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Conserved domains on  [gi|1907109136|ref|XP_036014971|]
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angiopoietin-1 isoform X3 [Mus musculus]

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 ...
 173-388 2.68e-128

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: 367.72  E-value: 2.68e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136 173 KPFRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNE 252
Cdd:cd00087     1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136 253 FIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSlILHGADFSTKDADNDNCMCKCA 332
Cdd:cd00087    81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALS-YHNGMKFSTFDRDNDGASGNCA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907109136 333 LMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 388
Cdd:cd00087   160 ESYSGGWWYNSCHASNLNGRYYSGGHRNEYDNGINWATWKGSTYSLKFTEMKIRPK 215
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 29-151 2.07e-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.


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  29 SQTAEQTRKLTDVETQVLNQTSRleIQLLENSLSTYKLEKQLLQQTNEILK--IHEKNSLLEHKILEMEGKhKEELDTLK 106
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKI--ISQLNEQISQLKKELTNSESENSEKQreLEEKQNEIEKLKKENQSY-KQEIKNLE 390

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907109136 107 EEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLELMDTV 151
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 173-388 2.68e-128

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: 367.72  E-value: 2.68e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136 173 KPFRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNE 252
Cdd:cd00087     1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136 253 FIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSlILHGADFSTKDADNDNCMCKCA 332
Cdd:cd00087    81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALS-YHNGMKFSTFDRDNDGASGNCA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907109136 333 LMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 388
Cdd:cd00087   160 ESYSGGWWYNSCHASNLNGRYYSGGHRNEYDNGINWATWKGSTYSLKFTEMKIRPK 215
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 175-388 4.26e-126

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: 361.98  E-value: 4.26e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  175 FRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFI 254
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  255 FAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALM 334
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDASLTYHNGMQFSTYDRDNDKYSGNCAEE 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907109136  335 LTGGWWFDACGPSNLNGMFYtagQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 388
Cdd:smart00186 162 YGGGWWYNNCHAANLNGRYY---PNNNYDNGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
176-388 3.66e-76

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 235.11  E-value: 3.66e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136 176 RDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPS-GEYWLGNEFI 254
Cdd:pfam00147   3 RDCSDVYNKGAKTSGLYTIRPDGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLSpGEFWLGNDKI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136 255 FAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQ-----SSLILH-GADFSTKDADNDNCM 328
Cdd:pfam00147  83 HLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDAGDAldtagRSMTYHnGMQFSTWDRDNDSPD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136 329 CKCALMLTGGWWFDACGPSNLNGMFYTaGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 388
Cdd:pfam00147 163 GNCALSYGGGWWYNNCHAANLNGVYYY-GGTYSKQNGIIWATWKGRWYSMKKAEMKIRPL 221
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 178-219 5.91e-08

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: 48.71  E-value: 5.91e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907109136 178 CADVYQAGFN-KSGIYTIYFNNMP--EPKKVFCNMDVNGGGWTVI 219
Cdd:NF040941    2 CWEILQAGPSaPSGVYWIDPDGMGglAPFQVYCDMTTDGGGWTLV 46
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 29-151 2.07e-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: 43.47  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  29 SQTAEQTRKLTDVETQVLNQTSRleIQLLENSLSTYKLEKQLLQQTNEILK--IHEKNSLLEHKILEMEGKhKEELDTLK 106
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKI--ISQLNEQISQLKKELTNSESENSEKQreLEEKQNEIEKLKKENQSY-KQEIKNLE 390

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907109136 107 EEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLELMDTV 151
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 29-147 4.86e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  29 SQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLStyKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEE 108
Cdd:COG1196   209 AEKAERYRELKEELKELEAELLLLKLRELEAELE--ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907109136 109 KENLQGLVSRqtfiIQELEKQLSRATNNNSILQKQQLEL 147
Cdd:COG1196   287 QAEEYELLAE----LARLEQDIARLEERRRELEERLEEL 321
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 69-137 6.32e-04

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 40.88  E-value: 6.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907109136  69 QLLQQTNEILKIHEKNSllehkilEMEGKHKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNN 137
Cdd:pfam17078  21 QLTVQSQNLLSKLEIAQ-------QKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSY 82
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
15-148 3.07e-03

nitrate/nitrite two-component system sensor histidine kinase NarQ;


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 39.45  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  15 NHTATmlEIGT---SLLSQTAEQTRKLTDV--ETQVLNQTSRLeiqllensLSTYKLEKQLLQQTNEILKIHEKNSLLEH 89
Cdd:PRK10935  216 NQMSS--ELHKlyrSLEASVEEKTRKLTQAnrSLEVLYQCSQA--------LNASQIDVHCFRHILQIVRDHEGLDYLEL 285

