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Conserved domains on  [gi|1167936614|gb|ARB03468|]
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putative gag-pro-pol polyprotein [Murine leukemia virus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gag_p30 pfam02093
Gag P30 core shell protein; According to Swiss-Prot annotation this protein is the viral core ...
 225-432 6.46e-149

Gag P30 core shell protein; According to Swiss-Prot annotation this protein is the viral core shell protein. P30 is essential for viral assembly.


:

Pssm-ID: 426597  Cd Length: 208  Bit Score: 455.28  E-value: 6.46e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  225 QYWPFSSSDLYNWKNNNPSFSEDPGKLTASIESVLTTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLP 304
Cdd:pfam02093    1 QYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLVTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  305 NEVDAAFPLERPDWDYTTQRGRNHLVLYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPE 384
Cdd:pfam02093   81 NEVDAAFPLERPDWDYTTPAGRNHLVLYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPE 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1167936614  385 DPGQETNVSMSFIWQSAPDIGRKLERLEDLKSKTLGDLVREAERIFNK 432
Cdd:pfam02093  161 DPGQETNVSMSFIWQSAPDIGRKLERLEDLKSKTLGDLVREAEKIFNK 208
RT_ZFREV_like cd03715
RT_ZFREV_like: A subfamily of reverse transcriptases (RTs) found in sequences similar to the ...
 716-931 2.88e-117

RT_ZFREV_like: A subfamily of reverse transcriptases (RTs) found in sequences similar to the intact endogenous retrovirus ZFERV from zebrafish and to Moloney murine leukemia virus RT. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses. These elements can be divided into two major groups. One group contains retroviruses and DNA viruses whose propagation involves an RNA intermediate. They are grouped together with transposable elements containing long terminal repeats (LTRs). The other group, also called poly(A)-type retrotransposons, contain fungal mitochondrial introns and transposable elements that lack LTRs. Phylogenetic analysis suggests that ZFERV belongs to a distinct group of retroviruses.


:

Pssm-ID: 239685 [Multi-domain]  Cd Length: 210  Bit Score: 368.60  E-value: 2.88e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  716 PVSIKQYPMSHEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPGTNDYRPVQDLREVNKRVEDIHPTVPNPYNLLS 795
Cdd:cd03715      1 PVNQKQYPLPREAREGITPHIQELLEAGILVPCQSPWNTPILPVKKPGGNDYRMVQDLRLVNQAVLPIHPAVPNPYTLLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  796 GLPPSHRWYTVLDLKDAFFCLRLHPTSQPLFAFEWRDpgmgisGQLTWTRLPQGFKNSPTLFDEALHRDLADFRIQHPDL 875
Cdd:cd03715     81 LLPPKHQWYTVLDLANAFFSLPLAPDSQPLFAFEWEG------QQYTFTRLPQGFKNSPTLFHEALARDLAPFPLEHEGT 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1167936614  876 ILLQYVDDILLAATSELDCQQGTRALLLTLGNLGYRASAKKAQICQKQVKYLGYLL 931
Cdd:cd03715    155 ILLQYVDDLLLAADSEEDCLKGTDALLTHLGELGYKVSPKKAQICRAEVKFLGVVW 210
Gag_MA pfam01140
Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved ...
 2-124 4.55e-58

Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved in pathogenicity.


:

Pssm-ID: 426076 [Multi-domain]  Cd Length: 126  Bit Score: 196.45  E-value: 4.55e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614    2 GQTVTTPLSLTLEHWKDVQRIASNQSVDVKKRRWVTFCSAEWPTFGVGWPQDGTFNLDIILQVKSKVFSPGPHGHPDQVP 81
Cdd:pfam01140    1 GQTVTTPLSLTLGHWSDVPSRACNQSVDVKKRRWVTFCSAEWPTLNVGWPRDGTFNLTTILQVKTRVFAPGPHGHPDQVP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1167936614   82 YIVTWEAIAYEPPPWVKPFVSPKLSP--SPTAPIL-PSGPSTQPPP 124
Cdd:pfam01140   81 YIVTWEALAADPPPWVRPFLTPKPPPpqPPAAPGLrPPLPPASAPP 126
RNase_HI_RT_Bel cd09273
Bel/Pao family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ...
 1178-1318 1.24e-55

Bel/Pao family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryote. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. Bel/Pao family has been described only in metazoan genomes. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.


:

Pssm-ID: 260005 [Multi-domain]  Cd Length: 131  Bit Score: 189.47  E-value: 1.24e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1178 TWYTDGSSFlqegqrKAGAAVTTETEVIWARALPAGTSAQRAELIALTQALKMAEGKRLNVYTDSRYAFATAHIHGEIYR 1257
Cdd:cd09273      1 TVFTDGSSF------KAGYAIVSGTEIVEAQPLPPGTSAQRAELIALIQALELAKGKPVNIYTDSAYAVHALHLLETIGI 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167936614 1258 RRGLLTSegreIKNKSEILALLKALFLPKRLSIIHCLGHQKGDSAEARGNRLADQAAREAA 1318
Cdd:cd09273     75 ERGFLKS----IKNLSLFLQLLEAVQRPKPVAIIHIRAHSKLPGPLAEGNAQADAAAKQAA 131
zf-H2C2 super family cl07828
H2C2 zinc finger; This domain binds to histone upstream activating sequence (UAS) elements ...
 1340-1434 1.40e-42

H2C2 zinc finger; This domain binds to histone upstream activating sequence (UAS) elements that are found in histone gene promoters.


The actual alignment was detected with superfamily member pfam16721:

Pssm-ID: 447530  Cd Length: 96  Bit Score: 151.03  E-value: 1.40e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1340 YFHYTETDLKKLRELGATYNQSKGYWVFQGKPVMPDQFVFELLDSLHRLTHLGYQKMKALLDRGESPYYMLNRDKTLQYV 1419
Cdd:pfam16721    2 HFHYTVTDIKDLTKLGAIYDKTKKYWVYQGKPVMPDQFTFELLDFLHQLTHLSFSKMKALLERSHSPYYMLNRDRTLKNI 81

                           90
                   ....*....|....*
gi 1167936614 1420 ADSCTVCAQVNASKA 1434
Cdd:pfam16721   82 TETCKACAQVNASKS 96
MLVIN_C pfam18697
Murine leukemia virus (MLV) integrase (IN) C-terminal domain; This is the C-terminal domain ...
 1654-1735 4.62e-39

Murine leukemia virus (MLV) integrase (IN) C-terminal domain; This is the C-terminal domain (CTD) which can be found in murine leukemia virus (MLV) integrase (IN) proteins. The MLV IN C-terminal domain interacts with the bromo and extraterminal (BET) proteins through the ET domain. This interaction provides a structural basis for global in vivo integration-site preferences andt disruption of this interaction through truncation mutations affects the global targeting profile of MLV. The CTD consists an SH3 fold followed by a long unstructured tail.


:

Pssm-ID: 436671  Cd Length: 83  Bit Score: 140.35  E-value: 4.62e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1654 HPFRVGDTVWVRRHQTKNLEPRWKGPYTVLLTTPTALKVDGIAAWIHAAHVKAATTPPAGTASGPTWKVQRS-QNPLKIR 1732
Cdd:pfam18697    1 HRYQPGDWVFVRRHQQKTLEPRWKGPYVVVLTTPTALKVDGIAAWVHYTHVRPADPHAVLEDFIPSWQVQKDrDNPLKLR 80


                   ...
gi 1167936614 1733 LTR 1735
Cdd:pfam18697   81 LRR 83
Gag_p12 pfam01141
Gag polyprotein, inner coat protein p12; The retroviral p12 is a virion structural protein. ...
 130-214 9.01e-39

Gag polyprotein, inner coat protein p12; The retroviral p12 is a virion structural protein. p12 is proline rich. The function carried out by p12 in assembly and replication is unknown. p12 is associated with pathogenicity of the virus.


:

Pssm-ID: 279483 [Multi-domain]  Cd Length: 85  Bit Score: 139.50  E-value: 9.01e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  130 PALTPSIKPRPSKPQVLSDNGGPLIDLLSEDPPPYGGQGLSSSDGDGDREEATSTSEIPAPSPIVSRLRGKRDPPAADST 209
Cdd:pfam01141    1 PALTPSIGAKPPKPQVLPDSGGPLIDLLTEDPPPYRDAQPPPSARDGNEEEAAPAGEAPDPSPMASRLRGRRDPPAADST 80


                   ....*
gi 1167936614  210 TSRAF 214
Cdd:pfam01141   81 TSQAF 85
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
 547-639 7.28e-28

Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026).


:

Pssm-ID: 425454  Cd Length: 101  Bit Score: 108.99  E-value: 7.28e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  547 PEPRITLTVGGQPVTFLVDTGAQHSVLTQNPGPLS----DRSAWVQGATGGKRYHWTTDRKVHLATGKVTH--SFLHVPD 620
Cdd:pfam00077    3 QRPLLTVKIGGKYFTALLDTGADDTVISQNDWPTNwpkqKATTNIQGIGGGINVRQSDQILILIGEDKFRGtvSPLILPT 82

                           90
                   ....*....|....*....
gi 1167936614  621 CPYPLLGRDLLTKLKAQIH 639
Cdd:pfam00077   83 CPVNIIGRDLLQQLGGRLT 101
rve pfam00665
Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into ...
 1447-1542 2.88e-24

Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain pfam02022. This domain is the central catalytic domain. The carboxyl terminal domain that is a non-specific DNA binding domain pfam00552. The catalytic domain acts as an endonuclease when two nucleotides are removed from the 3' ends of the blunt-ended viral DNA made by reverse transcription. This domain also catalyzes the DNA strand transfer reaction of the 3' ends of the viral DNA to the 5' ends of the integration site.


:

Pssm-ID: 459897 [Multi-domain]  Cd Length: 98  Bit Score: 98.54  E-value: 2.88e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1447 PGSHWEIDFTEVK-PGLYGYKYLLVFVDTFSGWVEAFPTKRETARVVSKKLLEEIF-PRFGMPRVLGSDNGPAFTSQVSQ 1524
Cdd:pfam00665    1 PNQLWQGDFTYIRiPGGGGKLYLLVIVDDFSREILAWALSSEMDAELVLDALERAIaFRGGVPLIIHSDNGSEYTSKAFR 80

                           90
                   ....*....|....*...
gi 1167936614 1525 SVADLLGIDWKLHCAYRP 1542
Cdd:pfam00665   81 EFLKDLGIKPSFSRPGNP 98
RT_RNaseH pfam17917
RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) ...
 1019-1124 4.24e-17

RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) activities allow reverse transcriptases to convert the single-stranded retroviral RNA genome into double-stranded DNA, which is integrated into the host chromosome during infection. This entry represents the RNase H like domain.


