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Conserved domains on  [gi|33469117|ref|NP_038941|]
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angiopoietin-related protein 3 preproprotein [Mus musculus]

Protein Classification

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 ...
 241-453 3.43e-102

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: 303.78  E-value: 3.43e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117 241 DLPADCSAVYNRGEHTSGVYTIKPRNS-QGFNVYCDTQS-GSPWTLIQHRKDGSQDFNETWENYEKGFGRLDGEFWLGLE 318
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTdGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117 319 KIYAIVQQSNYILRLELQDWKDSKHYVEYS-FHLGSHETNYTLHVAEIAGNIPGALPEHTDLMFSTWNHRAKGQL-YCPE 396
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDsFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGASgNCAE 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 33469117 397 SYSGGWWWNDiCGENNLNGKYNKPRTksRPERRRGIYWRPQSRKLYAIKSSKMMLQP 453
Cdd:cd00087 161 SYSGGWWYNS-CHASNLNGRYYSGGH--RNEYDNGINWATWKGSTYSLKFTEMKIRP 214
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
91-205 1.86e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 1.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  91 EIKEEEKELRRTTSTLQVKNEEVKNmsveLNSKLESLLEEKTALQHKVRALEEQLTNLILSPAGAQEhpevtSLKSfVEQ 170
Cdd:COG4372  39 ELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-----ELES-LQE 108

                        90       100       110
                ....*....|....*....|....*....|....*
gi 33469117 171 QDNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLRK 205
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQS 143
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 241-453 3.43e-102

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: 303.78  E-value: 3.43e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117 241 DLPADCSAVYNRGEHTSGVYTIKPRNS-QGFNVYCDTQS-GSPWTLIQHRKDGSQDFNETWENYEKGFGRLDGEFWLGLE 318
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTdGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117 319 KIYAIVQQSNYILRLELQDWKDSKHYVEYS-FHLGSHETNYTLHVAEIAGNIPGALPEHTDLMFSTWNHRAKGQL-YCPE 396
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDsFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGASgNCAE 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 33469117 397 SYSGGWWWNDiCGENNLNGKYNKPRTksRPERRRGIYWRPQSRKLYAIKSSKMMLQP 453
Cdd:cd00087 161 SYSGGWWYNS-CHASNLNGRYYSGGH--RNEYDNGINWATWKGSTYSLKFTEMKIRP 214
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 242-453 3.80e-67

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: 213.68  E-value: 3.80e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117    242 LPADCSAVYNRGEHTSGVYTIKPRNS-QGFNVYCDTQ-SGSPWTLIQHRKDGSQDFNETWENYEKGFGRLDGEFWLGLEK 319
Cdd:smart00186   1 LPRDCSDVLQNGGKTSGLYTIYPDGSsRPLKVYCDMEtDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNEN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117    320 IYAIVQQSNYILRLELQDWKDSKHYVEY-SFHLGSHETNYTLHVAE---IAGNIPgaLPEHTDLMFSTW---NHRAKGQl 392
Cdd:smart00186  81 IHLLTSQGKYELRIDLEDWEGNTAYALYdSFKVADEADGYRLHIGGysgTAGDAS--LTYHNGMQFSTYdrdNDKYSGN- 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33469117    393 yCPESYSGGWWWNDiCGENNLNGKYNKPRTKSrperrRGIYWRPQSRKLYAIKSSKMMLQP 453
Cdd:smart00186 158 -CAEEYGGGWWYNN-CHAANLNGRYYPNNNYD-----NGINWATWKGSWYSLKFTEMKIRP 211
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
243-453 3.25e-55

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 183.11  E-value: 3.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117   243 PADCSAVYNRGEHTSGVYTIKP-RNSQGFNVYCD-TQSGSPWTLIQHRKDGSQDFNETWENYEKGFGRLD-GEFWLGLEK 319
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDmETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLSpGEFWLGNDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117   320 IYAIVQQSNYILRLELQDWKDSKHYVEY-SFHLGSHETNYTLHVAEIAGNIPGALPEHTDLM-------FSTW---NHRA 388
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYdSFKVTNENDKYRLHVENYIGDAGDALDTAGRSMtyhngmqFSTWdrdNDSP 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33469117   389 KGQlyCPESYSGGWWWNDiCGENNLNGKYNKPRTKSrpeRRRGIYWRPQSRKLYAIKSSKMMLQP 453
Cdd:pfam00147 162 DGN--CALSYGGGWWYNN-CHAANLNGVYYYGGTYS---KQNGIIWATWKGRWYSMKKAEMKIRP 220
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
91-205 1.86e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 1.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  91 EIKEEEKELRRTTSTLQVKNEEVKNmsveLNSKLESLLEEKTALQHKVRALEEQLTNLILSPAGAQEhpevtSLKSfVEQ 170
Cdd:COG4372  39 ELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-----ELES-LQE 108