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907109136  90 KILE------MEGKHKEELD----TLKEEKENL------QGLVSRQTFIIQELEKQLSRA-TNNNSILQKQQLELM 148
Cdd:PRK10935  286 EVGEnehwriSEGQPNPELPwqilPLTMEDTVLgylhwqASLPCPDEPLMNNVAQMLGRGlYFNQAQKQQQQLLLM 361
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 173-388 2.68e-128

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: 367.72  E-value: 2.68e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136 173 KPFRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNE 252
Cdd:cd00087     1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136 253 FIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSlILHGADFSTKDADNDNCMCKCA 332
Cdd:cd00087    81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALS-YHNGMKFSTFDRDNDGASGNCA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907109136 333 LMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 388
Cdd:cd00087   160 ESYSGGWWYNSCHASNLNGRYYSGGHRNEYDNGINWATWKGSTYSLKFTEMKIRPK 215
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 175-388 4.26e-126

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: 361.98  E-value: 4.26e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  175 FRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFI 254
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  255 FAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALM 334
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDASLTYHNGMQFSTYDRDNDKYSGNCAEE 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907109136  335 LTGGWWFDACGPSNLNGMFYtagQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 388
Cdd:smart00186 162 YGGGWWYNNCHAANLNGRYY---PNNNYDNGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
176-388 3.66e-76

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 235.11  E-value: 3.66e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136 176 RDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPS-GEYWLGNEFI 254
Cdd:pfam00147   3 RDCSDVYNKGAKTSGLYTIRPDGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLSpGEFWLGNDKI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136 255 FAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQ-----SSLILH-GADFSTKDADNDNCM 328
Cdd:pfam00147  83 HLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDAGDAldtagRSMTYHnGMQFSTWDRDNDSPD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136 329 CKCALMLTGGWWFDACGPSNLNGMFYTaGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 388
Cdd:pfam00147 163 GNCALSYGGGWWYNNCHAANLNGVYYY-GGTYSKQNGIIWATWKGRWYSMKKAEMKIRPL 221
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 178-219 5.91e-08

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: 48.71  E-value: 5.91e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907109136 178 CADVYQAGFN-KSGIYTIYFNNMP--EPKKVFCNMDVNGGGWTVI 219
Cdd:NF040941    2 CWEILQAGPSaPSGVYWIDPDGMGglAPFQVYCDMTTDGGGWTLV 46
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 29-151 2.07e-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: 43.47  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  29 SQTAEQTRKLTDVETQVLNQTSRleIQLLENSLSTYKLEKQLLQQTNEILK--IHEKNSLLEHKILEMEGKhKEELDTLK 106
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKI--ISQLNEQISQLKKELTNSESENSEKQreLEEKQNEIEKLKKENQSY-KQEIKNLE 390

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907109136 107 EEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLELMDTV 151
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 29-147 4.86e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  29 SQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLStyKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEE 108
Cdd:COG1196   209 AEKAERYRELKEELKELEAELLLLKLRELEAELE--ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907109136 109 KENLQGLVSRqtfiIQELEKQLSRATNNNSILQKQQLEL 147
Cdd:COG1196   287 QAEEYELLAE----LARLEQDIARLEERRRELEERLEEL 321
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 69-137 6.32e-04

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 40.88  E-value: 6.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907109136  69 QLLQQTNEILKIHEKNSllehkilEMEGKHKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNN 137
Cdd:pfam17078  21 QLTVQSQNLLSKLEIAQ-------QKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSY 82
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 27-172 1.85e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136   27 LLSQTAEQTRKLTDVETQVlnqtSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEmegkhkEELDTLK 106
Cdd:TIGR02169  728 LEQEEEKLKERLEELEEDL----SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH------SRIPEIQ 797

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  107 EEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQ----QLELMDTVHNLISLCTKEVLLKGGKREEE 172
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEiqelQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
15-148 3.07e-03

nitrate/nitrite two-component system sensor histidine kinase NarQ;


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 39.45  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  15 NHTATmlEIGT---SLLSQTAEQTRKLTDV--ETQVLNQTSRLeiqllensLSTYKLEKQLLQQTNEILKIHEKNSLLEH 89
Cdd:PRK10935  216 NQMSS--ELHKlyrSLEASVEEKTRKLTQAnrSLEVLYQCSQA--------LNASQIDVHCFRHILQIVRDHEGLDYLEL 285

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907109136  90 KILE------MEGKHKEELD----TLKEEKENL------QGLVSRQTFIIQELEKQLSRA-TNNNSILQKQQLELM 148
Cdd:PRK10935  286 EVGEnehwriSEGQPNPELPwqilPLTMEDTVLgylhwqASLPCPDEPLMNNVAQMLGRGlYFNQAQKQQQQLLLM 361
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 26-151 3.51e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136   26 SLLSQTAEQTRKLTDVETQVLNQTSRL-----EIQLLENSLSTYKLEKQLLqqTNEILKIHEKNSLLEHKILEMEGKH-- 98
Cdd:TIGR02169  305 SLERSIAEKERELEDAEERLAKLEAEIdkllaEIEELEREIEEERKRRDKL--TEEYAELKEELEDLRAELEEVDKEFae 382

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907109136   99 --------KEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLELMDTV 151
Cdd:TIGR02169  383 trdelkdyREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
 65-110 3.87e-03

Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.


