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Conserved domains on  [gi|1622898967|ref|XP_028696005|]
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kinesin light chain 3 isoform X4 [Macaca mulatta]

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 12138572)

tetratricopeptide repeat (TPR) protein may adopt a right-handed helical structure with an amphipathic channel and may function as an interaction scaffold in the formation of multi-protein complexes

CATH:  1.25.40.10
Gene Ontology:  GO:0005515
PubMed:  10517866|30708253
SCOP:  3001345

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TPR_12 pfam13424
Tetratricopeptide repeat;
294-370 4.08e-17

Tetratricopeptide repeat;


:

Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 75.89  E-value: 4.08e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622898967 294 DVATMLNILALVYRDQNKYKEATELLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREK 370
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
TPR_12 pfam13424
Tetratricopeptide repeat;
253-328 2.19e-10

Tetratricopeptide repeat;


:

Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 56.63  E-value: 2.19e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898967 253 RLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQ 328
Cdd:pfam13424   2 VATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
68-195 9.53e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 9.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967   68 EELVRQTRQVVQGLEALRAEHRGLAGHLAEALAGQgpvtgLEMLEEKQQVVSHSLEAIELGLGEAQVLLALSAHvgALEA 147
Cdd:COG4913    312 ERLEARLDALREELDELEAQIRGNGGDRLEQLERE-----IERLERELEERERRRARLEALLAALGLPLPASAE--EFAA 384

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622898967  148 EKQRLRSQARRLAQENVWLREELEETQRRLRASEEAVAQLEEEKRHLE 195
Cdd:COG4913    385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
 
Name Accession Description Interval E-value
TPR_12 pfam13424
Tetratricopeptide repeat;
294-370 4.08e-17

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 75.89  E-value: 4.08e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622898967 294 DVATMLNILALVYRDQNKYKEATELLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREK 370
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
251-375 9.38e-14

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.81  E-value: 9.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEdlerssghCHPDVATMLNILALVYRDQNKYKEATELLHDALQIreqtl 330
Cdd:COG0457     5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALE--------LDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL----- 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622898967 331 gpeHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVPSPL 375
Cdd:COG0457    72 ---DPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEAL 113
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 251-366 5.01e-12

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 68.02  E-value: 5.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPD-VATMLNiLALVYRDQNKYKEATELLHDALQIREQT 329
Cdd:NF040586  602 PDTLRAAKSLAVALRRAGRLEEALELAEDTYERYRRRFGPDHPDtLAAALS-LANDLRALGDADEARELAREVLDRYRRV 680

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622898967 330 LGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALE 366
Cdd:NF040586  681 LGEDHPFTLACRNNLAVLLRALGDPEEARELAEAALE 717
TPR_12 pfam13424
Tetratricopeptide repeat;
253-328 2.19e-10

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 56.63  E-value: 2.19e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898967 253 RLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQ 328
Cdd:pfam13424   2 VATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 266-386 3.70e-09

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 59.16  E-value: 3.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 266 GQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQTLGPEHPAVAATLNNLA 345
Cdd:NF040586  490 ALGRFREALELDEETLERHRRVFGEDHPRTLRAANNLAVSLRLLGDYREALELDREVLRRRRRVLGPDHPRTLLSANNLA 569

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622898967 346 VLYGKRGRYREAEPLCQRALEIREKVPSPLPNPEEPLVALS 386
Cdd:NF040586  570 RDLRELGRYAEALDLLEEALERYREVLGGPDHPDTLRAAKS 610
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 267-371 3.73e-08

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 55.70  E-value: 3.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 267 QGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDAL--QIREQTLGPEHPAVAATLNNL 344
Cdd:NF040586  405 RGDYESARDLAERALERWRERLGPDDRQTLRLRFHLANALRSLGRYEEARELDEDTLerQRRVLGLGEDHPHTLMTAGGL 484

                          90       100
                  ....*....|....*....|....*..
gi 1622898967 345 AVLYGKRGRYREAEPLCQRALEIREKV 371
Cdd:NF040586  485 GADLRALGRFREALELDEETLERHRRV 511
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 259-398 1.38e-05

