|
Name |
Accession |
Description |
Interval |
E-value |
| PHP_PolX |
cd07436 |
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ... |
312-547 |
6.27e-143 |
|
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: 411.81 E-value: 6.27e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 312 DDLKGTLHNHSTYSDGVHSLAEMARYCKdELGLNYFGICDHSKTAVYANGLSIERVQKQWEEIDLLNQELAPFKIFKGIE 391
Cdd:cd07436 3 KDIRGDLHVHTTWSDGRNSIEEMAEAAR-ALGYEYIAITDHSKSLRVANGLSEERLREQIEEIDALNEKLPGIRILKGIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 392 SDILGDGSLDYPDEVLAGFDFVVASVHSNLKMDEEKATARLLKAIENPYTTILGHPTGRLLLSRSGYPLDYKKIIDACAV 471
Cdd:cd07436 82 VDILPDGSLDYPDEVLAELDVVVASVHSGFNQSEEEMTERLLKAIENPHVDILGHPTGRLLGRREGYEVDMERVIEAAAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740914082 472 NNVVIEINANPLRLDLDWRWHRYAIEKGVLLAINPDAHRTEGLKDMHYGIFVARKGGLSAKNCLNSFSLSEIEDFL 547
Cdd:cd07436 162 TGTALEINANPDRLDLDDRHARRAKEAGVKIAINTDAHSTDGLDNMRYGVGTARRGWLEKEDVLNTLPLEELLKFL 237
|
|
| PolX |
COG1796 |
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair]; |
1-546 |
4.77e-139 |
|
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
Pssm-ID: 441401 [Multi-domain] Cd Length: 567 Bit Score: 414.20 E-value: 4.77e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 1 MDNKTIAKKFKLCSQLMELHNENPFRTKAIASASFKLDKVPF----LLETASFEEIssqPGIGKSTAEKVKKLAETGSFD 76
Cdd:COG1796 1 MDNKEIARILEEIADLLELKGENPFKIRAYRRAARAIENLPEdieeLVAEGDLTEI---PGIGKAIAAKIEELLETGRLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 77 ELDAMLSITPEGILEMLNIKGLGPKKIQIIWNDLQIESVGELLYACNENRLIEAKGFGLKTQEDIKKSIEFSISNEGWFL 156
Cdd:COG1796 78 ELEELREEVPPGLLELLRIPGLGPKKVKKLYEELGITSLEELEAAAEEGRIRELPGFGEKTEENILKGIELLRKRGGRFL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 157 YAKVLSHAEKLFTKLQKSLSPTLISFTGDFRRKCEVLSSVDILLDTDKNSTLTYLNTNYPNsLKEEIEY----TALRDEN 232
Cdd:COG1796 158 LGEALPLAEEILAYLRALPGVERVEVAGSLRRRKETVGDIDILVASDDPEAVMDAFVKLPE-VKEVLAKgdtkASVRLKS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 233 GFSFHIYLTTTGDFHKNLLLTTGSKKH-------------------LEGLNHDLItALASEQALYMAQGMDYIEPELREG 293
Cdd:COG1796 237 GLQVDLRVVPPESFGAALQYFTGSKEHnvalrqlakerglklneygLFDVGGERI-AGETEEEVYAALGLPYIPPELRED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 294 LNEIILAKAHELPILINFDDLKGTLHNHSTYSDGVHSLAEMARYCKdELGLNYFGICDHSKTAVYANGLSIERVQKQWEE 373
Cdd:COG1796 316 RGEIEAAEEGRLPELVELDDIRGDLHHHTTWSDGGASIEEMAAAAA-ARGYYYIAITDHSSSLVVAGGLDEERLLQQEEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 374 IDLLNQELAPFKIFKGIESDILGDGSLDYPDEVLAGFDFVVASVHSNLKMDEEKATARLLKAIENPYTTILGHPTGRLLL 453
Cdd:COG1796 395 IDALNERLDGIILLLGGEEDILDDGGLDDDDDLLLEDDDVVAAVHHSFLLQDEEMTRRRLAAANEPVVVIIHHPTGRLLL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 454 SRSGYPLDYKKIIDACAVNNVVIEINANPLRLDLDWRWHRYAIEKGVLLAINPDAHRTEGLKDMHYGIFVARKGGLSAKN 533
Cdd:COG1796 475 RRRPYYVDDEAIIAAAAAAGALEEENNAPRRLLLLDDLARAAAEGGVVIIIIDDAHHTDLLLDLMGGGVAARRRWWLEKD 554
|
570
....*....|...
