|
Name |
Accession |
Description |
Interval |
E-value |
| YciV |
COG0613 |
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ... |
14-183 |
4.26e-29 |
|
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and metabolism];
Pssm-ID: 440378 [Multi-domain] Cd Length: 188 Bit Score: 115.01 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 14 WRKWDLHVHTPASydwDSKCkkTNSDIVDLAVKEGISAIAVTDHHTTESVDEIKKLGESKGLCVIPGVELRTDKGNDKIH 93
Cdd:COG0613 1 WMKIDLHVHTTAS---DGSL--SPEELVARAKAAGLDVLAITDHDTVAGYEEAAEAAKELGLLVIPGVEISTRWEGREVH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 94 IIALF-DPSvsgqsiYDNVLCPLGFskdDVKKatNEQVYCGFEDACKKIHEQGGLVFL-HAGNKSNGIEqLDSDLKALLK 171
Cdd:COG0613 76 ILGYGiDPE------DPALEALLGI---PVEK--AEREWLSLEEAIDLIREAGGVAVLaHPFRYKRGRW-LDDLLEELAD 143
|
170
....*....|..
gi 818522855 172 TDLafsvDIFEI 183
Cdd:COG0613 144 AGL----DGIEV 151
|
|
| PHP_HisPPase_AMP |
cd07438 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ... |
17-171 |
1.42e-21 |
|
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: 92.07 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 17 WDLHVHTPASydwDSKCkkTNSDIVDLAVKEGISAIAVTDHHTTESVDEIKKLGESKGLCVIPGVELRTDKGNDKIHIia 96
Cdd:cd07438 1 IDLHTHSTAS---DGTL--SPEELVELAKEAGLKVLAITDHDTVAGLEEALAAAKELGIELIPGVEISTEYEGREVHI-- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818522855 97 lfdpsvsgqsiydnvLCPLgfskddvkkatneqvycgfEDACKKIHEQGGLVFL-HAGNKSNGIEQLDSDLKALLK 171
Cdd:cd07438 74 ---------------LGSP-------------------EEAIELIHAAGGVAVLaHPGLYKLSRKKLEELIEELKE 115
|
|
| POLIIIAc |
smart00481 |
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ... |
18-83 |
1.27e-09 |
|
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: 54.96 E-value: 1.27e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818522855 18 DLHVHTPASYDwDSKCKKtnSDIVDLAVKEGISAIAVTDHHTTESVDEIKKLGESKGLCVIPGVEL 83
Cdd:smart00481 1 DLHVHSDYSLL-DGALSP--EELVKRAKELGLKAIAITDHGNLFGAVEFYKAAKKAGIKPIIGLEA 63
|
|
| CehA_McbA_metalo |
NF038032 |
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ... |
16-194 |
3.26e-09 |
|
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: 59.64 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 16 KW---DLHVHTPASydwDSKCkkTNSDIVDLAVKEGISAIAVTDHHTTESVDEIKKLGESK-GLCVIPGVELRTDKGndk 91
Cdd:NF038032 1 GWysgDLHIHTNHS---DGPT--TPEELARAALAEGLDVIALTDHNTISGRAYFAELLASErGLLVIPGMEVTTFWG--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 92 iHIIALfdpsvsGQSIYDNVlcplgfskdDVKKATNEQVYcgFEDACKKIHEQGGLVFL-HAGNKSNGIEQL---DSDLK 167
Cdd:NF038032 73 -HMNLL------GLDLDPYI---------DWRNTDPGSPD--IDEVIDEAHRQGGLVGIaHPFSPGGPLCTGcgwEALID 134
|
170 180
....*....|....*....|....*..
gi 818522855 168 ALLKtdlafsVDIFEINSEKNADDYHN 194
Cdd:NF038032 135 DLGK------VDAIEVWNTPDPAPTNE 155
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
429-696 |
3.68e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 429 KRTSSVDEAVQRNREEIDTKNHSIVALEEKRtdeykRKIEKELAEKENEYKNIKDPAVVKEPKGKLPEADQDKLQKIEEK 508
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSEL-----PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 509 ITDTDDQISKSKDR------QIAVNNELAFIDKLVAKLDALEDNKKKIITEISSEAKTYGFDLSKIIKLSIELNGINTKK 582
Cdd:PRK03918 261 IRELEERIEELKKEieeleeKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 583 KALTSEQEELETKLNENGTDPKK--SLFAKKKELETSKEAIT-KSFDESNKKYqqylsqkKAAENRRKTLMgvkgdsslk 659
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRLTgLTPEKLEKEL-------EELEKAKEEIE--------- 404
|
250 260 270
....*....|....*....|....*....|....*..
gi 818522855 660 titslkEELEYLSGKIGtDLEKLYGKRKTLLKELYKA 696
Cdd:PRK03918 405 ------EEISKITARIG-ELKKEIKELKKAIEELKKA 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
427-726 |
1.62e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 427 IEKRTSSVDEAVQRNREEIDTKNHSIVALEEKRTD--EYKRKIEKELAEKENEYKNIKdpAVVKEPKGKLpeaDQDKLQK 504
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkSELKELEARIEELEEDLHKLE--EALNDLEARL---SHSRIPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 505 IEEKITDTDDQISKSKDRQIAVNNELAFIDKLVAKLDALEDNKKKIITEISSEAKTygfdlskiIKLSIELngINTKKKA 584
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS--------IEKEIEN--LNGKKEE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 585 LTSEQEELETKLNENGtDPKKSLFAKKKELETSKEAITKSFDESNKKYQqylsQKKAAENRRKTLMGVKGDsSLKTITSL 664
Cdd:TIGR02169 866 LEEELEELEAALRDLE-SRLGDLKKERDELEAQLRELERKIEELEAQIE----KKRKRLSELKAKLEALEE-ELSEIEDP 939
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818522855 665 KEELEYLSGKIgTDLEKLYGKRKTLLKELYK--AISNK-ITLYKEIYKPLIDFIE-REKTEQEKSG 726
Cdd:TIGR02169 940 KGEDEEIPEEE-LSLEDVQAELQRVEEEIRAlePVNMLaIQEYEEVLKRLDELKEkRAKLEEERKA 1004
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
662-912 |
2.14e-07 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 53.93 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 662 TSLKEELEYLSGKIGTDlEKLYGKRKTLLKELY--KAISNKITLYKEIYKPLIDFIEREKTEQEKSGNTLTFDAGIVFNK 739
Cdd:pfam13304 52 IDPKEPIEFEISEFLED-GVRYRYGLDLEREDVeeKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIEL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 740 S------AFSDSFLTFINHTKDGTFQLKDGGSKQLKDIFG----KYNLQDEKSVADFADDIVHSLHFDITKSPEKPNEVK 809
Cdd:pfam13304 131 SlselsdLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDlaadLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 810 KQLNqkytPTDIYNFIFNLEYldvqfkilfNGKDLNENEFSPGEKGALLLIFYLLIDKEKVP-LIMDQPEENLDNESVYS 888
Cdd:pfam13304 211 LVDD----RLRERGLILLENG---------GGGELPAFELSDGTKRLLALLAALLSALPKGGlLLIDEPESGLHPKLLRR 277
|
250 260
....*....|....*....|....