                        90       100       110
                ....*....|....*....|....*....|....*
gi 33469117 171 QDNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLRK 205
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQS 143
PRK12704 PRK12704
phosphodiesterase; Provisional
 84-207 1.08e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117   84 DLSLRTNEIKEEEKELRRTTSTLQVKNEEVKNMSVELNSKLESLLEEKTALQHKVRALEEQLTNLIlspagaQEHPEVTS 163
Cdd:PRK12704  76 ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL------QELERISG 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 33469117  164 LksfveQQDNSIRELLQSVEEQYKQlsQQHMQIKEIEKQLRKTG 207
Cdd:PRK12704 150 L-----TAEEAKEILLEKVEEEARH--EAAVLIKEIEEEAKEEA 186
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 91-204 1.64e-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: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117     91 EIKEEEKELRRTTSTLQVKneevknmsvELNSKLESLLEEKTALQHKVRALEEQLTNLilspagaqeHPEVTSLKSFVEQ 170
Cdd:TIGR02168  217 ELKAELRELELALLVLRLE---------ELREELEELQEELKEAEEELEELTAELQEL---------EEKLEELRLEVSE 278

                           90       100       110
                   ....*....|....*....|....*....|....
gi 33469117    171 QDNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLR 204
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRLEQQKQILRERLA 312
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 37-201 3.16e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.70  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117     37 FAMLDDVKILANGLLQLghgLKDFVH-------------KTKGQINDIFQKLNIFDQSFYDLSLRTNEIKEEEKELRRTT 103
Cdd:smart00787 105 FSASPDVKLLMDKQFQL---VKTFARleakkmwyewrmkLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRK 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117    104 STLQVKNEEVKNMSVELNSKLESLLeekTALQHKVRALEEQLTNLILSPAGAQEhpEVTSLKSFVEQQDNSIRELLQSVE 183
Cdd:smart00787 182 DALEEELRQLKQLEDELEDCDPTEL---DRAKEKLKKLLQEIMIKVKKLEELEE--ELQELESKIEDLTNKKSELNTEIA 256

                          170
                   ....*....|....*....
gi 33469117    184 EQYKQLSQ-QHMQIKEIEK 201
Cdd:smart00787 257 EAEKKLEQcRGFTFKEIEK 275
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 256-285 2.00e-03

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 36.00  E-value: 2.00e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 33469117  256 TSGVYTIKPRNSQG---FNVYCD-TQSGSPWTLI 285
Cdd:NF040941  13 PSGVYWIDPDGMGGlapFQVYCDmTTDGGGWTLV 46
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 34-191 5.35e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 38.20  E-value: 5.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  34 KSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNifdqsfYDLSLRTNEIKEEEKELRRTTSTLQVKNEEV 113
Cdd:cd00176  50 AAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELR------ELAEERRQRLEEALDLQQFFRDADDLEQWLE 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117 114 KNMSVELNSKLESLLEEKTALQHKVRALEEQLTNLilspagaqeHPEVTSLKSFVEQ--------QDNSIRELLQSVEEQ 185
Cdd:cd00176 124 EKEAALASEDLGKDLESVEELLKKHKELEEELEAH---------EPRLKSLNELAEElleeghpdADEEIEEKLEELNER 194


                ....*.
gi 33469117 186 YKQLSQ 191
Cdd:cd00176 195 WEELLE 200
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 88-242 7.17e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 38.72  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117    88 RTNEIKEEEKELRRTTSTLQVKNEEVKNMSVELNSKLESLLEEKTAL-----QHKVRALEEQLTNLILSPAGAQEHPEVT 162
Cdd:pfam07888  74 QRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALlaqraAHEARIRELEEDIKTLTQRVLERETELE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117   163 SLKSFVEQQDNSIREllqsvEEQYKQLSQQHMQIKEIEKQLRKTGIQEpSENSLssksrAPRTTPPLQLNETENTEQDDL 242
Cdd:pfam07888 154 RMKERAKKAGAQRKE-----EEAERKQLQAKLQQTEEELRSLSKEFQE-LRNSL-----AQRDTQVLQLQDTITTLTQKL 222
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 241-453 3.43e-102