gi 740914082 534 CLNSFSLSEIEDF 546
Cdd:COG1796 555 VNNNTLLLELLLL 567
|
|
| PRK08609 |
PRK08609 |
DNA polymerase/3'-5' exonuclease PolX; |
1-551 |
1.08e-125 |
|
DNA polymerase/3'-5' exonuclease PolX;
Pssm-ID: 236311 [Multi-domain] Cd Length: 570 Bit Score: 380.07 E-value: 1.08e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 1 MDNKTIAKKFKLCSQLMELHNENPFRTKAI--ASASFKLDKVPfLLETASFEEIssqPGIGKSTAEKVKKLAETGSFDEL 78
Cdd:PRK08609 1 MNKKDVIKLLETIATYMELKGENPFKISAFrkAAQALELDERS-LSEIDDFTKL---KGIGKGTAEVIQEYRETGESSVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 79 DAMLSITPEGILEMLNIKGLGPKKIQIIWNDLQIESVGELLYACNENRLIEAKGFGLKTQEDIKKSIEFSISNEGWFLYA 158
Cdd:PRK08609 77 QELKKEVPEGLLPLLKLPGLGGKKIAKLYKELGVVDKESLKEACENGKVQALAGFGKKTEEKILEAVKELGKRPERLPIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 159 KVLSHAEKLFTKLQKSLSPTLISFTGDFRRKCEVLSSVDILLDTDKNSTLTYLNTNYPN------------SLKEEIEYT 226
Cdd:PRK08609 157 QVLPIAQEIEEYLATIDEIIRFSRAGSLRRARETVKDLDFIIATDEPEAVREQLLQLPNiveviaagdtkvSVELEYEYT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 227 ALRDengfsFHiyLTTTGDFHKNLLLTTGSKKH-------------------LEGLNHDLITALASEQALYMAQGMDYIE 287
Cdd:PRK08609 237 ISVD-----FR--LVEPEAFATTLHHFTGSKDHnvrmrqlakergekiseygVEQADTGEVKTFESEEAFFAHFGLPFIP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 288 PELREGLNEIilAKAHELPILINFDDLKGTLHNHSTYSDGVHSLAEMARYCKdELGLNYFGICDHSKTAVYANGLSIERV 367
Cdd:PRK08609 310 PEVREDGSEF--ERYKDLSNLITLSDIQGDLHMHTTWSDGAFSIEEMVEACI-AKGYEYMAITDHSQYLKVANGLTEERL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 368 QKQWEEIDLLNQELAPFKIFKGIESDILGDGSLDYPDEVLAGFDFVVASVHSNLKMDEEKATARLLKAIENPYTTILGHP 447
Cdd:PRK08609 387 LEQAEEIKALNEKYPEIDILSGIEMDILPDGSLDYDDEVLAELDYVIAAIHSSFSQSEEEIMKRLENACRNPYVRLIAHP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 448 TGRLLLSRSGYPLDYKKIIDACAVNNVVIEINANPLRLDLDWRWHRYAIEKGVLLAINPDAHRTEGLKDMHYGIFVARKG 527
Cdd:PRK08609 467 TGRLIGRRDGYDVNIDQLIELAKETNTALELNANPNRLDLSAEHLKKAQEAGVKLAINTDAHHTEMLDDMKYGVATARKG 546
|
570 580
....*....|....*....|....
gi 740914082 528 GLSAKNCLNSFSLSEIEDFLSKKD 551
Cdd:PRK08609 547 WIQKDRVINTWSREEFKDFIKRNK 570
|
|
| HIS2 |
COG1387 |
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ... |
314-546 |
3.15e-107 |
|
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: 320.56 E-value: 3.15e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 314 LKGTLHNHSTYSDGVHSLAEMARYCKdELGLNYFGICDHSKTAVYANGLSIERVQKQWEEIDLLNQELAPFKIFKGIESD 393
Cdd:COG1387 1 MRGDLHTHTTYSDGEGTIEEMVEAAI-ELGLEYIAITDHSPSLFVANGLSEERLLEYLEEIEELNEKYPDIKILKGIEVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 394 ILGDGSLDYPDEVLAGFDFVVASVHSNLKMDEEKATARLLKAIENPYTTILGHPTGRLLLSRSGYPLDYKKIIDACAVNN 473
Cdd:COG1387 80 ILPDGSLDYPDELLAPLDYVIGSVHSILEEDYEEYTERLLKAIENPLVDILGHPDGRLLGGRPGYEVDIEEVLEAAAENG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740914082 474 VVIEINANPLRLDLDWRWHRYAIEKGVLLAINPDAHRTEGLKDMHYGIFVARKGGLSAKNCLNSFSLSEIEDF 546
Cdd:COG1387 160 VALEINTRPLRLDPSDELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFNTLRKEELLKL 232
|
|
| PRK07945 |
PRK07945 |
PHP domain-containing protein; |
314-543 |
3.23e-65 |
|
PHP domain-containing protein;
Pssm-ID: 236135 [Multi-domain] Cd Length: 335 Bit Score: 215.61 E-value: 3.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 314 LKGTLHNHSTYSDGVHSLAEMARYCKDeLGLNYFGICDHSKTAVYANGLSIERVQKQWEEIDLLNQELAPFKIFKGIESD 393
Cdd:PRK07945 96 LRGDLHTHSDWSDGGSPIEEMARTAAA-LGHEYCALTDHSPRLTVANGLSAERLRKQLDVVAELNEELAPFRILTGIEVD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 394 ILGDGSLDYPDEVLAGFDFVVASVHSNLKMDEEKATARLLKAIENPYTTILGHPTGRLLL-SRSGYP---LDYKKIIDAC 469
Cdd:PRK07945 175 ILDDGSLDQEPELLDRLDVVVASVHSKLRMDAAAMTRRMLAAVANPHTDVLGHCTGRLVTgNRGTRPeskFDAEAVFAAC 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740914082 470 AVNNVVIEINANPLRLDLDWRWHRYAIEKGVLLAINPDAHRTEGLKDMHYGIFVARKGGLSAKNCLNSFSLSEI 543
Cdd:PRK07945 255 REHGTAVEINSRPERRDPPTRLLRLALDAGCLFSIDTDAHAPGQLDWLGYGCERAEEAGVPADRIVNTWPADRL 328
|
|
| NT_POLXc |
cd00141 |
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ... |
6-291 |
5.80e-27 |
|
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: 111.13 E-value: 5.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 6 IAKKFKLCSQLMELHNENPFRTKAIASASFKLDKVPFllETASFEEISSQPGIGKSTAEKVKKLAETGSFDELDAMLSIT 85
Cdd:cd00141 3 IADILEELADLLELLGGNPFRVRAYRKAARALESLPE--PIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELREDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 86 PEGILEMLNIKGLGPKKIQiIWNDLQIESVGELLYACnenrlieakgfGLKTQEDIKKSIEFSISNEGWFLYAKVLSHAE 165
Cdd:cd00141 81 PPGLLLLLRVPGVGPKTAR-KLYELGIRTLEDLRKAA-----------GAKLEQNILIGLEYYEDFQQRIPREEALAIAE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 166 KLFTKLQKSLSPTLISFTGDFRRKCEVLSSVDILL---DTDKNSTLTYL---NTNYPnslkeEIEYTALRDENGFSF--- 236
Cdd:cd00141 149 IIKEALREVDPVLQVEIAGSYRRGKETVGDIDILVthpDATSRGLLEKVvdaLVELG-----FVTEVLSKGDTKASGilk 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 237 --HIYLTTTGD--------FHKNLLLTTGSKKH-------------------LEGLNHDLITALASEQALYMAQGMDYIE 287
Cdd:cd00141 224 lpGGWKGRRVDlrvvppeeFGAALLYFTGSKQFnralrrlakekglklneygLFDGVDGERLPGETEEEIFEALGLPYIE 303
|
....
