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAaaaAKAKAAALAKQKASQGNGDSGDEDAK 236
|
250
....*....|....*
gi 7295875 374 ARGRKKAAAKAEEPD 388
Cdd:PRK07735 237 AKAIAAAKAKAAAAA 251
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
66-387 |
6.68e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.16 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 66 EVEPQKAPTAAARGKKKQPKDTDENGQmevvAKPKGRAKKATAEAEPEPKVDLPAGKATKPRA-----KKEPTPAPDEVT 140
Cdd:NF033838 182 DVEVKKAELELVKEEAKEPRDEEKIKQ----AKAKVESKKAEATRLEKIKTDREKAEEEAKRRadaklKEAVEKNVATSE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 141 SSPPKGRAKAEKPTNAQAKGRKRKELPAEANGGAEEAAEPPKQRARKEAVPTLKEQAEPGtiSKEKVQKAETAAKRARGT 220
Cdd:NF033838 258 QDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAK--KKAKDQKEEDRRNYPTNT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 221 KRLADSEIAAAldEPEVDEVPPKAASKRAKKGKMVEPSPEtvgdfqsVQEEVESPPKTAAAPKKRAKKTTNGET----AV 296
Cdd:NF033838 336 YKTLELEIAES--DVKVKEAELELVKEEAKEPRNEEKIKQ-------AKAKVESKKAEATRLEKIKTDRKKAEEeakrKA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 297 ELEPKTKAKPTKQrakkegKEPAPGKKQKKSADKENgvveeeaKPSTETKPAKgrkkaPVKAEDVEDIEEAAEEsKPARG 376
Cdd:NF033838 407 AEEDKVKEKPAEQ------PQPAPAPQPEKPAPKPE-------KPAEQPKAEK-----PADQQAEEDYARRSEE-EYNRL 467
|
330
....*....|.
gi 7295875 377 RKKAAAKAEEP 387
Cdd:NF033838 468 TQQQPPKTEKP 478
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
97-232 |
8.42e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 45.86 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 97 AKPKGRAKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQAKGrkrkelPAEanggAEE 176
Cdd:PRK14951 378 KKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAA------PAA----VAL 447
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7295875 177 AAEPPKQRARKEAVPTLKEQAEPGTISKEKVQKAETAAKRARGT----------KRLADSEIAAAL 232
Cdd:PRK14951 448 APAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTeegdvwhatvQQLAAAEAITAL 513
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
65-253 |
8.57e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 65 EEVEPQKAPTAAARGKKKQPKDTDENGQMEVVAKPKGRAKKATAEAEPEPKV-DLPAGKATKPRAKKEPTPAPDEVTSSP 143
Cdd:PRK05035 465 EKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNsAVIAAREARKAQARARQAEKQAAAAAD 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 144 PKG--------RAKAEKptnAQAKGRKRKELPAEANGGAEEAAEPPKQRARKEAVPTLKEQAEPGTiSKEKVQKAETAAK 215
Cdd:PRK05035 545 PKKaavaaaiaRAKAKK---AAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQV-AEVDPKKAAVAAA 620
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 7295875 216 RARGTKRLAdseiAAALDEPEVDEVPPK-----AASKRAKKGK 253
Cdd:PRK05035 621 IARAKAKKA----EQQANAEPEEPVDPRkaavaAAIARAKARK 659
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1-201 |
1.08e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 45.64 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 1 MPRVKAVKKQAEALASEPTDPTPNANGNGVDENADSAAEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARGK 80
Cdd:PRK12323 386 APAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPA 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 81 KKQPKdTDENGQMEVVAKPKGRAKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQAkg 160
Cdd:PRK12323 466 AAGPR-PVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLA-- 542
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 7295875 161 rkrkELPAEAnggaeeAAEPPKQRARKEAVPTLKEQAEPGT 201
Cdd:PRK12323 543 ----PAPAAA------PAPRAAAATEPVVAPRPPRASASGL 573
|
|
| PLN02967 |
PLN02967 |
kinase |
299-393 |
1.13e-04 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 45.42 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 299 EPKTKAKPTKQRAKKEGKEPAPGKKQKKSADKENGVVEEEAKPSTETKPAKGRKKAPVkAEDVEDIEEAAEESKPARGRK 378
