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Conserved domains on  [gi|2124314332|gb|KAH6603095|]
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hypothetical protein BASA61_000457 [Batrachochytrium salamandrivorans]

Protein Classification

PTZ00121 and zf-C3H1 domain-containing protein( domain architecture ID 10566355)

protein containing domains PTZ00121, zf-C3H1, and NrfG

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-C3H1 pfam10650
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ...
 1568-1589 1.18e-06

Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger domain as it contains three conserved Cs and an H in the C-x8-C-x5-C-x3-H conformation typical of a zinc-finger.


:

Pssm-ID: 431418  Cd Length: 22  Bit Score: 46.42  E-value: 1.18e-06
                           10        20
                   ....*....|....*....|..
gi 2124314332 1568 LCQYETRGGRCWDTTCAGQHFR 1589
Cdd:pfam10650    1 LCPYELAGGVCNDPSCEFQHFR 22
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1181-1302 2.72e-06

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 2.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332 1181 NQYEKMIAIILESNTKTQILLKAIQEQCSTVALSISIPERKETETKEKLGHIYIEQAQVDEQIITLEKRQAMLSAGATKL 1260
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2124314332 1261 EDEVAELRKLVASRRDNLAEYRLREKALEQDLLNGTTRLQEL 1302
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 447-567 1.30e-04

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.39  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  447 ERRQHNPEILRQSRLQNHQSHIPLSHWQQPQPPLHSYDQNVQPASQFPFFPQVEFLNQQVTPLVTTyiaPPPFHDALQPP 526
Cdd:PRK10263   752 VQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQY---QQPQQPVAPQP 828

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2124314332  527 SFMKPLPPIMFPGNGNIavtpTHSLNMANGITMPSNIPFPP 567
Cdd:PRK10263   829 QYQQPQQPVAPQPQDTL----LHPLLMRNGDSRPLHKPTTP 865
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 194-400 1.65e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 47.21  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  194 ESDNNSNHNHTSVQNDLYNDISNSPAYIEESGLYSLQELACSPEICDSTDSIDSSTHYQDSGSQSLDAASSLSPISDDAS 273
Cdd:NF033609   562 DSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSD 641

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  274 EDGSTKISCISLQALESSTDM-HNSASVSPSTSRECSPIKGASACDLARNNTVDGVIAESTYSQPTSNSKELSTEITEVD 352
Cdd:NF033609   642 SDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 721

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2124314332  353 IEIDSGDSVDKEEGEISDTDEPVVYVTDEVSSANLSKNDQSKDLSDSD 400
Cdd:NF033609   722 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 769
CwlO1 super family cl25603
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1235-1407 7.22e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


The actual alignment was detected with superfamily member COG3883:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 7.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332 1235 EQAQVDEQIITLEKRQAMLSAGATKLEDEVAELRKLVASRRDNLAEYRLREKALEQDLLNGTTRLQELQLQINKKRSAAA 1314
Cdd:COG3883    141 DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332 1315 AWLSSSGSLSINTTADLSSCIIANSADDLASASDMPIPKRPKLSDAVPLDAPICAISPDSTKSGSLYDDIAPTVIGTDPC 1394
Cdd:COG3883    221 AAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAAS 300

                          170
                   ....*....|...
gi 2124314332 1395 HVASSSIPAVSSV 1407
Cdd:COG3883    301 GGSGGGSGGAGGV 313
 
Name Accession Description Interval E-value
zf-C3H1 pfam10650
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ...
 1568-1589 1.18e-06

Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger domain as it contains three conserved Cs and an H in the C-x8-C-x5-C-x3-H conformation typical of a zinc-finger.


Pssm-ID: 431418  Cd Length: 22  Bit Score: 46.42  E-value: 1.18e-06
                           10        20
                   ....*....|....*....|..
gi 2124314332 1568 LCQYETRGGRCWDTTCAGQHFR 1589
Cdd:pfam10650    1 LCPYELAGGVCNDPSCEFQHFR 22
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1181-1302 2.72e-06

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: 53.14  E-value: 2.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332 1181 NQYEKMIAIILESNTKTQILLKAIQEQCSTVALSISIPERKETETKEKLGHIYIEQAQVDEQIITLEKRQAMLSAGATKL 1260
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2124314332 1261 EDEVAELRKLVASRRDNLAEYRLREKALEQDLLNGTTRLQEL 1302
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 447-567 1.30e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.39  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  447 ERRQHNPEILRQSRLQNHQSHIPLSHWQQPQPPLHSYDQNVQPASQFPFFPQVEFLNQQVTPLVTTyiaPPPFHDALQPP 526
Cdd:PRK10263   752 VQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQY---QQPQQPVAPQP 828