:

Pssm-ID: 465565  Cd Length: 104  Bit Score: 78.32  E-value: 4.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1019 DLTKPFELFVDEKqGYAKG-VLTQKL-GPWRRPVAYLSKKLDPVAAGWPPCLRMVAAIAVLTKDAGKLTMGQPLVILAPH 1096
Cdd:pfam17917    1 DPSKPFILETDAS-DYGIGaVLSQKDeDGKERPIAYASRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRKFTVYTDH 79

                           90       100
                   ....*....|....*....|....*...
gi 1167936614 1097 AVEALVKQPpdrWLSNARMTHYQAMLLD 1124
Cdd:pfam17917   80 KPLKYLFTP---KELNGRLARWALFLQE 104
ZnF_C2HC smart00343
zinc finger;
502-518 2.63e-04

zinc finger;


:

Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 39.73  E-value: 2.63e-04
                            10
                    ....*....|....*..
gi 1167936614   502 QCAYCKEKGHWARDCPK 518
Cdd:smart00343    1 KCYNCGKEGHIARDCPS 17
PTZ00368 super family cl31762
universal minicircle sequence binding protein (UMSBP); Provisional
 492-527 2.22e-03

universal minicircle sequence binding protein (UMSBP); Provisional


The actual alignment was detected with superfamily member PTZ00368:

Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 40.56  E-value: 2.22e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1167936614  492 ERRRPQLDKDQCAYCKEKGHWARDCPKKPRGPRGPR 527
Cdd:PTZ00368    95 NRAKGGAARRACYNCGGEGHISRDCPNAGKRPGGDK 130
 
Name Accession Description Interval E-value
Gag_p30 pfam02093
Gag P30 core shell protein; According to Swiss-Prot annotation this protein is the viral core ...
 225-432 6.46e-149

Gag P30 core shell protein; According to Swiss-Prot annotation this protein is the viral core shell protein. P30 is essential for viral assembly.


Pssm-ID: 426597  Cd Length: 208  Bit Score: 455.28  E-value: 6.46e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  225 QYWPFSSSDLYNWKNNNPSFSEDPGKLTASIESVLTTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLP 304
Cdd:pfam02093    1 QYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLVTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  305 NEVDAAFPLERPDWDYTTQRGRNHLVLYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPE 384
Cdd:pfam02093   81 NEVDAAFPLERPDWDYTTPAGRNHLVLYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPE 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1167936614  385 DPGQETNVSMSFIWQSAPDIGRKLERLEDLKSKTLGDLVREAERIFNK 432
Cdd:pfam02093  161 DPGQETNVSMSFIWQSAPDIGRKLERLEDLKSKTLGDLVREAEKIFNK 208
RT_ZFREV_like cd03715
RT_ZFREV_like: A subfamily of reverse transcriptases (RTs) found in sequences similar to the ...
 716-931 2.88e-117

RT_ZFREV_like: A subfamily of reverse transcriptases (RTs) found in sequences similar to the intact endogenous retrovirus ZFERV from zebrafish and to Moloney murine leukemia virus RT. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses. These elements can be divided into two major groups. One group contains retroviruses and DNA viruses whose propagation involves an RNA intermediate. They are grouped together with transposable elements containing long terminal repeats (LTRs). The other group, also called poly(A)-type retrotransposons, contain fungal mitochondrial introns and transposable elements that lack LTRs. Phylogenetic analysis suggests that ZFERV belongs to a distinct group of retroviruses.


Pssm-ID: 239685 [Multi-domain]  Cd Length: 210  Bit Score: 368.60  E-value: 2.88e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  716 PVSIKQYPMSHEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPGTNDYRPVQDLREVNKRVEDIHPTVPNPYNLLS 795
Cdd:cd03715      1 PVNQKQYPLPREAREGITPHIQELLEAGILVPCQSPWNTPILPVKKPGGNDYRMVQDLRLVNQAVLPIHPAVPNPYTLLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  796 GLPPSHRWYTVLDLKDAFFCLRLHPTSQPLFAFEWRDpgmgisGQLTWTRLPQGFKNSPTLFDEALHRDLADFRIQHPDL 875
Cdd:cd03715     81 LLPPKHQWYTVLDLANAFFSLPLAPDSQPLFAFEWEG------QQYTFTRLPQGFKNSPTLFHEALARDLAPFPLEHEGT 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1167936614  876 ILLQYVDDILLAATSELDCQQGTRALLLTLGNLGYRASAKKAQICQKQVKYLGYLL 931
Cdd:cd03715    155 ILLQYVDDLLLAADSEEDCLKGTDALLTHLGELGYKVSPKKAQICRAEVKFLGVVW 210
Gag_MA pfam01140
Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved ...
 2-124 4.55e-58

Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved in pathogenicity.


Pssm-ID: 426076 [Multi-domain]  Cd Length: 126  Bit Score: 196.45  E-value: 4.55e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614    2 GQTVTTPLSLTLEHWKDVQRIASNQSVDVKKRRWVTFCSAEWPTFGVGWPQDGTFNLDIILQVKSKVFSPGPHGHPDQVP 81
Cdd:pfam01140    1 GQTVTTPLSLTLGHWSDVPSRACNQSVDVKKRRWVTFCSAEWPTLNVGWPRDGTFNLTTILQVKTRVFAPGPHGHPDQVP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1167936614   82 YIVTWEAIAYEPPPWVKPFVSPKLSP--SPTAPIL-PSGPSTQPPP 124
Cdd:pfam01140   81 YIVTWEALAADPPPWVRPFLTPKPPPpqPPAAPGLrPPLPPASAPP 126
RNase_HI_RT_Bel cd09273
Bel/Pao family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ...
 1178-1318 1.24e-55

Bel/Pao family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryote. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. Bel/Pao family has been described only in metazoan genomes. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.


Pssm-ID: 260005 [Multi-domain]  Cd Length: 131  Bit Score: 189.47  E-value: 1.24e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1178 TWYTDGSSFlqegqrKAGAAVTTETEVIWARALPAGTSAQRAELIALTQALKMAEGKRLNVYTDSRYAFATAHIHGEIYR 1257
Cdd:cd09273      1 TVFTDGSSF------KAGYAIVSGTEIVEAQPLPPGTSAQRAELIALIQALELAKGKPVNIYTDSAYAVHALHLLETIGI 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167936614 1258 RRGLLTSegreIKNKSEILALLKALFLPKRLSIIHCLGHQKGDSAEARGNRLADQAAREAA 1318
Cdd:cd09273     75 ERGFLKS----IKNLSLFLQLLEAVQRPKPVAIIHIRAHSKLPGPLAEGNAQADAAAKQAA 131
zf-H3C2 pfam16721
Zinc-finger like, probable DNA-binding; This is a family of probably DNA-binding zinc-fingers ...
 1340-1434 1.40e-42

Zinc-finger like, probable DNA-binding; This is a family of probably DNA-binding zinc-fingers found on Gag-Pol polyproteins from mouse retroviruses. Added to clan to resolve overlaps with zf-H2C2, but neither are true members.


Pssm-ID: 293326  Cd Length: 96  Bit Score: 151.03  E-value: 1.40e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1340 YFHYTETDLKKLRELGATYNQSKGYWVFQGKPVMPDQFVFELLDSLHRLTHLGYQKMKALLDRGESPYYMLNRDKTLQYV 1419
Cdd:pfam16721    2 HFHYTVTDIKDLTKLGAIYDKTKKYWVYQGKPVMPDQFTFELLDFLHQLTHLSFSKMKALLERSHSPYYMLNRDRTLKNI 81

                           90
                   ....*....|....*
gi 1167936614 1420 ADSCTVCAQVNASKA 1434
Cdd:pfam16721   82 TETCKACAQVNASKS 96
MLVIN_C pfam18697
Murine leukemia virus (MLV) integrase (IN) C-terminal domain; This is the C-terminal domain ...
 1654-1735 4.62e-39

Murine leukemia virus (MLV) integrase (IN) C-terminal domain; This is the C-terminal domain (CTD) which can be found in murine leukemia virus (MLV) integrase (IN) proteins. The MLV IN C-terminal domain interacts with the bromo and extraterminal (BET) proteins through the ET domain. This interaction provides a structural basis for global in vivo integration-site preferences andt disruption of this interaction through truncation mutations affects the global targeting profile of MLV. The CTD consists an SH3 fold followed by a long unstructured tail.


Pssm-ID: 436671  Cd Length: 83  Bit Score: 140.35  E-value: 4.62e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1654 HPFRVGDTVWVRRHQTKNLEPRWKGPYTVLLTTPTALKVDGIAAWIHAAHVKAATTPPAGTASGPTWKVQRS-QNPLKIR 1732
Cdd:pfam18697    1 HRYQPGDWVFVRRHQQKTLEPRWKGPYVVVLTTPTALKVDGIAAWVHYTHVRPADPHAVLEDFIPSWQVQKDrDNPLKLR 80


                   ...
gi 1167936614 1733 LTR 1735
Cdd:pfam18697   81 LRR 83
Gag_p12 pfam01141
Gag polyprotein, inner coat protein p12; The retroviral p12 is a virion structural protein. ...
 130-214 9.01e-39

Gag polyprotein, inner coat protein p12; The retroviral p12 is a virion structural protein. p12 is proline rich. The function carried out by p12 in assembly and replication is unknown. p12 is associated with pathogenicity of the virus.


Pssm-ID: 279483 [Multi-domain]  Cd Length: 85  Bit Score: 139.50  E-value: 9.01e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  130 PALTPSIKPRPSKPQVLSDNGGPLIDLLSEDPPPYGGQGLSSSDGDGDREEATSTSEIPAPSPIVSRLRGKRDPPAADST 209
Cdd:pfam01141    1 PALTPSIGAKPPKPQVLPDSGGPLIDLLTEDPPPYRDAQPPPSARDGNEEEAAPAGEAPDPSPMASRLRGRRDPPAADST 80


                   ....*
gi 1167936614  210 TSRAF 214
Cdd:pfam01141   81 TSQAF 85
RNase_H pfam00075
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral ...
 1174-1319 8.11e-36

RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral replication cycle, and often found as a domain associated with reverse transcriptases. Structure is a mixed alpha+beta fold with three a/b/a layers.


