|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08609 |
PRK08609 |
DNA polymerase/3'-5' exonuclease PolX; |
1-566 |
0e+00 |
|
DNA polymerase/3'-5' exonuclease PolX;
Pssm-ID: 236311 [Multi-domain] Cd Length: 570 Bit Score: 1079.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 1 MTKKDVIKLLEQIATYMELKGENTFKISAYRKAAQSLELDERPLDEISDVTELKGIGKGVAEVINDYRETGESQYLQQLQ 80
Cdd:PRK08609 1 MNKKDVIKLLETIATYMELKGENPFKISAFRKAAQALELDERSLSEIDDFTKLKGIGKGTAEVIQEYRETGESSVLQELK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 81 EEVPEGLIPLLKIQGLGSKKIAKLYKELNIVDKASLQVACENGKVSELSGFAKKTEQNILEAVKQLGAKKDRYPIDQMRR 160
Cdd:PRK08609 81 KEVPEGLLPLLKLPGLGGKKIAKLYKELGVVDKESLKEACENGKVQALAGFGKKTEEKILEAVKELGKRPERLPIAQVLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 161 LNQEIIDYIDTLNYIDQYSSAGSFRRFKEMSKDLDFIISTDNPKAVQQQLLNIPNKVKEVAVGNTKVSLELAYdDETIGV 240
Cdd:PRK08609 161 IAQEIEEYLATIDEIIRFSRAGSLRRARETVKDLDFIIATDEPEAVREQLLQLPNIVEVIAAGDTKVSVELEY-EYTISV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 241 DFRLIEPRAFYHTLQHFTGSKEHNIRIRQLAKARDEKVSEYGIEQAD-GTLIQYDSEAKIYEHFNVNFIPPAMREDGSEF 319
Cdd:PRK08609 240 DFRLVEPEAFATTLHHFTGSKDHNVRMRQLAKERGEKISEYGVEQADtGEVKTFESEEAFFAHFGLPFIPPEVREDGSEF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 320 D--KDLSNIITLDDINGDIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDHSQSLRVANGLQVERLLRQNEEIKALDKE 397
Cdd:PRK08609 320 EryKDLSNLITLSDIQGDLHMHTTWSDGAFSIEEMVEACIAKGYEYMAITDHSQYLKVANGLTEERLLEQAEEIKALNEK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 398 YSEIDIYSGTEMDILPDGSLDYDDEILAQLDYVIGAIHQSFNQSEEQIMERLANACRNPYVRHIAHPTGRIIGRRDGYKP 477
Cdd:PRK08609 400 YPEIDILSGIEMDILPDGSLDYDDEVLAELDYVIAAIHSSFSQSEEEIMKRLENACRNPYVRLIAHPTGRLIGRRDGYDV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 478 NIEQLMALAEETNTVLEINANPHRLDLNAEIVRKYPN--VKLTINTDAHHTNHLDFMNYGVATAQKGFVTKDRVINALSR 555
Cdd:PRK08609 480 NIDQLIELAKETNTALELNANPNRLDLSAEHLKKAQEagVKLAINTDAHHTEMLDDMKYGVATARKGWIQKDRVINTWSR 559
|
570
....*....|.
gi 586232721 556 EAFKDFIENNI 566
Cdd:PRK08609 560 EEFKDFIKRNK 570
|
|
| PolX |
COG1796 |
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair]; |
1-559 |
0e+00 |
|
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
Pssm-ID: 441401 [Multi-domain] Cd Length: 567 Bit Score: 640.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 1 MTKKDVIKLLEQIATYMELKGENTFKISAYRKAAQSLELDERPLDEIS---DVTELKGIGKGVAEVINDYRETGESQYLQ 77
Cdd:COG1796 1 MDNKEIARILEEIADLLELKGENPFKIRAYRRAARAIENLPEDIEELVaegDLTEIPGIGKAIAAKIEELLETGRLEELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 78 QLQEEVPEGLIPLLKIQGLGSKKIAKLYKELNIVDKASLQVACENGKVSELSGFAKKTEQNILEAVKQLGAKKDRYPIDQ 157
Cdd:COG1796 81 ELREEVPPGLLELLRIPGLGPKKVKKLYEELGITSLEELEAAAEEGRIRELPGFGEKTEENILKGIELLRKRGGRFLLGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 158 MRRLNQEIIDYIDTLNYIDQYSSAGSFRRFKEMSKDLDFIISTDNPKAVQQQLLNIPNkVKEV-AVGNTKVSLELAYDde 236
Cdd:COG1796 161 ALPLAEEILAYLRALPGVERVEVAGSLRRRKETVGDIDILVASDDPEAVMDAFVKLPE-VKEVlAKGDTKASVRLKSG-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 237 tIGVDFRLIEPRAFYHTLQHFTGSKEHNIRIRQLAKARDEKVSEYGIEQADGTLIQYDSEAKIYEHFNVNFIPPAMREDG 316
Cdd:COG1796 238 -LQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAKERGLKLNEYGLFDVGGERIAGETEEEVYAALGLPYIPPELREDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 317 SEFD----KDLSNIITLDDINGDIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDHSQSLRVANGLQVERLLRQNEEIK 392
Cdd:COG1796 317 GEIEaaeeGRLPELVELDDIRGDLHHHTTWSDGGASIEEMAAAAAARGYYYIAITDHSSSLVVAGGLDEERLLQQEEEID 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 393 ALDKEYSEIDIYSGTEMDILPDGSLDYDDEILAQLDYVIGAIHQSFNQSEEQIMERLANACRNPYVRHIAHPTGRIIGRR 472
Cdd:COG1796 397 ALNERLDGIILLLGGEEDILDDGGLDDDDDLLLEDDDVVAAVHHSFLLQDEEMTRRRLAAANEPVVVIIHHPTGRLLLRR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 473 DGYKPNIEQLMALAEETNTVLEINANPHRLDLNAEIVR--KYPNVKLTINTDAHHTNHLDFMN-YGVATAQKGFVTKDRV 549
Cdd:COG1796 477 RPYYVDDEAIIAAAAAAGALEEENNAPRRLLLLDDLARaaAEGGVVIIIIDDAHHTDLLLDLMgGGVAARRRWWLEKDVN 556
|
570
....*....|
gi 586232721 550 INALSREAFK 559
Cdd:COG1796 557 NNTLLLELLL 566
|
|
| PHP_PolX |
cd07436 |
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ... |
328-562 |
1.59e-137 |
|
