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Conserved domains on  [gi|7656888|ref|NP_055310|]
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angiopoietin-related protein 3 preproprotein [Homo sapiens]

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 ...
 243-453 2.66e-99

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: 296.46  E-value: 2.66e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888  243 PAECTTIYNRGEHTSGMYAIRPSNS-QVFHVYCDV-ISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKI 320
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMdTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888  321 YSIVKQSNYVLRIELEDWKDNKHYIEYS-FYLGNHETNYTLHLVAITGNVPNAIPENKDLVFSTWDHKAKGH-FNCPEGY 398
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDsFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGAsGNCAESY 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7656888  399 SGGWWWhDECGENNLNGKYNKPRAksKPERRRGLSWKSQNGRLYSIKSTKMLIHP 453
Cdd:cd00087 163 SGGWWY-NSCHASNLNGRYYSGGH--RNEYDNGINWATWKGSTYSLKFTEMKIRP 214
GumC super family cl34566
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
81-205 4.95e-06

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


The actual alignment was detected with superfamily member COG3206:

Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 4.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   81 SFYDLSLQTSEIKEEEKELRRTTYKLQ---VKNEEVKNMSL----ELNSKLESLLEEKILLQQKVKYLEEQLTNLIQNQP 153
Cdd:COG3206 178 EFLEEQLPELRKELEEAEAALEEFRQKnglVDLSEEAKLLLqqlsELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 7656888  154 ETPEHPEVTSLKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRR 205
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ 309
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 243-453 2.66e-99

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: 296.46  E-value: 2.66e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888  243 PAECTTIYNRGEHTSGMYAIRPSNS-QVFHVYCDV-ISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKI 320
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMdTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888  321 YSIVKQSNYVLRIELEDWKDNKHYIEYS-FYLGNHETNYTLHLVAITGNVPNAIPENKDLVFSTWDHKAKGH-FNCPEGY 398
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDsFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGAsGNCAESY 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7656888  399 SGGWWWhDECGENNLNGKYNKPRAksKPERRRGLSWKSQNGRLYSIKSTKMLIHP 453
Cdd:cd00087 163 SGGWWY-NSCHASNLNGRYYSGGH--RNEYDNGINWATWKGSTYSLKFTEMKIRP 214
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 243-453 4.79e-66

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: 210.98  E-value: 4.79e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888     243 PAECTTIYNRGEHTSGMYAIRPSNS-QVFHVYCDV-ISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKI 320
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGSsRPLKVYCDMeTDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888     321 YSIVKQSNYVLRIELEDWKDNKHYIEY-SFYLGNHETNYTLHLVAITGNVPNA---IPENKDlvFSTWDH---KAKGhfN 393
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYdSFKVADEADGYRLHIGGYSGTAGDAsltYHNGMQ--FSTYDRdndKYSG--N 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888     394 CPEGYSGGwWWHDECGENNLNGKYNKPRAKSkperrRGLSWKSQNGRLYSIKSTKMLIHP 453
Cdd:smart00186 158 CAEEYGGG-WWYNNCHAANLNGRYYPNNNYD-----NGINWATWKGSWYSLKFTEMKIRP 211
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
242-453 1.71e-56

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 186.57  E-value: 1.71e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888    242 IPAECTTIYNRGEHTSGMYAIRPS-NSQVFHVYCDV-ISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLD-GEFWLGLE 318
Cdd:pfam00147   1 FGRDCSDVYNKGAKTSGLYTIRPDgATKPFEVYCDMeTDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLSpGEFWLGND 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888    319 KIYSIVKQSNYVLRIELEDWKDNKHYIEY-SFYLGNHETNYTLHLVAITGNVPNAIPENKD-------LVFSTWDH---K 387
Cdd:pfam00147  81 KIHLLTKQGPYVLRIDLEDWNGETVFALYdSFKVTNENDKYRLHVENYIGDAGDALDTAGRsmtyhngMQFSTWDRdndS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7656888    388 AKGhfNCPEGYSGGWWWhDECGENNLNGKYNKPRAKSKperRRGLSWKSQNGRLYSIKSTKMLIHP 453
Cdd:pfam00147 161 PDG--NCALSYGGGWWY-NNCHAANLNGVYYYGGTYSK---QNGIIWATWKGRWYSMKKAEMKIRP 220
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
81-205 4.95e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 4.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   81 SFYDLSLQTSEIKEEEKELRRTTYKLQ---VKNEEVKNMSL----ELNSKLESLLEEKILLQQKVKYLEEQLTNLIQNQP 153
Cdd:COG3206 178 EFLEEQLPELRKELEEAEAALEEFRQKnglVDLSEEAKLLLqqlsELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 7656888  154 ETPEHPEVTSLKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRR 205
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ 309
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 57-209 6.81e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888     57 LKDFVHKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRrttyKLQVKNEEVKNMSLELNSKLESLLEEKILLQQ 136
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEINEKTT 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888    137 KVKYLEEQLTNLIQNQPETPEHPEVTSLKtfVEKQDNSIKDL---LQTVEDQYKQLNQQ---------HSQIKEIENQLR 204
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKE--LEQNNKKIKELekqLNQLKSEISDLNNQkeqdwnkelKSELKNQEKKLE 324