Pssm-ID: 395028 [Multi-domain]  Cd Length: 141  Bit Score: 133.27  E-value: 8.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1174 DADHTWYTDGSSFLQEGQRKAGAAVTTETEvIWARALPAGTSAQRAELIALTQALK-MAEGKRLNVYTDSRYAFATAH-- 1250
Cdd:pfam00075    1 PKAVTVYTDGSCLGNPGPGGAGAVLYRGHE-NISAPLPGRTTNNRAELQAVIEALKaLKSPSKVNIYTDSQYVIGGITqw 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167936614 1251 IHGEIYRRRGlLTSEGREIKNKsEILALLKALFLPKRLSIIHCLGHqKGDSaearGNRLADQAAREAAI 1319
Cdd:pfam00075   80 VHGWKKNGWP-TTSEGKPVKNK-DLWQLLKALCKKHQVYWQWVKGH-AGNP----GNEMADRLAKQGAE 141
RVT_1 pfam00078
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually ...
 759-929 3.76e-33

Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. Reverse transcriptases occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses.


Pssm-ID: 395031 [Multi-domain]  Cd Length: 189  Bit Score: 127.42  E-value: 3.76e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  759 VKKPGTNDYRPV----QDLREVNKRVED-IHPTVPNPYNLlSGLPP------SHRWYTVLDLKDAFFCLRLHPTSQPLFA 827
Cdd:pfam00078    1 IPKKGKGKYRPIsllsIDYKALNKIIVKrLKPENLDSPPQ-PGFRPglaklkKAKWFLKLDLKKAFDQVPLDELDRKLTA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  828 F----EWRDP-GMGISGQLTWTRLPQGFKNSPTLFDEALHRDLADFRiQHPDLILLQYVDDILLAATSELDCQQGTRALL 902
Cdd:pfam00078   80 FttppININWnGELSGGRYEWKGLPQGLVLSPALFQLFMNELLRPLR-KRAGLTLVRYADDILIFSKSEEEHQEALEEVL 158

                          170       180
                   ....*....|....*....|....*....
gi 1167936614  903 LTLGNLGYRASAKKAQIC--QKQVKYLGY 929
Cdd:pfam00078  159 EWLKESGLKINPEKTQFFlkSKEVKYLGV 187
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
 547-639 7.28e-28

Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026).


Pssm-ID: 425454  Cd Length: 101  Bit Score: 108.99  E-value: 7.28e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  547 PEPRITLTVGGQPVTFLVDTGAQHSVLTQNPGPLS----DRSAWVQGATGGKRYHWTTDRKVHLATGKVTH--SFLHVPD 620
Cdd:pfam00077    3 QRPLLTVKIGGKYFTALLDTGADDTVISQNDWPTNwpkqKATTNIQGIGGGINVRQSDQILILIGEDKFRGtvSPLILPT 82

                           90
                   ....*....|....*....
gi 1167936614  621 CPYPLLGRDLLTKLKAQIH 639
Cdd:pfam00077   83 CPVNIIGRDLLQQLGGRLT 101
rve pfam00665
Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into ...
 1447-1542 2.88e-24

Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain pfam02022. This domain is the central catalytic domain. The carboxyl terminal domain that is a non-specific DNA binding domain pfam00552. The catalytic domain acts as an endonuclease when two nucleotides are removed from the 3' ends of the blunt-ended viral DNA made by reverse transcription. This domain also catalyzes the DNA strand transfer reaction of the 3' ends of the viral DNA to the 5' ends of the integration site.


Pssm-ID: 459897 [Multi-domain]  Cd Length: 98  Bit Score: 98.54  E-value: 2.88e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1447 PGSHWEIDFTEVK-PGLYGYKYLLVFVDTFSGWVEAFPTKRETARVVSKKLLEEIF-PRFGMPRVLGSDNGPAFTSQVSQ 1524
Cdd:pfam00665    1 PNQLWQGDFTYIRiPGGGGKLYLLVIVDDFSREILAWALSSEMDAELVLDALERAIaFRGGVPLIIHSDNGSEYTSKAFR 80

                           90
                   ....*....|....*...
gi 1167936614 1525 SVADLLGIDWKLHCAYRP 1542
Cdd:pfam00665   81 EFLKDLGIKPSFSRPGNP 98
RP_RTVL_H_like cd06095
Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family ...
 551-632 3.24e-23

Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family includes aspartate proteases from retroelements with LTR (long terminal repeats) including the RTVL_H family of human endogenous retrovirus-like elements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133159  Cd Length: 86  Bit Score: 95.09  E-value: 3.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  551 ITLTVGGQPVTFLVDTGAQHSVLTQNPGP---LSDRSAWVQGATGGKRYHWTTDRK-VHLATGKVTHSFLHVPDCPYPLL 626
Cdd:cd06095      1 VTITVEGVPIVFLVDTGATHSVLKSDLGPkqeLSTTSVLIRGVSGQSQQPVTTYRTlVDLGGHTVSHSFLVVPNCPDPLL 80


                   ....*.
gi 1167936614  627 GRDLLT 632
Cdd:cd06095     81 GRDLLS 86
RT_RNaseH pfam17917
RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) ...
 1019-1124 4.24e-17

RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) activities allow reverse transcriptases to convert the single-stranded retroviral RNA genome into double-stranded DNA, which is integrated into the host chromosome during infection. This entry represents the RNase H like domain.


Pssm-ID: 465565  Cd Length: 104  Bit Score: 78.32  E-value: 4.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1019 DLTKPFELFVDEKqGYAKG-VLTQKL-GPWRRPVAYLSKKLDPVAAGWPPCLRMVAAIAVLTKDAGKLTMGQPLVILAPH 1096
Cdd:pfam17917    1 DPSKPFILETDAS-DYGIGaVLSQKDeDGKERPIAYASRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRKFTVYTDH 79

                           90       100
                   ....*....|....*....|....*...
gi 1167936614 1097 AVEALVKQPpdrWLSNARMTHYQAMLLD 1124
Cdd:pfam17917   80 KPLKYLFTP---KELNGRLARWALFLQE 104
transpos_IS481 NF033577
IS481 family transposase; null
 1430-1595 7.27e-17

IS481 family transposase; null


Pssm-ID: 468094 [Multi-domain]  Cd Length: 283  Bit Score: 83.02  E-value: 7.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1430 NASKAKIGAGVRVRGHRPGSHWEIDFTEVKPGLY-GYKYLLVFVDTFSGWVEAFPTKRETARVVSKkLLEEIFPRFGMP- 1507
Cdd:NF033577   110 RALDRKTGKVKRYERAHPGELWHIDIKKLGRIPDvGRLYLHTAIDDHSRFAYAELYPDETAETAAD-FLRRAFAEHGIPi 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1508 -RVLgSDNGPAFTSQVS--QSVADLLGIDWKLHCAYRPQGSGQVERMNRTIKETLTKLTLAAGTRDWVLLLP--LALYra 1582
Cdd:NF033577   189 rRVL-TDNGSEFRSRAHgfELALAELGIEHRRTRPYHPQTNGKVERFHRTLKDEFAYARPYESLAELQAALDewLHHY-- 265

                          170
                   ....*....|....*..
gi 1167936614 1583 rNTPGPH----GLTPYE 1595
Cdd:NF033577   266 -NHHRPHsalgGKTPAE 281
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
1180-1318 3.68e-12

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 65.25  E-value: 3.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1180 YTDGSSFLQEGQRKAGAAVTTETEVIW-ARALPAGTSaQRAELIALTQALKMAE---GKRLNVYTDSRYAF--ATAHIHG 1253
Cdd:COG0328      6 YTDGACRGNPGPGGWGAVIRYGGEEKElSGGLGDTTN-NRAELTALIAALEALKelgPCEVEIYTDSQYVVnqITGWIHG 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167936614 1254 EiyRRRGLltsegREIKNKsEILALLKALFLPKRLSIIHCLGHQkGDsaeaRGNRLADQAAREAA 1318
Cdd:COG0328     85 W--KKNGW-----KPVKNP-DLWQRLDELLARHKVTFEWVKGHA-GH----PGNERADALANKAL 136
Tra5 COG2801
Transposase InsO and inactivated derivatives [Mobilome: prophages, transposons];
1348-1557 2.47e-08

Transposase InsO and inactivated derivatives [Mobilome: prophages, transposons];


Pssm-ID: 442053 [Multi-domain]  Cd Length: 309  Bit Score: 57.47  E-value: 2.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1348 LKKLRELGATYNQSKGYWVFQGKPVMPDQFVFELLDSLH-RLTHLGYQKMKALLDRGespYYMLNRDKTLQYVADSCTVC 1426
Cdd:COG2801     43 LRLLRRRRARSRRRRRLRRPRSYRADEDAELLERIKEIFaESPRYGYRRITAELRRE---GIAVNRKRVRRLMRELGLQA 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1427 AQVNASKAKIGAGVRVRGH--------RPGSHWEIDFTEVkPGLYGYKYLLVFVDTFS----GWVEAfptKRETARVVsK 1494
Cdd:COG2801    120 RRRRKKKYTTYSGHGGPIApnllftatAPNQVWVTDITYI-PTAEGWLYLAAVIDLFSreivGWSVS---DSMDAELV-V 194

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167936614 1495 KLLEEIFPRFG--MPRVLGSDNGPAFTSQVSQSVADLLGIDWKLHCAYRPQGSGQVERMNRTIKE 1557
Cdd:COG2801    195 DALEMAIERRGppKPLILHSDNGSQYTSKAYQELLKKLGITQSMSRPGNPQDNAFIESFFGTLKY 259
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
549-638 9.37e-07

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 50.33  E-value: 9.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  549 PRITLTVGGQPVTFLVDTGAQHSVLTQ--------NPGPLsDRSAWVQGATGGKRYHWTTDRKVHLATGKVTH---SFLH 617
Cdd:COG3577     42 FVVEGTINGQPVRFLVDTGASTVVLSEsdarrlglDPEDL-GRPVRVQTANGVVRAARVRLDSVRIGGITLRNvraVVLP 120

                           90       100
                   ....*....|....*....|.
gi 1167936614  618 VPDCPYPLLGRDLLTKLKAQI 638
Cdd:COG3577    121 GGELDDGLLGMSFLGRLDFEI 141
transpos_IS3 NF033516
IS3 family transposase;
1445-1556 1.45e-05

IS3 family transposase;