gi 818522855 889 LLVPYIKKAKQKRQVIIVTHNPNL 912
Cdd:pfam13304 278 LLELLKELSRNGAQLILTTHSPLL 301
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
461-649 |
4.04e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 461 DEYKRKIEKELAEKENEYKNIKDpavvkepkgKLPEADQdKLQKIEEKITDTDDQISKSKDRQIAVNNElafIDKLVAKL 540
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQA---------ELDALQA-ELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 541 DALEDNKKKII------------TEISSEAKTYGFDLSKIIKLSI-------ELNGINTKKKALTSEQEELETKLNEngt 601
Cdd:COG3883 82 EERREELGERAralyrsggsvsyLDVLLGSESFSDFLDRLSALSKiadadadLLEELKADKAELEAKKAELEAKLAE--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 818522855 602 dpkksLFAKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRKTL 649
Cdd:COG3883 159 -----LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
414-918 |
3.07e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.51 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 414 QANRFGTTSLAQLIEKRTSSVDEAVQRNREEIDTKNHSIVALEEKRTDEYKRKIEKELAEKENEYKNIKDPAVVKEPKGK 493
Cdd:pfam02463 658 LAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 494 LPEADQDKLQKIEEKITDTDDQISKSKDRQIAVNNELAFIDKLVAK-LDALEDNKKKIITEI-SSEAKTYGFDLSKIIKL 571
Cdd:pfam02463 738 LKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTeKLKVEEEKEEKLKAQeEELRALEEELKEEAELL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 572 SIELNGINTKKKALTSEQEELETKLNENGTDPKKSLfaKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRKTLMG 651
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE--EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 652 VKGDSSLKTITSLKEELEYLSGKIGTDLEKLYGKRKTLLKELYKAISNKITLYKEIYKPLIDFIEREKTEQEKSGNTLTF 731
Cdd:pfam02463 896 KEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV 975
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 732 DAGIVFNksafsdsfltFINHTKDGTFQLKDGGSKQLKDIFGKYNLQDEKS----VADFADDIVHSLHFDITKSPEKPNE 807
Cdd:pfam02463 976 NLMAIEE----------FEEKEERYNKDELEKERLEEEKKKLIRAIIEETCqrlkEFLELFVSINKGWNKVFFYLELGGS 1045
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 808 VKKQLNQKYTPTDIynfifnleylDVQFKILFNGKDL-NENEFSPGEKG--ALLLIFYLLIDKeKVPL-IMDQPEENLDN 883
Cdd:pfam02463 1046 AELRLEDPDDPFSG----------GIEISARPPGKGVkNLDLLSGGEKTlvALALIFAIQKYK-PAPFyLLDEIDAALDD 1114
|
490 500 510
....*....|....*....|....*....|....*
gi 818522855 884 ESVySLLVPYIKKAKQKRQVIIVTHNPNLAVVCDA 918
Cdd:pfam02463 1115 QNV-SRVANLLKELSKNAQFIVISLREEMLEKADK 1148
|
|
| PHP |
pfam02811 |
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ... |
18-83 |
4.01e-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: 45.23 E-value: 4.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818522855 18 DLHVHTPASYDwDSKCKKtnSDIVDLAVKEGISAIAVTDHHTTESVDEIKKLGESKGLCVIPGVEL 83
Cdd:pfam02811 1 HLHVHSEYSLL-DGAARI--EELVKRAKELGMPAIAITDHGNLFGAVEFYKAAKKAGIKPIIGCEV 63
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
836-913 |
3.56e-04 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 42.23 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 836 KILFNGKDLNEN-------------EFSPGEKgALLLIFYLLIDKEKVpLIMDQPEENLDNESVYSLLVpYIKK-AKQKR 901
Cdd:cd00267 55 EILIDGKDIAKLpleelrrrigyvpQLSGGQR-QRVALARALLLNPDL-LLLDEPTSGLDPASRERLLE-LLRElAEEGR 131
|
90
....*....|..
gi 818522855 902 QVIIVTHNPNLA 913
Cdd:cd00267 132 TVIIVTHDPELA 143
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
436-576 |
8.17e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 436 EAVQRNREEIDTKNHSIVALEEKRTDEYK--RKIEKELAEKENEYKNIKDPavvkepkgkLPEADQDKLQKIEEKITDTD 513
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPklRDRKDALEEELRQLKQLEDE---------LEDCDPTELDRAKEKLKKLL 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818522855 514 DQISKSKDRQIAVNNELafiDKLVAKLDALEDNKKKIITEISSEAKTY----GFDLSKIIKLSIELN 576
Cdd:smart00787 218 QEIMIKVKKLEELEEEL---QELESKIEDLTNKKSELNTEIAEAEKKLeqcrGFTFKEIEKLKEQLK 281
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YciV |
COG0613 |
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ... |
14-183 |
4.26e-29 |
|
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and metabolism];
Pssm-ID: 440378 [Multi-domain] Cd Length: 188 Bit Score: 115.01 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 14 WRKWDLHVHTPASydwDSKCkkTNSDIVDLAVKEGISAIAVTDHHTTESVDEIKKLGESKGLCVIPGVELRTDKGNDKIH 93
Cdd:COG0613 1 WMKIDLHVHTTAS---DGSL--SPEELVARAKAAGLDVLAITDHDTVAGYEEAAEAAKELGLLVIPGVEISTRWEGREVH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 94 IIALF-DPSvsgqsiYDNVLCPLGFskdDVKKatNEQVYCGFEDACKKIHEQGGLVFL-HAGNKSNGIEqLDSDLKALLK 171
Cdd:COG0613 76 ILGYGiDPE------DPALEALLGI---PVEK--AEREWLSLEEAIDLIREAGGVAVLaHPFRYKRGRW-LDDLLEELAD 143
|
170
....*....|..
gi 818522855 172 TDLafsvDIFEI 183
Cdd:COG0613 144 AGL----DGIEV 151
|
|
| PHP_HisPPase_AMP |
cd07438 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ... |
17-171 |
1.42e-21 |
|
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: 92.07 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 17 WDLHVHTPASydwDSKCkkTNSDIVDLAVKEGISAIAVTDHHTTESVDEIKKLGESKGLCVIPGVELRTDKGNDKIHIia 96
Cdd:cd07438 1 IDLHTHSTAS---DGTL--SPEELVELAKEAGLKVLAITDHDTVAGLEEALAAAKELGIELIPGVEISTEYEGREVHI-- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818522855 97 lfdpsvsgqsiydnvLCPLgfskddvkkatneqvycgfEDACKKIHEQGGLVFL-HAGNKSNGIEQLDSDLKALLK 171
Cdd:cd07438 74 ---------------LGSP-------------------EEAIELIHAAGGVAVLaHPGLYKLSRKKLEELIEELKE 115
|
|
| PHP_HisPPase |
cd07432 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ... |
18-104 |
7.26e-16 |
|
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: 74.97 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 18 DLHVHTPASYDwdskCKKTNSDIVDLAVKEGISAIAVTDHHTTESVDEIKKLGESKGLCVIPGVELRtdkgndkIHIIA- 96
Cdd:cd07432 2 DLHIHSVFSPD----SDMTPEEIVERAIELGLDGIAITDHNTIDGAEEALKEAYKDGLLVIPGVEVT-------LVVLAh 70
|
....*...