                  ....*
gi 7656888    205 RTSIQ 209
Cdd:TIGR04523 325 EIQNQ 329
PRK12704 PRK12704
phosphodiesterase; Provisional
 91-214 7.75e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 7.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888    91 EIKEEEKELRRTTYKLQVKNEEVKNmSLELNSKLESLLEEKIL----LQQKVKYLEEQLTNLIQNQPETPEHpeVTSLkt 166
Cdd:PRK12704  76 ELRERRNELQKLEKRLLQKEENLDR-KLELLEKREEELEKKEKeleqKQQELEKKEEELEELIEEQLQELER--ISGL-- 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 7656888   167 fveKQDNSIKDLLQTVEDQYKQlnQQHSQIKEIENQLRRTSIQEPTEI 214
Cdd:PRK12704 151 ---TAEEAKEILLEKVEEEARH--EAAVLIKEIEEEAKEEADKKAKEI 193
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 243-453 2.66e-99

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: 296.46  E-value: 2.66e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888  243 PAECTTIYNRGEHTSGMYAIRPSNS-QVFHVYCDV-ISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKI 320
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMdTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888  321 YSIVKQSNYVLRIELEDWKDNKHYIEYS-FYLGNHETNYTLHLVAITGNVPNAIPENKDLVFSTWDHKAKGH-FNCPEGY 398
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDsFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGAsGNCAESY 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7656888  399 SGGWWWhDECGENNLNGKYNKPRAksKPERRRGLSWKSQNGRLYSIKSTKMLIHP 453
Cdd:cd00087 163 SGGWWY-NSCHASNLNGRYYSGGH--RNEYDNGINWATWKGSTYSLKFTEMKIRP 214
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 243-453 4.79e-66

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: 210.98  E-value: 4.79e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888     243 PAECTTIYNRGEHTSGMYAIRPSNS-QVFHVYCDV-ISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKI 320
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGSsRPLKVYCDMeTDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888     321 YSIVKQSNYVLRIELEDWKDNKHYIEY-SFYLGNHETNYTLHLVAITGNVPNA---IPENKDlvFSTWDH---KAKGhfN 393
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYdSFKVADEADGYRLHIGGYSGTAGDAsltYHNGMQ--FSTYDRdndKYSG--N 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888     394 CPEGYSGGwWWHDECGENNLNGKYNKPRAKSkperrRGLSWKSQNGRLYSIKSTKMLIHP 453
Cdd:smart00186 158 CAEEYGGG-WWYNNCHAANLNGRYYPNNNYD-----NGINWATWKGSWYSLKFTEMKIRP 211
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
242-453 1.71e-56