Pssm-ID: 468052 [Multi-domain]  Cd Length: 369  Bit Score: 49.49  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1445 HRPGSHWEIDFTEVKPGlYGYKYLLVFVDTFS----GWVeafPTKRETARVVSKkLLEEIFPRFGMPR--VLGSDNGPAF 1518
Cdd:NF033516   213 TRPNQVWVTDITYIRTA-EGWLYLAVVLDLFSreivGWS---VSTSMSAELVLD-ALEMAIEWRGKPEglILHSDNGSQY 287

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1167936614 1519 TSQVSQSVADLLGIDWKLHCAYRPQGSGQVERMNRTIK 1556
Cdd:NF033516   288 TSKAYREWLKEHGITQSMSRPGNCWDNAVAESFFGTLK 325
Tra8 COG2826
Transposase and inactivated derivatives, IS30 family [Mobilome: prophages, transposons];
1446-1561 1.61e-05

Transposase and inactivated derivatives, IS30 family [Mobilome: prophages, transposons];


Pssm-ID: 442074 [Multi-domain]  Cd Length: 325  Bit Score: 49.11  E-value: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1446 RPGsHWEIDfteVKPGLYGYKYLLVFVDTFSGWVEAFPTKRETARVVSKKL--LEEIFPRFgMPRVLGSDNGPAFT--SQ 1521
Cdd:COG2826    171 EPG-HWEGD---LIIGKRGKSALLTLVERKSRFVILLKLPDKTAESVADALirLLRKLPAF-LRKSITTDNGKEFAdhKE 245

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1167936614 1522 VSQSvadlLGID-WKLHcAYRPQGSGQVERMNRTIKETLTK 1561
Cdd:COG2826    246 IEAA----LGIKvYFAD-PYSPWQRGTNENTNGLLRQYFPK 281
transpos_ISNCY_2 NF033594
ISNCY family transposase; The ISNCY insertion sequence family, as defined by ISFinder, encodes ...
 1467-1561 1.36e-04

ISNCY family transposase; The ISNCY insertion sequence family, as defined by ISFinder, encodes several apparently unrelated families of transposases. Members of this family resemble the transposases of ISNCY family elements such as IS1202, ISTde1, ISKpn21, and ISCARN1.


Pssm-ID: 468103 [Multi-domain]  Cd Length: 367  Bit Score: 46.32  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1467 YLLVFVD--TfSGWVEAFPTKRETA----RVvskklLEEIFPRFGMPRVLGSDNGPAFTSQVSQSVADL----------- 1529
Cdd:NF033594   148 TLLVAIDdaT-GRLMGLRFVESESTfgyfEV-----TRQYLEKHGKPVAFYSDKHSVFRVNEEELAGKGdgltqfgralk 221

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1167936614 1530 -LGIDWKlhCAYRPQGSGQVERMNRTIKETLTK 1561
Cdd:NF033594   222 eLGIEII--CANSPQAKGRVERANQTLQDRLVK 252
ZnF_C2HC smart00343
zinc finger;
502-518 2.63e-04

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 39.73  E-value: 2.63e-04
                            10
                    ....*....|....*..
gi 1167936614   502 QCAYCKEKGHWARDCPK 518
Cdd:smart00343    1 KCYNCGKEGHIARDCPS 17
PHA03247 PHA03247
large tegument protein UL36; Provisional
 71-215 7.61e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 7.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614   71 PGPHGHPDQVPYIVTWEAIAYE----PPPWVKPFVSPklsPSPTAPILPSGPSTQPPPRSALYPALTPSIKPRPSKPQVL 146
Cdd:PHA03247  2525 VGEPVHPRMLTWIRGLEELASDdagdPPPPLPPAAPP---AAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAP 2601

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  147 SDNGGPLI----------DLLSEDPPPYGGQGLSSSDGDGDrEEATSTSEIPAPSPIVSRLRGKR------DPPAADSTT 210
Cdd:PHA03247  2602 VDDRGDPRgpappsplppDTHAPDPPPPSPSPAANEPDPHP-PPTVPPPERPRDDPAPGRVSRPRrarrlgRAAQASSPP 2680


                   ....*
gi 1167936614  211 SRAFP 215
Cdd:PHA03247  2681 QRPRR 2685
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 501-518 1.15e-03

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 37.89  E-value: 1.15e-03
                           10
                   ....*....|....*...
gi 1167936614  501 DQCAYCKEKGHWARDCPK 518
Cdd:pfam00098    1 GKCYNCGEPGHIARDCPK 18
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 492-527 2.22e-03

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 40.56  E-value: 2.22e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1167936614  492 ERRRPQLDKDQCAYCKEKGHWARDCPKKPRGPRGPR 527
Cdd:PTZ00368    95 NRAKGGAARRACYNCGGEGHISRDCPNAGKRPGGDK 130
rnhA PRK00203
ribonuclease H; Reviewed
 1212-1320 9.74e-03

ribonuclease H; Reviewed


Pssm-ID: 178927 [Multi-domain]  Cd Length: 150  Bit Score: 38.65  E-value: 9.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1212 AGTSAQRAELIALTQALKM-AEGKRLNVYTDSRY---AFaTAHIHGeiYRRRGLLTSEGREIKNKSEILALLKALflpKR 1287
Cdd:PRK00203    39 ALTTNNRMELMAAIEALEAlKEPCEVTLYTDSQYvrqGI-TEWIHG--WKKNGWKTADKKPVKNVDLWQRLDAAL---KR 112

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1167936614 1288 lsiihclgHQ------KGDSAEArGNRLADQAAREAAIK 1320
Cdd:PRK00203   113 --------HQikwhwvKGHAGHP-ENERCDELARAGAEE 142
 
Name Accession Description Interval E-value
Gag_p30 pfam02093
Gag P30 core shell protein; According to Swiss-Prot annotation this protein is the viral core ...
 225-432 6.46e-149

Gag P30 core shell protein; According to Swiss-Prot annotation this protein is the viral core shell protein. P30 is essential for viral assembly.


Pssm-ID: 426597  Cd Length: 208  Bit Score: 455.28  E-value: 6.46e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  225 QYWPFSSSDLYNWKNNNPSFSEDPGKLTASIESVLTTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLP 304
Cdd:pfam02093    1 QYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLVTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  305 NEVDAAFPLERPDWDYTTQRGRNHLVLYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPE 384
Cdd:pfam02093   81 NEVDAAFPLERPDWDYTTPAGRNHLVLYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPE 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1167936614  385 DPGQETNVSMSFIWQSAPDIGRKLERLEDLKSKTLGDLVREAERIFNK 432
Cdd:pfam02093  161 DPGQETNVSMSFIWQSAPDIGRKLERLEDLKSKTLGDLVREAEKIFNK 208
RT_ZFREV_like cd03715
RT_ZFREV_like: A subfamily of reverse transcriptases (RTs) found in sequences similar to the ...
 716-931 2.88e-117

RT_ZFREV_like: A subfamily of reverse transcriptases (RTs) found in sequences similar to the intact endogenous retrovirus ZFERV from zebrafish and to Moloney murine leukemia virus RT. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses. These elements can be divided into two major groups. One group contains retroviruses and DNA viruses whose propagation involves an RNA intermediate. They are grouped together with transposable elements containing long terminal repeats (LTRs). The other group, also called poly(A)-type retrotransposons, contain fungal mitochondrial introns and transposable elements that lack LTRs. Phylogenetic analysis suggests that ZFERV belongs to a distinct group of retroviruses.


Pssm-ID: 239685 [Multi-domain]  Cd Length: 210  Bit Score: 368.60  E-value: 2.88e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  716 PVSIKQYPMSHEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPGTNDYRPVQDLREVNKRVEDIHPTVPNPYNLLS 795
Cdd:cd03715      1 PVNQKQYPLPREAREGITPHIQELLEAGILVPCQSPWNTPILPVKKPGGNDYRMVQDLRLVNQAVLPIHPAVPNPYTLLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  796 GLPPSHRWYTVLDLKDAFFCLRLHPTSQPLFAFEWRDpgmgisGQLTWTRLPQGFKNSPTLFDEALHRDLADFRIQHPDL 875
Cdd:cd03715     81 LLPPKHQWYTVLDLANAFFSLPLAPDSQPLFAFEWEG------QQYTFTRLPQGFKNSPTLFHEALARDLAPFPLEHEGT 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1167936614  876 ILLQYVDDILLAATSELDCQQGTRALLLTLGNLGYRASAKKAQICQKQVKYLGYLL 931
Cdd:cd03715    155 ILLQYVDDLLLAADSEEDCLKGTDALLTHLGELGYKVSPKKAQICRAEVKFLGVVW 210
Gag_MA pfam01140
Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved ...
 2-124 4.55e-58

Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved in pathogenicity.


Pssm-ID: 426076 [Multi-domain]  Cd Length: 126  Bit Score: 196.45  E-value: 4.55e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614    2 GQTVTTPLSLTLEHWKDVQRIASNQSVDVKKRRWVTFCSAEWPTFGVGWPQDGTFNLDIILQVKSKVFSPGPHGHPDQVP 81
Cdd:pfam01140    1 GQTVTTPLSLTLGHWSDVPSRACNQSVDVKKRRWVTFCSAEWPTLNVGWPRDGTFNLTTILQVKTRVFAPGPHGHPDQVP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1167936614   82 YIVTWEAIAYEPPPWVKPFVSPKLSP--SPTAPIL-PSGPSTQPPP 124
Cdd:pfam01140   81 YIVTWEALAADPPPWVRPFLTPKPPPpqPPAAPGLrPPLPPASAPP 126
RNase_HI_RT_Bel cd09273
Bel/Pao family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ...
 1178-1318 1.24e-55

Bel/Pao family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryote. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. Bel/Pao family has been described only in metazoan genomes. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.


Pssm-ID: 260005 [Multi-domain]  Cd Length: 131  Bit Score: 189.47  E-value: 1.24e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1178 TWYTDGSSFlqegqrKAGAAVTTETEVIWARALPAGTSAQRAELIALTQALKMAEGKRLNVYTDSRYAFATAHIHGEIYR 1257
Cdd:cd09273      1 TVFTDGSSF------KAGYAIVSGTEIVEAQPLPPGTSAQRAELIALIQALELAKGKPVNIYTDSAYAVHALHLLETIGI 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167936614 1258 RRGLLTSegreIKNKSEILALLKALFLPKRLSIIHCLGHQKGDSAEARGNRLADQAAREAA 1318
Cdd:cd09273     75 ERGFLKS----IKNLSLFLQLLEAVQRPKPVAIIHIRAHSKLPGPLAEGNAQADAAAKQAA 131
zf-H3C2 pfam16721
Zinc-finger like, probable DNA-binding; This is a family of probably DNA-binding zinc-fingers ...
 1340-1434 1.40e-42

Zinc-finger like, probable DNA-binding; This is a family of probably DNA-binding zinc-fingers found on Gag-Pol polyproteins from mouse retroviruses. Added to clan to resolve overlaps with zf-H2C2, but neither are true members.