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 47.61  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 259 NLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHP-DVATMLN---ILALVYRDQNKYKEATELLHDALQIREQTLGPEH 334
Cdd:NF040586  694 NLAVLLRALGDPEEARELAEAALEGLRERLGPDHPyTLAAAVNlanDLAALGDLDAALGEEALERLRRLLGEDLRAGPDH 773

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622898967 335 PAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVpsplPNPEEPLVALSMDPEHLHRDPDP 398
Cdd:NF040586  774 PDTLACAANLALDLRATGRTEEAEELRADTLARLRRV----LGPDHPDTVAAREGRRLDRDIEP 833
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 251-371 1.81e-05

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 47.22  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQTL 330
Cdd:NF040586  644 PDTLAAALSLANDLRALGDADEARELAREVLDRYRRVLGEDHPFTLACRNNLAVLLRALGDPEEARELAEAALEGLRERL 723

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622898967 331 GPEHPAVAATLNNLAVLYGKRGRYREAepLCQRALEIREKV 371
Cdd:NF040586  724 GPDHPYTLAAAVNLANDLAALGDLDAA--LGEEALERLRRL 762
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 338-370 8.36e-05

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 39.74  E-value: 8.36e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622898967  338 AATLNNLAVLYGKRGRYREAEPLCQRALEIREK 370
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
68-195 9.53e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 9.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967   68 EELVRQTRQVVQGLEALRAEHRGLAGHLAEALAGQgpvtgLEMLEEKQQVVSHSLEAIELGLGEAQVLLALSAHvgALEA 147
Cdd:COG4913    312 ERLEARLDALREELDELEAQIRGNGGDRLEQLERE-----IERLERELEERERRRARLEALLAALGLPLPASAE--EFAA 384

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622898967  148 EKQRLRSQARRLAQENVWLREELEETQRRLRASEEAVAQLEEEKRHLE 195
Cdd:COG4913    385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 292-372 1.09e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 44.69  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 292 HPDVATMLNILALVYRDQNKYKEATELLHDALQIreqtlgpeHPAVAATLNNLAVLYGKRGRYReAEPLCQRALEIREKV 371
Cdd:TIGR02917 766 HPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKK--------APDNAVVLNNLAWLYLELKDPR-ALEYAERALKLAPNI 836


                  .
gi 1622898967 372 P 372
Cdd:TIGR02917 837 P 837
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 81-195 1.71e-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: 44.28  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967   81 LEALRAEHRGLAGHLAEAlagqgpVTGLEMLEEKQQVVSHSLEAIELGLGEAQ--------VLLALSAHVGALEAEKQRL 152
Cdd:TIGR02168  234 LEELREELEELQEELKEA------EEELEELTAELQELEEKLEELRLEVSELEeeieelqkELYALANEISRLEQQKQIL 307

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1622898967  153 RSQARRLAQENVWLREELEETQRRLRASEEAVAQLEEEKRHLE 195
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 103-202 1.85e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.19  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 103 GPVTglEMLEEKQQVVSHSLEAIELGLGEAQVLLA-LSAHVGALEAEKQRLRSQARRLAQEnvwLREEL-----EETQRR 176
Cdd:cd06503    22 KPIL--KALDEREEKIAESLEEAEKAKEEAEELLAeYEEKLAEARAEAQEIIEEARKEAEK---IKEEIlaeakEEAERI 96

                          90       100
                  ....*....|....*....|....*.
gi 1622898967 177 LrasEEAVAQLEEEKRhlEFLGQLRQ 202
Cdd:cd06503    97 L---EQAKAEIEQEKE--KALAELRK 117
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 144-232 2.01e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.71  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967  144 ALEAEKQRLRSQARRLAQENVWLREELEETQRRLRASEEAVAQLEEEKRHLEF-LGQLRQYDPPTETQQSESPPRR-DSL 221
Cdd:PRK11448   146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAqLEQLQEKAAETSQERKQKRKEItDQA 225