Cdd:PLN02967 64 ENGAVSKKKPTRSVKRATKKTVVEISEPLEEGSELVVNEDAALDKESKKTPRRTRRKA-AAASSDVEEEKTEKKVRKRRK 142
|
90
....*....|....*
gi 7295875 379 KAAAKAEEPDVDEES 393
Cdd:PLN02967 143 VKKMDEDVEDQGSES 157
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
148-383 |
1.30e-04 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 45.62 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 148 AKAEKPTNAQAKGRKRKELPAEANGGAEEAAEPPKQRARKEAVPTLKEQAEPGTISKEKVQKAETAAKRARGTKRLAdsE 227
Cdd:PLN03237 1173 AKAEEAREKLQRAAARGESGAAKKVSRQAPKKPAPKKTTKKASESETTEETYGSSAMETENVAEVVKPKGRAGAKKK--A 1250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 228 IAAALDEPEVDEVPpkaASKRAKKGKMVEPSPETVGDFQSVQEEVESPPKTAAAPKKRAKKTTNGETAVELEPKTKAKPT 307
Cdd:PLN03237 1251 PAAAKEKEEEDEIL---DLKDRLAAYNLDSAPAQSAKMEETVKAVPARRAAARKKPLASVSVISDSDDDDDDFAVEVSLA 1327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 308 KQRAKKEGKEPAPGKKQKKsadkengvveeeAKPSTETKPAKGRKKAPVK--AEDVEDIEEA--AEESKPARGRKKAAAK 383
Cdd:PLN03237 1328 ERLKKKGGRKPAAANKKAA------------KPPAAAKKRGPATVQSGQKllTEMLKPAEAIgiSPEKKVRKMRASPFNK 1395
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
122-384 |
1.64e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 122 KATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQAKGRKRKELPAEANGGAEEAAEPPKQRARkeavptlkeQAEPGT 201
Cdd:PRK05035 469 REARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARAR---------QAEKQA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 202 ISKEKVQKAETAAKRARGTKRLADSEIAAALDEPEVDEVPPK--AASKRAKKGKmvepspetvgdfqSVQEEVESPPKTA 279
Cdd:PRK05035 540 AAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAvaAAIARAKAKK-------------AAQQAASAEPEEQ 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 280 AAPKKRAKKTTNGETAvelepKTKAKPTKQRAKKEGKEPAPGKKqkksadkengvveeeAKPSTETKPAKGRKKApvKAE 359
Cdd:PRK05035 607 VAEVDPKKAAVAAAIA-----RAKAKKAEQQANAEPEEPVDPRK---------------AAVAAAIARAKARKAA--QQQ 664
|
250 260
....*....|....*....|....*
gi 7295875 360 DVEDIEEAAEESKPARGRKKAAAKA 384
Cdd:PRK05035 665 ANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
44-248 |
1.76e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.87 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 44 PAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARGKKKQPKDTDENGQMEVVAKPKGRAKKATAEAEPEPKVDLPAGKA 123
Cdd:PRK12323 381 PVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAA 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 124 TKPRAKKEPTPAPDEVTSSPPKgRAKAEKPTNAQAKGRKRKELPAEANGGAEEAAEPPKQRARKEAVPtlkeqaEPGTIS 203
Cdd:PRK12323 461 AARPAAAGPRPVAAAAAAAPAR-AAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIP------DPATAD 533
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 7295875 204 KEKVQKAETAAKRArgtkrlADSEIAAALDEPEVDEVPPKAASKR 248
Cdd:PRK12323 534 PDDAFETLAPAPAA------APAPRAAAATEPVVAPRPPRASASG 572
|
|
| R1-I-EN |
cd09077 |
Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat ... |
446-578 |
2.34e-04 |
|
Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat retrotransposons; This family contains the endonuclease (EN) domain of various non-long terminal repeat (non-LTR) retrotransposons, long interspersed nuclear elements (LINEs) which belong to the subtype 2, R1- and I-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. Most non-LTR retrotransposons are inserted throughout the host genome; however, many retrotransposons of the R1 clade exhibit target-specific retrotransposition. This family includes the endonucleases of SART1 and R1bm, from the silkworm Bombyx mori, which belong to the R1-clade. It also includes the endonuclease of snail (Biomphalaria glabrata) Nimbus/Bgl and mosquito Aedes aegypti (MosquI), both which belong to the I-clade. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.