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal X-family DNA polymerases (PolXs) have a PHP domain at their C-terminus. The bacterial/archaeal PolX core domain and PHP domain interact with each other and together are involved in metal dependent 3'-5' exonuclease activity. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PolX is found in all kingdoms, however bacterial PolXs have a completely different domain structure from eukaryotic PolXs. Bacterial PolX has an extended conformation in contrast to the common closed 'right hand' conformation for DNA polymerases. This extended conformation is stabilized by the PHP domain. The PHP domain of PolX is structurally homologous to other members of the PHP family that has a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213991 [Multi-domain] Cd Length: 237 Bit Score: 398.72 E-value: 1.59e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 328 TLDDINGDIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDHSQSLRVANGLQVERLLRQNEEIKALDKEYSEIDIYSGT 407
Cdd:cd07436 1 ELKDIRGDLHVHTTWSDGRNSIEEMAEAARALGYEYIAITDHSKSLRVANGLSEERLREQIEEIDALNEKLPGIRILKGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 408 EMDILPDGSLDYDDEILAQLDYVIGAIHQSFNQSEEQIMERLANACRNPYVRHIAHPTGRIIGRRDGYKPNIEQLMALAE 487
Cdd:cd07436 81 EVDILPDGSLDYPDEVLAELDVVVASVHSGFNQSEEEMTERLLKAIENPHVDILGHPTGRLLGRREGYEVDMERVIEAAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586232721 488 ETNTVLEINANPHRLDLNAEIVRKYP--NVKLTINTDAHHTNHLDFMNYGVATAQKGFVTKDRVINALSREAFKDFI 562
Cdd:cd07436 161 ETGTALEINANPDRLDLDDRHARRAKeaGVKIAINTDAHSTDGLDNMRYGVGTARRGWLEKEDVLNTLPLEELLKFL 237
|
|
| POLXc |
smart00483 |
DNA polymerase X family; includes vertebrate polymerase beta and terminal ... |
1-314 |
1.30e-42 |
|
DNA polymerase X family; includes vertebrate polymerase beta and terminal deoxynucleotidyltransferases
Pssm-ID: 214688 Cd Length: 334 Bit Score: 155.60 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 1 MTKKDVIKLLEQIATYMELKGENTFKISAYRKAAQSLELDERPLDEISDVTELKGIGKGVAEVINDYRETGESQYLQQ-L 79
Cdd:smart00483 1 NLNRGIIDALEILAENYEVFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 80 QEEVPEGLIPLLKIQGLGSKKIAKLYKeLNIVDKASLQVACENgKVSELSGFAKKTEQNILEAVKQLGAKKDRYPIdqMR 159
Cdd:smart00483 81 NDEVYKSLKLFTNVFGVGPKTAAKWYR-KGIRTLEELKKNKEL-KLTKQQKAGLKYYEDILKKVSRAEAFAVEYIV--KR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 160 RLNQEIIDYIDTLnyidqyssAGSFRRFKEMSKDLDFIISTDNPKA-------------VQQQLLNIPN-KVKEVAVGNT 225
Cdd:smart00483 157 AVRKILPDAIVTL--------TGSFRRGKETGHDVDFLITSPHPAKekelevldlllleSTFEELQLPSiRVATLDHGQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 226 K---VSLELAYDDET------------IGVDFRLIEPRAFYHTLQHFTGSKEHNIRIRQLAKARdEKVSEYGIEQADGT- 289
Cdd:smart00483 229 KfmiLKLSPSREDKEksgkpdekgwkaRRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSK-FKLMLDGHELYDKTk 307
|
330 340
....*....|....*....|....*..
gi 586232721 290 --LIQYDSEAKIYEHFNVNFIPPAMRE 314
Cdd:smart00483 308 ekFLKVESEEDIFDHLGLPYIEPEERN 334
|
|
| HHH_8 |
pfam14716 |
Helix-hairpin-helix domain; |
3-69 |
5.60e-20 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434152 [Multi-domain] Cd Length: 67 Bit Score: 83.71 E-value: 5.60e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586232721 3 KKDVIKLLEQIATYMELKGENTFKISAYRKAAQSLELDERPLDEISDVTELKGIGKGVAEVINDYRE 69
Cdd:pfam14716 1 NQEIADALEELADLLELKGEDPFRVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
|
|
| hisJ_fam |
TIGR01856 |
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ... |
335-456 |
1.67e-09 |
|
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate phosphatase HisJ of Bacillus subtilis, and related proteins from a number of species within a larger family of phosphatases in the PHP hydrolase family. HisJ catalyzes the penultimate step of histidine biosynthesis but shows no homology to the functionally equivalent sequence in E. coli, a domain of the bifunctional HisB protein. Note, however, that many species have two members and that Clostridium perfringens, predicted not to make histidine, has five members of this family; this family is designated subfamily rather than equivalog to indicate that members may not all act as HisJ.
Pssm-ID: 273837 [Multi-domain] Cd Length: 253 Bit Score: 58.56 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 335 DIHMHTTYS-DGAFSIRDMVEANIAKGYKFMVITDHSQSLRVANG---LQVERLLRQ----NEEIKALDKEY-SEIDIYS 405
Cdd:TIGR01856 2 DSHSHSPFCaHGTDTLREVVQEAIQLGFEEICFTEHAPRPFYYPEedfLKKEMLFLSlpeyFQEINQLKQEYaDKIKILI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 586232721 406 GTEMDILPdGSLDYDDEIL--AQLDYVIGAIH----QSFNQSEEQIMERLANACRNP 456
Cdd:TIGR01856 82 GLEVDYIP-GFEEEIKDFLdsYNLDFVIGSVHhlggIPIDFDIEEFDETLFSFQKNL 137
|
|
| CehA_McbA_metalo |
NF038032 |
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ... |
334-369 |
1.17e-05 |
|
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is found in several partially characterized metallohydrolases, including McbA and CehA. Both were studied as hydrolases of carbaryl, a xenobiotic compound that does not contain a phosphate group, suggesting that presuming members of this family to be phosphoesterases (like many PHP domain-containing proteins) may be incorrect.