                           90
                   ....*....|..
gi 1622898967  222 ASLFP-SEEEER 232
Cdd:PRK11448   226 AKRLElSEEETR 237
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
251-330 5.25e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 36.30  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLcRQALEDlerssghcHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQTL 330
Cdd:COG3063    23 PDNADALNNLGLLLLEQGRYDEAIAL-EKALKL--------DPNNAEALLNLAELLLELGDYDEALAYLERALELDPSAL 93
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 108-189 9.11e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 34.93  E-value: 9.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 108 LEMLEEKQQVVSHSLEAIELglgeaqvllaLSAHVGALEAEKQRLRSQARRLAQENVWLREELEETQRRLRAseeAVAQL 187
Cdd:pfam06005   3 LELLEQLETKIQAAVDTIAL----------LQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRG---LLGKL 69


                  ..
gi 1622898967 188 EE 189
Cdd:pfam06005  70 DE 71
 
Name Accession Description Interval E-value
TPR_12 pfam13424
Tetratricopeptide repeat;
294-370 4.08e-17

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 75.89  E-value: 4.08e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622898967 294 DVATMLNILALVYRDQNKYKEATELLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREK 370
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
251-375 9.38e-14

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.81  E-value: 9.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEdlerssghCHPDVATMLNILALVYRDQNKYKEATELLHDALQIreqtl 330
Cdd:COG0457     5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALE--------LDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL----- 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622898967 331 gpeHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVPSPL 375
Cdd:COG0457    72 ---DPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEAL 113
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
251-377 1.00e-12

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 67.72  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDlerssghcHPDVATMLNILALVYRDQNKYKEATELLHDALQIReqtl 330
Cdd:COG0457    39 PDDAEALYNLGLAYLRLGRYEEALADYEQALEL--------DPDDAEALNNLGLALQALGRYEEALEDYDKALELD---- 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622898967 331 gpehPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVPSPLPN 377
Cdd:COG0457   107 ----PDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYN 149
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 251-368 2.39e-12

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 68.87  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEdlerssghCHPDVATMLNILALVYRDQNKYKEATELLHDALQIReqtl 330
Cdd:COG3914   109 PDNAEALFNLGNLLLALGRLEEALAALRRALA--------LNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELD---- 176

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622898967 331 gPEHPAVaatLNNLAVLYGKRGRYREAEPLCQRALEIR 368
Cdd:COG3914   177 -PDNAEA---LNNLGNALQDLGRLEEAIAAYRRALELD 210
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 251-366 5.01e-12

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 68.02  E-value: 5.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPD-VATMLNiLALVYRDQNKYKEATELLHDALQIREQT 329
Cdd:NF040586  602 PDTLRAAKSLAVALRRAGRLEEALELAEDTYERYRRRFGPDHPDtLAAALS-LANDLRALGDADEARELAREVLDRYRRV 680

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622898967 330 LGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALE 366
Cdd:NF040586  681 LGEDHPFTLACRNNLAVLLRALGDPEEARELAEAALE 717
TPR_12 pfam13424
Tetratricopeptide repeat;
253-328 2.19e-10

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 56.63  E-value: 2.19e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898967 253 RLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQ 328
Cdd:pfam13424   2 VATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
TPR_10 pfam13374
Tetratricopeptide repeat;
295-335 4.35e-10

Tetratricopeptide repeat;


Pssm-ID: 463861 [Multi-domain]  Cd Length: 42  Bit Score: 54.82  E-value: 4.35e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622898967 295 VATMLNILALVYRDQNKYKEATELLHDALQIREQTLGPEHP 335
Cdd:pfam13374   1 TASSLNNLANALRAQGRYDEAEELLEEALAIRERVLGPDHP 41
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
251-369 5.30e-10

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 59.64  E-value: 5.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEdlerssghCHPDVATMLNILALVYRDQNKYKEATELLHDALQIReqtl 330
Cdd:COG0457    73 PDDAEALNNLGLALQALGRYEEALEDYDKALE--------LDPDDAEALYNLGLALLELGRYDEAIEAYERALELD---- 140