Pssm-ID: 197311 [Multi-domain] Cd Length: 205 Bit Score: 43.05 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 446 LQLIDLEEPDIFCLQETKCANDQLPEEVTRLPGyhpywlcmpggyaGVAIYSKIMPIHVEYgignEEFDDVGRMITAEYE 525
Cdd:cd09077 19 LQTAREEGADIALIQEPYLVPVNNPNWVTDESG-------------RAAIVVSDRLPRKPI----QRLSLGLGIVAARVG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 7295875 526 KFYLINVYVPNSGrklvNLEPrmrweklFQAYVKKLDAL-----KPVVICGDMNVSHM 578
Cdd:cd09077 82 GITVVSCYAPPSE----SLEE-------FEEYLENLVRIvrglsRPVIIGGDFNAWSP 128
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
31-393 |
2.43e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 44.30 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 31 DENADSAAEELKVP-AKGKPrarkATKTAVSAENSEEVEPQKAPTAAARGKKKQPKDTDENGQMEVVAKPKGRAKKATAE 109
Cdd:PTZ00449 501 EEDSDKHDEPPEGPeASGLP----PKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLS 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 110 AEPE-PKvdlpagKATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQ-AKGRKRKELPAEANggaeeaAEPPKQRA-- 185
Cdd:PTZ00449 577 KKPEfPK------DPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDiPKSPKRPESPKSPK------RPPPPQRPss 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 186 --RKEAVPTLKEQAEPGTIS-------KEKVQKAET-AAKRARGTK--RLADSEIAAALDEPEVDE----------VPPK 243
Cdd:PTZ00449 645 peRPEGPKIIKSPKPPKSPKppfdpkfKEKFYDDYLdAAAKSKETKttVVLDESFESILKETLPETpgtpfttprpLPPK 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 244 ----AASKRAKKGKMVEPSPETVGDFQSVQEEV----ESPPKTAAAPKKRAKKTTNGETAVELEPKTKAK----PTKQRA 311
Cdd:PTZ00449 725 lprdEEFPFEPIGDPDAEQPDDIEFFTPPEEERtffhETPADTPLPDILAEEFKEEDIHAETGEPDEAMKrpdsPSEHED 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 312 KKEGKEPAPGKKQKKSADKENGVVEEEAKPSTETKPAKGRKKAPVKAEDVEDIE--EAAEESKPARGRKKAAAKAEEPDv 389
Cdd:PTZ00449 805 KPPGDHPSLPKKRHRLDGLALSTTDLESDAGRIAKDASGKIVKLKRSKSFDDLTtvEEAEEMGAEARKIVVDDDGTEAD- 883
|
....
