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Conserved domains on  [gi|1732743867|ref|WP_148682925|]
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hypothetical protein [Pyrobaculum ferrireducens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 11467523)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 40-111 4.77e-08

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


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 4.77e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732743867  40 LATIGKELDEIRREIAEVNQRIDQTNRRIDEISKKIDETNMRIDETNKRIDAIAQELGRRIDETNKRIDGVY 111
Cdd:COG3883    25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
 
Name Accession Description Interval E-value
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 40-111 4.77e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 4.77e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732743867  40 LATIGKELDEIRREIAEVNQRIDQTNRRIDEISKKIDETNMRIDETNKRIDAIAQELGRRIDETNKRIDGVY 111
Cdd:COG3883    25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 46-126 6.45e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 38.11  E-value: 6.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732743867   46 ELDEIRREIAEVNQRIDQTNRRIDEISKK----IDETNMRIDETNKRIDAI-----AQELGRRIDETNKRIDGVYALLLD 116
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKsenyIDEIKAQINDLEDVADKAisnddPEEIEKKIENIVTKIDKKKNIYDE 1191

                           90
                   ....*....|
gi 1732743867  117 MQKLLVEIAR 126
Cdd:TIGR01612 1192 IKKLLNEIAE 1201
 
Name Accession Description Interval E-value
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 40-111 4.77e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 4.77e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732743867  40 LATIGKELDEIRREIAEVNQRIDQTNRRIDEISKKIDETNMRIDETNKRIDAIAQELGRRIDETNKRIDGVY 111
Cdd:COG3883    25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 45-114 5.71e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 5.71e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732743867  45 KELDEIRREIAEVNQRIDQTNRRIDEISKKIDETNMRIDETNKRIDAIAQElgrrIDETNKRIDGVYALL 114
Cdd:COG3883    23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREEL 88
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 5-113 1.24e-06

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: 45.91  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732743867   5 LGVLAQEALRVAVESVLGKLREGKKLSTEDifllyLATIGKELDEIRREIAEVNQRIDQTNRRIDEISKKIDETNMRIDE 84
Cdd:COG4942    13 LAAAAQADAAAEAEAELEQLQQEIAELEKE-----LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                          90       100
                  ....*....|....*....|....*....
gi 1732743867  85 TNKRIDAIAQELGRRIDETNKRIDGVYAL 113
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAELLRALYRL 116
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 40-117 9.67e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 9.67e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732743867  40 LATIGKELDEIRREIAEVNQRIDQTNRRIDEISKKIDETNMRIDETNKRIdaiaQELGRRIDETNKRIDGVYALLLDM 117
Cdd:COG4942    36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIAELRAELEAQKEELAEL 109
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 53-126 2.00e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 2.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732743867  53 EIAEVNQRIDQTNRRIDEISKKIDETNMRIDETNKRIDAIAQELG---RRIDETNKRIDGVYALLLDMQKLLVEIAR 126
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEalqAEIDKLQAEIAEAEAEIEERREELGERAR 93
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 35-127 2.07e-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: 39.36  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732743867  35 IFLLYLATIGKELDEIRREIAEVNQRIDQTNRRIDEISKKID-------ETNMRIDETNKRIDAIAQELG---RRIDETN 104
Cdd:COG4942    10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKallkqlaALERRIAALARRIRALEQELAaleAELAELE 89

                          90       100
                  ....*....|....*....|...
gi 1732743867 105 KRIDGVYALLLDMQKLLVEIARK 127
Cdd:COG4942    90 KEIAELRAELEAQKEELAELLRA 112
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 46-126 6.45e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 38.11  E-value: 6.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732743867   46 ELDEIRREIAEVNQRIDQTNRRIDEISKK----IDETNMRIDETNKRIDAI-----AQELGRRIDETNKRIDGVYALLLD 116
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKsenyIDEIKAQINDLEDVADKAisnddPEEIEKKIENIVTKIDKKKNIYDE 1191

                           90
                   ....*....|
gi 1732743867  117 MQKLLVEIAR 126
Cdd:TIGR01612 1192 IKKLLNEIAE 1201
Lpp COG4238
Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis];
44-94 2.07e-03

Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443380 [Multi-domain]  Cd Length: 77  Bit Score: 34.56  E-value: 2.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1732743867  44 GKELDEIRREIAEVNQRIDQTNRRIDEISKKIDETNMRIDETNKRIDAIAQ 94
Cdd:COG4238    23 NSKIDQLSSDVQSLNAKVDQLSNDVSALRADVQAAKEEAARANQRLDNQAT 73
FtsL2 COG4839
Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning];
53-104 3.14e-03

Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443867  Cd Length: 123  Bit Score: 34.93  E-value: 3.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1732743867  53 EIAEVNQRIDQTNRRIDEISKKIDETNMRIDE--TNKRIDAIAQELGRRIDETN 104
Cdd:COG4839    63 SIYELNREIQSLESKISEQQKENEDLEQEVSElsSPERIYKIAKKLGLKLNNSN 116
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 45-103 6.13e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 35.43  E-value: 6.13e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1732743867   45 KELDEIRREIAEVNQRIDQTNRRIDEISKKIDETNMRIDETNKRIDAIAQELGRRIDET 103
Cdd:TIGR02169  237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK 295
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
40-127 9.11e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 34.50  E-value: 9.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732743867  40 LATIGKELDEIRREIAEVNQRIDQTNRRIDEISKKIDETNMRIDETNKRIDAI---AQELGRRIDETNKRIDGVYALLLD 116
Cdd:COG1340   162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELhkeIVEAQEKADELHEEIIELQKELRE 241

                          90
                  ....*....|.
gi 1732743867 117 MQKLLVEIARK 127
Cdd:COG1340   242 LRKELKKLRKK 252
 
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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