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: 303.78  E-value: 3.43e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117 241 DLPADCSAVYNRGEHTSGVYTIKPRNS-QGFNVYCDTQS-GSPWTLIQHRKDGSQDFNETWENYEKGFGRLDGEFWLGLE 318
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTdGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117 319 KIYAIVQQSNYILRLELQDWKDSKHYVEYS-FHLGSHETNYTLHVAEIAGNIPGALPEHTDLMFSTWNHRAKGQL-YCPE 396
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDsFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGASgNCAE 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 33469117 397 SYSGGWWWNDiCGENNLNGKYNKPRTksRPERRRGIYWRPQSRKLYAIKSSKMMLQP 453
Cdd:cd00087 161 SYSGGWWYNS-CHASNLNGRYYSGGH--RNEYDNGINWATWKGSTYSLKFTEMKIRP 214
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 242-453 3.80e-67

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: 213.68  E-value: 3.80e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117    242 LPADCSAVYNRGEHTSGVYTIKPRNS-QGFNVYCDTQ-SGSPWTLIQHRKDGSQDFNETWENYEKGFGRLDGEFWLGLEK 319
Cdd:smart00186   1 LPRDCSDVLQNGGKTSGLYTIYPDGSsRPLKVYCDMEtDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNEN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117    320 IYAIVQQSNYILRLELQDWKDSKHYVEY-SFHLGSHETNYTLHVAE---IAGNIPgaLPEHTDLMFSTW---NHRAKGQl 392
Cdd:smart00186  81 IHLLTSQGKYELRIDLEDWEGNTAYALYdSFKVADEADGYRLHIGGysgTAGDAS--LTYHNGMQFSTYdrdNDKYSGN- 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33469117    393 yCPESYSGGWWWNDiCGENNLNGKYNKPRTKSrperrRGIYWRPQSRKLYAIKSSKMMLQP 453
Cdd:smart00186 158 -CAEEYGGGWWYNN-CHAANLNGRYYPNNNYD-----NGINWATWKGSWYSLKFTEMKIRP 211
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
243-453 3.25e-55

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 183.11  E-value: 3.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117   243 PADCSAVYNRGEHTSGVYTIKP-RNSQGFNVYCD-TQSGSPWTLIQHRKDGSQDFNETWENYEKGFGRLD-GEFWLGLEK 319
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDmETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLSpGEFWLGNDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117   320 IYAIVQQSNYILRLELQDWKDSKHYVEY-SFHLGSHETNYTLHVAEIAGNIPGALPEHTDLM-------FSTW---NHRA 388
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYdSFKVTNENDKYRLHVENYIGDAGDALDTAGRSMtyhngmqFSTWdrdNDSP 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33469117   389 KGQlyCPESYSGGWWWNDiCGENNLNGKYNKPRTKSrpeRRRGIYWRPQSRKLYAIKSSKMMLQP 453
Cdd:pfam00147 162 DGN--CALSYGGGWWYNN-CHAANLNGVYYYGGTYS---KQNGIIWATWKGRWYSMKKAEMKIRP 220
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
91-205 1.86e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 1.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  91 EIKEEEKELRRTTSTLQVKNEEVKNmsveLNSKLESLLEEKTALQHKVRALEEQLTNLILSPAGAQEhpevtSLKSfVEQ 170
Cdd:COG4372  39 ELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-----ELES-LQE 108

                        90       100       110
                ....*....|....*....|....*....|....*
gi 33469117 171 QDNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLRK 205
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQS 143
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
93-205 4.84e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.90  E-value: 4.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  93 KEEEKELRRTTSTLQVKNEEVKNMsVELNSKLESLLEEKTALQHKVRALEEQLTNLIlspAGAQE-HPEVTSLKSFVEQQ 171
Cdd:COG1340 132 PEEEKELVEKIKELEKELEKAKKA-LEKNEKLKELRAELKELRKEAEEIHKKIKELA---EEAQElHEEMIELYKEADEL 207