gi 740914082 288 PELR 291
Cdd:cd00141 304 PELR 307
|
|
| POLXc |
smart00483 |
DNA polymerase X family; includes vertebrate polymerase beta and terminal ... |
3-292 |
2.66e-13 |
|
DNA polymerase X family; includes vertebrate polymerase beta and terminal deoxynucleotidyltransferases
Pssm-ID: 214688 Cd Length: 334 Bit Score: 71.24 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 3 NKTIAKKFKLCSQLMELHNENPFRTKAIASASFKLDKVPFLLEtaSFEEISSQPGIGKSTAEKVKKLAETG-SFDELDAM 81
Cdd:smart00483 3 NRGIIDALEILAENYEVFGENKRKCSYFRKAASVLKSLPFPIN--SMKDLKGLPGIGDKIKKKIEEIIETGkSSKVLEIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 82 LSITPEGILEMLNIKGLGPKKIQiIWNDLQIESVGELLYACNEnRLIEAKGFGLKTQEDIKKSI---EFSIsnegwflya 158
Cdd:smart00483 81 NDEVYKSLKLFTNVFGVGPKTAA-KWYRKGIRTLEELKKNKEL-KLTKQQKAGLKYYEDILKKVsraEAFA--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 159 kVLSHAEKLFTKLQKSLSPTLisfTGDFRRKCEVLSSVDILLDTD---KNSTLTYLNTNYPNSL---------------- 219
Cdd:smart00483 150 -VEYIVKRAVRKILPDAIVTL---TGSFRRGKETGHDVDFLITSPhpaKEKELEVLDLLLLESTfeelqlpsirvatldh 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 220 -------------KEEIEYTALRDENG---FSFHIYLTTTGDFHKNLLLTTGSKKHLEGL-------------NHDLITA 270
Cdd:smart00483 226 gqkkfmilklspsREDKEKSGKPDEKGwkaRRVDIVLCPEDQYPTALLGWTGSKQFNRDLrryatskfklmldGHELYDK 305
|
330 340
....*....|....*....|....*....
gi 740914082 271 -------LASEQALYMAQGMDYIEPELRE 292
Cdd:smart00483 306 tkekflkVESEEDIFDHLGLPYIEPEERN 334
|
|
| HHH_8 |
pfam14716 |
Helix-hairpin-helix domain; |
3-71 |
4.74e-10 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434152 [Multi-domain] Cd Length: 67 Bit Score: 55.59 E-value: 4.74e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740914082 3 NKTIAKKFKLCSQLMELHNENPFRTKAIASASFKLDKVPFllETASFEEISSQPGIGKSTAEKVKKLAE 71
Cdd:pfam14716 1 NQEIADALEELADLLELKGEDPFRVRAYRRAARALEALPE--EITSLEELTKLPGIGKKIAAKIEEILE 67
|
|
| PHP |
pfam02811 |
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ... |
318-481 |
1.23e-05 |
|
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative phosphoesterase domain.
Pssm-ID: 460705 [Multi-domain] Cd Length: 171 Bit Score: 45.61 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 318 LHNHSTYS--DGVHSLAEMARYCKdELGLNYFGICDHSktavyaNGLSIERVQKQWEEIDLlnqelapfKIFKGIESDIL 395
Cdd:pfam02811 2 LHVHSEYSllDGAARIEELVKRAK-ELGMPAIAITDHG------NLFGAVEFYKAAKKAGI--------KPIIGCEVYVA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 396 GDGSLDYPDEVLAGFDFVVASVH----SNL-KMDE----EKATARLLKAIENPYT--------TILGHPtGRLLLSRSGY 458
Cdd:pfam02811 67 PGSREETEKLLAKYFDLVLLAVHevgyKNLiKLSSraylEGFKPRIDKELLEEYFeglialsgCVLGHL-DLILLAPGDY 145
|
170 180
....*....|....*....|....*..