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2124314332  527 SFMKPLPPIMFPGNGNIavtpTHSLNMANGITMPSNIPFPP 567
Cdd:PRK10263   829 QYQQPQQPVAPQPQDTL----LHPLLMRNGDSRPLHKPTTP 865
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 194-400 1.65e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 47.21  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  194 ESDNNSNHNHTSVQNDLYNDISNSPAYIEESGLYSLQELACSPEICDSTDSIDSSTHYQDSGSQSLDAASSLSPISDDAS 273
Cdd:NF033609   562 DSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSD 641

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  274 EDGSTKISCISLQALESSTDM-HNSASVSPSTSRECSPIKGASACDLARNNTVDGVIAESTYSQPTSNSKELSTEITEVD 352
Cdd:NF033609   642 SDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 721

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2124314332  353 IEIDSGDSVDKEEGEISDTDEPVVYVTDEVSSANLSKNDQSKDLSDSD 400
Cdd:NF033609   722 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 769
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1235-1310 7.04e-04

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: 44.37  E-value: 7.04e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124314332 1235 EQAQVDEQIITLEKRQAMLSAGATKLEDEVAELRKLVASRRDNLAEYRLREKALEQDLLNGTTRLQELQLQINKKR 1310
Cdd:COG4942     28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 458-541 9.93e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.08  E-value: 9.93e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332   458 QSRLQNHQSHIPLSHWQQPQ---------PPLHS------YDQNVQPASQFPFFPQveflnqqvtplvttYIAPPPFHDA 522
Cdd:smart00818   48 PTHTLQPHHHIPVLPAQQPVvpqqplmpvPGQHSmtptqhHQPNLPQPAQQPFQPQ--------------PLQPPQPQQP 113

                            90
                    ....*....|....*....
gi 2124314332   523 LQPPSFMKPLPPIMFPGNG 541
Cdd:smart00818  114 MQPQPPVHPIPPLPPQPPL 132
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 194-400 1.11e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  194 ESDNNSNHNHTSVQNDLYNDISNSPAYIE-ESGLYSLQELACSPEICDSTDSIDSSTHYQDSGSQSLDAASSLSPISDDA 272
Cdd:NF033609   609 DSDSASDSDSASDSDSASDSDSASDSDSAsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  273 SEDGSTKISCISLQALESSTDmHNSASVSPSTSRECSPIKGASACDLARNNTVDGVIAESTYSQPTSNSKELSTEITEVD 352
Cdd:NF033609   689 DSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 767

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2124314332  353 IEIDSGDSVDKEEGEISDTDEPVVYVTDEVSSANLSKNDQSKDLSDSD 400
Cdd:NF033609   768 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 815
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 194-400 1.76e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 43.74  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  194 ESDNNSNHNHTSVQNDLYNDISNSPAYIEESGLYSLQELACSPEICDS-TDSIDSSTHYQDSGSQSLDAASSLSPISDDA 272
Cdd:NF033609   621 DSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  273 SEDGSTKISCISLQALESSTDMHN---SASVSPSTSRECSPIKGASACDLARNNTVDGVIAESTYSQPTSNSKELSTEIT 349
Cdd:NF033609   701 DSDSDSDSDSDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 780

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2124314332  350 EVDIEIDSGDSVDKEEGEISDTDEPVVYVTDEVSSANLSKNDQSKDLSDSD 400
Cdd:NF033609   781 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 831
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1235-1407 7.22e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 7.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332 1235 EQAQVDEQIITLEKRQAMLSAGATKLEDEVAELRKLVASRRDNLAEYRLREKALEQDLLNGTTRLQELQLQINKKRSAAA 1314
Cdd:COG3883    141 DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332 1315 AWLSSSGSLSINTTADLSSCIIANSADDLASASDMPIPKRPKLSDAVPLDAPICAISPDSTKSGSLYDDIAPTVIGTDPC 1394
Cdd:COG3883    221 AAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAAS 300

                          170
                   ....*....|...
gi 2124314332 1395 HVASSSIPAVSSV 1407
Cdd:COG3883    301 GGSGGGSGGAGGV 313
 
Name Accession Description Interval E-value
zf-C3H1 pfam10650
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ...
 1568-1589 1.18e-06

Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger domain as it contains three conserved Cs and an H in the C-x8-C-x5-C-x3-H conformation typical of a zinc-finger.


Pssm-ID: 431418  Cd Length: 22  Bit Score: 46.42  E-value: 1.18e-06
                           10        20
                   ....*....|....*....|..
gi 2124314332 1568 LCQYETRGGRCWDTTCAGQHFR 1589
Cdd:pfam10650    1 LCPYELAGGVCNDPSCEFQHFR 22
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1181-1302 2.72e-06

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: 53.14  E-value: 2.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332 1181 NQYEKMIAIILESNTKTQILLKAIQEQCSTVALSISIPERKETETKEKLGHIYIEQAQVDEQIITLEKRQAMLSAGATKL 1260
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2124314332 1261 EDEVAELRKLVASRRDNLAEYRLREKALEQDLLNGTTRLQEL 1302
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 447-567 1.30e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.39  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  447 ERRQHNPEILRQSRLQNHQSHIPLSHWQQPQPPLHSYDQNVQPASQFPFFPQVEFLNQQVTPLVTTyiaPPPFHDALQPP 526
Cdd:PRK10263   752 VQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQY---QQPQQPVAPQP 828