Pssm-ID: 468321 [Multi-domain] Cd Length: 315 Bit Score: 47.32 E-value: 1.17e-05
10 20 30
....*....|....*....|....*....|....*.
gi 586232721 334 GDIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDH 369
Cdd:NF038032 5 GDLHIHTNHSDGPTTPEELARAALAEGLDVIALTDH 40
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08609 |
PRK08609 |
DNA polymerase/3'-5' exonuclease PolX; |
1-566 |
0e+00 |
|
DNA polymerase/3'-5' exonuclease PolX;
Pssm-ID: 236311 [Multi-domain] Cd Length: 570 Bit Score: 1079.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 1 MTKKDVIKLLEQIATYMELKGENTFKISAYRKAAQSLELDERPLDEISDVTELKGIGKGVAEVINDYRETGESQYLQQLQ 80
Cdd:PRK08609 1 MNKKDVIKLLETIATYMELKGENPFKISAFRKAAQALELDERSLSEIDDFTKLKGIGKGTAEVIQEYRETGESSVLQELK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 81 EEVPEGLIPLLKIQGLGSKKIAKLYKELNIVDKASLQVACENGKVSELSGFAKKTEQNILEAVKQLGAKKDRYPIDQMRR 160
Cdd:PRK08609 81 KEVPEGLLPLLKLPGLGGKKIAKLYKELGVVDKESLKEACENGKVQALAGFGKKTEEKILEAVKELGKRPERLPIAQVLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 161 LNQEIIDYIDTLNYIDQYSSAGSFRRFKEMSKDLDFIISTDNPKAVQQQLLNIPNKVKEVAVGNTKVSLELAYdDETIGV 240
Cdd:PRK08609 161 IAQEIEEYLATIDEIIRFSRAGSLRRARETVKDLDFIIATDEPEAVREQLLQLPNIVEVIAAGDTKVSVELEY-EYTISV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 241 DFRLIEPRAFYHTLQHFTGSKEHNIRIRQLAKARDEKVSEYGIEQAD-GTLIQYDSEAKIYEHFNVNFIPPAMREDGSEF 319
Cdd:PRK08609 240 DFRLVEPEAFATTLHHFTGSKDHNVRMRQLAKERGEKISEYGVEQADtGEVKTFESEEAFFAHFGLPFIPPEVREDGSEF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 320 D--KDLSNIITLDDINGDIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDHSQSLRVANGLQVERLLRQNEEIKALDKE 397
Cdd:PRK08609 320 EryKDLSNLITLSDIQGDLHMHTTWSDGAFSIEEMVEACIAKGYEYMAITDHSQYLKVANGLTEERLLEQAEEIKALNEK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 398 YSEIDIYSGTEMDILPDGSLDYDDEILAQLDYVIGAIHQSFNQSEEQIMERLANACRNPYVRHIAHPTGRIIGRRDGYKP 477
Cdd:PRK08609 400 YPEIDILSGIEMDILPDGSLDYDDEVLAELDYVIAAIHSSFSQSEEEIMKRLENACRNPYVRLIAHPTGRLIGRRDGYDV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 478 NIEQLMALAEETNTVLEINANPHRLDLNAEIVRKYPN--VKLTINTDAHHTNHLDFMNYGVATAQKGFVTKDRVINALSR 555
Cdd:PRK08609 480 NIDQLIELAKETNTALELNANPNRLDLSAEHLKKAQEagVKLAINTDAHHTEMLDDMKYGVATARKGWIQKDRVINTWSR 559
|
570
....*....|.
gi 586232721 556 EAFKDFIENNI 566
Cdd:PRK08609 560 EEFKDFIKRNK 570
|
|
| PolX |
COG1796 |
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair]; |
1-559 |
0e+00 |
|
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
Pssm-ID: 441401 [Multi-domain] Cd Length: 567 Bit Score: 640.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 1 MTKKDVIKLLEQIATYMELKGENTFKISAYRKAAQSLELDERPLDEIS---DVTELKGIGKGVAEVINDYRETGESQYLQ 77
Cdd:COG1796 1 MDNKEIARILEEIADLLELKGENPFKIRAYRRAARAIENLPEDIEELVaegDLTEIPGIGKAIAAKIEELLETGRLEELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 78 QLQEEVPEGLIPLLKIQGLGSKKIAKLYKELNIVDKASLQVACENGKVSELSGFAKKTEQNILEAVKQLGAKKDRYPIDQ 157
Cdd:COG1796 81 ELREEVPPGLLELLRIPGLGPKKVKKLYEELGITSLEELEAAAEEGRIRELPGFGEKTEENILKGIELLRKRGGRFLLGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 158 MRRLNQEIIDYIDTLNYIDQYSSAGSFRRFKEMSKDLDFIISTDNPKAVQQQLLNIPNkVKEV-AVGNTKVSLELAYDde 236
Cdd:COG1796 161 ALPLAEEILAYLRALPGVERVEVAGSLRRRKETVGDIDILVASDDPEAVMDAFVKLPE-VKEVlAKGDTKASVRLKSG-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 237 tIGVDFRLIEPRAFYHTLQHFTGSKEHNIRIRQLAKARDEKVSEYGIEQADGTLIQYDSEAKIYEHFNVNFIPPAMREDG 316
Cdd:COG1796 238 -LQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAKERGLKLNEYGLFDVGGERIAGETEEEVYAALGLPYIPPELREDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 317 SEFD----KDLSNIITLDDINGDIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDHSQSLRVANGLQVERLLRQNEEIK 392