Pssm-ID: 293326  Cd Length: 96  Bit Score: 151.03  E-value: 1.40e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1340 YFHYTETDLKKLRELGATYNQSKGYWVFQGKPVMPDQFVFELLDSLHRLTHLGYQKMKALLDRGESPYYMLNRDKTLQYV 1419
Cdd:pfam16721    2 HFHYTVTDIKDLTKLGAIYDKTKKYWVYQGKPVMPDQFTFELLDFLHQLTHLSFSKMKALLERSHSPYYMLNRDRTLKNI 81

                           90
                   ....*....|....*
gi 1167936614 1420 ADSCTVCAQVNASKA 1434
Cdd:pfam16721   82 TETCKACAQVNASKS 96
RT_Rtv cd01645
RT_Rtv: Reverse transcriptases (RTs) from retroviruses (Rtvs). RTs catalyze the conversion of ...
 716-931 1.54e-42

RT_Rtv: Reverse transcriptases (RTs) from retroviruses (Rtvs). RTs catalyze the conversion of single-stranded RNA into double-stranded viral DNA for integration into host chromosomes. Proteins in this subfamily contain long terminal repeats (LTRs) and are multifunctional enzymes with RNA-directed DNA polymerase, DNA directed DNA polymerase, and ribonuclease hybrid (RNase H) activities. The viral RNA genome enters the cytoplasm as part of a nucleoprotein complex, and the process of reverse transcription generates in the cytoplasm forming a linear DNA duplex via an intricate series of steps. This duplex DNA is colinear with its RNA template, but contains terminal duplications known as LTRs that are not present in viral RNA. It has been proposed that two specialized template switches, known as strand-transfer reactions or "jumps", are required to generate the LTRs.


Pssm-ID: 238823 [Multi-domain]  Cd Length: 213  Bit Score: 155.13  E-value: 1.54e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  716 PVSIKQYPMSHEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPgTNDYRPVQDLREVNKRVED---IHPTVPNPyn 792
Cdd:cd01645      1 PVWIKQWPLTEEKLEALTELVTEQLKEGHIEPSTSPWNTPVFVIKKK-SGKWRLLHDLRAVNAQTQDmgaLQPGLPHP-- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  793 llSGLPpsHRWY-TVLDLKDAFFCLRLHPTSQPLFAFEWrdPGMGISG---QLTWTRLPQGFKNSPTLFDEALHRDLADF 868
Cdd:cd01645     78 --AALP--KGWPlIVLDLKDCFFSIPLHPDDRERFAFTV--PSINNKGpakRYQWKVLPQGMKNSPTICQSFVAQALEPF 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167936614  869 RIQHPDLILLQYVDDILLAATSELDCQQGTRALLLTLGNLGYRASAKKAQIcQKQVKYLGYLL 931
Cdd:cd01645    152 RKQYPDIVIYHYMDDILIASDLEGQLREIYEELRQTLLRWGLTIPPEKVQK-EPPFQYLGYEL 213
MLVIN_C pfam18697
Murine leukemia virus (MLV) integrase (IN) C-terminal domain; This is the C-terminal domain ...
 1654-1735 4.62e-39

Murine leukemia virus (MLV) integrase (IN) C-terminal domain; This is the C-terminal domain (CTD) which can be found in murine leukemia virus (MLV) integrase (IN) proteins. The MLV IN C-terminal domain interacts with the bromo and extraterminal (BET) proteins through the ET domain. This interaction provides a structural basis for global in vivo integration-site preferences andt disruption of this interaction through truncation mutations affects the global targeting profile of MLV. The CTD consists an SH3 fold followed by a long unstructured tail.


Pssm-ID: 436671  Cd Length: 83  Bit Score: 140.35  E-value: 4.62e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1654 HPFRVGDTVWVRRHQTKNLEPRWKGPYTVLLTTPTALKVDGIAAWIHAAHVKAATTPPAGTASGPTWKVQRS-QNPLKIR 1732
Cdd:pfam18697    1 HRYQPGDWVFVRRHQQKTLEPRWKGPYVVVLTTPTALKVDGIAAWVHYTHVRPADPHAVLEDFIPSWQVQKDrDNPLKLR 80


                   ...
gi 1167936614 1733 LTR 1735
Cdd:pfam18697   81 LRR 83
Gag_p12 pfam01141
Gag polyprotein, inner coat protein p12; The retroviral p12 is a virion structural protein. ...
 130-214 9.01e-39

Gag polyprotein, inner coat protein p12; The retroviral p12 is a virion structural protein. p12 is proline rich. The function carried out by p12 in assembly and replication is unknown. p12 is associated with pathogenicity of the virus.


Pssm-ID: 279483 [Multi-domain]  Cd Length: 85  Bit Score: 139.50  E-value: 9.01e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  130 PALTPSIKPRPSKPQVLSDNGGPLIDLLSEDPPPYGGQGLSSSDGDGDREEATSTSEIPAPSPIVSRLRGKRDPPAADST 209
Cdd:pfam01141    1 PALTPSIGAKPPKPQVLPDSGGPLIDLLTEDPPPYRDAQPPPSARDGNEEEAAPAGEAPDPSPMASRLRGRRDPPAADST 80


                   ....*
gi 1167936614  210 TSRAF 214
Cdd:pfam01141   81 TSQAF 85
RNase_H pfam00075
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral ...
 1174-1319 8.11e-36

RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral replication cycle, and often found as a domain associated with reverse transcriptases. Structure is a mixed alpha+beta fold with three a/b/a layers.


Pssm-ID: 395028 [Multi-domain]  Cd Length: 141  Bit Score: 133.27  E-value: 8.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1174 DADHTWYTDGSSFLQEGQRKAGAAVTTETEvIWARALPAGTSAQRAELIALTQALK-MAEGKRLNVYTDSRYAFATAH-- 1250
Cdd:pfam00075    1 PKAVTVYTDGSCLGNPGPGGAGAVLYRGHE-NISAPLPGRTTNNRAELQAVIEALKaLKSPSKVNIYTDSQYVIGGITqw 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167936614 1251 IHGEIYRRRGlLTSEGREIKNKsEILALLKALFLPKRLSIIHCLGHqKGDSaearGNRLADQAAREAAI 1319
Cdd:pfam00075   80 VHGWKKNGWP-TTSEGKPVKNK-DLWQLLKALCKKHQVYWQWVKGH-AGNP----GNEMADRLAKQGAE 141
RT_LTR cd01647
RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long ...
 743-930 1.29e-34

RT_LTR: Reverse transcriptases (RTs) from retrotransposons and retroviruses which have long terminal repeats (LTRs) in their DNA copies but not in their RNA template. RT catalyzes DNA replication from an RNA template, and is responsible for the replication of retroelements. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs are present in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and Caulimoviruses.


Pssm-ID: 238825  Cd Length: 177  Bit Score: 131.18  E-value: 1.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  743 GILVPCQSPWNTPLLPVKKPGtNDYRPVQDLREVNKRVE-DIHPtVPNPYNLLSGLPPsHRWYTVLDLKDAFFCLRLHPT 821
Cdd:cd01647      1 GIIEPSSSPYASPVVVVKKKD-GKLRLCVDYRKLNKVTIkDRYP-LPTIDELLEELAG-AKVFSKLDLRSGYHQIPLAEE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  822 SQPLFAFewRDPGmgisGQLTWTRLPQGFKNSPTLF----DEALHRDLADFriqhpdliLLQYVDDILLAATSELDCQQG 897
Cdd:cd01647     78 SRPKTAF--RTPF----GLYEYTRMPFGLKNAPATFqrlmNKILGDLLGDF--------VEVYLDDILVYSKTEEEHLEH 143

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1167936614  898 TRALLLTLGNLGYRASAKKAQICQKQVKYLGYL 930
Cdd:cd01647    144 LREVLERLREAGLKLNPEKCEFGVPEVEFLGHI 176
RVT_1 pfam00078
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually ...
 759-929 3.76e-33

Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. Reverse transcriptases occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses.


Pssm-ID: 395031 [Multi-domain]  Cd Length: 189  Bit Score: 127.42  E-value: 3.76e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  759 VKKPGTNDYRPV----QDLREVNKRVED-IHPTVPNPYNLlSGLPP------SHRWYTVLDLKDAFFCLRLHPTSQPLFA 827
Cdd:pfam00078    1 IPKKGKGKYRPIsllsIDYKALNKIIVKrLKPENLDSPPQ-PGFRPglaklkKAKWFLKLDLKKAFDQVPLDELDRKLTA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  828 F----EWRDP-GMGISGQLTWTRLPQGFKNSPTLFDEALHRDLADFRiQHPDLILLQYVDDILLAATSELDCQQGTRALL 902
Cdd:pfam00078   80 FttppININWnGELSGGRYEWKGLPQGLVLSPALFQLFMNELLRPLR-KRAGLTLVRYADDILIFSKSEEEHQEALEEVL 158

                          170       180
                   ....*....|....*....|....*....
gi 1167936614  903 LTLGNLGYRASAKKAQIC--QKQVKYLGY 929
Cdd:pfam00078  159 EWLKESGLKINPEKTQFFlkSKEVKYLGV 187
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
 547-639 7.28e-28

Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026).


Pssm-ID: 425454  Cd Length: 101  Bit Score: 108.99  E-value: 7.28e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  547 PEPRITLTVGGQPVTFLVDTGAQHSVLTQNPGPLS----DRSAWVQGATGGKRYHWTTDRKVHLATGKVTH--SFLHVPD 620
Cdd:pfam00077    3 QRPLLTVKIGGKYFTALLDTGADDTVISQNDWPTNwpkqKATTNIQGIGGGINVRQSDQILILIGEDKFRGtvSPLILPT 82

                           90
                   ....*....|....*....
gi 1167936614  621 CPYPLLGRDLLTKLKAQIH 639
Cdd:pfam00077   83 CPVNIIGRDLLQQLGGRLT 101
rve pfam00665
Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into ...
 1447-1542 2.88e-24

Integrase core domain; Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain pfam02022. This domain is the central catalytic domain. The carboxyl terminal domain that is a non-specific DNA binding domain pfam00552. The catalytic domain acts as an endonuclease when two nucleotides are removed from the 3' ends of the blunt-ended viral DNA made by reverse transcription. This domain also catalyzes the DNA strand transfer reaction of the 3' ends of the viral DNA to the 5' ends of the integration site.