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622898967 331 gpehPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIRE 369
Cdd:COG0457   141 ----PDDADALYNLGIALEKLGRYEEALELLEKLEAAAL 175
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 266-386 3.70e-09

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 59.16  E-value: 3.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 266 GQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQTLGPEHPAVAATLNNLA 345
Cdd:NF040586  490 ALGRFREALELDEETLERHRRVFGEDHPRTLRAANNLAVSLRLLGDYREALELDREVLRRRRRVLGPDHPRTLLSANNLA 569

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622898967 346 VLYGKRGRYREAEPLCQRALEIREKVPSPLPNPEEPLVALS 386
Cdd:NF040586  570 RDLRELGRYAEALDLLEEALERYREVLGGPDHPDTLRAAKS 610
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
264-367 1.31e-08

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 52.09  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 264 YAGQGRYEVAVPLCRQALEDlerssghcHPDVATMLNILALVYRDQNKYKEATELlHDALQIreqtlgpeHPAVAATLNN 343
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALEL--------DPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL--------DPNNAEALLN 64

                          90       100
                  ....*....|....*....|....
gi 1622898967 344 LAVLYGKRGRYREAEPLCQRALEI 367
Cdd:COG3063    65 LAELLLELGDYDEALAYLERALEL 88
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
293-377 2.57e-08

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 54.63  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 293 PDVATMLNILALVYRDQNKYKEATELLHDALQIreqtlgpeHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVP 372
Cdd:COG0457     5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALEL--------DPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDA 76


                  ....*
gi 1622898967 373 SPLPN 377
Cdd:COG0457    77 EALNN 81
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 267-371 3.73e-08

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 55.70  E-value: 3.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 267 QGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDAL--QIREQTLGPEHPAVAATLNNL 344
Cdd:NF040586  405 RGDYESARDLAERALERWRERLGPDDRQTLRLRFHLANALRSLGRYEEARELDEDTLerQRRVLGLGEDHPHTLMTAGGL 484

                          90       100
                  ....*....|....*....|....*..
gi 1622898967 345 AVLYGKRGRYREAEPLCQRALEIREKV 371
Cdd:NF040586  485 GADLRALGRFREALELDEETLERHRRV 511
TPR_10 pfam13374
Tetratricopeptide repeat;
337-371 4.50e-08

Tetratricopeptide repeat;


Pssm-ID: 463861 [Multi-domain]  Cd Length: 42  Bit Score: 49.04  E-value: 4.50e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1622898967 337 VAATLNNLAVLYGKRGRYREAEPLCQRALEIREKV 371
Cdd:pfam13374   1 TASSLNNLANALRAQGRYDEAEELLEEALAIRERV 35
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 252-375 1.16e-07

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 50.58  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 252 ARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDlerssghcHPDVATMLNILALVYRDQNKYKEATELLHDALQIReqtlg 331
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALLEKALEL--------DPDNPEAFALLGEILLQLGDLDEAIVLLHEALELD----- 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622898967 332 PEHPAVaatLNNLAVLYGKRGRYREAEPLCQRALEIREKVPSPL 375
Cdd:COG4783    69 PDEPEA---RLNLGLALLKAGDYDEALALLEKALKLDPEHPEAY 109
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 264-367 8.31e-07

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 48.80  E-value: 8.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 264 YAGQGRYEVAVPLCRQALEdlerssghCHPDVATMLNILALVYRDQNKYKEATELLHDALQIreqtlgpeHPAVAATLNN 343
Cdd:COG5010    64 YNKLGDFEESLALLEQALQ--------LDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL--------SPDNPNAYSN 127

                          90       100
                  ....*....|....*....|....
gi 1622898967 344 LAVLYGKRGRYREAEPLCQRALEI 367
Cdd:COG5010   128 LAALLLSLGQDDEAKAALQRALGT 151
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 251-367 1.31e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 49.73  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDlerssghcHPDVATMLNILALVYRDQNKYKEATELLHDALQIreqtl 330
Cdd:COG2956   107 PDDAEALRLLAEIYEQEGDWEKAIEVLERLLKL--------GPENAHAYCELAELYLEQGDYDEAIEALEKALKL----- 173