gi 7295875 390 DEES 393
Cdd:PTZ00449 884 DEDT 887
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
6-231 |
5.19e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.77 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 6 AVKKQAEALASEPTDPTPNANGNGVDENADSAAEELKVP--------AKGKPRARKATKTAVSAE---NSEEVEPQKAPT 74
Cdd:PHA03247 301 ALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAMEVVSPlprprqhyPLGFPKRRRPTWTPPSSLedlSAGRHHPKRASL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 75 AAaRGKKKQPKdtdenGQMEVVAKPKGRAKKATAEAEP--EPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAEK 152
Cdd:PHA03247 381 PT-RKRRSARH-----AATPFARGPGGDDQTRPAAPVPasVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPERQP 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7295875 153 PTNAQakgrkrkelpaeanggaeEAAEPPKQRARKEAVPTLKEQAEPGTISKEKVQKAETAAKRARGTKRLADSEIAAA 231
Cdd:PHA03247 455 PAPAT------------------EPAPDDPDDATRKALDALRERRPPEPPGADLAELLGRHPDTAGTVVRLAAREAAIA 515
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
97-261 |
9.78e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.53 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 97 AKPKGRAKKATA-EAEPEPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAekPTNAQAKGRKRKELPAEANGGAE 175
Cdd:PRK07003 379 AVPAPGARAAAAvGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPP--ATADRGDDAADGDAPVPAKANAR 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 176 EAAEPPKQRARKEAVPTLKEQAEPgtiskekvqkAETAAKRARGTKRLADSEIAAALDEPEVDEVPPKAASKRAKKGKMV 255
Cdd:PRK07003 457 ASADSRCDERDAQPPADSGSASAP----------ASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAA 526
|
....*.
gi 7295875 256 EPSPET 261
Cdd:PRK07003 527 PPAPEA 532
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
88-395 |
1.17e-03 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 42.16 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 88 DENGQMEVVAKPKGRAKKATAEAEPEPKVDLPAGKATKPRA---KKEPTPAPDEVTSSPPKGRAKAEKPTNAQAKGRKRK 164
Cdd:PLN03237 1169 DKEDAKAEEAREKLQRAAARGESGAAKKVSRQAPKKPAPKKttkKASESETTEETYGSSAMETENVAEVVKPKGRAGAKK 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 165 ELPAEANgGAEEAAEPPKQRARKEAVPTLKEQAEPGtiSKEKVQKAETAAKRARGTKRLADSEIAAALDEPEVDEVPPKA 244
Cdd:PLN03237 1249 KAPAAAK-EKEEEDEILDLKDRLAAYNLDSAPAQSA--KMEETVKAVPARRAAARKKPLASVSVISDSDDDDDDFAVEVS 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 245 ASKRAKKGKMVEPSpetvgdfQSVQEEVESPPKTAAAPKKRAKKTTNGETAVELEPKTKAKPTKQRAKKEGKEPAPgkkq 324
Cdd:PLN03237 1326 LAERLKKKGGRKPA-------AANKKAAKPPAAAKKRGPATVQSGQKLLTEMLKPAEAIGISPEKKVRKMRASPFN---- 1394
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7295875 325 KKSADKENGVVEEEAKPSTETKPAkgrkkapvKAEDVEDIEEAAEESKPARGRKKAAAKAeepDVDEESGS 395
Cdd:PLN03237 1395 KKSGSVLGRAATNKETESSENVSG--------SSSSEKDEIDVSAKPRPQRANRKQTTYV---LSDSESES 1454
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
54-377 |
1.29e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 54 ATKTAVSAENSEEVEPQKAPTAAARGKKKQPKDTDENGQMEVVAKPKGRAKKATAEAEPEPkvdlpagkatkprakkEPT 133
Cdd:PHA03307 57 AGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPP----------------PPT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 134 PAPDEVTSSPPKGRAKAEKPTNAQAKGRKRKELPAEANGGAEEAAEPPkqrARKEAVP-TLKEQAEPGTISKEKVQKAET 212
Cdd:PHA03307 121 PPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAAS---SRQAALPlSSPEETARAPSSPPAEPPPST 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 213 AAKRARGTKRLADSEIAAALDEPevDEVPPKAASKRAKKGKMVEPSPETVGDFQSVQEEVESPPktaaapkkrakkttng 292
Cdd:PHA03307 198 PPAAASPRPPRRSSPISASASSP--APAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPR---------------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 293 etavelePKTKAKPTKQRAKKEGKEPAPGK--KQKKSADKENGVVEEEAKPSTETKPAKGRKKAPVKAEDVEDIEEAAEE 370
Cdd:PHA03307 260 -------PAPITLPTRIWEASGWNGPSSRPgpASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSS 332
|
....*..