Pssm-ID: 459897 [Multi-domain]  Cd Length: 98  Bit Score: 98.54  E-value: 2.88e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1447 PGSHWEIDFTEVK-PGLYGYKYLLVFVDTFSGWVEAFPTKRETARVVSKKLLEEIF-PRFGMPRVLGSDNGPAFTSQVSQ 1524
Cdd:pfam00665    1 PNQLWQGDFTYIRiPGGGGKLYLLVIVDDFSREILAWALSSEMDAELVLDALERAIaFRGGVPLIIHSDNGSEYTSKAFR 80

                           90
                   ....*....|....*...
gi 1167936614 1525 SVADLLGIDWKLHCAYRP 1542
Cdd:pfam00665   81 EFLKDLGIKPSFSRPGNP 98
RP_RTVL_H_like cd06095
Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family ...
 551-632 3.24e-23

Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family includes aspartate proteases from retroelements with LTR (long terminal repeats) including the RTVL_H family of human endogenous retrovirus-like elements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133159  Cd Length: 86  Bit Score: 95.09  E-value: 3.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  551 ITLTVGGQPVTFLVDTGAQHSVLTQNPGP---LSDRSAWVQGATGGKRYHWTTDRK-VHLATGKVTHSFLHVPDCPYPLL 626
Cdd:cd06095      1 VTITVEGVPIVFLVDTGATHSVLKSDLGPkqeLSTTSVLIRGVSGQSQQPVTTYRTlVDLGGHTVSHSFLVVPNCPDPLL 80


                   ....*.
gi 1167936614  627 GRDLLT 632
Cdd:cd06095     81 GRDLLS 86
RNase_HI_eukaryote_like cd09280
Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic ...
 1180-1318 2.09e-17

Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic counterparts; Ribonuclease H (RNase H) is classified into two families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. RNase H is widely present in various organisms, including bacteria, archaea and eukaryote and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. Eukaryotic RNase H is longer and more complex than in prokaryotes. Almost all eukaryotic RNase HI have highly conserved regions at their N-termini called hybrid binding domain (HBD). It is speculated that the HBD contributes to binding the RNA/DNA hybrid. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability, but RNase H is essential in higher eukaryotes. RNase H knockout mice lack mitochondrial DNA replication and die as embryos.


Pssm-ID: 260012 [Multi-domain]  Cd Length: 145  Bit Score: 80.69  E-value: 2.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1180 YTDGSsFLQEGQR--KAGAAVtteteviW---------ARALP--AGTSaQRAELIALTQALKMA---EGKRLNVYTDSR 1243
Cdd:cd09280      3 YTDGS-CLNNGKPgaRAGIGV-------YfgpgdprnvSEPLPgrKQTN-NRAELLAVIHALEQApeeGIRKLEIRTDSK 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167936614 1244 YAFATAHIHGEIYRRRGLLTSEGREIKNKSEILALLKAL-FLPKRLSIIHCLGHQkGDsaeaRGNRLADQAAREAA 1318
Cdd:cd09280     74 YAINCITKWIPKWKKNGWKTSKGKPVKNQDLIKELDKLLrKRGIKVKFEHVKGHS-GD----PGNEEADRLAREGA 144
RT_like cd00304
RT_like: Reverse transcriptase (RT, RNA-dependent DNA polymerase)_like family. An RT gene is ...
 845-931 4.20e-17

RT_like: Reverse transcriptase (RT, RNA-dependent DNA polymerase)_like family. An RT gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. RTs occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses. These elements can be divided into two major groups. One group contains retroviruses and DNA viruses whose propagation involves an RNA intermediate. They are grouped together with transposable elements containing long terminal repeats (LTRs). The other group, also called poly(A)-type retrotransposons, contain fungal mitochondrial introns and transposable elements that lack LTRs.


Pssm-ID: 238185 [Multi-domain]  Cd Length: 98  Bit Score: 78.16  E-value: 4.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  845 RLPQGFKNSPTLFDEALHRDLADFRIQHPDLILLQYVDDILLAATSElDCQQGTRALLLTLGNLGYRASAKKAQ--ICQK 922
Cdd:cd00304     11 PLPQGSPLSPALANLYMEKLEAPILKQLLDITLIRYVDDLVVIAKSE-QQAVKKRELEEFLARLGLNLSDEKTQftEKEK 89


                   ....*....
gi 1167936614  923 QVKYLGYLL 931
Cdd:cd00304     90 KFKFLGILV 98
RT_RNaseH pfam17917
RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) ...
 1019-1124 4.24e-17

RNase H-like domain found in reverse transcriptase; DNA polymerase and ribonuclease H (RNase H) activities allow reverse transcriptases to convert the single-stranded retroviral RNA genome into double-stranded DNA, which is integrated into the host chromosome during infection. This entry represents the RNase H like domain.


Pssm-ID: 465565  Cd Length: 104  Bit Score: 78.32  E-value: 4.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1019 DLTKPFELFVDEKqGYAKG-VLTQKL-GPWRRPVAYLSKKLDPVAAGWPPCLRMVAAIAVLTKDAGKLTMGQPLVILAPH 1096
Cdd:pfam17917    1 DPSKPFILETDAS-DYGIGaVLSQKDeDGKERPIAYASRKLTPAERNYSTTEKELLAIVWALKKFRHYLLGRKFTVYTDH 79

                           90       100
                   ....*....|....*....|....*...
gi 1167936614 1097 AVEALVKQPpdrWLSNARMTHYQAMLLD 1124
Cdd:pfam17917   80 KPLKYLFTP---KELNGRLARWALFLQE 104
transpos_IS481 NF033577
IS481 family transposase; null
 1430-1595 7.27e-17

IS481 family transposase; null


Pssm-ID: 468094 [Multi-domain]  Cd Length: 283  Bit Score: 83.02  E-value: 7.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1430 NASKAKIGAGVRVRGHRPGSHWEIDFTEVKPGLY-GYKYLLVFVDTFSGWVEAFPTKRETARVVSKkLLEEIFPRFGMP- 1507
Cdd:NF033577   110 RALDRKTGKVKRYERAHPGELWHIDIKKLGRIPDvGRLYLHTAIDDHSRFAYAELYPDETAETAAD-FLRRAFAEHGIPi 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1508 -RVLgSDNGPAFTSQVS--QSVADLLGIDWKLHCAYRPQGSGQVERMNRTIKETLTKLTLAAGTRDWVLLLP--LALYra 1582
Cdd:NF033577   189 rRVL-TDNGSEFRSRAHgfELALAELGIEHRRTRPYHPQTNGKVERFHRTLKDEFAYARPYESLAELQAALDewLHHY-- 265

                          170
                   ....*....|....*..
gi 1167936614 1583 rNTPGPH----GLTPYE 1595
Cdd:NF033577   266 -NHHRPHsalgGKTPAE 281
RT_RNaseH_2 pfam17919
RNase H-like domain found in reverse transcriptase;
994-1074 2.11e-16

RNase H-like domain found in reverse transcriptase;


Pssm-ID: 465567 [Multi-domain]  Cd Length: 100  Bit Score: 76.38  E-value: 2.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  994 WGPDQQKAYQEIKQALLTAPALGLPDLTKPFELFVD-EKQGYAkGVLTQKL--GPWrRPVAYLSKKLDPVAAGWPPCLRM 1070
Cdd:pfam17919    1 WTEECQKAFEKLKQALTSAPVLAHPDPDKPFILETDaSDYGIG-AVLSQEDddGGE-RPIAYASRKLSPAERNYSTTEKE 78


                   ....
gi 1167936614 1071 VAAI 1074
Cdd:pfam17919   79 LLAI 82
RNase_H_like cd06222
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ...
 1179-1315 1.05e-13

Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of spliceosomal protein Prp8; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as anti-HIV drug targets since RNase H inactivation inhibits reverse transcription. This model also includes the Prp8 domain IV, which adopts the RNase fold but shows low sequence homology; domain IV is implicated in key spliceosomal interactions.


Pssm-ID: 259998 [Multi-domain]  Cd Length: 121  Bit Score: 69.27  E-value: 1.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1179 WYTDGSSFLQEGQRKAGAAVT-TETEVIWARALPAGT-SAQRAELIALTQALKMA---EGKRLNVYTDSRYAFATahIHG 1253
Cdd:cd06222      1 INVDGSCRGNPGPAGIGGVLRdHEGGWLGGFALKIGApTALEAELLALLLALELAldlGYLKVIIESDSKYVVDL--INS 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167936614 1254 EIYRRrglltsegreIKNKSEILALLKALFLPKRLSIIHCLGHqkgdsaearGNRLADQAAR 1315
Cdd:cd06222     79 GSFKW----------SPNILLIEDILLLLSRFWSVKISHVPRE---------GNQVADALAK 121
RNase_HI_prokaryote_like cd09278
RNase HI family found mainly in prokaryotes; Ribonuclease H (RNase H) is classified into two ...
 1180-1318 4.51e-13

RNase HI family found mainly in prokaryotes; Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD), residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Prokaryotic RNase H varies greatly in domain structures and substrate specificities. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability.


Pssm-ID: 260010 [Multi-domain]  Cd Length: 139  Bit Score: 67.89  E-value: 4.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1180 YTDGSSFLQEGqrKAG--AAVTTETEVIWARALPAGTSAQRAELIALTQALKMA-EGKRLNVYTDSRYAF--ATAHIHGe 1254
Cdd:cd09278      5 YTDGACLGNPG--PGGwaAVIRYGDHEKELSGGEPGTTNNRMELTAAIEALEALkEPCPVTIYTDSQYVIngITKWIKG- 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167936614 1255 iYRRRGLLTSEGREIKNKSEILALLKALfLPKRLSIIHCLGHQkGDsaeaRGNRLADQAAREAA 1318
Cdd:cd09278     82 -WKKNGWKTADGKPVKNRDLWQELDALL-AGHKVTWEWVKGHA-GH----PGNERADRLANKAA 138
zf-H2C2 pfam09337
H2C2 zinc finger; This domain binds to histone upstream activating sequence (UAS) elements ...
 1386-1427 1.42e-12

H2C2 zinc finger; This domain binds to histone upstream activating sequence (UAS) elements that are found in histone gene promoters.