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 186.57  E-value: 1.71e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888    242 IPAECTTIYNRGEHTSGMYAIRPS-NSQVFHVYCDV-ISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLD-GEFWLGLE 318
Cdd:pfam00147   1 FGRDCSDVYNKGAKTSGLYTIRPDgATKPFEVYCDMeTDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLSpGEFWLGND 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888    319 KIYSIVKQSNYVLRIELEDWKDNKHYIEY-SFYLGNHETNYTLHLVAITGNVPNAIPENKD-------LVFSTWDH---K 387
Cdd:pfam00147  81 KIHLLTKQGPYVLRIDLEDWNGETVFALYdSFKVTNENDKYRLHVENYIGDAGDALDTAGRsmtyhngMQFSTWDRdndS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7656888    388 AKGhfNCPEGYSGGWWWhDECGENNLNGKYNKPRAKSKperRRGLSWKSQNGRLYSIKSTKMLIHP 453
Cdd:pfam00147 161 PDG--NCALSYGGGWWY-NNCHAANLNGVYYYGGTYSK---QNGIIWATWKGRWYSMKKAEMKIRP 220
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
81-205 4.95e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 4.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   81 SFYDLSLQTSEIKEEEKELRRTTYKLQ---VKNEEVKNMSL----ELNSKLESLLEEKILLQQKVKYLEEQLTNLIQNQP 153
Cdd:COG3206 178 EFLEEQLPELRKELEEAEAALEEFRQKnglVDLSEEAKLLLqqlsELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 7656888  154 ETPEHPEVTSLKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRR 205
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ 309
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
57-211 7.25e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 7.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   57 LKDFvhKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKEL--RRTTYKLQVKNEEVKNMSLELNSKLESLLEEKILL 134
Cdd:COG3206 198 LEEF--RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAeaRLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL 275

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888  135 QQKvkyLEEQLTNLiqnqpeTPEHPEVTSLKTFVEKQDNSIKD----LLQTVEDQYKQLNQQHSQIKEIENQLRRTSIQE 210
Cdd:COG3206 276 EAE---LAELSARY------TPNHPDVIALRAQIAALRAQLQQeaqrILASLEAELEALQAREASLQAQLAQLEARLAEL 346


                .
gi 7656888  211 P 211
Cdd:COG3206 347 P 347
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 15-214 1.16e-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: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   15 ISSRIDQDNSSFDSLSpepKSRFAMLDDVKILANGLLQLghglKDFVHKTKGQINDIFQKLNIFDQsfyDLSLQTSEIKE 94
Cdd:COG4942  32 LQQEIAELEKELAALK---KEEKALLKQLAALERRIAAL----ARRIRALEQELAALEAELAELEK---EIAELRAELEA 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   95 EEKELRRTTYKLQvKNEEVKNMSLELNSK-LESLLEEKILLQQKVKYLEEQLTNLIQNQpetpehPEVTSLKTFVEKQDN 173
Cdd:COG4942 102 QKEELAELLRALY-RLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADL------AELAALRAELEAERA 174

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 7656888  174 SIKDLLQTVEDQYKQLNQQHSQIKEIENQLRRTSIQEPTEI 214
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
90-205 2.20e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   90 SEIKEEEKELRRTTYKLQVKNEEVKNMSLELN---SKLESLLEEKILLQQKVKYLEEQLTNLIQNQpetpehpevtslkt 166
Cdd:COG4372  66 EELEQARSELEQLEEELEELNEQLQAAQAELAqaqEELESLQEEAEELQEELEELQKERQDLEQQR-------------- 131

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 7656888  167 fvEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRR 205
Cdd:COG4372 132 --KQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
84-206 3.77e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 3.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   84 DLSLQTSEIKEEEKELRRTTYKLQVKNEEVKnmslELNSKLESLLEEKILLQQKVKYLEEQLTNLIQnqpetpehpEVTS 163
Cdd:COG4372  53 ELEQAREELEQLEEELEQARSELEQLEEELE----ELNEQLQAAQAELAQAQEELESLQEEAEELQE---------ELEE 119

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 7656888  164 LKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRRT 206
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 57-209 6.81e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888     57 LKDFVHKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRrttyKLQVKNEEVKNMSLELNSKLESLLEEKILLQQ 136
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEINEKTT 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888    137 KVKYLEEQLTNLIQNQPETPEHPEVTSLKtfVEKQDNSIKDL---LQTVEDQYKQLNQQ---------HSQIKEIENQLR 204
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKE--LEQNNKKIKELekqLNQLKSEISDLNNQkeqdwnkelKSELKNQEKKLE 324