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622898967 331 gpeHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEI 367
Cdd:COG2956   174 ---DPDCARALLLLAELYLEQGDYEEAIAALERALEQ 207
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 251-367 4.28e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 46.34  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDlerssghcHPDVATMLNILALVYRDQNKYKEATELLHDALQireqtL 330
Cdd:COG4783    35 PDNPEAFALLGEILLQLGDLDEAIVLLHEALEL--------DPDEPEARLNLGLALLKAGDYDEALALLEKALK-----L 101

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622898967 331 GPEHPAVaatLNNLAVLYGKRGRYREAEPLCQRALEI 367
Cdd:COG4783   102 DPEHPEA---YLRLARAYRALGRPDEAIAALEKALEL 135
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 251-367 9.04e-06

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 45.00  E-value: 9.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLerssghchPDVATMLNILALVYRDQNKYKEATELLHDALQireqtL 330
Cdd:COG4235    14 PNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLD--------PDNADALLDLAEALLAAGDTEEAEELLERALA-----L 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622898967 331 GPEHPAVaatLNNLAVLYGKRGRYREAEPLCQRALEI 367
Cdd:COG4235    81 DPDNPEA---LYLLGLAAFQQGDYAEAIAAWQKLLAL 114
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 259-398 1.38e-05

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 47.61  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 259 NLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHP-DVATMLN---ILALVYRDQNKYKEATELLHDALQIREQTLGPEH 334
Cdd:NF040586  694 NLAVLLRALGDPEEARELAEAALEGLRERLGPDHPyTLAAAVNlanDLAALGDLDAALGEEALERLRRLLGEDLRAGPDH 773

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622898967 335 PAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVpsplPNPEEPLVALSMDPEHLHRDPDP 398
Cdd:NF040586  774 PDTLACAANLALDLRATGRTEEAEELRADTLARLRRV----LGPDHPDTVAAREGRRLDRDIEP 833
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 249-368 1.71e-05

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 47.30  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 249 EIPARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSsgHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIreq 328
Cdd:COG3914    33 EAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAA--AALLLLAALLELAALLLQALGRYEEALALYRRALAL--- 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622898967 329 tlgpeHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIR 368
Cdd:COG3914   108 -----NPDNAEALFNLGNLLLALGRLEEALAALRRALALN 142
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 251-371 1.81e-05

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 47.22  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQTL 330
Cdd:NF040586  644 PDTLAAALSLANDLRALGDADEARELAREVLDRYRRVLGEDHPFTLACRNNLAVLLRALGDPEEARELAEAALEGLRERL 723

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622898967 331 GPEHPAVAATLNNLAVLYGKRGRYREAepLCQRALEIREKV 371
Cdd:NF040586  724 GPDHPYTLAAAVNLANDLAALGDLDAA--LGEEALERLRRL 762
TPR_1 pfam00515
Tetratricopeptide repeat;
338-370 2.17e-05

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 41.25  E-value: 2.17e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622898967 338 AATLNNLAVLYGKRGRYREAEPLCQRALEIREK 370
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPN 33
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 338-370 8.36e-05

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 39.74  E-value: 8.36e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622898967  338 AATLNNLAVLYGKRGRYREAEPLCQRALEIREK 370
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
68-195 9.53e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 9.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967   68 EELVRQTRQVVQGLEALRAEHRGLAGHLAEALAGQgpvtgLEMLEEKQQVVSHSLEAIELGLGEAQVLLALSAHvgALEA 147
Cdd:COG4913    312 ERLEARLDALREELDELEAQIRGNGGDRLEQLERE-----IERLERELEERERRRARLEALLAALGLPLPASAE--EFAA 384

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622898967  148 EKQRLRSQARRLAQENVWLREELEETQRRLRASEEAVAQLEEEKRHLE 195
Cdd:COG4913    385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 292-372 1.09e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 44.69  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 292 HPDVATMLNILALVYRDQNKYKEATELLHDALQIreqtlgpeHPAVAATLNNLAVLYGKRGRYReAEPLCQRALEIREKV 371
Cdd:TIGR02917 766 HPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKK--------APDNAVVLNNLAWLYLELKDPR-ALEYAERALKLAPNI 836