gi 740914082 459 PlDYKKIIDAC----AVNNVVIEINAN 481
Cdd:pfam02811 146 E-EAEELAEEYleifGEDGFYLEINTH 171
|
|
| POLIIIAc |
smart00481 |
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ... |
318-395 |
1.35e-04 |
|
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: 40.33 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 318 LHNHSTYS--DGVHSLAEMARYCKdELGLNYFGICDHSktaVYANGLSIERVQKQweeidllnqelAPFKIFKGIESDIL 395
Cdd:smart00481 2 LHVHSDYSllDGALSPEELVKRAK-ELGLKAIAITDHG---NLFGAVEFYKAAKK-----------AGIKPIIGLEANIV 66
|
|
| CehA_McbA_metalo |
NF038032 |
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ... |
314-356 |
3.37e-03 |
|
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: 39.61 E-value: 3.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 740914082 314 LKGTLHNHSTYSDGVHSLAEMARYCKDElGLNYFGICDHSKTA 356
Cdd:NF038032 3 YSGDLHIHTNHSDGPTTPEELARAALAE-GLDVIALTDHNTIS 44
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PHP_PolX |
cd07436 |
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ... |
312-547 |
6.27e-143 |
|
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: 411.81 E-value: 6.27e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 312 DDLKGTLHNHSTYSDGVHSLAEMARYCKdELGLNYFGICDHSKTAVYANGLSIERVQKQWEEIDLLNQELAPFKIFKGIE 391
Cdd:cd07436 3 KDIRGDLHVHTTWSDGRNSIEEMAEAAR-ALGYEYIAITDHSKSLRVANGLSEERLREQIEEIDALNEKLPGIRILKGIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 392 SDILGDGSLDYPDEVLAGFDFVVASVHSNLKMDEEKATARLLKAIENPYTTILGHPTGRLLLSRSGYPLDYKKIIDACAV 471
Cdd:cd07436 82 VDILPDGSLDYPDEVLAELDVVVASVHSGFNQSEEEMTERLLKAIENPHVDILGHPTGRLLGRREGYEVDMERVIEAAAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740914082 472 NNVVIEINANPLRLDLDWRWHRYAIEKGVLLAINPDAHRTEGLKDMHYGIFVARKGGLSAKNCLNSFSLSEIEDFL 547
Cdd:cd07436 162 TGTALEINANPDRLDLDDRHARRAKEAGVKIAINTDAHSTDGLDNMRYGVGTARRGWLEKEDVLNTLPLEELLKFL 237
|
|
| PolX |
COG1796 |
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair]; |
1-546 |
4.77e-139 |
|
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
Pssm-ID: 441401 [Multi-domain] Cd Length: 567 Bit Score: 414.20 E-value: 4.77e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 1 MDNKTIAKKFKLCSQLMELHNENPFRTKAIASASFKLDKVPF----LLETASFEEIssqPGIGKSTAEKVKKLAETGSFD 76
Cdd:COG1796 1 MDNKEIARILEEIADLLELKGENPFKIRAYRRAARAIENLPEdieeLVAEGDLTEI---PGIGKAIAAKIEELLETGRLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 77 ELDAMLSITPEGILEMLNIKGLGPKKIQIIWNDLQIESVGELLYACNENRLIEAKGFGLKTQEDIKKSIEFSISNEGWFL 156
Cdd:COG1796 78 ELEELREEVPPGLLELLRIPGLGPKKVKKLYEELGITSLEELEAAAEEGRIRELPGFGEKTEENILKGIELLRKRGGRFL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 157 YAKVLSHAEKLFTKLQKSLSPTLISFTGDFRRKCEVLSSVDILLDTDKNSTLTYLNTNYPNsLKEEIEY----TALRDEN 232
Cdd:COG1796 158 LGEALPLAEEILAYLRALPGVERVEVAGSLRRRKETVGDIDILVASDDPEAVMDAFVKLPE-VKEVLAKgdtkASVRLKS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 233 GFSFHIYLTTTGDFHKNLLLTTGSKKH-------------------LEGLNHDLItALASEQALYMAQGMDYIEPELREG 293
Cdd:COG1796 237 GLQVDLRVVPPESFGAALQYFTGSKEHnvalrqlakerglklneygLFDVGGERI-AGETEEEVYAALGLPYIPPELRED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 294 LNEIILAKAHELPILINFDDLKGTLHNHSTYSDGVHSLAEMARYCKdELGLNYFGICDHSKTAVYANGLSIERVQKQWEE 373
Cdd:COG1796 316 RGEIEAAEEGRLPELVELDDIRGDLHHHTTWSDGGASIEEMAAAAA-ARGYYYIAITDHSSSLVVAGGLDEERLLQQEEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 374 IDLLNQELAPFKIFKGIESDILGDGSLDYPDEVLAGFDFVVASVHSNLKMDEEKATARLLKAIENPYTTILGHPTGRLLL 453
Cdd:COG1796 395 IDALNERLDGIILLLGGEEDILDDGGLDDDDDLLLEDDDVVAAVHHSFLLQDEEMTRRRLAAANEPVVVIIHHPTGRLLL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 454 SRSGYPLDYKKIIDACAVNNVVIEINANPLRLDLDWRWHRYAIEKGVLLAINPDAHRTEGLKDMHYGIFVARKGGLSAKN 533
Cdd:COG1796 475 RRRPYYVDDEAIIAAAAAAGALEEENNAPRRLLLLDDLARAAAEGGVVIIIIDDAHHTDLLLDLMGGGVAARRRWWLEKD 554
|
570
....*....|...