gi 818522855 97 LFDPSVSG 104
Cdd:cd07432 71 PDRPSRYG 78
|
|
| POLIIIAc |
smart00481 |
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ... |
18-83 |
1.27e-09 |
|
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: 54.96 E-value: 1.27e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818522855 18 DLHVHTPASYDwDSKCKKtnSDIVDLAVKEGISAIAVTDHHTTESVDEIKKLGESKGLCVIPGVEL 83
Cdd:smart00481 1 DLHVHSDYSLL-DGALSP--EELVKRAKELGLKAIAITDHGNLFGAVEFYKAAKKAGIKPIIGLEA 63
|
|
| CehA_McbA_metalo |
NF038032 |
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ... |
16-194 |
3.26e-09 |
|
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: 59.64 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 16 KW---DLHVHTPASydwDSKCkkTNSDIVDLAVKEGISAIAVTDHHTTESVDEIKKLGESK-GLCVIPGVELRTDKGndk 91
Cdd:NF038032 1 GWysgDLHIHTNHS---DGPT--TPEELARAALAEGLDVIALTDHNTISGRAYFAELLASErGLLVIPGMEVTTFWG--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 92 iHIIALfdpsvsGQSIYDNVlcplgfskdDVKKATNEQVYcgFEDACKKIHEQGGLVFL-HAGNKSNGIEQL---DSDLK 167
Cdd:NF038032 73 -HMNLL------GLDLDPYI---------DWRNTDPGSPD--IDEVIDEAHRQGGLVGIaHPFSPGGPLCTGcgwEALID 134
|
170 180
....*....|....*....|....*..
gi 818522855 168 ALLKtdlafsVDIFEINSEKNADDYHN 194
Cdd:NF038032 135 DLGK------VDAIEVWNTPDPAPTNE 155
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
429-696 |
3.68e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 429 KRTSSVDEAVQRNREEIDTKNHSIVALEEKRtdeykRKIEKELAEKENEYKNIKDPAVVKEPKGKLPEADQDKLQKIEEK 508
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSEL-----PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 509 ITDTDDQISKSKDR------QIAVNNELAFIDKLVAKLDALEDNKKKIITEISSEAKTYGFDLSKIIKLSIELNGINTKK 582
Cdd:PRK03918 261 IRELEERIEELKKEieeleeKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 583 KALTSEQEELETKLNENGTDPKK--SLFAKKKELETSKEAIT-KSFDESNKKYqqylsqkKAAENRRKTLMgvkgdsslk 659
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRLTgLTPEKLEKEL-------EELEKAKEEIE--------- 404
|
250 260 270
....*....|....*....|....*....|....*..
gi 818522855 660 titslkEELEYLSGKIGtDLEKLYGKRKTLLKELYKA 696
Cdd:PRK03918 405 ------EEISKITARIG-ELKKEIKELKKAIEELKKA 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
427-726 |
1.62e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 427 IEKRTSSVDEAVQRNREEIDTKNHSIVALEEKRTD--EYKRKIEKELAEKENEYKNIKdpAVVKEPKGKLpeaDQDKLQK 504
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkSELKELEARIEELEEDLHKLE--EALNDLEARL---SHSRIPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 505 IEEKITDTDDQISKSKDRQIAVNNELAFIDKLVAKLDALEDNKKKIITEISSEAKTygfdlskiIKLSIELngINTKKKA 584
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS--------IEKEIEN--LNGKKEE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 585 LTSEQEELETKLNENGtDPKKSLFAKKKELETSKEAITKSFDESNKKYQqylsQKKAAENRRKTLMGVKGDsSLKTITSL 664
Cdd:TIGR02169 866 LEEELEELEAALRDLE-SRLGDLKKERDELEAQLRELERKIEELEAQIE----KKRKRLSELKAKLEALEE-ELSEIEDP 939
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818522855 665 KEELEYLSGKIgTDLEKLYGKRKTLLKELYK--AISNK-ITLYKEIYKPLIDFIE-REKTEQEKSG 726
Cdd:TIGR02169 940 KGEDEEIPEEE-LSLEDVQAELQRVEEEIRAlePVNMLaIQEYEEVLKRLDELKEkRAKLEEERKA 1004
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
295-724 |
8.32e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 295 IPLSNELVAVIGKKGSGKSALVDVV--ALCGKS--HVPTDNYSFLkpakFRKSSGTAKKYEANITWY---DKSKISMNLV 367
Cdd:TIGR02169 19 IPFSKGFTVISGPNGSGKSNIGDAIlfALGLSSskAMRAERLSDL----ISNGKNGQSGNEAYVTVTfknDDGKFPDELE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 368 DSVDVATEPE-RVTYLP-----------QSFVEKIC-NEDGVSPLFQNEINKVIfSYVPQANRfgttslaQLIEK--RTS 432
Cdd:TIGR02169 95 VVRRLKVTDDgKYSYYYlngqrvrlseiHDFLAAAGiYPEGYNVVLQGDVTDFI-SMSPVERR-------KIIDEiaGVA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 433 SVDEAVQRNREEIDTKNHSI----VALEEKRTDEYKRKIEKELAEKENEYKNIKDPAVVKEPKGKLPEADQDK------L 502
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIerldLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKeaierqL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 503 QKIEEKITDTDDQIS----------------------KSKDRQIAVNNEL----AFIDKLVAKLDALEDNKKKIITEISS 556
Cdd:TIGR02169 247 ASLEEELEKLTEEISelekrleeieqlleelnkkikdLGEEEQLRVKEKIgeleAEIASLERSIAEKERELEDAEERLAK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 557 EAKTYGFDLSKIIKLSIELNGINTKKKALTSEQEELETKLNEngtdpkksLFAKKKELETSKEAitkSFDESnKKYQQYL 636
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED--------LRAELEEVDKEFAE---TRDEL-KDYREKL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 637 SQKKAAENRRKTLMGVKGDSSLKT---ITSLKEELEYLSGKIG---TDLEKLYGKRKTLLKELYKAISNKITLYKEIY-- 708
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLseeLADLNAAIAGIEAKINeleEEKEDKALEIKKQEWKLEQLAADLSKYEQELYdl 474
|
490
....*....|....*.
gi 818522855 709 KPLIDFIEREKTEQEK 724
Cdd:TIGR02169 475 KEEYDRVEKELSKLQR 490
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
662-912 |
2.14e-07 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 53.93 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 662 TSLKEELEYLSGKIGTDlEKLYGKRKTLLKELY--KAISNKITLYKEIYKPLIDFIEREKTEQEKSGNTLTFDAGIVFNK 739
Cdd:pfam13304 52 IDPKEPIEFEISEFLED-GVRYRYGLDLEREDVeeKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIEL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 740 S------AFSDSFLTFINHTKDGTFQLKDGGSKQLKDIFG----KYNLQDEKSVADFADDIVHSLHFDITKSPEKPNEVK 809
Cdd:pfam13304 131 SlselsdLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDlaadLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 810 KQLNqkytPTDIYNFIFNLEYldvqfkilfNGKDLNENEFSPGEKGALLLIFYLLIDKEKVP-LIMDQPEENLDNESVYS 888
Cdd:pfam13304 211 LVDD----RLRERGLILLENG---------GGGELPAFELSDGTKRLLALLAALLSALPKGGlLLIDEPESGLHPKLLRR 277
|
250 260
....*....|....*....|....