Cdd:COG1796 317 GEIEaaeeGRLPELVELDDIRGDLHHHTTWSDGGASIEEMAAAAAARGYYYIAITDHSSSLVVAGGLDEERLLQQEEEID 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 393 ALDKEYSEIDIYSGTEMDILPDGSLDYDDEILAQLDYVIGAIHQSFNQSEEQIMERLANACRNPYVRHIAHPTGRIIGRR 472
Cdd:COG1796 397 ALNERLDGIILLLGGEEDILDDGGLDDDDDLLLEDDDVVAAVHHSFLLQDEEMTRRRLAAANEPVVVIIHHPTGRLLLRR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 473 DGYKPNIEQLMALAEETNTVLEINANPHRLDLNAEIVR--KYPNVKLTINTDAHHTNHLDFMN-YGVATAQKGFVTKDRV 549
Cdd:COG1796 477 RPYYVDDEAIIAAAAAAGALEEENNAPRRLLLLDDLARaaAEGGVVIIIIDDAHHTDLLLDLMgGGVAARRRWWLEKDVN 556
|
570
....*....|
gi 586232721 550 INALSREAFK 559
Cdd:COG1796 557 NNTLLLELLL 566
|
|
| PHP_PolX |
cd07436 |
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ... |
328-562 |
1.59e-137 |
|
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal X-family DNA polymerases (PolXs) have a PHP domain at their C-terminus. The bacterial/archaeal PolX core domain and PHP domain interact with each other and together are involved in metal dependent 3'-5' exonuclease activity. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PolX is found in all kingdoms, however bacterial PolXs have a completely different domain structure from eukaryotic PolXs. Bacterial PolX has an extended conformation in contrast to the common closed 'right hand' conformation for DNA polymerases. This extended conformation is stabilized by the PHP domain. The PHP domain of PolX is structurally homologous to other members of the PHP family that has a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213991 [Multi-domain] Cd Length: 237 Bit Score: 398.72 E-value: 1.59e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 328 TLDDINGDIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDHSQSLRVANGLQVERLLRQNEEIKALDKEYSEIDIYSGT 407
Cdd:cd07436 1 ELKDIRGDLHVHTTWSDGRNSIEEMAEAARALGYEYIAITDHSKSLRVANGLSEERLREQIEEIDALNEKLPGIRILKGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 408 EMDILPDGSLDYDDEILAQLDYVIGAIHQSFNQSEEQIMERLANACRNPYVRHIAHPTGRIIGRRDGYKPNIEQLMALAE 487
Cdd:cd07436 81 EVDILPDGSLDYPDEVLAELDVVVASVHSGFNQSEEEMTERLLKAIENPHVDILGHPTGRLLGRREGYEVDMERVIEAAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586232721 488 ETNTVLEINANPHRLDLNAEIVRKYP--NVKLTINTDAHHTNHLDFMNYGVATAQKGFVTKDRVINALSREAFKDFI 562
Cdd:cd07436 161 ETGTALEINANPDRLDLDDRHARRAKeaGVKIAINTDAHSTDGLDNMRYGVGTARRGWLEKEDVLNTLPLEELLKFL 237
|
|
| HIS2 |
COG1387 |
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ... |
334-561 |
9.98e-102 |
|
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and metabolism, General function prediction only]; Histidinol phosphatase or related hydrolase of the PHP family is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 440997 [Multi-domain] Cd Length: 232 Bit Score: 307.08 E-value: 9.98e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 334 GDIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDHSQSLRVANGLQVERLLRQNEEIKALDKEYSEIDIYSGTEMDILP 413
Cdd:COG1387 3 GDLHTHTTYSDGEGTIEEMVEAAIELGLEYIAITDHSPSLFVANGLSEERLLEYLEEIEELNEKYPDIKILKGIEVDILP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 414 DGSLDYDDEILAQLDYVIGAIHQSFNQSEEQIMERLANACRNPYVRHIAHPTGRIIGRRDGYKPNIEQLMALAEETNTVL 493
Cdd:COG1387 83 DGSLDYPDELLAPLDYVIGSVHSILEEDYEEYTERLLKAIENPLVDILGHPDGRLLGGRPGYEVDIEEVLEAAAENGVAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 494 EINANPHRLDLNAEIVRKY--PNVKLTINTDAHHTNHLDFMNYGVATAQKGFVTKDRVINALSREAFKDF 561
Cdd:COG1387 163 EINTRPLRLDPSDELLKLAkeLGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFNTLRKEELLKL 232
|
|
| NT_POLXc |
cd00141 |
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ... |
4-313 |
8.41e-78 |
|
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family.