gi 7295875 371 SKPARGR 377
Cdd:PHA03307 333 SESSRGA 339
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2-261 |
1.32e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 2 PRVKAVKKQAEALASE----PTDPTPNAngngvdenADSAAEELKVPAKgKPRARKATKTAVSAENSEEVEPQKAPTAAA 77
Cdd:PHA03247 2531 PRMLTWIRGLEELASDdagdPPPPLPPA--------APPAAPDRSVPPP-RPAPRPSEPAVTSRARRPDAPPQSARPRAP 2601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 78 RGKKKQPKdtdengqmevvakpkgrakkATAEAEPEPkvdlPAGKATKPRAKkEPTPAPDEVTSSPPKGRAKAEKPTNAQ 157
Cdd:PHA03247 2602 VDDRGDPR--------------------GPAPPSPLP----PDTHAPDPPPP-SPSPAANEPDPHPPPTVPPPERPRDDP 2656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 158 AKGRKRKELPAEANGGAEEAAEPP---KQRARKEAVPTLKEQAEPGTISKEKvQKAETAAKRARGTKRLADSEIAAALDE 234
Cdd:PHA03247 2657 APGRVSRPRRARRLGRAAQASSPPqrpRRRAARPTVGSLTSLADPPPPPPTP-EPAPHALVSATPLPPGPAAARQASPAL 2735
|
250 260
....*....|....*....|....*..
gi 7295875 235 PEVDEVPPKAASKRAKKGKMVEPSPET 261
Cdd:PHA03247 2736 PAAPAPPAVPAGPATPGGPARPARPPT 2762
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
49-214 |
1.64e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 41.50 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 49 PRARKATKTAVSAENSEEVEPQKAPTA-AARGKKKQPKDTDENGQMEVvAKPKGRAKKATAEAEPEPKVDLPAGKATKPR 127
Cdd:PRK13108 276 PKGREAPGALRGSEYVVDEALEREPAElAAAAVASAASAVGPVGPGEP-NQPDDVAEAVKAEVAEVTDEVAAESVVQVAD 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 128 AKKEPTPAPDEVTssppkgRAKAEKP----TNAQAKGRKRKELPAEANGGAEEAAEPPKQRARKEAVPTLKEQAEPGTIS 203
Cdd:PRK13108 355 RDGESTPAVEETS------EADIEREqpgdLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAK 428
|
170
....*....|.
gi 7295875 204 KEKVQKAETAA 214
Cdd:PRK13108 429 PDELAVAGPGD 439
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
22-191 |
2.26e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 40.91 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 22 TPNANGNGVdENADSAAEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARGKKKQPKDTDENGQMEVVAKPKG 101
Cdd:NF040712 169 DPGAHGGTV-TALDDEARWLIDPDFGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 102 -RAKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPdEVTSSPPKGRAKAEKPTNAQAKGRKRKELPAEAnggAEEAAEP 180
Cdd:NF040712 248 rRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAP-GAAETPEAAEPPAPAPAAPAAPAAPEAEEPARP---EPPPAPK 323
|
170
....*....|.