Pssm-ID: 428400 [Multi-domain]  Cd Length: 188  Bit Score: 38.02  E-value: 3.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907109136  65 KLEKQLLQQTNEILKIHEKNSLLEHKILEMEgkhkEELDTLKEEKE 110
Cdd:pfam05266 113 KLEKKIAEEESEKRKLEEEIDELEKKILELE----RQLALAKEKKE 154
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 27-151 4.24e-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: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  27 LLSQTAEQTRKLTDVETQVlnQTSRLEIQLLENSLSTY-----KLEKQLLQQTN---------EILKIHEKNSLLEHKIL 92
Cdd:COG1579    36 LEDELAALEARLEAAKTEL--EDLEKEIKRLELEIEEVearikKYEEQLGNVRNnkeyealqkEIESLKRRISDLEDEIL 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907109136  93 EMEGKHKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLELMDTV 151
Cdd:COG1579   114 ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1-154 4.84e-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: 39.11  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136   1 MKSEMAQIQQN-AVQNHTATMLeiGTSLLSQTAEQTRKLTDVEtQVLNQTSRLEIQLLENSL------STYKLEKQLLQQ 73
Cdd:pfam07888 235 LLEELRSLQERlNASERKVEGL--GEELSSMAAQRDRTQAELH-QARLQAAQLTLQLADASLalregrARWAQERETLQQ 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  74 TNEilKIHEKNSLLEHKILEMEGKHKEE------LDT-LKEEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLE 146
Cdd:pfam07888 312 SAE--ADKDRIEKLSAELQRLEERLQEErmerekLEVeLGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQE 389


                  ....*...
gi 1907109136 147 LMDTVHNL 154
Cdd:pfam07888 390 LLEYIRQL 397
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 66-155 8.28e-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: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  66 LEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQL 145
Cdd:COG4942   144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223

                          90
                  ....*....|
gi 1907109136 146 ELMDTVHNLI 155
Cdd:COG4942   224 ELEALIARLE 233
PRK12704 PRK12704
phosphodiesterase; Provisional
 65-172 9.19e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 9.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  65 KLEKQLLQQTNEILKiheknslLEHKILEMEGKHKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNnnsiLQKQQ 144
Cdd:PRK12704   72 EFEKELRERRNELQK-------LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE----LIEEQ 140

                          90       100
                  ....*....|....*....|....*...
gi 1907109136 145 LELMDTVHNLISLCTKEVLLKggKREEE 172
Cdd:PRK12704  141 LQELERISGLTAEEAKEILLE--KVEEE 166
PRK12704 PRK12704
phosphodiesterase; Provisional
 32-128 9.68e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 9.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  32 AEQTRK--LTDVETQVLNQTSRLEIQLLE--NSLStyKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKE 107
Cdd:PRK12704   51 AEAIKKeaLLEAKEEIHKLRNEFEKELRErrNELQ--KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEK 128

                          90       100
                  ....*....|....*....|.
gi 1907109136 108 EKENLQGLVSRQtfiIQELEK 128
Cdd:PRK12704  129 KEEELEELIEEQ---LQELER 146
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-181 9.94e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 9.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  28 LSQTAEQTRKLTDVETQV---LNQTSRL--------EIQLLENSLSTYKLEKqLLQQTNEILKIHEKNSLLEHKIL---- 92
Cdd:PRK03918  468 LKEIEEKERKLRKELRELekvLKKESELiklkelaeQLKELEEKLKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKslkk 546

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907109136  93 ------EMEGKHKE---ELDTLKEEKENLQGLVSRQTF-IIQELEKQLSRATNnnsiLQKQQLELMDTVHNLISlctKEV 162
Cdd:PRK03918  547 elekleELKKKLAElekKLDELEEELAELLKELEELGFeSVEELEERLKELEP----FYNEYLELKDAEKELER---EEK 619

                         170
                  ....*....|....*....
gi 1907109136 163 LLKGGKREEEKPFRDCADV 181
Cdd:PRK03918  620 ELKKLEEELDKAFEELAET 638
 
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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