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Conserved domains on  [gi|442622911|ref|NP_610396|]
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uncharacterized protein Dmel_CG8642 [Drosophila melanogaster]

Protein Classification

fibrinogen-related domain-containing protein( domain architecture ID 10053370)

fibrinogen-related domain-containing protein contains a C terminal globular domain similar to that of fibrinogen, and may be involved in one or more of a variety of binding interactions and functions including complement activation, signaling and regulation

CATH:  3.90.215.10|4.10.530.10
PubMed:  1304888
SCOP:  4002544

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 213-413 4.79e-105

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


:

Pssm-ID: 238040 [Multi-domain]  Cd Length: 215  Bit Score: 309.94  E-value: 4.79e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911 213 GRSPGIHLIHLPGFL-PFLVPCEGQTAaGPGWTCIQRRLDGSVNFYRNWDAYSKGFGKLNGEFFIGLEKLHRLTSSQPHE 291
Cdd:cd00087   14 GRTSGVYTIQPPGSNePFQVYCDMDTD-GGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKIHLLTSQGPYE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911 292 LYISIRRFGGETSYAHYDDFLIGSEEEGYELKLLGhYQGNASDALRTHDKMKFSTYDRDNDAFTHmNCAEHHQGAWWYDF 371
Cdd:cd00087   93 LRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGG-YSGTAGDALSYHNGMKFSTFDRDNDGASG-NCAESYSGGWWYNS 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 442622911 372 CSRSNLNGRYFKGEVDN--PQSIYWEPWYSFR-SLKSVQMLIRPK 413
Cdd:cd00087  171 CHASNLNGRYYSGGHRNeyDNGINWATWKGSTySLKFTEMKIRPK 215
MAD super family cl37733
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 71-198 3.86e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


The actual alignment was detected with superfamily member pfam05557:

Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 48.97  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911   71 SKGDLDDLLDVYMGKIAESAATIKDKENEI----NKLQTKDQTGDELLRKFENLTQVCSAQQSSfTTAIKEKDEQIKELE 146
Cdd:pfam05557  98 QLADAREVISCLKNELSELRRQIQRAELELqstnSELEELQERLDLLKAKASEAEQLRQNLEKQ-QSSLAEAEQRIKELE 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622911  147 QKVKVY--------------------ETRLKRKQHVLAELRKLNGSSALL---IEHLKGKVVYFErKFREKKDDL 198
Cdd:pfam05557 177 FEIQSQeqdseivknskselaripelEKELERLREHNKHLNENIENKLLLkeeVEDLKRKLEREE-KYREEAATL 250
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 213-413 4.79e-105

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040 [Multi-domain]  Cd Length: 215  Bit Score: 309.94  E-value: 4.79e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911 213 GRSPGIHLIHLPGFL-PFLVPCEGQTAaGPGWTCIQRRLDGSVNFYRNWDAYSKGFGKLNGEFFIGLEKLHRLTSSQPHE 291
Cdd:cd00087   14 GRTSGVYTIQPPGSNePFQVYCDMDTD-GGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKIHLLTSQGPYE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911 292 LYISIRRFGGETSYAHYDDFLIGSEEEGYELKLLGhYQGNASDALRTHDKMKFSTYDRDNDAFTHmNCAEHHQGAWWYDF 371
Cdd:cd00087   93 LRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGG-YSGTAGDALSYHNGMKFSTFDRDNDGASG-NCAESYSGGWWYNS 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 442622911 372 CSRSNLNGRYFKGEVDN--PQSIYWEPWYSFR-SLKSVQMLIRPK 413
Cdd:cd00087  171 CHASNLNGRYYSGGHRNeyDNGINWATWKGSTySLKFTEMKIRPK 215
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 213-413 9.92e-76