                        90       100       110
                ....*....|....*....|....*....|....
gi 33469117 172 DNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLRK 205
Cdd:COG1340 208 RKEADELHKEIVEAQEKADELHEEIIELQKELRE 241
PRK12704 PRK12704
phosphodiesterase; Provisional
 84-207 1.08e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117   84 DLSLRTNEIKEEEKELRRTTSTLQVKNEEVKNMSVELNSKLESLLEEKTALQHKVRALEEQLTNLIlspagaQEHPEVTS 163
Cdd:PRK12704  76 ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL------QELERISG 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 33469117  164 LksfveQQDNSIRELLQSVEEQYKQlsQQHMQIKEIEKQLRKTG 207
Cdd:PRK12704 150 L-----TAEEAKEILLEKVEEEARH--EAAVLIKEIEEEAKEEA 186
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 91-204 1.64e-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: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117     91 EIKEEEKELRRTTSTLQVKneevknmsvELNSKLESLLEEKTALQHKVRALEEQLTNLilspagaqeHPEVTSLKSFVEQ 170
Cdd:TIGR02168  217 ELKAELRELELALLVLRLE---------ELREELEELQEELKEAEEELEELTAELQEL---------EEKLEELRLEVSE 278

                           90       100       110
                   ....*....|....*....|....*....|....
gi 33469117    171 QDNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLR 204
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRLEQQKQILRERLA 312
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
118-205 2.27e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 2.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117 118 VELNSKLESLLEEKTALQHKVRALEEQLTNLILSPAGAQEHPEVTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQHMQIK 197
Cdd:COG3206 222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301


                ....*...
gi 33469117 198 EIEKQLRK 205
Cdd:COG3206 302 ALRAQLQQ 309
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
84-209 2.63e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 2.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  84 DLSLRTNEIKEEEKELRRTTSTLQVKNEEVKnmsvELNSKLESLLEEKTALQHKVRALEEQLTNLILSPAGAQEhpEVTS 163
Cdd:COG4372  53 ELEQAREELEQLEEELEQARSELEQLEEELE----ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK--ERQD 126

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 33469117 164 LKSFVEQQDNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLRKTGIQ 209
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 37-201 3.16e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.70  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117     37 FAMLDDVKILANGLLQLghgLKDFVH-------------KTKGQINDIFQKLNIFDQSFYDLSLRTNEIKEEEKELRRTT 103
Cdd:smart00787 105 FSASPDVKLLMDKQFQL---VKTFARleakkmwyewrmkLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRK 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117    104 STLQVKNEEVKNMSVELNSKLESLLeekTALQHKVRALEEQLTNLILSPAGAQEhpEVTSLKSFVEQQDNSIRELLQSVE 183
Cdd:smart00787 182 DALEEELRQLKQLEDELEDCDPTEL---DRAKEKLKKLLQEIMIKVKKLEELEE--ELQELESKIEDLTNKKSELNTEIA 256

                          170
                   ....*....|....*....
gi 33469117    184 EQYKQLSQ-QHMQIKEIEK 201
Cdd:smart00787 257 EAEKKLEQcRGFTFKEIEK 275
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
90-206 3.61e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 3.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  90 NEIKEEEKELRRTTSTLQVKNEEVKNMSvELNSKLESLLEEKTALQHKVRALEEQLtnlilspagaqEHPEVTSLKSFVE 169
Cdd:COG4717  71 KELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLL-----------QLLPLYQELEALE 138

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 33469117 170 QQDNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLRKT 206
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAEL 175
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
91-205 7.09e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 7.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  91 EIKEEEKELRRTTSTLQVKNEEvknmsvELNSKLEsLLEEKTALQHKVRALEEQLTNLilspAGAQEHPEVTSLKSFVEQ 170
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEE------ELRAALE-QAEEYQELKEELEELEEQLEEL----LGELEELLEALDEEELEE 432

                        90       100       110
                ....*....|....*....|....*....|....*
gi 33469117 171 QDNSIRELLQSVEEQYKQLSQqhmQIKEIEKQLRK 205
Cdd:COG4717 433 ELEELEEELEELEEELEELRE---ELAELEAELEQ 464
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
84-206 1.15e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  84 DLSLRTNEIKEEEKELRRTTSTLQVKNEEVKNMSVELNS----------KLESLLEEKTALQHKVRALEEQLTNLILSPA 153
Cdd:COG4372  67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESlqeeaeelqeELEELQKERQDLEQQRKQLEAQIAELQSEIA 146