gi 818522855 889 LLVPYIKKAKQKRQVIIVTHNPNL 912
Cdd:pfam13304 278 LLELLKELSRNGAQLILTTHSPLL 301
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
461-649 |
4.04e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 461 DEYKRKIEKELAEKENEYKNIKDpavvkepkgKLPEADQdKLQKIEEKITDTDDQISKSKDRQIAVNNElafIDKLVAKL 540
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQA---------ELDALQA-ELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 541 DALEDNKKKII------------TEISSEAKTYGFDLSKIIKLSI-------ELNGINTKKKALTSEQEELETKLNEngt 601
Cdd:COG3883 82 EERREELGERAralyrsggsvsyLDVLLGSESFSDFLDRLSALSKiadadadLLEELKADKAELEAKKAELEAKLAE--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 818522855 602 dpkksLFAKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRKTL 649
Cdd:COG3883 159 -----LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
427-599 |
1.26e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 427 IEKRTSSVDEAVQRNREEIDTKNHSIVALEEKRTDeykrkIEKELAEKENEYKNIKdpAVVKEPKGKLPEA-DQDKLQKI 505
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELED-----LEKEIKRLELEIEEVE--ARIKKYEEQLGNVrNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 506 EEKITDTDDQISKSKDRQIAVNNElafIDKLVAKLDALEDNKKKIITEISSEAKtygfdlskiiKLSIELNGINTKKKAL 585
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMER---IEELEEELAELEAELAELEAELEEKKA----------ELDEELAELEAELEEL 161
|
170
....*....|....
gi 818522855 586 TSEQEELETKLNEN 599
Cdd:COG1579 162 EAEREELAAKIPPE 175
|
|
| PHP_HisPPase_Chlorobi_like |
cd12112 |
Polymerase and Histidinol Phosphatase domain of Chlorobi like; The PHP (also called histidinol ... |
11-98 |
2.36e-06 |
|
Polymerase and Histidinol Phosphatase domain of Chlorobi 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. Chlorobi PHP is uncharacterized protein. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce 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: 213996 [Multi-domain] Cd Length: 235 Bit Score: 49.64 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 11 GSEWRKWDLHVHTPASydwDSKCKKTNSdiVDLAVKEGISAIAVTDH-----HTTE--------SVDEIKKLGESKGLCV 77
Cdd:cd12112 9 GYKTLKCDFHTHTVFS---DGHVWPEIR--VREAWREGLDAIAITEHieyrpHKEDiphpdrnrSYKIAKEAAESKGLLI 83
|
90 100
....*....|....*....|.
gi 818522855 78 IPGVELRTDKGNDkiHIIALF 98
Cdd:cd12112 84 IPGAEITREKPPG--HLNALF 102
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
414-918 |
3.07e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.51 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 414 QANRFGTTSLAQLIEKRTSSVDEAVQRNREEIDTKNHSIVALEEKRTDEYKRKIEKELAEKENEYKNIKDPAVVKEPKGK 493
Cdd:pfam02463 658 LAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 494 LPEADQDKLQKIEEKITDTDDQISKSKDRQIAVNNELAFIDKLVAK-LDALEDNKKKIITEI-SSEAKTYGFDLSKIIKL 571
Cdd:pfam02463 738 LKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTeKLKVEEEKEEKLKAQeEELRALEEELKEEAELL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 572 SIELNGINTKKKALTSEQEELETKLNENGTDPKKSLfaKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRKTLMG 651
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE--EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 652 VKGDSSLKTITSLKEELEYLSGKIGTDLEKLYGKRKTLLKELYKAISNKITLYKEIYKPLIDFIEREKTEQEKSGNTLTF 731
Cdd:pfam02463 896 KEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV 975
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 732 DAGIVFNksafsdsfltFINHTKDGTFQLKDGGSKQLKDIFGKYNLQDEKS----VADFADDIVHSLHFDITKSPEKPNE 807
Cdd:pfam02463 976 NLMAIEE----------FEEKEERYNKDELEKERLEEEKKKLIRAIIEETCqrlkEFLELFVSINKGWNKVFFYLELGGS 1045
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 808 VKKQLNQKYTPTDIynfifnleylDVQFKILFNGKDL-NENEFSPGEKG--ALLLIFYLLIDKeKVPL-IMDQPEENLDN 883
Cdd:pfam02463 1046 AELRLEDPDDPFSG----------GIEISARPPGKGVkNLDLLSGGEKTlvALALIFAIQKYK-PAPFyLLDEIDAALDD 1114
|
490 500 510
....*....|....*....|....*....|....*
gi 818522855 884 ESVySLLVPYIKKAKQKRQVIIVTHNPNLAVVCDA 918
Cdd:pfam02463 1115 QNV-SRVANLLKELSKNAQFIVISLREEMLEKADK 1148
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
420-732 |
4.85e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 420 TTSLAQLIEKRtSSVDEAVQRNREEIDTKNHSIVALEEKRtDEYKRKIeKELAEKENEYKNIKDPAV--VKEPKgklpea 497
Cdd:COG1340 7 SSSLEELEEKI-EELREEIEELKEKRDELNEELKELAEKR-DELNAQV-KELREEAQELREKRDELNekVKELK------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 498 dqDKLQKIEEKITDTDDQISKSKDRQIAVNNELAFIDKLVAKLDALEdnkKKIITEIsseaktygFDLSKIIKLSIELNG 577
Cdd:COG1340 78 --EERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLE---WRQQTEV--------LSPEEEKELVEKIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 578 INTKKKALtSEQEELETKLNENgtdpKKSLFAKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRKtlmgvKGDSS 657
Cdd:COG1340 145 LEKELEKA-KKALEKNEKLKEL----RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRK-----EADEL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818522855 658 LKTITSLKEELEYLSGKIgtdlEKLYGKRKTLLKELYKAISNKITLYKEIYKPLIDFIEREKTEQEKSGNTLTFD 732
Cdd:COG1340 215 HKEIVEAQEKADELHEEI----IELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTE 285
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
456-698 |
1.28e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 456 EEKRTDEYKRKIEKELAEKENEYKNIKDPAVVKEPKGKLPEADQDKLQKIEEKITDTDDQISKSKDRQIAVNNELAFIDK 535
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 536 LVAKLDALE---DNKKKIITEISSEAKTYGF-----------DLSKIIKLSIELNGINTKKKALTSEQEELETKLNEngt 601
Cdd:PRK03918 554 LKKKLAELEkklDELEEELAELLKELEELGFesveeleerlkELEPFYNEYLELKDAEKELEREEKELKKLEEELDK--- 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 602 dpkksLFAKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRKTLMGVKGDSSLKTITSLKEELEYLSGKIGTDLEK 681
Cdd:PRK03918 631 -----AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
250
....*....|....*..