gi 7295875 181 PKQRARKEAVP 191
Cdd:NF040712 324 PKRRRRRASVP 334
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
4-239 |
2.68e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 40.73 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 4 VKAVKKQAEALASEPTDPTPNANGNGVDENADSAAEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARGK--K 81
Cdd:PRK07735 64 AAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAalA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 82 KQPKDTDENGQMEVVAKPKGRAKKATAEAepepkvdlpAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQAKGR 161
Cdd:PRK07735 144 KQKREGTEEVTEEEEETDKEKAKAKAAAA---------AKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAK 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7295875 162 krkelpaeanggaeeAAEPPKQRARKEAVPTLKEQAEPGTISKEKVQKAETAAKRARGTKrlADSEIAAALDEPEVDE 239
Cdd:PRK07735 215 ---------------AAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTKGAE--GKKEEEPKQEEPSVNQ 275
|
|
| PLN02967 |
PLN02967 |
kinase |
329-393 |
2.69e-03 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 40.80 E-value: 2.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7295875 329 DKENGVVEEEAKPSTETKPAKGRKKAPVKAEDV-EDIEE--------AAEESKPARGRKKAAAKAEEPDVDEES 393
Cdd:PLN02967 59 DEEPDENGAVSKKKPTRSVKRATKKTVVEISEPlEEGSElvvnedaaLDKESKKTPRRTRRKAAAASSDVEEEK 132
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
32-198 |
3.33e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 32 ENADSAAEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARGKKKQPKDTDENGQMEVVAkpkgrAKKATAEAE 111
Cdd:PRK09510 94 QKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAA-----AKKAAAEAK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 112 PEPKVDlpAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQAKGRKRKElpAEANGGAEEAAEPPKQRARKEAVP 191
Cdd:PRK09510 169 KKAEAE--AAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA--AEAKAAAAKAAAEAKAAAEKAAAA 244
|
....*..
gi 7295875 192 TLKEQAE 198
Cdd:PRK09510 245 KAAEKAA 251
|
|
| PLN02967 |
PLN02967 |
kinase |
70-242 |
3.37e-03 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 40.41 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 70 QKAPTAAARGKKKQPKDTDENGQMEVVAKPKGRAKKATAEAEPEpkvdlpagkatKPRAKKEPTPAPDEVTSSPPKGRAK 149
Cdd:PLN02967 40 NKFLLAAGSRKKIESALAVDEEPDENGAVSKKKPTRSVKRATKK-----------TVVEISEPLEEGSELVVNEDAALDK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 150 AEKPTnaqaKGRKRKELPAEANGGAEEAAEPPKQRARKeaVPTLKEQAEPGTISKEKVQKAETAAKRARGTKRLADSEIA 229
Cdd:PLN02967 109 ESKKT----PRRTRRKAAAASSDVEEEKTEKKVRKRRK--VKKMDEDVEDQGSESEVSDVEESEFVTSLENESEEELDLE 182
|
170
....*....|....*
gi 7295875 230 AALDE--PEVDEVPP 242
Cdd:PLN02967 183 KDDGEdiSHTYGWPP 197
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
99-177 |
4.07e-03 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 40.64 E-value: 4.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7295875 99 PKGRAKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQAKGRKRKELPAEANGGAEEA 177
Cdd:PRK12270 39 GSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEV 117
|
|
| Exo_endo_phos_2 |
pfam14529 |
Endonuclease-reverse transcriptase; This domain represents the endonuclease region of ... |
527-673 |
4.26e-03 |
|
Endonuclease-reverse transcriptase; This domain represents the endonuclease region of retrotransposons from a range of bacteria, archaea and eukaryotes. These are enzymes largely from class EC:2.7.7.49.