gi 740914082 534 CLNSFSLSEIEDF 546
Cdd:COG1796 555 VNNNTLLLELLLL 567
|
|
| PRK08609 |
PRK08609 |
DNA polymerase/3'-5' exonuclease PolX; |
1-551 |
1.08e-125 |
|
DNA polymerase/3'-5' exonuclease PolX;
Pssm-ID: 236311 [Multi-domain] Cd Length: 570 Bit Score: 380.07 E-value: 1.08e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 1 MDNKTIAKKFKLCSQLMELHNENPFRTKAI--ASASFKLDKVPfLLETASFEEIssqPGIGKSTAEKVKKLAETGSFDEL 78
Cdd:PRK08609 1 MNKKDVIKLLETIATYMELKGENPFKISAFrkAAQALELDERS-LSEIDDFTKL---KGIGKGTAEVIQEYRETGESSVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 79 DAMLSITPEGILEMLNIKGLGPKKIQIIWNDLQIESVGELLYACNENRLIEAKGFGLKTQEDIKKSIEFSISNEGWFLYA 158
Cdd:PRK08609 77 QELKKEVPEGLLPLLKLPGLGGKKIAKLYKELGVVDKESLKEACENGKVQALAGFGKKTEEKILEAVKELGKRPERLPIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 159 KVLSHAEKLFTKLQKSLSPTLISFTGDFRRKCEVLSSVDILLDTDKNSTLTYLNTNYPN------------SLKEEIEYT 226
Cdd:PRK08609 157 QVLPIAQEIEEYLATIDEIIRFSRAGSLRRARETVKDLDFIIATDEPEAVREQLLQLPNiveviaagdtkvSVELEYEYT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 227 ALRDengfsFHiyLTTTGDFHKNLLLTTGSKKH-------------------LEGLNHDLITALASEQALYMAQGMDYIE 287
Cdd:PRK08609 237 ISVD-----FR--LVEPEAFATTLHHFTGSKDHnvrmrqlakergekiseygVEQADTGEVKTFESEEAFFAHFGLPFIP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 288 PELREGLNEIilAKAHELPILINFDDLKGTLHNHSTYSDGVHSLAEMARYCKdELGLNYFGICDHSKTAVYANGLSIERV 367
Cdd:PRK08609 310 PEVREDGSEF--ERYKDLSNLITLSDIQGDLHMHTTWSDGAFSIEEMVEACI-AKGYEYMAITDHSQYLKVANGLTEERL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 368 QKQWEEIDLLNQELAPFKIFKGIESDILGDGSLDYPDEVLAGFDFVVASVHSNLKMDEEKATARLLKAIENPYTTILGHP 447
Cdd:PRK08609 387 LEQAEEIKALNEKYPEIDILSGIEMDILPDGSLDYDDEVLAELDYVIAAIHSSFSQSEEEIMKRLENACRNPYVRLIAHP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 448 TGRLLLSRSGYPLDYKKIIDACAVNNVVIEINANPLRLDLDWRWHRYAIEKGVLLAINPDAHRTEGLKDMHYGIFVARKG 527
Cdd:PRK08609 467 TGRLIGRRDGYDVNIDQLIELAKETNTALELNANPNRLDLSAEHLKKAQEAGVKLAINTDAHHTEMLDDMKYGVATARKG 546
|
570 580
....*....|....*....|....
gi 740914082 528 GLSAKNCLNSFSLSEIEDFLSKKD 551
Cdd:PRK08609 547 WIQKDRVINTWSREEFKDFIKRNK 570
|
|
| HIS2 |
COG1387 |
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ... |
314-546 |
3.15e-107 |
|
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: 320.56 E-value: 3.15e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 314 LKGTLHNHSTYSDGVHSLAEMARYCKdELGLNYFGICDHSKTAVYANGLSIERVQKQWEEIDLLNQELAPFKIFKGIESD 393
Cdd:COG1387 1 MRGDLHTHTTYSDGEGTIEEMVEAAI-ELGLEYIAITDHSPSLFVANGLSEERLLEYLEEIEELNEKYPDIKILKGIEVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 394 ILGDGSLDYPDEVLAGFDFVVASVHSNLKMDEEKATARLLKAIENPYTTILGHPTGRLLLSRSGYPLDYKKIIDACAVNN 473
Cdd:COG1387 80 ILPDGSLDYPDELLAPLDYVIGSVHSILEEDYEEYTERLLKAIENPLVDILGHPDGRLLGGRPGYEVDIEEVLEAAAENG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740914082 474 VVIEINANPLRLDLDWRWHRYAIEKGVLLAINPDAHRTEGLKDMHYGIFVARKGGLSAKNCLNSFSLSEIEDF 546
Cdd:COG1387 160 VALEINTRPLRLDPSDELLKLAKELGVKITIGSDAHSPEDLGDLEYGVALARRAGLTKEDVFNTLRKEELLKL 232
|
|
| PRK07945 |
PRK07945 |
PHP domain-containing protein; |
314-543 |
3.23e-65 |
|
PHP domain-containing protein;
Pssm-ID: 236135 [Multi-domain] Cd Length: 335 Bit Score: 215.61 E-value: 3.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 314 LKGTLHNHSTYSDGVHSLAEMARYCKDeLGLNYFGICDHSKTAVYANGLSIERVQKQWEEIDLLNQELAPFKIFKGIESD 393
Cdd:PRK07945 96 LRGDLHTHSDWSDGGSPIEEMARTAAA-LGHEYCALTDHSPRLTVANGLSAERLRKQLDVVAELNEELAPFRILTGIEVD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 394 ILGDGSLDYPDEVLAGFDFVVASVHSNLKMDEEKATARLLKAIENPYTTILGHPTGRLLL-SRSGYP---LDYKKIIDAC 469
Cdd:PRK07945 175 ILDDGSLDQEPELLDRLDVVVASVHSKLRMDAAAMTRRMLAAVANPHTDVLGHCTGRLVTgNRGTRPeskFDAEAVFAAC 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740914082 470 AVNNVVIEINANPLRLDLDWRWHRYAIEKGVLLAINPDAHRTEGLKDMHYGIFVARKGGLSAKNCLNSFSLSEI 543
Cdd:PRK07945 255 REHGTAVEINSRPERRDPPTRLLRLALDAGCLFSIDTDAHAPGQLDWLGYGCERAEEAGVPADRIVNTWPADRL 328
|
|
| PHP_HisPPase_Ycdx_like |
cd07437 |
Polymerase and Histidinol Phosphatase domain of Ycdx like; PHP Ycdx-like is a stand alone PHP ... |
318-550 |
4.60e-31 |
|
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: 120.62 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 318 LHNHSTYSDgvH---SLAEMARYCKdELGLNYFGICDH------SKTAVYANGLSIerVQKQWEEIdllnqelapfKIFK 388
Cdd:cd07437 5 LHTHTIASG--HaysTIEEMARAAA-EKGLKLLGITDHgpampgAPHPWYFGNLKV--IPREIYGV----------RILR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 389 GIESDILG-DGSLDYPDEVLAGFDFVVASVHSN--LKMDEEKATARLLKAIENPYTTILGHPTgrlllsRSGYPLDYKKI 465
Cdd:cd07437 70 GVEANIIDyDGNLDLPERVLKRLDYVIASLHEPcfAPGTKEENTRAYINAMENPYVDIIGHPG------NPRYPIDYEAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 466 IDACAVNNVVIEINANPLRLdldWRWH---------RYAIEKGVLLAINPDAHRTEGLKDMHYGIFVARKGGLSAKNCLN 536
Cdd:cd07437 144 VKAAKEYNVLLEINNSSLSP---SRKGsrencreiaELCKKYGVPVIVGSDAHIAYDIGNFDEALELLEEIGFPEELILN 220
|
250
....*....|....