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548 [Multi-domain]  Cd Length: 212  Bit Score: 234.86  E-value: 9.92e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911   213 GRSPGIHLIHLPGF-LPFLVPCEGQTAAGpGWTCIQRRLDGSVNFYRNWDAYSKGFGKLNGEFFIGLEKLHRLTSSQPHE 291
Cdd:smart00186  13 GKTSGLYTIYPDGSsRPLKVYCDMETDGG-GWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENIHLLTSQGKYE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911   292 LYISIRRFGGETSYAHYDDFLIGSEEEGYELKLlGHYQGNASDA-LRTHDKMKFSTYDRDNDAFThMNCAEHHQGAWWYD 370
Cdd:smart00186  92 LRIDLEDWEGNTAYALYDSFKVADEADGYRLHI-GGYSGTAGDAsLTYHNGMQFSTYDRDNDKYS-GNCAEEYGGGWWYN 169

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 442622911   371 FCSRSNLNGRYFKGEVDNpQSIYWEPWYSF-RSLKSVQMLIRPK 413
Cdd:smart00186 170 NCHAANLNGRYYPNNNYD-NGINWATWKGSwYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
213-413 1.43e-62

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 201.60  E-value: 1.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911  213 GRSPGIHLIHLPGFL-PFLVPCEGQTAAGpGWTCIQRRLDGSVNFYRNWDAYSKGFGKL-NGEFFIGLEKLHRLTSSQPH 290
Cdd:pfam00147  13 AKTSGLYTIRPDGATkPFEVYCDMETDGG-GWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDKIHLLTKQGPY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911  291 ELYISIRRFGGETSYAHYDDFLIGSEEEGYELKlLGHYQGNASDALRT-------HDKMKFSTYDRDNDAFThMNCAEHH 363
Cdd:pfam00147  92 VLRIDLEDWNGETVFALYDSFKVTNENDKYRLH-VENYIGDAGDALDTagrsmtyHNGMQFSTWDRDNDSPD-GNCALSY 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442622911  364 QGAWWYDFCSRSNLNGRYFKGE-VDNPQSIYWEPWYSFR-SLKSVQMLIRPK 413
Cdd:pfam00147 170 GGGWWYNNCHAANLNGVYYYGGtYSKQNGIIWATWKGRWySMKKAEMKIRPL 221
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 71-198 3.86e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 48.97  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911   71 SKGDLDDLLDVYMGKIAESAATIKDKENEI----NKLQTKDQTGDELLRKFENLTQVCSAQQSSfTTAIKEKDEQIKELE 146
Cdd:pfam05557  98 QLADAREVISCLKNELSELRRQIQRAELELqstnSELEELQERLDLLKAKASEAEQLRQNLEKQ-QSSLAEAEQRIKELE 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622911  147 QKVKVY--------------------ETRLKRKQHVLAELRKLNGSSALL---IEHLKGKVVYFErKFREKKDDL 198
Cdd:pfam05557 177 FEIQSQeqdseivknskselaripelEKELERLREHNKHLNENIENKLLLkeeVEDLKRKLEREE-KYREEAATL 250
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 74-200 7.23e-05

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: 45.43  E-value: 7.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911    74 DLDDLLDVYMGKIAESAATIKDKENEINKLQTKDQTGDELLRKFENLTQVCSAQQSSFTTAIKEKDEQIKELEQKVKVYE 153
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 442622911   154 TRLKRKQHVLAELRK-LNGSSALLIEhLKGKVVYFERKFREKKDDLLA 200
Cdd:TIGR02168  337 EELAELEEKLEELKEeLESLEAELEE-LEAELEELESRLEELEEQLET 383
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 85-166 2.60e-03

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: 39.75  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911  85 KIAESAATIKDKENEINKLQTKDQTGDELLRKFENLTQVCSAQQSSFTTAIKEKDEQIKELEQKVKVYETRLKRKQHVLA 164
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107


                 ..
gi 442622911 165 EL 166
Cdd:COG4942  108 EL 109
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 213-413 4.79e-105