                  ....*
gi 7656888    205 RTSIQ 209
Cdd:TIGR04523 325 EIQNQ 329
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 42-201 7.24e-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: 42.35  E-value: 7.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888      42 DVKILANGLLQLGhgLKDFVHKTKGQINDIFQKLNIFDQSFydlSLQTSEIKEEEKELRRTTYKLQ---VKNEEVKNMSL 118
Cdd:TIGR01612 1522 DVTELLNKYSALA--IKNKFAKTKKDSEIIIKEIKDAHKKF---ILEAEKSEQKIKEIKKEKFRIEddaAKNDKSNKAAI 1596

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888     119 ELNSKLESLlEEKILLQQKVK-----------YLEEQLTNLIQNQPET---PEHPEVTSLKTFVEkqdnSIKDLLQTVED 184
Cdd:TIGR01612 1597 DIQLSLENF-ENKFLKISDIKkkindclketeSIEKKISSFSIDSQDTelkENGDNLNSLQEFLE----SLKDQKKNIED 1671

                          170
                   ....*....|....*..
gi 7656888     185 QYKQLNQQHSQIKEIEN 201
Cdd:TIGR01612 1672 KKKELDELDSEIEKIEI 1688
PRK12704 PRK12704
phosphodiesterase; Provisional
 91-214 7.75e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 7.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888    91 EIKEEEKELRRTTYKLQVKNEEVKNmSLELNSKLESLLEEKIL----LQQKVKYLEEQLTNLIQNQPETPEHpeVTSLkt 166
Cdd:PRK12704  76 ELRERRNELQKLEKRLLQKEENLDR-KLELLEKREEELEKKEKeleqKQQELEKKEEELEELIEEQLQELER--ISGL-- 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 7656888   167 fveKQDNSIKDLLQTVEDQYKQlnQQHSQIKEIENQLRRTSIQEPTEI 214
Cdd:PRK12704 151 ---TAEEAKEILLEKVEEEARH--EAAVLIKEIEEEAKEEADKKAKEI 193
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 57-209 1.09e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888     57 LKDFVHKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRRTTYKLQV----KNEEVKNMSLELNSKLESL----- 127
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQReleeKQNEIEKLKKENQSYKQEIknles 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888    128 ----LEEKILLQQKV-KYLEEQLTNLIQNQPETPEhpEVTSLKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQ 202
Cdd:TIGR04523 392 qindLESKIQNQEKLnQQKDEQIKKLQQEKELLEK--EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469


                  ....*..
gi 7656888    203 LRRTSIQ 209
Cdd:TIGR04523 470 LKVLSRS 476
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
91-215 1.83e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   91 EIKEEEKELRRTTYKLQVKNEEVKNmsleLNSKLESLLEEKILLQQKVKYLEEQLTNLIQNQPETPEhpevtSLKTfVEK 170
Cdd:COG4372  39 ELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-----ELES-LQE 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 7656888  171 QDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRRTSIQEPTEIS 215
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
TFB3 COG5220
Cdk activating kinase (CAK)/RNA polymerase II transcription initiation/nucleotide excision ...
 69-243 3.62e-03

Cdk activating kinase (CAK)/RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit TFB3 [Cell division and chromosome partitioning / Transcription / DNA replication, recombination, and repair];


Pssm-ID: 227545 [Multi-domain]  Cd Length: 314  Bit Score: 39.23  E-value: 3.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   69 NDIFQKLNIFDQSFYDLSLqtseikEEEKELRRTTYKLQVKNEEVKNMSL-ELNSKLESL------LEEKI---LLQQKV 138
Cdd:COG5220  60 GKILRKIKFIKQTFEDITV------EKEVDVRKRLLRAFNKEEEEFGGDLaKYNDYLEEVeelvfeLLELIdvsLTEEKV 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888  139 KYLEEQLTNLIQNQPETPEhPEVTSLKT--FVEKQDNSIKDLLQTVEDQYKQLNQQHSQiKEIENQLRRTS-----IQEP 211
Cdd:COG5220 134 KKYEEMNQDSILNNLERPT-PEVMPGKQknVLQKRMKLKKRQLERQIEEEERMNKEWTK-KEIGNRLGTASedgnkTIKI 211