Pssm-ID: 143386 [Multi-domain] Cd Length: 307 Bit Score: 247.88 E-value: 8.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 4 KDVIKLLEQIATYMELKGENTFKISAYRKAAQSLELDERPLDEISDVTELKGIGKGVAEVINDYRETGESQYLQQLQEEV 83
Cdd:cd00141 1 QEIADILEELADLLELLGGNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELREDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 84 PEGLIPLLKIQGLGSKKIAKLYkELNIVDKASLQVACEngkvselsgfaKKTEQNILEAVKQLGAKKDRYPIDQMRRLNQ 163
Cdd:cd00141 81 PPGLLLLLRVPGVGPKTARKLY-ELGIRTLEDLRKAAG-----------AKLEQNILIGLEYYEDFQQRIPREEALAIAE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 164 EIIDYIDTLNYIDQYSSAGSFRRFKEMSKDLDFIISTDN------PKAVQQQLLNIPNKVKEVAVGNTKVSLELAYDDET 237
Cdd:cd00141 149 IIKEALREVDPVLQVEIAGSYRRGKETVGDIDILVTHPDatsrglLEKVVDALVELGFVTEVLSKGDTKASGILKLPGGW 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586232721 238 IG--VDFRLIEPRAFYHTLQHFTGSKEHNIRIRQLAKARDEKVSEYGI-EQADGTLIQYDSEAKIYEHFNVNFIPPAMR 313
Cdd:cd00141 229 KGrrVDLRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLfDGVDGERLPGETEEEIFEALGLPYIEPELR 307
|
|
| PRK07945 |
PRK07945 |
PHP domain-containing protein; |
334-560 |
4.83e-55 |
|
PHP domain-containing protein;
Pssm-ID: 236135 [Multi-domain] Cd Length: 335 Bit Score: 189.04 E-value: 4.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 334 GDIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDHSQSLRVANGLQVERLLRQNEEIKALDKEYSEIDIYSGTEMDILP 413
Cdd:PRK07945 98 GDLHTHSDWSDGGSPIEEMARTAAALGHEYCALTDHSPRLTVANGLSAERLRKQLDVVAELNEELAPFRILTGIEVDILD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 414 DGSLDYDDEILAQLDYVIGAIHQSFNQSEEQIMERLANACRNPYVRHIAHPTGRIIGRRDGYKP----NIEQLMALAEET 489
Cdd:PRK07945 178 DGSLDQEPELLDRLDVVVASVHSKLRMDAAAMTRRMLAAVANPHTDVLGHCTGRLVTGNRGTRPeskfDAEAVFAACREH 257
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586232721 490 NTVLEINANPHRLDLNAEIVRKYPN--VKLTINTDAHHTNHLDFMNYGVATAQKGFVTKDRVINALSREAFKD 560
Cdd:PRK07945 258 GTAVEINSRPERRDPPTRLLRLALDagCLFSIDTDAHAPGQLDWLGYGCERAEEAGVPADRIVNTWPADRLLA 330
|
|
| POLXc |
smart00483 |
DNA polymerase X family; includes vertebrate polymerase beta and terminal ... |
1-314 |
1.30e-42 |
|
DNA polymerase X family; includes vertebrate polymerase beta and terminal deoxynucleotidyltransferases
Pssm-ID: 214688 Cd Length: 334 Bit Score: 155.60 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 1 MTKKDVIKLLEQIATYMELKGENTFKISAYRKAAQSLELDERPLDEISDVTELKGIGKGVAEVINDYRETGESQYLQQ-L 79
Cdd:smart00483 1 NLNRGIIDALEILAENYEVFGENKRKCSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 80 QEEVPEGLIPLLKIQGLGSKKIAKLYKeLNIVDKASLQVACENgKVSELSGFAKKTEQNILEAVKQLGAKKDRYPIdqMR 159
Cdd:smart00483 81 NDEVYKSLKLFTNVFGVGPKTAAKWYR-KGIRTLEELKKNKEL-KLTKQQKAGLKYYEDILKKVSRAEAFAVEYIV--KR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 160 RLNQEIIDYIDTLnyidqyssAGSFRRFKEMSKDLDFIISTDNPKA-------------VQQQLLNIPN-KVKEVAVGNT 225
Cdd:smart00483 157 AVRKILPDAIVTL--------TGSFRRGKETGHDVDFLITSPHPAKekelevldlllleSTFEELQLPSiRVATLDHGQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 226 K---VSLELAYDDET------------IGVDFRLIEPRAFYHTLQHFTGSKEHNIRIRQLAKARdEKVSEYGIEQADGT- 289
Cdd:smart00483 229 KfmiLKLSPSREDKEksgkpdekgwkaRRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSK-FKLMLDGHELYDKTk 307
|
330 340
....*....|....*....|....*..
gi 586232721 290 --LIQYDSEAKIYEHFNVNFIPPAMRE 314
Cdd:smart00483 308 ekFLKVESEEDIFDHLGLPYIEPEERN 334
|
|
| PHP_HisPPase_Ycdx_like |
cd07437 |
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ... |
335-565 |
2.77e-30 |
|
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP domain similar to Ycdx E. coli protein with an unknown physiological role. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. It has also been shown that the PHP domain functions in DNA repair. The PHP structures have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel. YcdX may be involved in swarming.
Pssm-ID: 213992 [Multi-domain] Cd Length: 233 Bit Score: 118.70 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 335 DIHMHTTYSDGAFS-IRDMVEANIAKGYKFMVITDHSQSLRVA-------NglqverllrqneeIKALDKEYSEIDIYSG 406
Cdd:cd07437 4 DLHTHTIASGHAYStIEEMARAAAEKGLKLLGITDHGPAMPGAphpwyfgN-------------LKVIPREIYGVRILRG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 407 TEMDIL-PDGSLDYDDEILAQLDYVIGAIHQ--SFNQSEEQIMERLANACRNPYVRHIAHPTgriigrRDGYKPNIEQLM 483
Cdd:cd07437 71 VEANIIdYDGNLDLPERVLKRLDYVIASLHEpcFAPGTKEENTRAYINAMENPYVDIIGHPG------NPRYPIDYEAVV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 484 ALAEETNTVLEINAN---PHRLDLN------AEIVRKYpNVKLTINTDAHHTNHLDFMNYGVATAQKGFVTKDRVINAlS 554
Cdd:cd07437 145 KAAKEYNVLLEINNSslsPSRKGSRencreiAELCKKY-GVPVIVGSDAHIAYDIGNFDEALELLEEIGFPEELILNT-S 222
|
250
....*....|.
gi 586232721 555 REAFKDFIENN 565
Cdd:cd07437 223 PERLLDFLKLR 233
|
|
| PHP_HisPPase_Hisj_like |
cd12110 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ... |
335-531 |
5.15e-22 |
|
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; Bacillus subtilis YtvP HisJ has strong histidinol phosphate phosphatase (HisPPase) activity. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213994 [Multi-domain] Cd Length: 244 Bit Score: 95.32 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 335 DIHMHTTYSDGAF-SIRDMVEANIAKGYKFMVITDHS-----QSLRVANGLQVERLLRQNEEIKALDKEYSE-IDIYSGT 407
Cdd:cd12110 2 DYHTHTPRCDHASgTLEEYVEAAIELGFTEIGFSEHAplpfeFDDYPESRMAEEELEDYVEEIRRLKEKYADqIEIKLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 408 EMDILPDGSLDYDDEILA-QLDYVIGAIH---------------QSFNQSEEQIMER----LANACRNPYVRHIAHPT-- 465
Cdd:cd12110 82 EVDYFPGYEEELRELLYGyPLDYVIGSVHflggwgfdfpedgiaEYFEGDIDELYERyfdlVEKAIESGLFDIIGHPDli 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586232721 466 ---GRIIGRRDGYKPNIEQLMALAEETNTVLEINAN----------PHRlDLnAEIVRKYpNVKLTINTDAHHTNHLDF 531
Cdd:cd12110 162 kkfGKNDEPDEDYEELIERILRAIAEAGVALEINTAglrkpvgepyPSP-EF-LELAKEL-GIPVTLGSDAHSPEDVGQ 237
|
|
| HHH_8 |
pfam14716 |
Helix-hairpin-helix domain; |
3-69 |
5.60e-20 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434152 [Multi-domain] Cd Length: 67 Bit Score: 83.71 E-value: 5.60e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586232721 3 KKDVIKLLEQIATYMELKGENTFKISAYRKAAQSLELDERPLDEISDVTELKGIGKGVAEVINDYRE 69
Cdd:pfam14716 1 NQEIADALEELADLLELKGEDPFRVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
|
|
| DNA_pol_B_thumb |
pfam14791 |
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three ... |
253-314 |
1.91e-19 |
|
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three domains. An N-terminal fingers domain, a central palm domain and a C-terminal thumb domain. This entry represents the thumb domain.