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040 [Multi-domain]  Cd Length: 215  Bit Score: 309.94  E-value: 4.79e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911 213 GRSPGIHLIHLPGFL-PFLVPCEGQTAaGPGWTCIQRRLDGSVNFYRNWDAYSKGFGKLNGEFFIGLEKLHRLTSSQPHE 291
Cdd:cd00087   14 GRTSGVYTIQPPGSNePFQVYCDMDTD-GGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKIHLLTSQGPYE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911 292 LYISIRRFGGETSYAHYDDFLIGSEEEGYELKLLGhYQGNASDALRTHDKMKFSTYDRDNDAFTHmNCAEHHQGAWWYDF 371
Cdd:cd00087   93 LRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGG-YSGTAGDALSYHNGMKFSTFDRDNDGASG-NCAESYSGGWWYNS 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 442622911 372 CSRSNLNGRYFKGEVDN--PQSIYWEPWYSFR-SLKSVQMLIRPK 413
Cdd:cd00087  171 CHASNLNGRYYSGGHRNeyDNGINWATWKGSTySLKFTEMKIRPK 215
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 213-413 9.92e-76

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548 [Multi-domain]  Cd Length: 212  Bit Score: 234.86  E-value: 9.92e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911   213 GRSPGIHLIHLPGF-LPFLVPCEGQTAAGpGWTCIQRRLDGSVNFYRNWDAYSKGFGKLNGEFFIGLEKLHRLTSSQPHE 291
Cdd:smart00186  13 GKTSGLYTIYPDGSsRPLKVYCDMETDGG-GWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENIHLLTSQGKYE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911   292 LYISIRRFGGETSYAHYDDFLIGSEEEGYELKLlGHYQGNASDA-LRTHDKMKFSTYDRDNDAFThMNCAEHHQGAWWYD 370
Cdd:smart00186  92 LRIDLEDWEGNTAYALYDSFKVADEADGYRLHI-GGYSGTAGDAsLTYHNGMQFSTYDRDNDKYS-GNCAEEYGGGWWYN 169

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 442622911   371 FCSRSNLNGRYFKGEVDNpQSIYWEPWYSF-RSLKSVQMLIRPK 413
Cdd:smart00186 170 NCHAANLNGRYYPNNNYD-NGINWATWKGSwYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
213-413 1.43e-62

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 201.60  E-value: 1.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911  213 GRSPGIHLIHLPGFL-PFLVPCEGQTAAGpGWTCIQRRLDGSVNFYRNWDAYSKGFGKL-NGEFFIGLEKLHRLTSSQPH 290
Cdd:pfam00147  13 AKTSGLYTIRPDGATkPFEVYCDMETDGG-GWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDKIHLLTKQGPY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911  291 ELYISIRRFGGETSYAHYDDFLIGSEEEGYELKlLGHYQGNASDALRT-------HDKMKFSTYDRDNDAFThMNCAEHH 363
Cdd:pfam00147  92 VLRIDLEDWNGETVFALYDSFKVTNENDKYRLH-VENYIGDAGDALDTagrsmtyHNGMQFSTWDRDNDSPD-GNCALSY 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442622911  364 QGAWWYDFCSRSNLNGRYFKGE-VDNPQSIYWEPWYSFR-SLKSVQMLIRPK 413
Cdd:pfam00147 170 GGGWWYNNCHAANLNGVYYYGGtYSKQNGIIWATWKGRWySMKKAEMKIRPL 221
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 71-198 3.86e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 48.97  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911   71 SKGDLDDLLDVYMGKIAESAATIKDKENEI----NKLQTKDQTGDELLRKFENLTQVCSAQQSSfTTAIKEKDEQIKELE 146
Cdd:pfam05557  98 QLADAREVISCLKNELSELRRQIQRAELELqstnSELEELQERLDLLKAKASEAEQLRQNLEKQ-QSSLAEAEQRIKELE 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622911  147 QKVKVY--------------------ETRLKRKQHVLAELRKLNGSSALL---IEHLKGKVVYFErKFREKKDDL 198
Cdd:pfam05557 177 FEIQSQeqdseivknskselaripelEKELERLREHNKHLNENIENKLLLkeeVEDLKRKLEREE-KYREEAATL 250
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 74-200 7.23e-05