                  .
gi 1622898967 372 P 372
Cdd:TIGR02917 837 P 837
TPR_12 pfam13424
Tetratricopeptide repeat;
337-374 1.11e-04

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 40.45  E-value: 1.11e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622898967 337 VAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVPSP 374
Cdd:pfam13424   2 VATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGP 39
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 251-368 1.24e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 43.56  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDlerssghcHPDVATMLNILALVYRDQNKYKEATELLHDALQireqtl 330
Cdd:COG2956   175 PDCARALLLLAELYLEQGDYEEAIAALERALEQ--------DPDYLPALPRLAELYEKLGDPEEALELLRKALE------ 240

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622898967 331 gpEHPAVAAtLNNLAVLYGKRGRYREAEPLCQRALEIR 368
Cdd:COG2956   241 --LDPSDDL-LLALADLLERKEGLEAALALLERQLRRH 275
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 68-195 1.60e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967  68 EELVRQTRQVVQGLEALRAEHRGLAGHLAEALAGqgpvtgLEMLEEKQQVVSHSLEAIELGLGEAQ-VLLALSAHVGALE 146
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAE------LAELEAELEELRLELEELELELEEAQaEEYELLAELARLE 301

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1622898967 147 AEKQRLRSQARRLAQENVWLREELEETQRRLRASEEAVAQLEEEKRHLE 195
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 81-195 1.71e-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: 44.28  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967   81 LEALRAEHRGLAGHLAEAlagqgpVTGLEMLEEKQQVVSHSLEAIELGLGEAQ--------VLLALSAHVGALEAEKQRL 152
Cdd:TIGR02168  234 LEELREELEELQEELKEA------EEELEELTAELQELEEKLEELRLEVSELEeeieelqkELYALANEISRLEQQKQIL 307

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1622898967  153 RSQARRLAQENVWLREELEETQRRLRASEEAVAQLEEEKRHLE 195
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
305-377 3.28e-04

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 39.77  E-value: 3.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898967 305 VYRDQNKYKEATELLHDALQIreqtlgpeHPAVAATLNNLAVLYGKRGRYREAEPLcQRALEIREKVPSPLPN 377
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALEL--------DPDNADALNNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLN 64
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
292-368 3.72e-04

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 41.82  E-value: 3.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622898967 292 HPDVATMLNILALVYRDQNKYKEATELLHDALQIReqtlgpehPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIR 368
Cdd:COG4785    69 LPDLAQLYYERGVAYDSLGDYDLAIADFDQALELD--------PDLAEAYNNRGLAYLLLGDYDAALEDFDRALELD 137
TPR_7 pfam13176
Tetratricopeptide repeat;
340-374 3.73e-04

Tetratricopeptide repeat;


Pssm-ID: 433012 [Multi-domain]  Cd Length: 36  Bit Score: 37.90  E-value: 3.73e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1622898967 340 TLNNLAVLYGKRGRYREAEPLCQRALEIREKVPSP 374
Cdd:pfam13176   1 ALLNLGRIYRKLGDYDEAISLYEQALALAKDPYDR 35
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 263-375 5.81e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 41.64  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 263 QYAGQGRYEVAVPLCRQALEDlerssghcHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQTlgpehpavAATLN 342
Cdd:COG2956    17 NYLLNGQPDKAIDLLEEALEL--------DPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDR--------AEALL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622898967 343 NLAVLYGKRGRYREAEPLCQRALEIREKVPSPL 375
Cdd:COG2956    81 ELAQDYLKAGLLDRAEELLEKLLELDPDDAEAL 113
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
251-372 6.73e-04