Pssm-ID: 430537  Cd Length: 39  Bit Score: 63.50  E-value: 1.42e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1167936614 1386 HRLTHLGYQKMKALLDRGespYYMLNRDKTLQYVADSCTVCA 1427
Cdd:pfam09337    1 HALTHLGINKLTALLARK---YHWLGIKETVSEVISSCVACQ 39
RnhA COG0328
Ribonuclease HI [Replication, recombination and repair];
1180-1318 3.68e-12

Ribonuclease HI [Replication, recombination and repair];


Pssm-ID: 440097 [Multi-domain]  Cd Length: 136  Bit Score: 65.25  E-value: 3.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1180 YTDGSSFLQEGQRKAGAAVTTETEVIW-ARALPAGTSaQRAELIALTQALKMAE---GKRLNVYTDSRYAF--ATAHIHG 1253
Cdd:COG0328      6 YTDGACRGNPGPGGWGAVIRYGGEEKElSGGLGDTTN-NRAELTALIAALEALKelgPCEVEIYTDSQYVVnqITGWIHG 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167936614 1254 EiyRRRGLltsegREIKNKsEILALLKALFLPKRLSIIHCLGHQkGDsaeaRGNRLADQAAREAA 1318
Cdd:COG0328     85 W--KKNGW-----KPVKNP-DLWQRLDELLARHKVTFEWVKGHA-GH----PGNERADALANKAL 136
RT_DIRS1 cd03714
RT_DIRS1: Reverse transcriptases (RTs) occurring in the DIRS1 group of retransposons. Members ...
 807-928 7.59e-11

RT_DIRS1: Reverse transcriptases (RTs) occurring in the DIRS1 group of retransposons. Members of the subfamily include the Dictyostelium DIRS-1, Volvox carteri kangaroo, and Panagrellus redivivus PAT elements. These elements differ from LTR and conventional non-LTR retrotransposons. They contain split direct repeat (SDR) termini, and have been proposed to integrate via double-stranded closed-circle DNA intermediates assisted by an encoded recombinase which is similar to gamma-site-specific integrase.


Pssm-ID: 239684 [Multi-domain]  Cd Length: 119  Bit Score: 61.21  E-value: 7.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  807 LDLKDAFFCLRLHPTSQPLFAFEWRDPgmgisgQLTWTRLPQGFKNSPTLFDEALHRDLADFRIQHPDLILlqYVDDILL 886
Cdd:cd03714      1 VDLKDAYFHIPILPRSRDLLGFAWQGE------TYQFKALPFGLSLAPRVFTKVVEALLAPLRLLGVRIFS--YLDDLLI 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1167936614  887 AATSELDCQQGTRALLLT-LGNLGYRASAKKAQIC-QKQVKYLG 928
Cdd:cd03714     73 IASSIKTSEAVLRHLRATlLANLGFTLNLEKSKLGpTQRITFLG 116
Rnase_HI_RT_non_LTR cd09276
non-LTR RNase HI domain of reverse transcriptases; Ribonuclease H (RNase H) is classified into ...
 1180-1318 3.69e-10

non-LTR RNase HI domain of reverse transcriptases; Ribonuclease H (RNase H) is classified into two families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). Ribonuclease HI (RNase HI) is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as an adjunct domain to the reverse transcriptase gene in retroviruses, long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. The position of the RNase domain of non-LTR and LTR transposons is at the carboxyl terminal of the reverse transcriptase (RT) domain and their RNase domains group together, indicating a common evolutionary origin. Many non-LTR transposons have lost the RNase domain because their activity is at the nucleus and cellular RNase may suffice; however LTR retrotransposons always encode their own RNase domain because it requires RNase activity in RNA-protein particles in the cytoplasm. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.


Pssm-ID: 260008 [Multi-domain]  Cd Length: 131  Bit Score: 59.54  E-value: 3.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1180 YTDGSSflQEGQRKAGAAVTTETEVI-WARALPAGTSAQRAELIALTQALKMA-----EGKRLNVYTDSRYAfatahihg 1253
Cdd:cd09276      3 YTDGSK--LEGSVGAGFVIYRGGEVIsRSYRLGTHASVFDAELEAILEALELAlatarRARKVTIFTDSQSA-------- 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167936614 1254 eIYRRRGLLTSEGREIKnkSEILALLKALF-LPKRLSIIHCLGHQkgdsaEARGNRLADQAAREAA 1318
Cdd:cd09276     73 -LQALRNPRRSSGQVIL--IRILRLLRLLKaKGVKVRLRWVPGHV-----GIEGNEAADRLAKEAA 130
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 551-631 6.46e-09

gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins.


Pssm-ID: 464060  Cd Length: 92  Bit Score: 54.50  E-value: 6.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  551 ITLTVGGQPVTFLVDTGAQHSVLTQN--------PGPLSdRSAWVQGATGGKRYHWTTDRKVHLATGKVTHSFLHV--PD 620
Cdd:pfam13975    1 VDVTINGRPVRFLVDTGASVTVISEAlaerlgldRLVDA-YPVTVRTANGTVRAARVRLDSVKIGGIELRNVPAVVlpGD 79

                           90
                   ....*....|.
gi 1167936614  621 CPYPLLGRDLL 631
Cdd:pfam13975   80 LDDVLLGMDFL 90
Tra5 COG2801
Transposase InsO and inactivated derivatives [Mobilome: prophages, transposons];
1348-1557 2.47e-08

Transposase InsO and inactivated derivatives [Mobilome: prophages, transposons];


Pssm-ID: 442053 [Multi-domain]  Cd Length: 309  Bit Score: 57.47  E-value: 2.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1348 LKKLRELGATYNQSKGYWVFQGKPVMPDQFVFELLDSLH-RLTHLGYQKMKALLDRGespYYMLNRDKTLQYVADSCTVC 1426
Cdd:COG2801     43 LRLLRRRRARSRRRRRLRRPRSYRADEDAELLERIKEIFaESPRYGYRRITAELRRE---GIAVNRKRVRRLMRELGLQA 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1427 AQVNASKAKIGAGVRVRGH--------RPGSHWEIDFTEVkPGLYGYKYLLVFVDTFS----GWVEAfptKRETARVVsK 1494
Cdd:COG2801    120 RRRRKKKYTTYSGHGGPIApnllftatAPNQVWVTDITYI-PTAEGWLYLAAVIDLFSreivGWSVS---DSMDAELV-V 194

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167936614 1495 KLLEEIFPRFG--MPRVLGSDNGPAFTSQVSQSVADLLGIDWKLHCAYRPQGSGQVERMNRTIKE 1557
Cdd:COG2801    195 DALEMAIERRGppKPLILHSDNGSQYTSKAYQELLKKLGITQSMSRPGNPQDNAFIESFFGTLKY 259
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 551-632 8.38e-08

Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133136  Cd Length: 92  Bit Score: 51.57  E-value: 8.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  551 ITLTVGGQPVTFLVDTGAQHSVLTQ------NPGPLSDRSAW-VQGATGGKRYHWTTDRKVHLATGK--VTHSFLHVPDC 621
Cdd:cd00303      1 LKGKINGVPVRALVDSGASVNFISEslakklGLPPRLLPTPLkVKGANGSSVKTLGVILPVTIGIGGktFTVDFYVLDLL 80

                           90
                   ....*....|..
gi 1167936614  622 PYP-LLGRDLLT 632
Cdd:cd00303     81 SYDvILGRPWLE 92
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
549-638 9.37e-07

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 50.33  E-value: 9.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  549 PRITLTVGGQPVTFLVDTGAQHSVLTQ--------NPGPLsDRSAWVQGATGGKRYHWTTDRKVHLATGKVTH---SFLH 617
Cdd:COG3577     42 FVVEGTINGQPVRFLVDTGASTVVLSEsdarrlglDPEDL-GRPVRVQTANGVVRAARVRLDSVRIGGITLRNvraVVLP 120

                           90       100
                   ....*....|....*....|.
gi 1167936614  618 VPDCPYPLLGRDLLTKLKAQI 638
Cdd:COG3577    121 GGELDDGLLGMSFLGRLDFEI 141
retropepsin_like_bacteria cd05483
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ...
 549-606 4.23e-06

Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria aspartate proteases is a subfamily of retropepsin-like protease family, which includes enzymes from retrovirus and retrotransposons. While fungal and mammalian pepsin-like aspartate proteases are bilobal proteins with structurally related N- and C-termini, this family of bacteria aspartate proteases is half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate proteases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133150  Cd Length: 96  Bit Score: 46.85  E-value: 4.23e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167936614  549 PRITLTVGGQPVTFLVDTGAQHSVLTQ------NPGPLSDRSAWVQGATGGKRYHWTTDRKVHL 606
Cdd:cd05483      3 FVVPVTINGQPVRFLLDTGASTTVISEelaerlGLPLTLGGKVTVQTANGRVRAARVRLDSLQI 66
transpos_IS3 NF033516
IS3 family transposase;
1445-1556 1.45e-05

IS3 family transposase;


Pssm-ID: 468052 [Multi-domain]  Cd Length: 369  Bit Score: 49.49  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1445 HRPGSHWEIDFTEVKPGlYGYKYLLVFVDTFS----GWVeafPTKRETARVVSKkLLEEIFPRFGMPR--VLGSDNGPAF 1518
Cdd:NF033516   213 TRPNQVWVTDITYIRTA-EGWLYLAVVLDLFSreivGWS---VSTSMSAELVLD-ALEMAIEWRGKPEglILHSDNGSQY 287

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1167936614 1519 TSQVSQSVADLLGIDWKLHCAYRPQGSGQVERMNRTIK 1556
Cdd:NF033516   288 TSKAYREWLKEHGITQSMSRPGNCWDNAVAESFFGTLK 325
Tra8 COG2826
Transposase and inactivated derivatives, IS30 family [Mobilome: prophages, transposons];
1446-1561 1.61e-05

Transposase and inactivated derivatives, IS30 family [Mobilome: prophages, transposons];


Pssm-ID: 442074 [Multi-domain]  Cd Length: 325  Bit Score: 49.11  E-value: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1446 RPGsHWEIDfteVKPGLYGYKYLLVFVDTFSGWVEAFPTKRETARVVSKKL--LEEIFPRFgMPRVLGSDNGPAFT--SQ 1521
Cdd:COG2826    171 EPG-HWEGD---LIIGKRGKSALLTLVERKSRFVILLKLPDKTAESVADALirLLRKLPAF-LRKSITTDNGKEFAdhKE 245

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1167936614 1522 VSQSvadlLGID-WKLHcAYRPQGSGQVERMNRTIKETLTK 1561
Cdd:COG2826    246 IEAA----LGIKvYFAD-PYSPWQRGTNENTNGLLRQYFPK 281
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 551-612 4.52e-05

Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to 230 amino acids in length, in MEROPS clan AA. This model describes the well-conserved 121-residue C-terminal region. The poorly conserved, variable length N-terminal region usually contains a predicted transmembrane helix.