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: 45.43  E-value: 7.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911    74 DLDDLLDVYMGKIAESAATIKDKENEINKLQTKDQTGDELLRKFENLTQVCSAQQSSFTTAIKEKDEQIKELEQKVKVYE 153
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 442622911   154 TRLKRKQHVLAELRK-LNGSSALLIEhLKGKVVYFERKFREKKDDLLA 200
Cdd:TIGR02168  337 EELAELEEKLEELKEeLESLEAELEE-LEAELEELESRLEELEEQLET 383
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 85-166 2.60e-03

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: 39.75  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911  85 KIAESAATIKDKENEINKLQTKDQTGDELLRKFENLTQVCSAQQSSFTTAIKEKDEQIKELEQKVKVYETRLKRKQHVLA 164
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107


                 ..
gi 442622911 165 EL 166
Cdd:COG4942  108 EL 109
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 74-168 4.11e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 4.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911  74 DLDDLLDVYMGKIAESAATIKDKENEINKLQTKDQTGDELLRKFEN-LTQVCSA---------------QQSSFTTAIKE 137
Cdd:COG1579   35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqLGNVRNNkeyealqkeieslkrRISDLEDEILE 114

                         90       100       110
                 ....*....|....*....|....*....|.
gi 442622911 138 KDEQIKELEQKVKVYETRLKRKQHVLAELRK 168
Cdd:COG1579  115 LMERIEELEEELAELEAELAELEAELEEKKA 145
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 89-180 4.98e-03

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: 38.98  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911  89 SAATIKDKENEINKLQTKDQTGDELLRKFENLTQVCSAQQSSFTTAIKEKDEQIKELEQKVKVYETRLKRKQHVLAELRK 168
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90
                 ....*....|...
gi 442622911 169 -LNGSSALLIEHL 180
Cdd:COG4942   98 eLEAQKEELAELL 110
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 58-164 5.80e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.07  E-value: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911   58 AEVHIDQHKTIRISK--GDLDDLLDVYMGKIAESAATIKD--KENEINKLQTkdqtgDELLRKFENLTQVCSAQQSSFTT 133
Cdd:pfam06160  72 AEELNDKYRFKKAKKalDEIEELLDDIEEDIKQILEELDEllESEEKNREEV-----EELKDKYRELRKTLLANRFSYGP 146

                          90       100       110
                  ....*....|....*....|....*....|.
gi 442622911  134 AIKEKDEQIKELEQKVKVYETRLKRKQHVLA 164
Cdd:pfam06160 147 AIDELEKQLAEIEEEFSQFEELTESGDYLEA 177
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 68-203 7.03e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 38.87  E-value: 7.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911    68 IRISKGDLDDLLDVYMGKIAESAATIKDKENEINKLQTKD--------QTGDELLRK--FENLTQVCSAQQSSFTTAIKE 137
Cdd:TIGR00606  827 VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTnelkseklQIGTNLQRRqqFEEQLVELSTEVQSLIREIKD 906

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911   138 KDEQIKELEQKVKVYETRLKRKQHVLAELRKLNGSSALLI-EHLKGKVVY---FERKFREKKDDLLADWE 203
Cdd:TIGR00606  907 AKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIkEKVKNIHGYmkdIENKIQDGKDDYLKQKE 976
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 85-204 9.32e-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: 38.50  E-value: 9.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911    85 KIAESAATIKDKENEINKLQTKdqtGDELLRKFENLTQvcsaQQSSFTTAIKEKDEQIKELEQKVKVYETRLKRKQHVLA 164
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEEL---IEELESELEALLN----ERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 442622911   165 ELRKLNGSSALLIEHLKGKVVYFERKFREKKDDLLADWEA 204
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
85-175 9.90e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.96  E-value: 9.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622911  85 KIAESAATIKDKENEINKLQTKDQtgdELLRKFENLTQVCS---AQQSSFTTAIKEKDEQIKELEQKVKVYETRLKRKQH 161
Cdd:COG4372   95 ELAQAQEELESLQEEAEELQEELE---ELQKERQDLEQQRKqleAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171

                         90
                 ....*....|....
gi 442622911 162 VLAELRKLNGSSAL 175
Cdd:COG4372  172 ELQALSEAEAEQAL 185
 
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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