gi 818522855 682 LYGKRKTlLKELYKAIS 698
Cdd:PRK03918 706 REKAKKE-LEKLEKALE 721
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
456-682 |
1.43e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 456 EEKRTDEYKRKIEKELAEKENEYKNIKDPAVVKEPKGKlpeADQDKLQKIEEKITDTDDQISKSKDRQIAVNNELAFIDK 535
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKIN---NSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 536 LV----AKLDALEDNKKKIITEISSEAKTYGFDLSKIIKLSIELNGINTKKKALTSEQEELETKLN--ENGTDPKKSLFA 609
Cdd:TIGR04523 111 EIkndkEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNllEKEKLNIQKNID 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818522855 610 KKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRKTLMgvkgdsslKTITSLKEELEYLSGKIGTDLEKL 682
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLK--------DNIEKKQQEINEKTTEISNTQTQL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
496-727 |
1.94e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 496 EADQDKLQKIEEKITDTDDQISKSKDRQIAVNNELAFIDKlvaKLDALEDnkkkiiteisseaktygfdlsKIIKLSIEL 575
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER---RIAALAR---------------------RIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 576 NGINTKKKALTSEQEELETKLNENGTDPKKSLFAKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRKTLMGVKGD 655
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 656 ssLKTITSLKEELEYLSGKIGT----------DLEKLYGKRKTLLKEL---YKAISNKITLYKEIYKPLIDFIEREKTEQ 722
Cdd:COG4942 159 --LAELAALRAELEAERAELEAllaeleeeraALEALKAERQKLLARLekeLAELAAELAELQQEAEELEALIARLEAEA 236
|
....*
gi 818522855 723 EKSGN 727
Cdd:COG4942 237 AAAAE 241
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
294-723 |
3.05e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 294 SIPLSNELVAVIGKKGSGKSALVDVVALC-GKSHvptdnYSFLKPAK-----FRKSSGTAKKYEANITwYDKSKISMNLV 367
Cdd:pfam02463 18 ILPFSPGFTAIVGPNGSGKSNILDAILFVlGERS-----AKSLRSERlsdliHSKSGAFVNSAEVEIT-FDNEDHELPID 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 368 DSVDVATepeRVTYLPQSFVEKICNEDG----VSPLFQNE-INKVIFSYVPQANRfgTTSLAQLIEKRTSSVDEAV---- 438
Cdd:pfam02463 92 KEEVSIR---RRVYRGGDSEYYINGKNVtkkeVAELLESQgISPEAYNFLVQGGK--IEIIAMMKPERRLEIEEEAagsr 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 439 ------QRNREEIDTKNHSIVALEEKRTDEYKRKIEKELAEKENEYKNIKDpavvKEPKGKLPEADQDKLQKIEEKITDT 512
Cdd:pfam02463 167 lkrkkkEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE----KLELEEEYLLYLDYLKLNEERIDLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 513 DDQISKSKDRQIAVNNELAFIDKLVAKLDALEDNKKKIITEISSEAKTY----GFDLSKIIKLSIELNGINTKKKALTSE 588
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLakeeEELKSELLKLERRKVDDEEKLKESEKE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 589 QEELETKLNEngtdpKKSLFAKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRKTLMGVKGDSSLKTITSLKEEL 668
Cdd:pfam02463 323 KKKAEKELKK-----EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 818522855 669 EYLSGKIGTDLEKLYGKRKtlLKELYKAISNKITLYKEIYKPLIDFIEREKTEQE 723
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQ--LEDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
|
| PHP |
pfam02811 |
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ... |
18-83 |
4.01e-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: 45.23 E-value: 4.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818522855 18 DLHVHTPASYDwDSKCKKtnSDIVDLAVKEGISAIAVTDHHTTESVDEIKKLGESKGLCVIPGVEL 83
Cdd:pfam02811 1 HLHVHSEYSLL-DGAARI--EELVKRAKELGMPAIAITDHGNLFGAVEFYKAAKKAGIKPIIGCEV 63
|
|
| PHP |
cd07309 |
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ... |
18-82 |
7.77e-05 |
|
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: 42.41 E-value: 7.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818522855 18 DLHVHTPAS---YDWdskckktNSDIVDLAVKEGISAIAVTDH---------HTTESVDEIKKlGESKGLCVIPGVE 82
Cdd:cd07309 2 DLHTHTVFSdgdHAK-------LTELVDKAKELGPDALAITDHgnlrglaefNTAGK*NHIKA-AEAAGIKIIIGSE 70
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
454-696 |
9.61e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 454 ALEEKRTDEYKRKIEKELAEKENEYKNIKDPAVVKEPKGKLPEADQDKLQKIEEKITDTDDQISKSKDRQIAVNNELAFI 533
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 534 DKL-VAKLDALEDNKKKIITEISSEAKTYGFDLSKiiKLSIELNGINTKKKAltsEQEELETKLNENGTDPKKSLFAKKK 612
Cdd:PTZ00121 1391 KKAdEAKKKAEEDKKKADELKKAAAAKKKADEAKK--KAEEKKKADEAKKKA---EEAKKADEAKKKAEEAKKAEEAKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 613 ELETSKEAITKSFDESNKKYQQylSQKKAAENRRKTLMGVKGDSSLKTITSLKEELEylsGKIGTDLEKLYGKRKTllKE 692
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADE--AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE---AKKADEAKKAEEAKKA--DE 1538
|
....
gi 818522855 693 LYKA 696
Cdd:PTZ00121 1539 AKKA 1542
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
438-910 |
2.12e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 45.11 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 438 VQRNREEIDTKNHsIVALEE------KRTDEYKRKIEKELAEKENEYKNIKDpavVKEPKGKLPEadqdklqKIEEKITD 511
Cdd:COG4694 81 VEENLRSGEEIKG-IFTLGEenieleEEIEELEKEIEDLKKELDKLEKELKE---AKKALEKLLE-------DLAKSIKD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 512 TDDQISKSKDRQIAVNNelaFIDKLVAKLDALEDNKKKIITEISSEAKTYGFDLSKIIKLSIELNGINT--KKKALTSEQ 589
Cdd:COG4694 150 DLKKLFASSGRNYRKAN---LEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEAETllEKSAVSSAI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 590 EELETKLNENGTDpkkslfakkkelETSKEAItkSFDESNKKYQQYLSQKKAAENRRKTLMGVKGDSSLKTITSLKEELE 669
Cdd:COG4694 227 EELAALIQNPGNS------------DWVEQGL--AYHKEEEDDTCPFCQQELAAERIEALEAYFDDEYEKLLAALKDLLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 670 YLSGKIGTDLEKLYGKRKTLLKELYKAISNKITLYKEIYKPLIDFIEREKTEQEKSGNTLTFDAGIVFNKS--------- 740
Cdd:COG4694 293 ELESAINALSALLLEILRTLLPSAKEDLKAALEALNALLETLLAALEEKIANPSTSIDLDDQELLDELNDLiaalnalie 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 741 AFSDSFLTFINHTKDGTFQLKDGGSKQLKDIFGKYnlqdEKSVADFADDIVHslhfdITKSPEKPNEVKKQLNQKYT--- 817
Cdd:COG4694 373 EHNAKIANLKAEKEEARKKLEAHELAELKEDLSRY----KAEVEELIEELKT-----IKALKKALEDLKTEISELEAels 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 818 PTDIYNFIFN--LEYL-------------DVQFKILFNGKDLNE--NEFSPGEKGAL-LLIFYLLI-----DKEKVPLIM 874
Cdd:COG4694 444 SVDEAADEINeeLKALgfdefsleavedgRSSYRLKRNGENDAKpaKTLSEGEKTAIaLAYFLAELegdenDLKKKIVVI 523
|
490 500 510
....*....|....*....|....*....|....*....
gi 818522855 875 DQPEENLDNES---VYSLLVpyiKKAKQKRQVIIVTHNP 910
Cdd:COG4694 524 DDPVSSLDSNHrfaVASLLK---ELSKKAKQVIVLTHNL 559
|
|
| HIS2 |
COG1387 |
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ... |
16-83 |
2.20e-04 |
|
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: 43.60 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 16 KWDLHVHTPASydwDSKCkkTNSDIVDLAVKEGISAIAVTDH-------------HTTESVDEIKKLGES-KGLCVIPGV 81
Cdd:COG1387 2 RGDLHTHTTYS---DGEG--TIEEMVEAAIELGLEYIAITDHspslfvanglseeRLLEYLEEIEELNEKyPDIKILKGI 76
|
..