Pssm-ID: 464317 [Multi-domain] Cd Length: 63 Bit Score: 82.03 E-value: 1.91e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586232721 253 TLQHFTGSKEHNIRIRQLAKARDEKVSEYGIEQ-ADGTLIQYDSEAKIYEHFNVNFIPPAMRE 314
Cdd:pfam14791 1 ALLYFTGSKEFNRDLRLLAKKKGLKLNEYGLFDlKDGELLEGETEEDIFEALGLPYIPPELRE 63
|
|
| PRK09248 |
PRK09248 |
putative hydrolase; Validated |
335-563 |
3.01e-19 |
|
putative hydrolase; Validated
Pssm-ID: 236429 [Multi-domain] Cd Length: 246 Bit Score: 87.20 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 335 DIHMHTTYSDGAFS-IRDMVEANIAKGYKFMVITDHSQSLRVA------NGLQVerllrqneeikaLDKEYSEIDIYSGT 407
Cdd:PRK09248 6 DTHTHTIASGHAYStLHENAAEAKQKGLKLFAITDHGPDMPGAphywhfGNLRV------------LPRKVDGVGILRGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 408 EMDILP-DGSLDYDDEILAQLDYVIGAIHQS-F-NQSEEQIMERLANACRNPYVRHIAHPtgriigrrdG---YKPNIEQ 481
Cdd:PRK09248 74 EANIKNyDGEIDLPGDMLKKLDIVIAGFHEPvFaPGDKETNTQALINAIKNGRVDIIGHP---------GnpkYPIDIEA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 482 LMALAEETNTVLEIN------------ANPHRLdlnAEIVRKYpNVKLTINTDAHhtNHLDFMNYGVATA---QKGFvTK 546
Cdd:PRK09248 145 VVKAAKEHNVALEINnssfghsrkgseDNCRAI---AALCKKA-GVWVALGSDAH--IAFDIGNFEEALKildEVGF-PE 217
|
250
....*....|....*..
gi 586232721 547 DRVINAlSREAFKDFIE 563
Cdd:PRK09248 218 ERILNV-SPRRLLDFLE 233
|
|
| PRK08392 |
PRK08392 |
hypothetical protein; Provisional |
335-550 |
4.18e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 169423 [Multi-domain] Cd Length: 215 Bit Score: 83.29 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 335 DIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDHSQSLRVANGLQVERLLRQNeeikaldKEYSEIDIYSGTEMDILPD 414
Cdd:PRK08392 2 DLHTHTVYSDGIGSVRDNIAEAERKGLRLVGISDHIHYFTPSKFNAYINEIRQW-------GEESEIVVLAGIEANITPN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 415 GsLDYDDEILAQLDYVIGAIHQSFNQSE-EQIMERLANACRNPYVRHIAHptgriIGRRDGY--KPNIEQL---MALAEE 488
Cdd:PRK08392 75 G-VDITDDFAKKLDYVIASVHEWFGRPEhHEYIELVKLALMDENVDIIGH-----FGNSFPYigYPSEEELkeiLDLAEA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586232721 489 TNTVLEINAN---PHrLDLNAEIVRKypNVKLTINTDAHHTNHLDFMNYGVATAQKGFVTKDRVI 550
Cdd:PRK08392 149 YGKAFEISSRyrvPD-LEFIRECIKR--GIKLTFASDAHRPEDVGNVSWSLKVFKKAGGKKEDLL 210
|
|
| YciV |
COG0613 |
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ... |
332-528 |
3.48e-11 |
|
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and metabolism];
Pssm-ID: 440378 [Multi-domain] Cd Length: 188 Bit Score: 62.23 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 332 INGDIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDHsqslrvanglqveRLLRQNEEIKALDKEYsEIDIYSGTEMDI 411
Cdd:COG0613 2 MKIDLHVHTTASDGSLSPEELVARAKAAGLDVLAITDH-------------DTVAGYEEAAEAAKEL-GLLVIPGVEIST 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 412 LPDGS--------LDYDDEILAQLDYVIGAIHQSFNQSEEQIMERLANACRnpyVRHIAHPtgriiGRRDGYKPNIEQLM 483
Cdd:COG0613 68 RWEGRevhilgygIDPEDPALEALLGIPVEKAEREWLSLEEAIDLIREAGG---VAVLAHP-----FRYKRGRWLDDLLE 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 586232721 484 ALAEETNTVLEInANP-HRLDLN---AEIVRKYpNVKLTINTDAHHTNH 528
Cdd:COG0613 140 ELADAGLDGIEV-YNGrHSPEDNeraAELAEEY-GLLATGGSDAHGPEK 186
|
|
| PHP_HisPPase_AMP |
cd07438 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ... |
335-437 |
1.48e-10 |
|
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) AMP bound; The PHP domain of this HisPPase family has an unknown function. It has a second domain inserted in the middle that binds adenosine 5-monophosphate (AMP). The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to give histidinol. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to the other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213993 [Multi-domain] Cd Length: 155 Bit Score: 59.71 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 335 DIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDHSqslrVANGLqverllrqnEEIKALDKEYSeIDIYSGTEMdilpd 414
Cdd:cd07438 2 DLHTHSTASDGTLSPEELVELAKEAGLKVLAITDHD----TVAGL---------EEALAAAKELG-IELIPGVEI----- 62
|
90 100
....*....|....*....|....*.
gi 586232721 415 gSLDYDDE---ILAQLDYVIGAIHQS 437
Cdd:cd07438 63 -STEYEGRevhILGSPEEAIELIHAA 87
|
|
| PHP |
pfam02811 |
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ... |
335-436 |
3.48e-10 |
|
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative phosphoesterase domain.