Pssm-ID: 433378  Cd Length: 90  Bit Score: 43.81  E-value: 4.52e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167936614  551 ITLTVGGQPVTFLVDTGAQHSVLtqnpgplsdrSAWVQGATGGKRYHWTTDRKVHLATGKVT 612
Cdd:pfam13650    1 VPVTINGKPVRFLVDTGASGTVI----------SPSLAERLGLKVRGLAYTVRVSTAGGRVS 52
RNase_HI_like cd09279
RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease ...
 1180-1318 7.43e-05

RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Most archaeal genomes contain only type 2 RNase H (RNase HII); however, a few contain RNase HI as well. Although archaeal RNase HI sequences conserve the DEDD active-site motif, they lack other common features important for catalytic function, such as the basic protrusion region. Archaeal RNase HI homologs are more closely related to retroviral RNase HI than bacterial and eukaryotic type I RNase H in enzymatic properties.


Pssm-ID: 260011 [Multi-domain]  Cd Length: 128  Bit Score: 44.00  E-value: 7.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1180 YTDGSSFLQEGQRKAGAAVTTETEVIWARALPAGTSAQ--RAELIALTQALKMAEG---KRLNVYTDSRyaFATAHIHGE 1254
Cdd:cd09279      4 YFDGASRGNPGPAGAGVVIYSPGGEVLELSERLGFPATnnEAEYEALIAGLELALElgaEKLEIYGDSQ--LVVNQLNGE 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1255 IyrrrglltsegrEIKNK------SEILALLKALflpKRLSIIHCLGHQkgdsaeargNRLADQAAREAA 1318
Cdd:cd09279     82 Y------------KVKNErlkpllEKVLELLAKF---ELVELKWIPREQ---------NKEADALANQAL 127
transpos_ISNCY_2 NF033594
ISNCY family transposase; The ISNCY insertion sequence family, as defined by ISFinder, encodes ...
 1467-1561 1.36e-04

ISNCY family transposase; The ISNCY insertion sequence family, as defined by ISFinder, encodes several apparently unrelated families of transposases. Members of this family resemble the transposases of ISNCY family elements such as IS1202, ISTde1, ISKpn21, and ISCARN1.


Pssm-ID: 468103 [Multi-domain]  Cd Length: 367  Bit Score: 46.32  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1467 YLLVFVD--TfSGWVEAFPTKRETA----RVvskklLEEIFPRFGMPRVLGSDNGPAFTSQVSQSVADL----------- 1529
Cdd:NF033594   148 TLLVAIDdaT-GRLMGLRFVESESTfgyfEV-----TRQYLEKHGKPVAFYSDKHSVFRVNEEELAGKGdgltqfgralk 221

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1167936614 1530 -LGIDWKlhCAYRPQGSGQVERMNRTIKETLTK 1561
Cdd:NF033594   222 eLGIEII--CANSPQAKGRVERANQTLQDRLVK 252
ZnF_C2HC smart00343
zinc finger;
502-518 2.63e-04

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 39.73  E-value: 2.63e-04
                            10
                    ....*....|....*..
gi 1167936614   502 QCAYCKEKGHWARDCPK 518
Cdd:smart00343    1 KCYNCGKEGHIARDCPS 17
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
 71-212 3.13e-04

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


Pssm-ID: 434857 [Multi-domain]  Cd Length: 668  Bit Score: 45.53  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614   71 PGPHGHPDQV--PYIVTWEAIAYEPPPWVKPFVSPKLSPSPTAPILPSGPSTQPPPRSALyPALTPSIKP--RPSKPQVL 146
Cdd:pfam15685  404 PGPRRPAPALlaPPMFIFPAPTNGEPVRPGPPAPQALLPRPPPPTPPATPPPVPPPIPQL-PALQPMPLAaaRPPTPRPC 482

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167936614  147 SdngGPLIDLLSEDPPPYGGQGLSSsdgdgDREEATSTSEIPAPSPIVSRLRGKRDPPAADSTTSR 212
Cdd:pfam15685  483 P---GHGESALAPAPTAPLPPALAA-----DQAPAPALAAAPAPSPAPAPATADPLPPAPAPIKAR 540
Integrase_H2C2 pfam17921
Integrase zinc binding domain; This zinc binding domain is found in a wide variety of ...
 1374-1432 4.22e-04

Integrase zinc binding domain; This zinc binding domain is found in a wide variety of integrase proteins.


Pssm-ID: 465569 [Multi-domain]  Cd Length: 58  Bit Score: 39.92  E-value: 4.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1374 PDQFVFELLDSLH-RLTHLGYQKMKALLDRGespYYMLNRDKTLQYVADSCTVCAQVNAS 1432
Cdd:pfam17921    2 PKSLRKEILKEAHdSGGHLGIEKTLARLRRR---YWWPGMRKDVKKYVKSCETCQRRKPS 58
PHA03247 PHA03247
large tegument protein UL36; Provisional
 71-215 7.61e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 7.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614   71 PGPHGHPDQVPYIVTWEAIAYE----PPPWVKPFVSPklsPSPTAPILPSGPSTQPPPRSALYPALTPSIKPRPSKPQVL 146
Cdd:PHA03247  2525 VGEPVHPRMLTWIRGLEELASDdagdPPPPLPPAAPP---AAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAP 2601

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  147 SDNGGPLI----------DLLSEDPPPYGGQGLSSSDGDGDrEEATSTSEIPAPSPIVSRLRGKR------DPPAADSTT 210
Cdd:PHA03247  2602 VDDRGDPRgpappsplppDTHAPDPPPPSPSPAANEPDPHP-PPTVPPPERPRDDPAPGRVSRPRrarrlgRAAQASSPP 2680


                   ....*
gi 1167936614  211 SRAFP 215
Cdd:PHA03247  2681 QRPRR 2685
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 501-518 1.15e-03

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 37.89  E-value: 1.15e-03
                           10
                   ....*....|....*...
gi 1167936614  501 DQCAYCKEKGHWARDCPK 518
Cdd:pfam00098    1 GKCYNCGEPGHIARDCPK 18
HIV_retropepsin_like cd05482
Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family ...
 551-632 1.38e-03

Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133149  Cd Length: 87  Bit Score: 39.56  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  551 ITLTVGGQPVTFLVDTGAQHSVLTQN--PGPLSDRSAW-----VQGATGGKRY---HWTTDRKVHLATGKVthsflHVPD 620
Cdd:cd05482      1 LTLYINGKLFEGLLDTGADVSIIAENdwPKNWPIQPAPsnltgIGGAITPSQSsvlLLEIDGEGHLGTILV-----YVLS 75

                           90
                   ....*....|..
gi 1167936614  621 CPYPLLGRDLLT 632
Cdd:cd05482     76 LPVNLWGRDILS 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
 103-215 1.84e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  103 PKLSPSPTAPILPSGPSTQPPPRSALYPALTPSIKPRPSKPQVLSDNGGPLIdllSEDPPPYGGQGLSSSDGDGDREEAT 182
Cdd:PHA03247  2592 PPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPP---PTVPPPERPRDDPAPGRVSRPRRAR 2668

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1167936614  183 STSEIPAPSPIVSRLRGKRDPPAADSTTSRAFP 215
Cdd:PHA03247  2669 RLGRAAQASSPPQRPRRRAARPTVGSLTSLADP 2701
RT_pepA17 cd01644
RT_pepA17: Reverse transcriptase (RTs) in retrotransposons. This subfamily represents the RT ...
 808-891 1.95e-03

RT_pepA17: Reverse transcriptase (RTs) in retrotransposons. This subfamily represents the RT domain of a multifunctional enzyme. C-terminal to the RT domain is a domain homologous to aspartic proteinases (corresponding to Merops family A17) encoded by retrotransposons and retroviruses. RT catalyzes DNA replication from an RNA template and is responsible for the replication of retroelements.


Pssm-ID: 238822  Cd Length: 213  Bit Score: 41.52  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614  808 DLKDAFFCLRLHPTSQPLFAFEWR-DPGMGISGQLTWTRLPQGFKNSPTLFDEALHRDLADFriQHPDL--ILLQ--YVD 882
Cdd:cd01644     65 DIEKMFHQVKVRPEDRDVLRFLWRkDGDEPKPIEYRMTVVPFGAASAPFLANRALKQHAEDH--PHEAAakIIKRnfYVD 142


                   ....*....
gi 1167936614  883 DILLAATSE 891
Cdd:cd01644    143 DILVSTDTL 151
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 492-527 2.22e-03

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 40.56  E-value: 2.22e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1167936614  492 ERRRPQLDKDQCAYCKEKGHWARDCPKKPRGPRGPR 527
Cdd:PTZ00368    95 NRAKGGAARRACYNCGGEGHISRDCPNAGKRPGGDK 130
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 93-222 3.59e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614   93 PPPWVKPFVSPklsPSPTAPILPSGPSTQPPPRSALYPALTPSIKPRPSKPQVLSDNGGPLIDLLSEDPPPyGGQGLSSS 172
Cdd:PHA03307   256 PLPRPAPITLP---TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRE-SSSSSTSS 331

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1167936614  173 DGDGDREEATSTSEIPAPSPIVSRlrgKRDPPAADSTTSRAFPLRLGGNG 222
Cdd:PHA03307   332 SSESSRGAAVSPGPSPSRSPSPSR---PPPPADPSSPRKRPRPSRAPSSP 378
rnhA PRK00203
ribonuclease H; Reviewed
 1212-1320 9.74e-03

ribonuclease H; Reviewed


Pssm-ID: 178927 [Multi-domain]  Cd Length: 150  Bit Score: 38.65  E-value: 9.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167936614 1212 AGTSAQRAELIALTQALKM-AEGKRLNVYTDSRY---AFaTAHIHGeiYRRRGLLTSEGREIKNKSEILALLKALflpKR 1287
Cdd:PRK00203    39 ALTTNNRMELMAAIEALEAlKEPCEVTLYTDSQYvrqGI-TEWIHG--WKKNGWKTADKKPVKNVDLWQRLDAAL---KR 112

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1167936614 1288 lsiihclgHQ------KGDSAEArGNRLADQAAREAAIK 1320
Cdd:PRK00203   113 --------HQikwhwvKGHAGHP-ENERCDELARAGAEE 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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