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 33469117 154 GAQEhpEVTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQhmQIKEIEKQLRKT 206
Cdd:COG4372 147 EREE--ELKELEEQLESLQEELAALEQELQALSEAEAEQ--ALDELLKEANRN 195
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 256-285 2.00e-03

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 36.00  E-value: 2.00e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 33469117  256 TSGVYTIKPRNSQG---FNVYCD-TQSGSPWTLI 285
Cdd:NF040941  13 PSGVYWIDPDGMGGlapFQVYCDmTTDGGGWTLV 46
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 85-205 3.37e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117   85 LSLRTNEIKEEEKELRRTTSTLQVKNEEVKNmSVELNSKLE---SLLEEKTaLQHKVRALEEQLTNlilspagAQEHpev 161
Cdd:COG3096  841 LRQRRSELERELAQHRAQEQQLRQQLDQLKE-QLQLLNKLLpqaNLLADET-LADRLEELREELDA-------AQEA--- 908

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 33469117  162 tslKSFVEQQDNSIREL------LQSVEEQYKQLSQQHMQIKEIEKQLRK 205
Cdd:COG3096  909 ---QAFIQQHGKALAQLeplvavLQSDPEQFEQLQADYLQAKEQQRRLKQ 955
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
91-206 4.02e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117   91 EIKEEEKELRRTTSTLQVKNEEVKNMSVELNSKLESLLEEKTALQHKVRALEE----QLTNLILSpagaQEHPEVTSLKS 166
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekAEEYIKLS----EFYEEYLDELR 310

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 33469117  167 FVEQQDNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLRKT 206
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL 350
COG5022 COG5022
Myosin heavy chain [General function prediction only];
69-219 4.43e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 39.68  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117   69 NDIFQKLNIFDQSFYDLSLRTNEIKEEEKELRRTtstLQVKNEEVKNmsveLNSKLESLLEEKTALQHKVRALEE---QL 145
Cdd:COG5022  953 LPELNKLHEVESKLKETSEEYEDLLKKSTILVRE---GNKANSELKN----FKKELAELSKQYGALQESTKQLKElpvEV 1025

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33469117  146 TNLI-LSPAGAQEHPEVTSLKSFVEQQDNSIRElLQSVEEQYKQLSQQHMQIKEIEKQLRKTGIQEPSENSLSSK 219
Cdd:COG5022 1026 AELQsASKIISSESTELSILKPLQKLKGLLLLE-NNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVK 1099
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 89-223 4.83e-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: 4.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  89 TNEIKEEEKELRRTTSTLQVKNEEVKNMSVELNSKLESLLEEKTALQHKVRALEEQLTNLilspagaqehpevtslksfv 168
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL-------------------- 204

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 33469117 169 EQQDNSIRELLQSVEEQYKQLSQqhmQIKEIEKQLRKTGIQEPSENSLSSKSRAP 223
Cdd:COG4942 205 EKELAELAAELAELQQEAEELEA---LIARLEAEAAAAAERTPAAGFAALKGKLP 256
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 34-191 5.35e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 38.20  E-value: 5.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  34 KSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNifdqsfYDLSLRTNEIKEEEKELRRTTSTLQVKNEEV 113
Cdd:cd00176  50 AAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELR------ELAEERRQRLEEALDLQQFFRDADDLEQWLE 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117 114 KNMSVELNSKLESLLEEKTALQHKVRALEEQLTNLilspagaqeHPEVTSLKSFVEQ--------QDNSIRELLQSVEEQ 185
Cdd:cd00176 124 EKEAALASEDLGKDLESVEELLKKHKELEEELEAH---------EPRLKSLNELAEElleeghpdADEEIEEKLEELNER 194


                ....*.
gi 33469117 186 YKQLSQ 191
Cdd:cd00176 195 WEELLE 200
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
62-206 6.91e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 6.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117   62 HKTKGQINDIFQKLNIFDqsfydlslrTNEIKEEEKELRRTTSTLQVKNEEVKNMSVELNsKLESLLEEKTALQHKVRAL 141
Cdd:PRK03918 499 KELAEQLKELEEKLKKYN---------LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDEL 568