gi 818522855 82 EL 83
Cdd:COG1387 77 EV 78
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
457-917 |
2.92e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 457 EKRTDEYKRKIEK---ELAEKENEYKNIKDPAV-VKEPKGKLP----EADQD-----------KLQKIEEKITDTDDQIS 517
Cdd:PRK03918 397 EKAKEEIEEEISKitaRIGELKKEIKELKKAIEeLKKAKGKCPvcgrELTEEhrkelleeytaELKRIEKELKEIEEKER 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 518 KSKDRQIAVNNELAFIDKLVA------KLDALEDNKKKI-ITEISSEAKTYGFDLSKIIKLSIELNGINT---KKKALTS 587
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKlkelaeQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKSLKKeleKLEELKK 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 588 EQEELETKLNEngtdpkksLFAKKKELETS-KEAITKSFDESNKK-------YQQYLSQKKA-----AENRRKTLMGVKG 654
Cdd:PRK03918 557 KLAELEKKLDE--------LEEELAELLKElEELGFESVEELEERlkelepfYNEYLELKDAekeleREEKELKKLEEEL 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 655 DSSLKTITSLKEELEYLSGKIGT--------DLEKLYGKRKTLLKELYKAISNKITLYK--EIYKPLIDFIEREKTEQEK 724
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEElekkyseeEYEELREEYLELSRELAGLRAELEELEKrrEEIKKTLEKLKEELEEREK 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 725 SGNTLTfdagiVFNKSafsdsfLTFInhtkdgtfqlkdggsKQLKDIFGKY-NLQDEKSVAdfaddivhslhfditkspe 803
Cdd:PRK03918 709 AKKELE-----KLEKA------LERV---------------EELREKVKKYkALLKERALS------------------- 743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 804 KPNEVKKQLNQKYTPTDIYNFIFNLEYLDVQFKILFNGKDLNENEFSPGEKGALLLIFYLLIDKEKVP----LIMDQPEE 879
Cdd:PRK03918 744 KVGEIASEIFEELTEGKYSGVRVKAEENKVKLFVVYQGKERPLTFLSGGERIALGLAFRLALSLYLAGniplLILDEPTP 823
|
490 500 510
....*....|....*....|....*....|....*...
gi 818522855 880 NLDNESVYSLLVPYIKKAKQKRQVIIVTHNPNLAVVCD 917
Cdd:PRK03918 824 FLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKDAAD 861
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
460-730 |
3.06e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 460 TDEYKRKIEKELAEKENEYKNIKD-PAVVKEPKGKLPEADQDKLQKIEEKITDTDDQISKSKDRQIAVNNELAFIDKLVA 538
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERlDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 539 KLDALEDNKKKIITEISSEAKTYGfdlskiiKLSIELNGINTKKKALTS-EQEELETKLNENGTD---PKKSLFAKKKEL 614
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLE-------EIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEiasLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 615 ETSKEAITKSFDESNKKYQQY--LSQKKAAENRRKTLMGVKGDSSLKTITSLKEELEYLSGKIGTDLEKLygkrKTLLKE 692
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIeeLEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----KDYREK 393
|
250 260 270
....*....|....*....|....*....|....*...
gi 818522855 693 LYKAISNKITLYKEIYKpLIDFIEREKTEQEKSGNTLT 730
Cdd:TIGR02169 394 LEKLKREINELKRELDR-LQEELQRLSEELADLNAAIA 430
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
499-724 |
3.08e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 499 QDKLQKIEEKITDTDDQISKSKDRQIAVNNELAFIDKLVAKLDALEDNKKKIITEISSEAKTYGFDLSKIIKlsiELNGI 578
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK---ERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 579 NTKKKALTSEQEELETKLNENGtdpkkslfAKKKELETSKEAITKSFDESNKKYQQYLSQKkaAENRRKTLMGVKGDSSL 658
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAERE--------EELKELEEQLESLQEELAALEQELQALSEAE--AEQALDELLKEANRNAE 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818522855 659 KTITSLKEELEYLSGKIGTDLEKLYGKRKTLLKELYKAISNKITLYKEIYKPLIDFIEREKTEQEK 724
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
459-730 |
3.21e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 459 RTDEYKRKIEKE---LAEKENEYKNIKDpaVVKEPKGKLpeadqDKLQKIEEKITDTDDQISKSKDRQIAVNNELAFIDK 535
Cdd:PRK03918 142 ESDESREKVVRQilgLDDYENAYKNLGE--VIKEIKRRI-----ERLEKFIKRTENIEELIKEKEKELEEVLREINEISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 536 ----LVAKLDALEDNKK---KIITEISSEAKTYGFDLSKIIKLSIELNGINTKKKALTSEQEELETKLNEngtdpKKSLF 608
Cdd:PRK03918 215 elpeLREELEKLEKEVKeleELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE-----LKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 609 AKKKELETSKEAITKSFDESN---KKYQQYLSQKKAAENRRKTLMgvKGDSSLKTITSLKEELEYLSGKIGTDlEKLYGK 685
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELReieKRLSRLEEEINGIEERIKELE--EKEERLEELKKKLKELEKRLEELEER-HELYEE 366
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 818522855 686 RKTLLKELYKAISNKITLYKEIYKPLIDFIEREKTEQEKSGNTLT 730
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
836-913 |
3.56e-04 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 42.23 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 836 KILFNGKDLNEN-------------EFSPGEKgALLLIFYLLIDKEKVpLIMDQPEENLDNESVYSLLVpYIKK-AKQKR 901
Cdd:cd00267 55 EILIDGKDIAKLpleelrrrigyvpQLSGGQR-QRVALARALLLNPDL-LLLDEPTSGLDPASRERLLE-LLRElAEEGR 131
|
90
....*....|..