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 7656888  212 TEISLSSKPRA--------PRTTPFLqLNEIRNVKHDGIP 243
Cdd:COG5220 212 GIISDKFDPEElprivvepTRNNKIY-LSNVQGFLKDLQP 250
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 91-205 5.36e-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: 38.37  E-value: 5.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   91 EIKEEEKELRRTTYKLQVKNEEVKNMSLELnSKLESLLEEkilLQQKVKYLEEQLTNlIQNQPE--TPEHpEVTSLKTFV 168
Cdd:COG1579  32 ELAELEDELAALEARLEAAKTELEDLEKEI-KRLELEIEE---VEARIKKYEEQLGN-VRNNKEyeALQK-EIESLKRRI 105

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 7656888  169 EKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRR 205
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 88-219 5.59e-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: 5.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   88 QTSEIKEEEKELRRTTYKLQvkneevknmslELNSKLESLLEEKILLQQKVKYLEEQLTNLIQnqpetpehpEVTSLKTF 167
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIA-----------ELEKELAALKKEEKALLKQLAALERRIAALAR---------RIRALEQE 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 7656888  168 VEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRRTSIQEPTEISLSSK 219
Cdd:COG4942  78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE 129
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 57-201 6.20e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888     57 LKDFVHKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRRTTYKLQVKNEEVKNMSLELNSKLESLLEEKILLQQ 136
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE 510

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7656888    137 KVKYLEEQLTNLIQNQPE-----TPEHPEVTSLKTFVEKQD-NSIKDLLQTVEDQY-KQLNQQHSQIKEIEN 201
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKlesekKEKESKISDLEDELNKDDfELKKENLEKEIDEKnKEIEELKQTQKSLKK 582
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 84-217 7.14e-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: 38.88  E-value: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888      84 DLSLQTSEIKEEEKELRRTTYKLQvkneevknmslELNSKLESLLEEKILLQQKVKYLEEQLTNLIQ-NQPETPEHP--- 159
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELE-----------ELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALEnki 963

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888     160 --EVTSLKTFVEKQDNSIKDL----------LQTVEDQYKQLNQQHSQIKEIENQLRRTsIQEPTEISLS 217
Cdd:TIGR02168  964 edDEEEARRRLKRLENKIKELgpvnlaaieeYEELKERYDFLTAQKEDLTEAKETLEEA-IEEIDREARE 1032
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
65-202 7.76e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 7.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   65 KGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRRTTYKLQVKNEEVKNMSLELNSKLESLLEEKILLQQKVKYLE-- 142
Cdd:COG1340  28 KEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNka 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888  143 -----------EQLTNLIQNQPETPEHP-----EVTSLKTFVEK------QDNSIKDLLQTVEDQYKQLNQQHSQIKEIE 200
Cdd:COG1340 108 ggsidklrkeiERLEWRQQTEVLSPEEEkelveKIKELEKELEKakkaleKNEKLKELRAELKELRKEAEEIHKKIKELA 187


                ..
gi 7656888  201 NQ 202
Cdd:COG1340 188 EE 189
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
62-203 8.34e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 8.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888    62 HKTKGQINDIFQKLNIFDqsfydlslqTSEIKEEEKELRRTTYKLQVKNEEVKNMSLELNsKLESLLEEKILLQQKVKYL 141
Cdd:PRK03918 499 KELAEQLKELEEKLKKYN---------LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDEL 568

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   142 EEQLTNLIQNQPET----------------PEHPEVTSLKTFV---EKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQ 202
Cdd:PRK03918 569 EEELAELLKELEELgfesveeleerlkelePFYNEYLELKDAEkelEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648


                 .
gi 7656888   203 L 203
Cdd:PRK03918 649 L 649
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
91-205 9.55e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 9.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656888   91 EIKEEEKELRRTTYKLQVKNEEvknmslELNSKLEsLLEEKILLQQKVKYLEEQLtnliQNQPETPEHPEVTSLKTFVEK 170
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEE------ELRAALE-QAEEYQELKEELEELEEQL----EELLGELEELLEALDEEELEE 432

                        90       100       110
                ....*....|....*....|....*....|....*
gi 7656888  171 QDNSIKDLLQTVEDQYKQLNQqhsQIKEIENQLRR 205
Cdd:COG4717 433 ELEELEEELEELEEELEELRE---ELAELEAELEQ 464
 
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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