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 41.05  E-value: 6.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDlerssghcHPDVATMLNILALVYRDQNKYKEATELLHDALQIReqtl 330
Cdd:COG4785    70 PDLAQLYYERGVAYDSLGDYDLAIADFDQALEL--------DPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELD---- 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622898967 331 gPEHpavAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVP 372
Cdd:COG4785   138 -PDY---AYAYLNRGIALYYLGRYELAIADLEKALELDPNDP 175
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-195 7.45e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 7.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967   81 LEALRAEHRGLAGHLAEAlagQGPVTGLEMLEEKQQVVSHSLEAIELGLGEAQVLLALSAHVGALEAEKQRLRSQARRLA 160
Cdd:COG4913    612 LAALEAELAELEEELAEA---EERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA 688

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1622898967  161 QenvwLREELEETQRRLRASEEAVAQLEEEKRHLE 195
Cdd:COG4913    689 A----LEEQLEELEAELEELEEELDELKGEIGRLE 719
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 251-377 8.53e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 39.94  E-value: 8.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIreqtl 330
Cdd:COG5010     9 RLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQL----- 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622898967 331 gpeHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVPSPLPN 377
Cdd:COG5010    84 ---DPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSN 127
TPR_10 pfam13374
Tetratricopeptide repeat;
254-294 9.48e-04

Tetratricopeptide repeat;


Pssm-ID: 463861 [Multi-domain]  Cd Length: 42  Bit Score: 36.71  E-value: 9.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622898967 254 LRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPD 294
Cdd:pfam13374   2 ASSLNNLANALRAQGRYDEAEELLEEALAIRERVLGPDHPD 42
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 264-367 1.62e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.10  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 264 YAGQGRYEVAVPLCRQALEDlerssghcHPDVATMLNILALVYRDQNKYKEATELLHDALQIReqtlgpehPAVAATLNN 343
Cdd:COG2956    52 YRRRGEYDRAIRIHQKLLER--------DPDRAEALLELAQDYLKAGLLDRAEELLEKLLELD--------PDDAEALRL 115

                          90       100
                  ....*....|....*....|....
gi 1622898967 344 LAVLYGKRGRYREAEPLCQRALEI 367
Cdd:COG2956   116 LAEIYEQEGDWEKAIEVLERLLKL 139
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 103-202 1.85e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.19  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 103 GPVTglEMLEEKQQVVSHSLEAIELGLGEAQVLLA-LSAHVGALEAEKQRLRSQARRLAQEnvwLREEL-----EETQRR 176
Cdd:cd06503    22 KPIL--KALDEREEKIAESLEEAEKAKEEAEELLAeYEEKLAEARAEAQEIIEEARKEAEK---IKEEIlaeakEEAERI 96

                          90       100
                  ....*....|....*....|....*.
gi 1622898967 177 LrasEEAVAQLEEEKRhlEFLGQLRQ 202
Cdd:cd06503    97 L---EQAKAEIEQEKE--KALAELRK 117
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 144-232 2.01e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.71  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967  144 ALEAEKQRLRSQARRLAQENVWLREELEETQRRLRASEEAVAQLEEEKRHLEF-LGQLRQYDPPTETQQSESPPRR-DSL 221
Cdd:PRK11448   146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAqLEQLQEKAAETSQERKQKRKEItDQA 225

                           90
                   ....*....|..
gi 1622898967  222 ASLFP-SEEEER 232
Cdd:PRK11448   226 AKRLElSEEETR 237
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 68-195 2.32e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967  68 EELVRQTRQVVQGLEALRAEHRGLAGHLAEALAGqgpvtgLEMLEEKQQVVSHSLEAIELGLGEAQVLLAlsahvgALEA 147
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARLEERRRELEERLE------ELEE 323