gi 818522855 902 QVIIVTHNPNLA 913
Cdd:cd00267 132 TVIIVTHDPELA 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
421-652 |
3.82e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 421 TSLAQLIEKRTSSVDEAVQRNREEIDTKNHSIVALEEKRTD--EYKRKIEKELAEKENEYKNIKdpAVVKEPKGKLPEAD 498
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEleELIEELESELEALLNERASLE--EALALLRSELEELS 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 499 qDKLQKIEEKITDTDDQISKSKDRQIAVNNELAfidklvaKLDALEDNKKKIITEisseaktygfdlskiiKLSIELNGI 578
Cdd:TIGR02168 901 -EELRELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQERLSE----------------EYSLTLEEA 956
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818522855 579 NTKKKALTSEQEELETKLnengtdpkKSLFAKKKEL-ETSKEAITKsFDESNKKYQQYLSQKKAAENRRKTLMGV 652
Cdd:TIGR02168 957 EALENKIEDDEEEARRRL--------KRLENKIKELgPVNLAAIEE-YEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
412-776 |
7.66e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 412 VPQANRFGTTSLAQLIEKRTSSVDEAVQRNREEIDTKNHSIVALEEKRTDEYKR--KIEKELAEKENEYKNIKDPAV-VK 488
Cdd:TIGR01612 520 VPSKNIIGFDIDQNIKAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDsiHLEKEIKDLFDKYLEIDDEIIyIN 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 489 EPKGKLPEadqdklqKIEeKITDTDDQISKSKDRQIAVNNELAFIDKLvAKLDALE-----DNKKKIITEISSE-AKTYG 562
Cdd:TIGR01612 600 KLKLELKE-------KIK-NISDKNEYIKKAIDLKKIIENNNAYIDEL-AKISPYQvpehlKNKDKIYSTIKSElSKIYE 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 563 FDLSKIIKlsielngintkkkaltseqeELETKLNENGTDPKKSlfakKKELETSKEAITKSFDE-SNKKYQQYLSQKKA 641
Cdd:TIGR01612 671 DDIDALYN--------------------ELSSIVKENAIDNTED----KAKLDDLKSKIDKEYDKiQNMETATVELHLSN 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 642 AENRRKTLmgvkgdssLKTITSLKeelEYLSGKIGTDLEKLYGKRKTLLKELykaiSNKITLYKE------IYKPLIDFI 715
Cdd:TIGR01612 727 IENKKNEL--------LDIIVEIK---KHIHGEINKDLNKILEDFKNKEKEL----SNKINDYAKekdelnKYKSKISEI 791
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818522855 716 EREKTEQEKSGNTLTFDAGIVFNKsafSDSFLTFINHTKDGTFQLKDGGSKQLKDIFGKYN 776
Cdd:TIGR01612 792 KNHYNDQINIDNIKDEDAKQNYDK---SKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVD 849
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
850-912 |
1.07e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 1.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818522855 850 SPGEKGALLLIFYLLIDK---EKVP-LIMDQPEENLDNESVYSLLVPYIKKAKQK--RQVIIVTHNPNL 912
Cdd:cd03240 117 SGGEKVLASLIIRLALAEtfgSNCGiLALDEPTTNLDEENIEESLAEIIEERKSQknFQLIVITHDEEL 185
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
442-917 |
1.26e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 442 REEIDTKNHSIVALEEKRTD--EYKRKIEKELAEKENEYKNIKDPAVVKEPKGKLPEADQDKLQKIEEKITDTDDQISKS 519
Cdd:PRK01156 345 KSRYDDLNNQILELEGYEMDynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 520 kdrqiaVNNELAFIDKLVAKLDALEDNKKKII---------TEISSEA-----KTYGFDLS----KIIKLSIELNGINTK 581
Cdd:PRK01156 425 ------VSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgTTLGEEKsnhiiNHYNEKKSrleeKIREIEIEVKDIDEK 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 582 KKALTSEQEELETK---LNENGTDPKKSLFAKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRKT----LMGVKG 654
Cdd:PRK01156 499 IVDLKKRKEYLESEeinKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTswlnALAVIS 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 655 DSSLKTITSLKEE-------LEYLSGKIGTDLEKLYGKRKTLLKELYKAISNKITLYKEIY--KPLIDFIeREKTEQEKS 725
Cdd:PRK01156 579 LIDIETNRSRSNEikkqlndLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQenKILIEKL-RGKIDNYKK 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 726 gnTLTFDAGIVFNKSAFSDSFLTFINHTKDGTFQLKDGGSKQL-KDIFGKYNLQDEKSVADFADDIVHSLHF--DITKSP 802
Cdd:PRK01156 658 --QIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRArLESTIEILRTRINELSDRINDINETLESmkKIKKAI 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 803 EKPNEVKKQLNQKYTPTDI--------------YNFIFNLEYLDVQFKILFN------GKDLNENEFSPGEKGALLLIFY 862
Cdd:PRK01156 736 GDLKRLREAFDKSGVPAMIrksasqamtsltrkYLFEFNLDFDDIDVDQDFNitvsrgGMVEGIDSLSGGEKTAVAFALR 815
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818522855 863 LLI----DKEKVPLIMDQPEENLDNESVYSL--LVPY-IKKAKQKRQVIIVTHNPNLAVVCD 917
Cdd:PRK01156 816 VAVaqflNNDKSLLIMDEPTAFLDEDRRTNLkdIIEYsLKDSSDIPQVIMISHHRELLSVAD 877
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
415-650 |
2.40e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 415 ANRFGTTSLAQLIEKRTSSVDEAVQRNREEIDtknhsivaleekrtdeykrKIEKELAEKENEYKNIKDpavvkepkgkl 494
Cdd:COG3206 154 ANALAEAYLEQNLELRREEARKALEFLEEQLP-------------------ELRKELEEAEAALEEFRQ----------- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 495 peadQDKLQKIEEKITDTDDQISKSKDRQIAVNNELAfidKLVAKLDALEDNKKKIITEIS--SEAKTYGFDLSKIIKLS 572
Cdd:COG3206 204 ----KNGLVDLSEEAKLLLQQLSELESQLAEARAELA---EAEARLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 573 IELNGINTKK-------KALTSEQEELETKLNENGTDPK-------KSLFAKKKELETSKEAITKSFDESNKKYQQYLSQ 638
Cdd:COG3206 277 AELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRILasleaelEALQAREASLQAQLAQLEARLAELPELEAELRRL 356
|
250
....*....|..
gi 818522855 639 KKAAENRRKTLM 650
Cdd:COG3206 357 EREVEVARELYE 368
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
435-645 |
2.89e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 435 DEAVQRNREEIDTKNHSIVALEEKrtdeyKRKIEKELAEKENEYKNIKDpavvkepkgKLpEADQDKLQKIEEKITDTDD 514
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE-----LDALQAELEELNEEYNELQA---------EL-EALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 515 QISKSKD----------RQIAVNNELA----------FIDKLVAkLDALEDNKKKIITEISS---EAKTYGFDLSKIIK- 570
Cdd:COG3883 80 EIEERREelgeraralyRSGGSVSYLDvllgsesfsdFLDRLSA-LSKIADADADLLEELKAdkaELEAKKAELEAKLAe 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818522855 571 LSIELNGINTKKKALTSEQEELETKLNengtdpkkSLFAKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENR 645
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLA--------QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
453-692 |
3.57e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 453 VALEEKRT--DEYKRKIEKELAEK---ENEYKNIKDPAVVKEPKGKLPeadQDKLQKIEEKITDTDDQISKSKDRQIAVN 527
Cdd:pfam10174 352 LRLEEKESflNKKTKQLQDLTEEKstlAGEIRDLKDMLDVKERKINVL---QKKIENLQEQLRDKDKQLAGLKERVKSLQ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 528 NELAFIDKLVAKL-DALEDnKKKIIT----EISSEAKTYGFDLSKIIKlsiELNGINTKKKALTSEQEELETKLN---EN 599
Cdd:pfam10174 429 TDSSNTDTALTTLeEALSE-KERIIErlkeQREREDRERLEELESLKK---ENKDLKEKVSALQPELTEKESSLIdlkEH 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 600 GTDPKKSLFAKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRktlmgVKGDSSLKtITSLKEELEYL---SGKIG 676
Cdd:pfam10174 505 ASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVR-----TNPEINDR-IRLLEQEVARYkeeSGKAQ 578
|
250
....*....|....*.
gi 818522855 677 TDLEKLYGkrktLLKE 692
Cdd:pfam10174 579 AEVERLLG----ILRE 590
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
427-707 |
3.80e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 427 IEKRTSSVDEAVQRNREEIDTKNHSIVALEEKR---------TDEY-------------KRKIEKELAEKENEYKNI--- 481
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVkelkelkekAEEYiklsefyeeyldeLREIEKRLSRLEEEINGIeer 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 482 -----KDPAVVKEPKGKLPEAdQDKLQKIEEKITDTDDQISKSKD-RQIAVNNELAFIDKLVAKLDALEDNKKKIITEIS 555
Cdd:PRK03918 330 ikeleEKEERLEELKKKLKEL-EKRLEELEERHELYEEAKAKKEElERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 556 ------SEAKTYGFDLSKIIklsIELNGINTK----KKALTSEQEEletKLNENGTDPKKSLFAKKKELETSKEAITKSF 625
Cdd:PRK03918 409 kitariGELKKEIKELKKAI---EELKKAKGKcpvcGRELTEEHRK---ELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 626 DESNK---------KYQQYLSQKKAAENRRKTLMGVKGDSSLKTITSLKEELEYLSGKIGT---DLEK---LYGKRKTLL 690
Cdd:PRK03918 483 RELEKvlkkeseliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSlkkELEKleeLKKKLAELE 562
|
330
....*....|....*..