gi 740914082 537 SfSLSEIEDFLSKK 550
Cdd:cd07437 221 T-SPERLLDFLKLR 233
|
|
| NT_POLXc |
cd00141 |
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ... |
6-291 |
5.80e-27 |
|
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: 111.13 E-value: 5.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 6 IAKKFKLCSQLMELHNENPFRTKAIASASFKLDKVPFllETASFEEISSQPGIGKSTAEKVKKLAETGSFDELDAMLSIT 85
Cdd:cd00141 3 IADILEELADLLELLGGNPFRVRAYRKAARALESLPE--PIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELREDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 86 PEGILEMLNIKGLGPKKIQiIWNDLQIESVGELLYACnenrlieakgfGLKTQEDIKKSIEFSISNEGWFLYAKVLSHAE 165
Cdd:cd00141 81 PPGLLLLLRVPGVGPKTAR-KLYELGIRTLEDLRKAA-----------GAKLEQNILIGLEYYEDFQQRIPREEALAIAE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 166 KLFTKLQKSLSPTLISFTGDFRRKCEVLSSVDILL---DTDKNSTLTYL---NTNYPnslkeEIEYTALRDENGFSF--- 236
Cdd:cd00141 149 IIKEALREVDPVLQVEIAGSYRRGKETVGDIDILVthpDATSRGLLEKVvdaLVELG-----FVTEVLSKGDTKASGilk 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 237 --HIYLTTTGD--------FHKNLLLTTGSKKH-------------------LEGLNHDLITALASEQALYMAQGMDYIE 287
Cdd:cd00141 224 lpGGWKGRRVDlrvvppeeFGAALLYFTGSKQFnralrrlakekglklneygLFDGVDGERLPGETEEEIFEALGLPYIE 303
|
....
gi 740914082 288 PELR 291
Cdd:cd00141 304 PELR 307
|
|
| PRK09248 |
PRK09248 |
putative hydrolase; Validated |
318-551 |
4.41e-19 |
|
putative hydrolase; Validated
Pssm-ID: 236429 [Multi-domain] Cd Length: 246 Bit Score: 86.82 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 318 LHNHsTYSDGvH---SLAEMARYCKdELGLNYFGICDHsktavyanGLSIERVQKQWEEIDL--LNQELAPFKIFKGIES 392
Cdd:PRK09248 7 THTH-TIASG-HaysTLHENAAEAK-QKGLKLFAITDH--------GPDMPGAPHYWHFGNLrvLPRKVDGVGILRGIEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 393 DILG-DGSLDYPDEVLAGFDFVVASVHSNL--KMDEEKATARLLKAIENPYTTILGHPtgrlllSRSGYPLDYKKIIDAC 469
Cdd:PRK09248 76 NIKNyDGEIDLPGDMLKKLDIVIAGFHEPVfaPGDKETNTQALINAIKNGRVDIIGHP------GNPKYPIDIEAVVKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 470 AVNNVVIEINANPL---RLDLDWRWHRYAI---EKGVLLAINPDAHRTEGLKDMHYGIFVARKGGLSAKNCLNSfSLSEI 543
Cdd:PRK09248 150 KEHNVALEINNSSFghsRKGSEDNCRAIAAlckKAGVWVALGSDAHIAFDIGNFEEALKILDEVGFPEERILNV-SPRRL 228
|
....*...