Pssm-ID: 434019 [Multi-domain] Cd Length: 118 Bit Score: 37.73 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 527 FYLINVYVPNSGrKLVNLEprmrweKLFQAYVKKLDAlKPVVICGDMNVSHmpIDLENPKNNTKNAgftqeerdkmTELl 606
Cdd:pfam14529 1 ILIISVYCPPSD-QLRNLL------DTLEDILRSLDR-PPIIIGGDFNAHH--PLWGSNSTDVSRG----------EEL- 59
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7295875 607 gLGFVDTFR-HLYPDRKGAYTFWtymaNARARNVgwrLDYCLVSERFVPKVVEHEIrsQCLGSDHCPI 673
Cdd:pfam14529 60 -IEFLNEHGlNLLNLPKSGPTFI----SSNGDST---IDLTLTSDPLAVRVLSDLG--PDSGSDHRPI 117
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
186-383 |
4.65e-03 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 40.36 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 186 RKEAVPTLKEQAEPGTISKEKVQKAETAAKRAR---GTKRLADSEIAAALDEPEVDEvppkaaskRAKKGKMVEPSPETV 262
Cdd:PRK14900 863 RKLQNPSFVQNAPPAVVEKDRARAEELREKRGKleaHRAMLSGSEANSARRDTMEIQ--------NEQKPTQDGPAAEAQ 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 263 GDFQS-VQEEVESppKTAAAPKKRAKKTTNGETAVELEPKTKAKPTKQRAKKEGKEPAPGKKQ--KKSADKENGVVEEEA 339
Cdd:PRK14900 935 PAQENtVVESAEK--AVAAVSEAAQQAATAVASGIEKVAEAVRKTVRRSVKKAAATRAAMKKKvaKKAPAKKAAAKKAAA 1012
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 7295875 340 KPSTETKPAKgrKKAPVKAEdvedIEEAAEESKPARGRKKAAAK 383
Cdd:PRK14900 1013 KKAAAKKKVA--KKAPAKKV----ARKPAAKKAAKKPARKAAGR 1050
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
218-394 |
4.66e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 40.27 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 218 RGTKRLADSEIAAALDEPEVDEVPPKAASKRAKKgkmvePSPETVGDFQSVQEEVESPPKTAAAPKKRAKKTTNGETAVE 297
Cdd:PRK12678 41 KGTSGMRKGELIAAIKEARGGGAAAAAATPAAPA-----AAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 298 LEPKTKAKPTKQRAKKEGKEPAPGKKQKKSADKENGVVEEEAKPSTETKPAKGRKKAPVKAEDVEDIEEAAEESKPARGR 377
Cdd:PRK12678 116 AEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREE 195
|
170
....*....|....*..
gi 7295875 378 KKAAAKAEEPDVDEESG 394
Cdd:PRK12678 196 RGRDGDDRDRRDRREQG 212
|
|
| PTZ00436 |
PTZ00436 |
60S ribosomal protein L19-like protein; Provisional |
75-250 |
5.33e-03 |
|
60S ribosomal protein L19-like protein; Provisional
Pssm-ID: 185616 [Multi-domain] Cd Length: 357 Bit Score: 39.55 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 75 AAARGKKKQPKDTDENGQMEVVAKPKGRAKKATAEAEPEPKVDLPAGKATKPRAKKEP-TPAPDEVTSSPPKGRAKAEK- 152
Cdd:PTZ00436 160 AAKRLKDEQHRHKARKQELRKREKDRERARREDAAAAAAAKQKAAAKKAAAPSGKKSAkAAAPAKAAAAPAKAAAPPAKa 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 153 ---PTNAQAKGRKRKELPAEANGGAEEAAEPPKQRAR---KEAVPTLKEQAEPGTISKEKVQKAETAAKRARGTKRLADS 226
Cdd:PTZ00436 240 aaaPAKAAAAPAKAAAPPAKAAAPPAKAAAPPAKAAAppaKAAAPPAKAAAPPAKAAAAPAKAAAAPAKAAAAPAKAAAP 319
|
170 180
....*....|....*....|....