Pssm-ID: 460705 [Multi-domain] Cd Length: 171 Bit Score: 59.09 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 335 DIHMHTTYS--DGAFSIRDMVEANIAKGYKFMVITDHSqslrvaNGLQVERLLrqnEEIKALdkeysEIDIYSGTEMDIL 412
Cdd:pfam02811 1 HLHVHSEYSllDGAARIEELVKRAKELGMPAIAITDHG------NLFGAVEFY---KAAKKA-----GIKPIIGCEVYVA 66
|
90 100
....*....|....*....|....
gi 586232721 413 PDGSLDYDDEILAQLDYVIGAIHQ 436
Cdd:pfam02811 67 PGSREETEKLLAKYFDLVLLAVHE 90
|
|
| hisJ_fam |
TIGR01856 |
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate ... |
335-456 |
1.67e-09 |
|
histidinol phosphate phosphatase, HisJ family; This model represents the histidinol phosphate phosphatase HisJ of Bacillus subtilis, and related proteins from a number of species within a larger family of phosphatases in the PHP hydrolase family. HisJ catalyzes the penultimate step of histidine biosynthesis but shows no homology to the functionally equivalent sequence in E. coli, a domain of the bifunctional HisB protein. Note, however, that many species have two members and that Clostridium perfringens, predicted not to make histidine, has five members of this family; this family is designated subfamily rather than equivalog to indicate that members may not all act as HisJ.
Pssm-ID: 273837 [Multi-domain] Cd Length: 253 Bit Score: 58.56 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 335 DIHMHTTYS-DGAFSIRDMVEANIAKGYKFMVITDHSQSLRVANG---LQVERLLRQ----NEEIKALDKEY-SEIDIYS 405
Cdd:TIGR01856 2 DSHSHSPFCaHGTDTLREVVQEAIQLGFEEICFTEHAPRPFYYPEedfLKKEMLFLSlpeyFQEINQLKQEYaDKIKILI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 586232721 406 GTEMDILPdGSLDYDDEIL--AQLDYVIGAIH----QSFNQSEEQIMERLANACRNP 456
Cdd:TIGR01856 82 GLEVDYIP-GFEEEIKDFLdsYNLDFVIGSVHhlggIPIDFDIEEFDETLFSFQKNL 137
|
|
| PHP_HisPPase |
cd07432 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ... |
335-525 |
1.09e-08 |
|
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. HisPPase can be classified into two types: the bifunctional HisPPase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213987 [Multi-domain] Cd Length: 129 Bit Score: 53.78 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 335 DIHMHTTYSDGAF-SIRDMVEANIAKGYKFMVITDHsqsLRVANGLQVERLlrqneeikaldKEYSEIDIYSGTEMDIlp 413
Cdd:cd07432 2 DLHIHSVFSPDSDmTPEEIVERAIELGLDGIAITDH---NTIDGAEEALKE-----------AYKDGLLVIPGVEVTL-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 414 dgsldyddeilaqldyVIgaihqsfnqseeqimerlanacrnpyvrhIAHPtgriiGRRDGYKPNIEQLMALAEEtNTVL 493
Cdd:cd07432 66 ----------------VV-----------------------------LAHP-----DRPSRYGLSDLILKPLIKN-GDAI 94
|
170 180 190
....*....|....*....|....*....|....*
gi 586232721 494 EINANPHRLDLNAEIVRKYPNVK---LTINTDAHH 525
Cdd:cd07432 95 EVNNSRLRYGLNNLAAKRYAELGglpITGGSDAHT 129
|
|
| PRK07945 |
PRK07945 |
PHP domain-containing protein; |
5-82 |
2.19e-08 |
|
PHP domain-containing protein;
Pssm-ID: 236135 [Multi-domain] Cd Length: 335 Bit Score: 56.14 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 5 DVIKLLEQIATYMELKGENTFKISAYRKAAQSLE-LDERPLDE---ISDVTELKGIGKGVAEVINDYRETGESQYLQQLQ 80
Cdd:PRK07945 2 DPVAALRRIAFLLERARADTYRVRAFRRAADVVEaLDAAERARrarAGSLTSLPGIGPKTAKVIAQALAGRVPDYLAELR 81
|
..
gi 586232721 81 EE 82
Cdd:PRK07945 82 AD 83
|
|
| PRK06361 |
PRK06361 |
histidinol phosphate phosphatase domain-containing protein; |
338-534 |
8.15e-08 |
|
histidinol phosphate phosphatase domain-containing protein;
Pssm-ID: 180543 [Multi-domain] Cd Length: 212 Bit Score: 53.04 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 338 MHTTYSDGAFSIRDMVEANIAKGYKFMVITDHsqslrvANGLQVERLLRQNEEIKALDKEYSEIDIYSGTEMDILPDGSL 417
Cdd:PRK06361 1 THTIFSDGELIPSELVRRARVLGYRAIAITDH------ADASNLEEILEKLVRAAEELELYWDIEVIPGVELTHVPPKLI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 418 DYddeiLAQLDYVIGA----IHQsfnqseEQIMERLAN-----ACRNPYVRHIAHPTgrIIGRRDGykpnieqlmALAEE 488
Cdd:PRK06361 75 PK----LAKKARDLGAeivvVHG------ETIVEPVEEgtnlaAIECEDVDILAHPG--LITEEEA---------ELAAE 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 586232721 489 TNTVLEINANP-HRLDlN---AEIVRKYpNVKLTINTDAHHTNhlDFMNY 534
Cdd:PRK06361 134 NGVFLEITARKgHSLT-NghvARIAREA-GAPLVINTDTHAPS--DLITY 179
|
|
| POLIIIAc |
smart00481 |
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ... |
335-370 |
5.30e-07 |
|
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family of hypothetical proteins
Pssm-ID: 197753 [Multi-domain] Cd Length: 67 Bit Score: 46.88 E-value: 5.30e-07
10 20 30
....*....|....*....|....*....|....*...