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33469117  142 EEQLTNLilspagaqeHPEVTSLK-SFVEQQDNSIRElLQSVEEQYKQLSQQHMQIKEIEKQLRKT 206
Cdd:PRK03918 569 EEELAEL---------LKELEELGfESVEELEERLKE-LEPFYNEYLELKDAEKELEREEKELKKL 624
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 88-242 7.17e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 38.72  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117    88 RTNEIKEEEKELRRTTSTLQVKNEEVKNMSVELNSKLESLLEEKTAL-----QHKVRALEEQLTNLILSPAGAQEHPEVT 162
Cdd:pfam07888  74 QRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALlaqraAHEARIRELEEDIKTLTQRVLERETELE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117   163 SLKSFVEQQDNSIREllqsvEEQYKQLSQQHMQIKEIEKQLRKTGIQEpSENSLssksrAPRTTPPLQLNETENTEQDDL 242
Cdd:pfam07888 154 RMKERAKKAGAQRKE-----EEAERKQLQAKLQQTEEELRSLSKEFQE-LRNSL-----AQRDTQVLQLQDTITTLTQKL 222
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 58-190 7.19e-03

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: 39.26  E-value: 7.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117     58 KDFVHKTKGQINDIFQKLNifDQSFYDlSLRTNEIKEEEKELRRTTSTLQVKNEE-------VKNMSVELNSKLESLLEE 130
Cdd:TIGR01612  778 KDELNKYKSKISEIKNHYN--DQINID-NIKDEDAKQNYDKSKEYIKTISIKEDEifkiineMKFMKDDFLNKVDKFINF 854

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117    131 KTALQHKVRALEEQLTNLILSPAGAQEHPEVTSLKSFVEQQDNSIRELLQSVEEQYKQLS 190
Cdd:TIGR01612  855 ENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNIN 914
mukB PRK04863
chromosome partition protein MukB;
84-205 8.00e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.78  E-value: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117    84 DLSLRTNEIKEEEKELRRTTSTLQVKNEEVKNMSVELNsKLE---SLLEEKTaLQHKVRALEEQLtnlilspAGAQEHpe 160
Cdd:PRK04863  841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALN-RLLprlNLLADET-LADRVEEIREQL-------DEAEEA-- 909

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 33469117   161 vtslKSFVEQQDNSIREL------LQSVEEQYKQLSQQHMQIKEIEKQLRK 205
Cdd:PRK04863  910 ----KRFVQQHGNALAQLepivsvLQSDPEQFEQLKQDYQQAQQTQRDAKQ 956
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 57-242 8.31e-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: 38.21  E-value: 8.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  57 LKDFVHKTKGQINDIFQKLNIFDQSfydLSLRTNEIKEEEKELRRTTSTLQVKNEEVKNMSVELNSKLESLLEEKTALQh 136
Cdd:COG4942  39 LEKELAALKKEEKALLKQLAALERR---IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY- 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117 137 kvRALEEQLTNLILSPAGAQEHPE-VTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLRKtgiQEPSENS 215
Cdd:COG4942 115 --RLGRQPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE---LEEERAA 189

                       170       180
                ....*....|....*....|....*..
gi 33469117 216 LSSKsRAPRTTPPLQLNETENTEQDDL 242
Cdd:COG4942 190 LEAL-KAERQKLLARLEKELAELAAEL 215
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
89-205 8.97e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 37.97  E-value: 8.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  89 TNEIKEEEKELRRTTSTLQVKNEEVKNMSVELNSKLESLLEEKTALQHKVRALEEQltnlilspagAQEH--------PE 160
Cdd:COG1340   3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE----------AQELrekrdelnEK 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 33469117 161 VTSLKSFVEQQDNSIRELLQSVEE---QYKQLSQQHMQIKEIEKQLRK 205
Cdd:COG1340  73 VKELKEERDELNEKLNELREELDElrkELAELNKAGGSIDKLRKEIER 120
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 91-205 9.13e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 9.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469117  91 EIKEEEKELRRTTSTLQVKN-----EEVKNMSVELNSKLESLLEEKTALQHKVRALEEQLTNLI--LSPAGAQEHPEVTS 163
Cdd:COG1196 217 ELKEELKELEAELLLLKLREleaelEELEAELEELEAELEELEAELAELEAELEELRLELEELEleLEEAQAEEYELLAE 296

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 33469117 164 LKSfVEQQDNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLRK 205
Cdd:COG1196 297 LAR-LEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
 
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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