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622898967 148 EKQRLRSQARRLAQENVWLREELEETQRRLRASEEAVAQLEEEKRHLE 195
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-195 2.43e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967  81 LEALRAEHRGLAGHLAEALAGQgpvtgLEMLEEKQQVVSHSLEAIELGLGEAQVLLALSAHVGALEAEKQRLRSQARRLA 160
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAEL-----AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622898967 161 QENVWLREELEETQRRLRASEEAVAQLEEEKRHLE 195
Cdd:COG1196   428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
251-330 5.25e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 36.30  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLcRQALEDlerssghcHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQTL 330
Cdd:COG3063    23 PDNADALNNLGLLLLEQGRYDEAIAL-EKALKL--------DPNNAEALLNLAELLLELGDYDEALAYLERALELDPSAL 93
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
68-197 5.71e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 5.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967   68 EELVRQTRQVVQGLEALRAEHRGLAGHLAEALAGQGPVTGLEMLEEKqqvvshsLEAIELGLGEaqvLLALSAHVGALEA 147
Cdd:COG4913    630 EERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE-------LERLDASSDD---LAALEEQLEELEA 699

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622898967  148 EKQRLRSQARRLAQENVWLREELEETQRRLRASEEAVAQLEEEKRHLEFL 197
Cdd:COG4913    700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 301-370 5.76e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 38.56  E-value: 5.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 301 ILALVYRDQNKYKEATELLHDALQIreqtlgpeHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREK 370
Cdd:COG2956    13 FKGLNYLLNGQPDKAIDLLEEALEL--------DPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPD 74
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
251-369 6.03e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 38.45  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQALEdlerssghCHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQTL 330
Cdd:COG0457   107 PDDAEALYNLGLALLELGRYDEAIEAYERALE--------LDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAAL 178

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622898967 331 GPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIRE 369
Cdd:COG0457   179 LAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLA 217
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 67-194 7.49e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 38.78  E-value: 7.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967   67 PEELVRQTRQVVQGLEALRAEhrglaghlaealagqgpvtglemLEEKQQVVSHSLEAIELGLGEAQVLLALSAhvgALE 146
Cdd:PRK11448   137 PEDPENLLHALQQEVLTLKQQ-----------------------LELQAREKAQSQALAEAQQQELVALEGLAA---ELE 190

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622898967  147 AEKQRLRSQARRLAQENvwLREELEETQRRLRASEEAVAQL---EEEKRHL 194
Cdd:PRK11448   191 EKQQELEAQLEQLQEKA--AETSQERKQKRKEITDQAAKRLelsEEETRIL 239
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 108-189 9.11e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 34.93  E-value: 9.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 108 LEMLEEKQQVVSHSLEAIELglgeaqvllaLSAHVGALEAEKQRLRSQARRLAQENVWLREELEETQRRLRAseeAVAQL 187
Cdd:pfam06005   3 LELLEQLETKIQAAVDTIAL----------LQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRG---LLGKL 69


                  ..
gi 1622898967 188 EE 189
Cdd:pfam06005  70 DE 71
TPR_MalT pfam17874
MalT-like TPR region; This entry contains a series of TPR repeats.
 251-372 9.59e-03

MalT-like TPR region; This entry contains a series of TPR repeats.


Pssm-ID: 436107 [Multi-domain]  Cd Length: 336  Bit Score: 38.06  E-value: 9.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 251 PARLRTLHNLVIQYAGQGRYEVAVPLCRQAlEDLERSSGHCHPDVATMLnILALVYRDQNKYKEATELLHDALQIREQTL 330
Cdd:pfam17874  37 LARGLATFVLGEAYLCLGDLDAALQAMREA-EALARRADSPHVTLWALL-QQGEILRAQGRLHQALETYQQALQLARDHG 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622898967 331 GPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVP 372
Cdd:pfam17874 115 LQHLPLHGFLLVGLADLLYEWNDLEEAEQHAQQGIQLGRQWE 156
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 262-357 9.70e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 35.74  E-value: 9.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898967 262 IQYAGQGRYEVAVPLCRQALEDLERSsghchPDVATMLNILALVYRDQNKYKEATELLHDALQireqtLGPEHPAVAATL 341
Cdd:COG1729     1 KALLKAGDYDEAIAAFKAFLKRYPNS-----PLAPDALYWLGEAYYALGDYDEAAEAFEKLLK-----RYPDSPKAPDAL 70

                          90
                  ....*....|....*.
gi 1622898967 342 NNLAVLYGKRGRYREA 357
Cdd:COG1729    71 LKLGLSYLELGDYDKA 86
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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