gi 740914082 544 EDFLSKKD 551
Cdd:PRK09248 229 LDFLESRG 236
|
|
| PRK08392 |
PRK08392 |
hypothetical protein; Provisional |
318-528 |
1.80e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 169423 [Multi-domain] Cd Length: 215 Bit Score: 78.29 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 318 LHNHSTYSDGVHSLAEMARYCkDELGLNYFGICDHSKTAVYANGLSIERVQKQWEEidllNQELApfkIFKGIESDILGD 397
Cdd:PRK08392 3 LHTHTVYSDGIGSVRDNIAEA-ERKGLRLVGISDHIHYFTPSKFNAYINEIRQWGE----ESEIV---VLAGIEANITPN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 398 GsLDYPDEVLAGFDFVVASVHSNLKMDEEKATARLLK-AIENPYTTILGHPTGrlLLSRSGYPL--DYKKIIDACAVNNV 474
Cdd:PRK08392 75 G-VDITDDFAKKLDYVIASVHEWFGRPEHHEYIELVKlALMDENVDIIGHFGN--SFPYIGYPSeeELKEILDLAEAYGK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 740914082 475 VIEINANPLRLDLDWRwhRYAIEKGVLLAINPDAHRTEGLKDMHYGIFVARKGG 528
Cdd:PRK08392 152 AFEISSRYRVPDLEFI--RECIKRGIKLTFASDAHRPEDVGNVSWSLKVFKKAG 203
|
|
| POLXc |
smart00483 |
DNA polymerase X family; includes vertebrate polymerase beta and terminal ... |
3-292 |
2.66e-13 |
|
DNA polymerase X family; includes vertebrate polymerase beta and terminal deoxynucleotidyltransferases
Pssm-ID: 214688 Cd Length: 334 Bit Score: 71.24 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 3 NKTIAKKFKLCSQLMELHNENPFRTKAIASASFKLDKVPFLLEtaSFEEISSQPGIGKSTAEKVKKLAETG-SFDELDAM 81
Cdd:smart00483 3 NRGIIDALEILAENYEVFGENKRKCSYFRKAASVLKSLPFPIN--SMKDLKGLPGIGDKIKKKIEEIIETGkSSKVLEIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 82 LSITPEGILEMLNIKGLGPKKIQiIWNDLQIESVGELLYACNEnRLIEAKGFGLKTQEDIKKSI---EFSIsnegwflya 158
Cdd:smart00483 81 NDEVYKSLKLFTNVFGVGPKTAA-KWYRKGIRTLEELKKNKEL-KLTKQQKAGLKYYEDILKKVsraEAFA--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 159 kVLSHAEKLFTKLQKSLSPTLisfTGDFRRKCEVLSSVDILLDTD---KNSTLTYLNTNYPNSL---------------- 219
Cdd:smart00483 150 -VEYIVKRAVRKILPDAIVTL---TGSFRRGKETGHDVDFLITSPhpaKEKELEVLDLLLLESTfeelqlpsirvatldh 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 220 -------------KEEIEYTALRDENG---FSFHIYLTTTGDFHKNLLLTTGSKKHLEGL-------------NHDLITA 270
Cdd:smart00483 226 gqkkfmilklspsREDKEKSGKPDEKGwkaRRVDIVLCPEDQYPTALLGWTGSKQFNRDLrryatskfklmldGHELYDK 305
|
330 340
....*....|....*....|....*....
gi 740914082 271 -------LASEQALYMAQGMDYIEPELRE 292
Cdd:smart00483 306 tkekflkVESEEDIFDHLGLPYIEPEERN 334
|
|
| PHP_HisPPase_Hisj_like |
cd12110 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ... |
318-524 |
9.97e-11 |
|
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: 62.19 E-value: 9.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 318 LHNHSTYSDgvHSLAEMARYCKD--ELGLNYFGICDHS-----KTAVYANGLSIERVQKQWEEIDLLNQELA-PFKIFKG 389
Cdd:cd12110 3 YHTHTPRCD--HASGTLEEYVEAaiELGFTEIGFSEHAplpfeFDDYPESRMAEEELEDYVEEIRRLKEKYAdQIEIKLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 390 IESDILGDGSLDYPDEVLA-GFDFVVASVH---------------SNLKMDEEKATAR----LLKAIENPYTTILGHPT- 448
Cdd:cd12110 81 LEVDYFPGYEEELRELLYGyPLDYVIGSVHflggwgfdfpedgiaEYFEGDIDELYERyfdlVEKAIESGLFDIIGHPDl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 449 ----GRLLLSRSGYPLDYKKIIDACAVNNVVIEINANPLRLDLD----WRWH-RYAIEKGVLLAINPDAHRTEGLkDMHY 519
Cdd:cd12110 161 ikkfGKNDEPDEDYEELIERILRAIAEAGVALEINTAGLRKPVGepypSPEFlELAKELGIPVTLGSDAHSPEDV-GQGY 239
|
....*
gi 740914082 520 GIFVA 524
Cdd:cd12110 240 DEALA 244
|
|
| HHH_8 |
pfam14716 |
Helix-hairpin-helix domain; |
3-71 |
4.74e-10 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434152 [Multi-domain] Cd Length: 67 Bit Score: 55.59 E-value: 4.74e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740914082 3 NKTIAKKFKLCSQLMELHNENPFRTKAIASASFKLDKVPFllETASFEEISSQPGIGKSTAEKVKKLAE 71
Cdd:pfam14716 1 NQEIADALEELADLLELKGEDPFRVRAYRRAARALEALPE--EITSLEELTKLPGIGKKIAAKIEEILE 67
|
|
| YciV |
COG0613 |
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ... |
318-391 |
1.04e-07 |
|
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and metabolism];
Pssm-ID: 440378 [Multi-domain] Cd Length: 188 Bit Score: 52.22 E-value: 1.04e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740914082 318 LHNHSTYSDGVHSLAEMARYCKdELGLNYFGICDHSKTAvyanglSIERVQKQWEEIDLLnqelapfkIFKGIE 391
Cdd:COG0613 6 LHVHTTASDGSLSPEELVARAK-AAGLDVLAITDHDTVA------GYEEAAEAAKELGLL--------VIPGVE 64
|
|
| PHP_HisPPase_AMP |
cd07438 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ... |
318-352 |
4.80e-06 |
|
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: 46.62 E-value: 4.80e-06
10 20 30
....*....|....*....|....*....|....*
gi 740914082 318 LHNHSTYSDGVHSLAEMARYCKdELGLNYFGICDH 352
Cdd:cd07438 3 LHTHSTASDGTLSPEELVELAK-EAGLKVLAITDH 36
|
|
| PHP_HisPPase |
cd07432 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ... |
318-510 |
5.47e-06 |
|
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: 45.69 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 318 LHNHSTYSDGVH-SLAEMARYCKdELGLNYFGICDHsktAVYANGLSIERVqkqweeidllnQELAPFKIFKGIEsdilg 396
Cdd:cd07432 3 LHIHSVFSPDSDmTPEEIVERAI-ELGLDGIAITDH---NTIDGAEEALKE-----------AYKDGLLVIPGVE----- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 397 dgsldypdevlagFDFVvasvhsnlkmdeekatarllkaienpyttILGHPTGRlllSRSGYPLDYKKIIDAcavNNVVI 476
Cdd:cd07432 63 -------------VTLV-----------------------------VLAHPDRP---SRYGLSDLILKPLIK---NGDAI 94
|
170 180 190
....*....|....*....|....*....|....*
gi 740914082 477 EINANPLRLDLDWR-WHRYAIEKGVLLAINPDAHR 510
Cdd:cd07432 95 EVNNSRLRYGLNNLaAKRYAELGGLPITGGSDAHT 129
|
|
| PHP |
pfam02811 |
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ... |
318-481 |
1.23e-05 |
|
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative phosphoesterase domain.