gi 586232721 335 DIHMHTTYS--DGAFSIRDMVEANIAKGYKFMVITDHS 370
Cdd:smart00481 1 DLHVHSDYSllDGALSPEELVKRAKELGLKAIAITDHG 38
|
|
| PHP |
cd07309 |
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ... |
334-411 |
7.76e-07 |
|
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PHP in polymerases has trinuclear zinc/magnesium dependent proofreading activity. It has also been shown that the PHP domain functions in DNA repair. The PHP structures have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213985 [Multi-domain] Cd Length: 88 Bit Score: 47.04 E-value: 7.76e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586232721 334 GDIHMHTTYSDGAF-SIRDMVEANIAKGYKFMVITDHSQSLRVANGLQVErllrQNEEIKALDKeySEIDIYSGTEMDI 411
Cdd:cd07309 1 VDLHTHTVFSDGDHaKLTELVDKAKELGPDALAITDHGNLRGLAEFNTAG----K*NHIKAAEA--AGIKIIIGSEVNL 73
|
|
| PHP_HisPPase_Thermotoga_like |
cd12111 |
Polymerase and Histidinol Phosphatase domain of Thermotoga like; The PHP (also called ... |
335-400 |
9.80e-06 |
|
Polymerase and Histidinol Phosphatase domain of Thermotoga like; The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. Thermotoga PHP is an uncharacterized protein. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to give histidinol. The HisPPase can be classified into two types: the bifunctional HisPPase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213995 [Multi-domain] Cd Length: 226 Bit Score: 47.03 E-value: 9.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586232721 335 DIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDHsqslrVANGLQVERLLRQNEEIKALDKEYSE 400
Cdd:cd12111 5 DFHIHTTYSDGALSLSEVVDLYGQHGFDVIAITDH-----VVDRASLIGKFPQGTHPGVTEANFED 65
|
|
| PRK07328 |
PRK07328 |
histidinol-phosphatase; Provisional |
335-524 |
1.15e-05 |
|
histidinol-phosphatase; Provisional
Pssm-ID: 235992 [Multi-domain] Cd Length: 269 Bit Score: 47.32 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 335 DIHMHTTYSDGAF-SIRDMVEANIAKGYKFMVITDHS------QSLRVANG-LQVERLLRQNEEIKALDKEYSEIDIYSG 406
Cdd:PRK07328 5 DYHMHTPLCGHAVgTPEEYVQAARRAGLKEIGFTDHLpmyflpPEWRDPGLaMRLEELPFYVSEVERLRARFPDLYVRLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586232721 407 TEMDILPdGSLDYDDEILAQ--LDYVIGAIH----QSFNQSE--EQIMER------------LANACRNPYVRHIAHPTg 466
Cdd:PRK07328 85 IEADYHP-GTEEFLERLLEAypFDYVIGSVHylgaWGFDNPDfvAEYEERdldelyrryfalVEQAARSGLFDIIGHPD- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586232721 467 riIGRRDGYKPNiEQLMALAEETNTVleINANPHRLDLNAEIVRK-----YP-----------NVKLTINTDAH 524
Cdd:PRK07328 163 --LIKKFGHRPR-EDLTELYEEALDV--IAAAGLALEVNTAGLRKpvgeiYPspallracrerGIPVVLGSDAH 231
|
|
| CehA_McbA_metalo |
NF038032 |
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ... |
334-369 |
1.17e-05 |
|
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is found in several partially characterized metallohydrolases, including McbA and CehA. Both were studied as hydrolases of carbaryl, a xenobiotic compound that does not contain a phosphate group, suggesting that presuming members of this family to be phosphoesterases (like many PHP domain-containing proteins) may be incorrect.
Pssm-ID: 468321 [Multi-domain] Cd Length: 315 Bit Score: 47.32 E-value: 1.17e-05
10 20 30
....*....|....*....|....*....|....*.
gi 586232721 334 GDIHMHTTYSDGAFSIRDMVEANIAKGYKFMVITDH 369
Cdd:NF038032 5 GDLHIHTNHSDGPTTPEELARAALAEGLDVIALTDH 40
|
|
| DnaE |
COG0587 |
DNA polymerase III, alpha subunit [Replication, recombination and repair]; |
337-369 |
2.61e-03 |
|
DNA polymerase III, alpha subunit [Replication, recombination and repair];
Pssm-ID: 440352 [Multi-domain] Cd Length: 1050 Bit Score: 40.82 E-value: 2.61e-03
10 20 30
....*....|....*....|....*....|....*
gi 586232721 337 HMHTTYS--DGAFSIRDMVEANIAKGYKFMVITDH 369
Cdd:COG0587 9 HVHSEYSllDGASRPEELVARAAELGMPALAITDH 43
|
|
| PHP_PolIIIA |
cd07431 |
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III; ... |
337-369 |
9.55e-03 |
|
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III; PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that is responsible for the replication of the DNA duplex. The alpha subunit of DNA polymerase III core enzyme catalyzes the reaction for polymerizing both DNA strands. The PolIIIA PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination, and like other PHP structures, exhibits a distorted (beta/alpha) 7 barrel and coordinates up to 3 metals. Initially, it was proposed that PHP region might be involved in pyrophosphate hydrolysis, but such activity has not been found. It has been shown that the PHP domain of PolIIIA has a trinuclear metal complex and is capable of proofreading activity.
Pssm-ID: 213986 [Multi-domain] Cd Length: 179 Bit Score: 37.57 E-value: 9.55e-03
10 20 30
....*....|....*....|....*....|....*
gi 586232721 337 HMHTTYS--DGAFSIRDMVEANIAKGYKFMVITDH 369
Cdd:cd07431 4 HVHSSYSllDSAIRPEDLVARAKELGYSALALTDR 38
|
|
| |