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2124314332  527 SFMKPLPPIMFPGNGNIavtpTHSLNMANGITMPSNIPFPP 567
Cdd:PRK10263   829 QYQQPQQPVAPQPQDTL----LHPLLMRNGDSRPLHKPTTP 865
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 194-400 1.65e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 47.21  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  194 ESDNNSNHNHTSVQNDLYNDISNSPAYIEESGLYSLQELACSPEICDSTDSIDSSTHYQDSGSQSLDAASSLSPISDDAS 273
Cdd:NF033609   562 DSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSD 641

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  274 EDGSTKISCISLQALESSTDM-HNSASVSPSTSRECSPIKGASACDLARNNTVDGVIAESTYSQPTSNSKELSTEITEVD 352
Cdd:NF033609   642 SDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 721

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2124314332  353 IEIDSGDSVDKEEGEISDTDEPVVYVTDEVSSANLSKNDQSKDLSDSD 400
Cdd:NF033609   722 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 769
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1235-1310 7.04e-04

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: 44.37  E-value: 7.04e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124314332 1235 EQAQVDEQIITLEKRQAMLSAGATKLEDEVAELRKLVASRRDNLAEYRLREKALEQDLLNGTTRLQELQLQINKKR 1310
Cdd:COG4942     28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 458-541 9.93e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.08  E-value: 9.93e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332   458 QSRLQNHQSHIPLSHWQQPQ---------PPLHS------YDQNVQPASQFPFFPQveflnqqvtplvttYIAPPPFHDA 522
Cdd:smart00818   48 PTHTLQPHHHIPVLPAQQPVvpqqplmpvPGQHSmtptqhHQPNLPQPAQQPFQPQ--------------PLQPPQPQQP 113

                            90
                    ....*....|....*....
gi 2124314332   523 LQPPSFMKPLPPIMFPGNG 541
Cdd:smart00818  114 MQPQPPVHPIPPLPPQPPL 132
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 194-400 1.11e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  194 ESDNNSNHNHTSVQNDLYNDISNSPAYIE-ESGLYSLQELACSPEICDSTDSIDSSTHYQDSGSQSLDAASSLSPISDDA 272
Cdd:NF033609   609 DSDSASDSDSASDSDSASDSDSASDSDSAsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  273 SEDGSTKISCISLQALESSTDmHNSASVSPSTSRECSPIKGASACDLARNNTVDGVIAESTYSQPTSNSKELSTEITEVD 352
Cdd:NF033609   689 DSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 767

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2124314332  353 IEIDSGDSVDKEEGEISDTDEPVVYVTDEVSSANLSKNDQSKDLSDSD 400
Cdd:NF033609   768 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 815
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 194-400 1.76e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 43.74  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  194 ESDNNSNHNHTSVQNDLYNDISNSPAYIEESGLYSLQELACSPEICDS-TDSIDSSTHYQDSGSQSLDAASSLSPISDDA 272
Cdd:NF033609   621 DSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332  273 SEDGSTKISCISLQALESSTDMHN---SASVSPSTSRECSPIKGASACDLARNNTVDGVIAESTYSQPTSNSKELSTEIT 349
Cdd:NF033609   701 DSDSDSDSDSDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 780

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2124314332  350 EVDIEIDSGDSVDKEEGEISDTDEPVVYVTDEVSSANLSKNDQSKDLSDSD 400
Cdd:NF033609   781 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 831
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1178-1310 4.54e-03

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: 42.35  E-value: 4.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332 1178 ADNNQYEKMIAIILESNTK---TQILLKAIQEQCSTVALSISIPER-------KETETKEKLGHIYIEQAQVDEQIITLE 1247
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKelteleaEIEELEERLEEAEEELAEAEAEIEELE 788

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124314332 1248 KRQAMLSAGATKLEDEVAELRKLVASRRDNLAEYRLREKALEQDLLNGTTRLQELQLQINKKR 1310
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1235-1407 7.22e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 7.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332 1235 EQAQVDEQIITLEKRQAMLSAGATKLEDEVAELRKLVASRRDNLAEYRLREKALEQDLLNGTTRLQELQLQINKKRSAAA 1314
Cdd:COG3883    141 DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124314332 1315 AWLSSSGSLSINTTADLSSCIIANSADDLASASDMPIPKRPKLSDAVPLDAPICAISPDSTKSGSLYDDIAPTVIGTDPC 1394
Cdd:COG3883    221 AAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAAS 300

                          170
                   ....*....|...
gi 2124314332 1395 HVASSSIPAVSSV 1407
Cdd:COG3883    301 GGSGGGSGGAGGV 313
 
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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