Pssm-ID: 460705 [Multi-domain] Cd Length: 171 Bit Score: 45.61 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 318 LHNHSTYS--DGVHSLAEMARYCKdELGLNYFGICDHSktavyaNGLSIERVQKQWEEIDLlnqelapfKIFKGIESDIL 395
Cdd:pfam02811 2 LHVHSEYSllDGAARIEELVKRAK-ELGMPAIAITDHG------NLFGAVEFYKAAKKAGI--------KPIIGCEVYVA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 396 GDGSLDYPDEVLAGFDFVVASVH----SNL-KMDE----EKATARLLKAIENPYT--------TILGHPtGRLLLSRSGY 458
Cdd:pfam02811 67 PGSREETEKLLAKYFDLVLLAVHevgyKNLiKLSSraylEGFKPRIDKELLEEYFeglialsgCVLGHL-DLILLAPGDY 145
|
170 180
....*....|....*....|....*..
gi 740914082 459 PlDYKKIIDAC----AVNNVVIEINAN 481
Cdd:pfam02811 146 E-EAEELAEEYleifGEDGFYLEINTH 171
|
|
| POLIIIAc |
smart00481 |
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ... |
318-395 |
1.35e-04 |
|
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: 40.33 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 318 LHNHSTYS--DGVHSLAEMARYCKdELGLNYFGICDHSktaVYANGLSIERVQKQweeidllnqelAPFKIFKGIESDIL 395
Cdd:smart00481 2 LHVHSDYSllDGALSPEELVKRAK-ELGLKAIAITDHG---NLFGAVEFYKAAKK-----------AGIKPIIGLEANIV 66
|
|
| PHP |
cd07309 |
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ... |
318-394 |
1.04e-03 |
|
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: 38.18 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 318 LHNHSTYSDGVH-SLAEMARYCKdELGLNYFGICDHSKTAVYANGLSIERVQ--KQWEEIDLlnqelapfKIFKGIESDI 394
Cdd:cd07309 3 LHTHTVFSDGDHaKLTELVDKAK-ELGPDALAITDHGNLRGLAEFNTAGK*NhiKAAEAAGI--------KIIIGSEVNL 73
|
|
| HHH_3 |
pfam12836 |
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain. |
39-106 |
1.38e-03 |
|
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
Pssm-ID: 463723 [Multi-domain] Cd Length: 62 Bit Score: 37.08 E-value: 1.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740914082 39 KVPFLLETASFEEISSQPGIGKSTAEK-VKKLAETGSFDELDamlsitpegilEMLNIKGLGPKKIQII 106
Cdd:pfam12836 1 AVGVDINTASAELLSRVPGLGPKLAKNiVEYREENGPFRSRE-----------DLLKVKGLGPKTFEQL 58
|
|
| ComEA |
COG1555 |
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ... |
26-111 |
1.96e-03 |
|
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];
Pssm-ID: 441164 [Multi-domain] Cd Length: 72 Bit Score: 37.15 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740914082 26 RTKAIASASFKLDkvpflLETASFEEISSQPGIGKSTAEKVKKL-AETGSFDELDamlsitpegilEMLNIKGLGPKKIQ 104
Cdd:COG1555 2 PASASAAAGGKVD-----INTATAEELQTLPGIGPKLAQRIVEYrEKNGPFKSVE-----------DLLEVKGIGPKTLE 65
|
....*..
gi 740914082 105 IIWNDLQ 111
Cdd:COG1555 66 KLKPYLT 72
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
44-66 |
3.17e-03 |
|
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.
Pssm-ID: 425789 [Multi-domain] Cd Length: 30 Bit Score: 35.09 E-value: 3.17e-03
|
| CehA_McbA_metalo |
NF038032 |
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ... |
314-356 |
3.37e-03 |
|
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: 39.61 E-value: 3.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 740914082 314 LKGTLHNHSTYSDGVHSLAEMARYCKDElGLNYFGICDHSKTA 356
Cdd:NF038032 3 YSGDLHIHTNHSDGPTTPEELARAALAE-GLDVIALTDHNTIS 44
|
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