gi 7295875 227 EIAAALDEPEVDEVPPKAASKRAK 250
Cdd:PTZ00436 320 PAKAAAPPAKAATPPAKAAAPPAK 343
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
103-306 |
5.73e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 40.08 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 103 AKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPDEVTSS-----------PPKGRAKAEKPTNAQAKGRKRKELPAEAn 171
Cdd:PRK08691 365 SCDANAVIENTELQSPSAQTAEKETAAKKPQPRPEAETAQtpvqtasaaamPSEGKTAGPVSNQENNDVPPWEDAPDEA- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 172 ggaeEAAEPPKQRARKeavpTLKEQAEPGTISKEKVQKAETAAKRARGTKRLADSE---IAAALDEPEVDEVPPKAASKR 248
Cdd:PRK08691 444 ----QTAAGTAQTSAK----SIQTASEAETPPENQVSKNKAADNETDAPLSEVPSEnpiQATPNDEAVETETFAHEAPAE 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 249 AKKGKMVEPSPETVGDfqsvQEEVESPPKTAAAPKKRAKKTT--NGETAVELEPKTKAKP 306
Cdd:PRK08691 516 PFYGYGFPDNDCPPED----GAEIPPPDWEHAAPADTAGGGAdeEAEAGGIGGNNTPSAP 571
|
|
| PRK13808 |
PRK13808 |
adenylate kinase; Provisional |
38-164 |
7.11e-03 |
|
adenylate kinase; Provisional
Pssm-ID: 172341 [Multi-domain] Cd Length: 333 Bit Score: 39.10 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 38 AEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARGKKKQPKDTDENGQMEVVAKPKGRAKKATAEAEPEPKVD 117
Cdd:PRK13808 196 AANAKKAAKTPAAKSGAKKASAKAKSAAKKVSKKKAAKTAVSAKKAAKTAAKAAKKAKKTAKKALKKAAKAVKKAAKKAA 275
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 7295875 118 LPAGKATKPRAKKEPTPAPdevTSSPPKGRAKAEKPTNAQAKGRKRK 164
Cdd:PRK13808 276 KAAAKAAKGAAKATKGKAK---AKKKAGKKAAAGSKAKATAKAPKRG 319
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
112-392 |
9.55e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 39.21 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 112 PEPKV----DLPAGKATKPRAKKEPTPApdevtssppkgraKAEKPTNAQAKGRKRKELPAEANGGAEEAAEPPKqrark 187
Cdd:TIGR00927 620 PVAKVmalgDLSKGDVAEAEHTGERTGE-------------EGERPTEAEGENGEESGGEAEQEGETETKGENES----- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 188 eavptlkEQAEPGTISKEKVQKAETAAKRARgTKRLADSEIAAALDEPEVDEVPPKAASKRAKKGKMVEPspETVGDFQS 267
Cdd:TIGR00927 682 -------EGEIPAERKGEQEGEGEIEAKEAD-HKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVED--EGEGEAEG 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 268 VQE-EVESPPKTAAAPKKRAKKTTNGETAVELEpktkakpTKQRAKKEGKEPAPGKKQKKSADKENGVVEEEAKPSTETK 346
Cdd:TIGR00927 752 KHEvETEGDRKETEHEGETEAEGKEDEDEGEIQ-------AGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQAD 824
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 7295875 347 PAKGRKKAPVKAEDVEDIEEAAEESKPARGRKKAAAKAEEPDVDEE 392
Cdd:TIGR00927 825 DTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEE 870
|
|
| PRK12373 |
PRK12373 |
NADH-quinone oxidoreductase subunit E; |
45-176 |
9.90e-03 |
|
NADH-quinone oxidoreductase subunit E;
Pssm-ID: 237082 [Multi-domain] Cd Length: 400 Bit Score: 39.01 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7295875 45 AKGKPRARKATKTAVSAenseevepqKAPTAAARGKKKQPKDTDENGQMEVVakPKGRAKKATAEAEPEPKVDLP----- 119
Cdd:PRK12373 200 EAGKARYNASKALAEDI---------GDTVKRIDGTEVPLLAPWQGDAAPVP--PSEAARPKSADAETNAALKTPatapk 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 7295875 120 AGKATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTnAQAKGRKRKELPAEANGGAEE 176
Cdd:PRK12373 269 AAAKNAKAPEAQPVSGTAAAEPAPKEAAKAAAAAA-KPALEDKPRPLGIARPGGADD 324
|
|
| |