gi 818522855 691 KELYKAISNKITLYKEI 707
Cdd:PRK03918 563 KKLDELEEELAELLKEL 579
|
|
| PHP_PolIIIA_POLC |
cd07435 |
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III at ... |
19-97 |
3.85e-03 |
|
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III at PolC gene; DNA polymerase III alphas (PolIIIAs) that contain a PHP domain have been classified into four basic groups based on phylogenetic and domain structural analyses: polC, dnaE1, dnaE2, and dnaE3. The PolC group is distinct from the other three and is clustered together. 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 are 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. PolC PHP is located in different location compare to dnaE1, 2, and 3. The PHP domain has four conserved sequence motifs and and contains an invariant histidine that is involved in metal ion coordination.The PHP domain of PolC 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. PHP domains found in dnaEs of thermophilic origin exhibit 3'-5' exonuclease activity. In contrast, PolC PHP lacks detectable nuclease activity.
Pssm-ID: 213990 [Multi-domain] Cd Length: 268 Bit Score: 40.15 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 19 LHVHTPASyDWDSKCKKtnSDIVDLAVKEGISAIAVTDHHTTESVDEIKKLGESKGLCVIPGVElrtdkGN--DKIHIIA 96
Cdd:cd07435 4 LHAHTKMS-AMDGVTSV--KELVKRAAEWGHKAIAITDHGVVQAFPEAYEAAKKNGIKVIYGVE-----AYlvDPYHITI 75
|
.
gi 818522855 97 L 97
Cdd:cd07435 76 L 76
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
425-709 |
4.70e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 425 QLIEKRTSSVDEAVQRNREEIDTKNHSIVALEEKRTDEYK--RKIEKELAEKENEYKNIKDpavvkepkgklpeadqdKL 502
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeiKDLTNQDSVKELIIKNLDN-----------------TR 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 503 QKIEEKITDTDDQISKSKDRQIAVNNELafiDKLVAKLDALEDNKKKIITEISSEAKTYGFDLSKIIKLSIELNGINTKK 582
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKEL---KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 583 KALTSEQEELETKLNENGTdpKKSLFAKKKELETSKEAItKSFDESNKKYQQYLSQKKAAENRRK---TLMGVKGDSSLK 659
Cdd:TIGR04523 541 SDLEDELNKDDFELKKENL--EKEIDEKNKEIEELKQTQ-KSLKKKQEEKQELIDQKEKEKKDLIkeiEEKEKKISSLEK 617
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 818522855 660 TITSLKEELEYLSGKIgTDLEKLYGKRKTLLKELYKAISNKITLYKEIYK 709
Cdd:TIGR04523 618 ELEKAKKENEKLSSII-KNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
430-598 |
4.78e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 430 RTSSVDEAVQRNREEIDTKNHSIVALEEkRTDEYKRKIeKELAEKENEYKNIKDPAVVKEPKGKLPEADQdKLQKIEEKI 509
Cdd:PRK02224 593 RIRTLLAAIADAEDEIERLREKREALAE-LNDERRERL-AEKRERKRELEAEFDEARIEEAREDKERAEE-YLEQVEEKL 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 510 TDTDDQISKSKDRQIAVNNELAFIDKLVAKLDALEDNKKKIIT---EISSEAKTYGfdlskiiKLSIELNGINTkkkalt 586
Cdd:PRK02224 670 DELREERDDLQAEIGAVENELEELEELRERREALENRVEALEAlydEAEELESMYG-------DLRAELRQRNV------ 736
|
170
....*....|..
gi 818522855 587 seqEELETKLNE 598
Cdd:PRK02224 737 ---ETLERMLNE 745
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
428-700 |
5.78e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 428 EKRTSSVDEAVQRNREEIDTKNHSIVALEEKR-TDEYKRKIEKELAEKENEYKNIKDPAVVKEPKGKLPEADQDKlQKIE 506
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARkADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK-KKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 507 EKITDTDDQISKSKDRQIAVNNELAFIDKLVAKLDALEDnKKKIITEISSEAKTYGFDLSKiiKLSIELNGINTKKKALT 586
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEEAKKKADAAKK--KAEEKKKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 587 SEQEELETKLNEngTDPKKSLFAKKKELETSKEAITKSFDESNKKYQQYlsqKKAAENRRKTLMGVKGDSSLKTITSLKE 666
Cdd:PTZ00121 1403 DKKKADELKKAA--AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA---KKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
250 260 270
....*....|....*....|....*....|....
gi 818522855 667 ELEylSGKIGTDLEKLYGKRKTLLKELYKAISNK 700
Cdd:PTZ00121 1478 KAE--EAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
417-795 |
7.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 417 RFGTTSLAQLIEKRTSSVDEAVQRNREEIDTKNHsivalEEKRTDEYKRKIEKELAEKENEYKNIkdpavvkepkgklpe 496
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLRE-----ELEQAREELEQLEEELEQARSELEQL--------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 497 adQDKLQKIEEKITDTDDQISKSKDRQIAVNNEL----AFIDKLVAKLDALEDNKKKIITEISSEAKTYGFDLSKIIKLS 572
Cdd:COG4372 79 --EEELEELNEQLQAAQAELAQAQEELESLQEEAeelqEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 573 IELNGINTKKKALTSEQEELETKLNENgtdpkkslfAKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRKTLMGV 652
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQ---------ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 653 KGDSSLKTITSLKEELEYLSGKIGTDLEKLYGKRKTLLKELYKAISNKITLYKEIYKPLIDFIEREKTEQEKSGNTLTFD 732
Cdd:COG4372 228 EAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818522855 733 AGIVFNKSAFSDSFLTFINHTKDGTFQLKDGGSKQLKDIFGKYNLQDEKSVADFADDIVHSLH 795
Cdd:COG4372 308 SLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
436-576 |
8.17e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 436 EAVQRNREEIDTKNHSIVALEEKRTDEYK--RKIEKELAEKENEYKNIKDPavvkepkgkLPEADQDKLQKIEEKITDTD 513
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPklRDRKDALEEELRQLKQLEDE---------LEDCDPTELDRAKEKLKKLL 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818522855 514 DQISKSKDRQIAVNNELafiDKLVAKLDALEDNKKKIITEISSEAKTY----GFDLSKIIKLSIELN 576
Cdd:smart00787 218 QEIMIKVKKLEELEEEL---QELESKIEDLTNKKSELNTEIAEAEKKLeqcrGFTFKEIEKLKEQLK 281
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
496-648 |
8.89e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 496 EADQDKLQKIEEKITDTDDQISKSKDRqiaVNNELAFIDKLVAK----LDALEDNKKKIITEissEAKTYGFDLSKIIKL 571
Cdd:pfam12128 279 EERQETSAELNQLLRTLDDQWKEKRDE---LNGELSAADAAVAKdrseLEALEDQHGAFLDA---DIETAAADQEQLPSW 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818522855 572 SIELNGINTKKKALTSEQEELETKLNEN----GTDPKKSLFAKKKELETSKEAITKSFDESNKKYQQYLSQKKAAENRRK 647
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYNRRrskiKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK 432
|
.
gi 818522855 648 T 648
Cdd:pfam12128 433 L 433
|
|
| |
