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Conserved domains on  [gi|21699062|ref|NP_660136|]
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angiopoietin-related protein 6 precursor [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

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 ...
242-453 8.11e-115

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: 335.75  E-value: 8.11e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062 242 GPWRDCAEAHGAGHWQSGVYDLRLG--RRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFGRPEGEYWLGLE 319
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPgsNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062 320 PVHQVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGDSLSWHNDKPFSTVDRDRDSYSGNCAL 399
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGASGNCAE 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21699062 400 YHRGGWWYHACAHSNLNGVWYHGGHyRSRYQDGVYWAEFRGGAYSLKKAVMLTR 453
Cdd:cd00087 161 SYSGGWWYNSCHASNLNGRYYSGGH-RNEYDNGINWATWKGSTYSLKFTEMKIR 213
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-168 5.67e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 5.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062   48 ATQDSELATLRMRLGRHEELLRAL--QRRAAEGGALAD---EVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAA 122
Cdd:COG4913  305 ARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQlerEIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 21699062  123 ALGLLAERALDAEAEARRTTARLQQLDAQL----REHAQLMSQHSSLLGR 168
Cdd:COG4913  385 LRAEAAALLEALEEELEALEEALAEAEAALrdlrRELRELEAEIASLERR 434
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
242-453 8.11e-115

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: 335.75  E-value: 8.11e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062 242 GPWRDCAEAHGAGHWQSGVYDLRLG--RRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFGRPEGEYWLGLE 319
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPgsNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062 320 PVHQVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGDSLSWHNDKPFSTVDRDRDSYSGNCAL 399
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGASGNCAE 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21699062 400 YHRGGWWYHACAHSNLNGVWYHGGHyRSRYQDGVYWAEFRGGAYSLKKAVMLTR 453
Cdd:cd00087 161 SYSGGWWYNSCHASNLNGRYYSGGH-RNEYDNGINWATWKGSTYSLKFTEMKIR 213
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
245-453 1.48e-89

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: 271.46  E-value: 1.48e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062    245 RDCAEAHGAGHWQSGVYDLRL--GRRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFGRPEGEYWLGLEPVH 322
Cdd:smart00186   3 RDCSDVLQNGGKTSGLYTIYPdgSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENIH 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062    323 QVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGD-SLSWHNDKPFSTVDRDRDSYSGNCALYH 401
Cdd:smart00186  83 LLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDaSLTYHNGMQFSTYDRDNDKYSGNCAEEY 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 21699062    402 RGGWWYHACAHSNLNGVWYHggHYrsRYQDGVYWAEFRGGAYSLKKAVMLTR 453
Cdd:smart00186 163 GGGWWYNNCHAANLNGRYYP--NN--NYDNGINWATWKGSWYSLKFTEMKIR 210
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
245-453 4.99e-75

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 234.34  E-value: 4.99e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062   245 RDCAEAHGAGHWQSGVYDLRL--GRRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFG-RPEGEYWLGLEPV 321
Cdd:pfam00147   3 RDCSDVYNKGAKTSGLYTIRPdgATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGnLSPGEFWLGNDKI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062   322 HQVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGD-------SLSWHNDKPFSTVDRDRDSYS 394
Cdd:pfam00147  83 HLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDAGDaldtagrSMTYHNGMQFSTWDRDNDSPD 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 21699062   395 GNCALYHRGGWWYHACAHSNLNGVWYHGGHYRSryQDGVYWAEFRGGAYSLKKAVMLTR 453
Cdd:pfam00147 163 GNCALSYGGGWWYNNCHAANLNGVYYYGGTYSK--QNGIIWATWKGRWYSMKKAEMKIR 219
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-168 5.67e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 5.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062   48 ATQDSELATLRMRLGRHEELLRAL--QRRAAEGGALAD---EVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAA 122
Cdd:COG4913  305 ARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQlerEIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 21699062  123 ALGLLAERALDAEAEARRTTARLQQLDAQL----REHAQLMSQHSSLLGR 168
Cdd:COG4913  385 LRAEAAALLEALEEELEALEEALAEAEAALrdlrRELRELEAEIASLERR 434
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
50-164 2.42e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.52  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062    50 QDSELATLRMRlgrHEELLRAlqrrAAEGGALADEVRALREHSltlnTRLGQLRAQLQQEARAEPDLGaEPAAALGLLAE 129
Cdd:pfam05622  92 LEKEVLELQHR---NEELTSL----AEEAQALKDEMDILRESS----DKVKKLEATVETYKKKLEDLG-DLRRQVKLLEE 159
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 21699062   130 R-------ALDAEAEARRTTARLQQLDAQLREHAQLMSQHSS 164
Cdd:pfam05622 160 RnaeymqrTLQLEEELKKANALRGQLETYKRQVQELHGKLSE 201
PRK09039 PRK09039
peptidoglycan -binding protein;
57-154 3.16e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.65  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062   57 LRMRLGRHEELLRALQRRAAEggaLADEVRALREHSLTLNTRLGQLRAQLQQeARAEPD----LGAEPAAALGLLAERA- 131
Cdd:PRK09039  44 LSREISGKDSALDRLNSQIAE---LADLLSLERQGNQDLQDSVANLRASLSA-AEAERSrlqaLLAELAGAGAAAEGRAg 119
                         90       100       110
                 ....*....|....*....|....*....|..
gi 21699062  132 -----LDAE----AEARRTTARLQQLDAQLRE 154
Cdd:PRK09039 120 elaqeLDSEkqvsARALAQVELLNQQIAALRR 151
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
52-172 6.83e-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: 6.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062     52 SELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEpaaalgllaERA 131
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE---------LEA 365
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 21699062    132 LDAEAEARRTTARlQQLDAQLREHAQLMSQHSSLLGRLQRA 172
Cdd:TIGR02168  366 ELEELESRLEELE-EQLETLRSKVAQLELQIASLNNEIERL 405
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
242-453 8.11e-115

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: 335.75  E-value: 8.11e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062 242 GPWRDCAEAHGAGHWQSGVYDLRLG--RRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFGRPEGEYWLGLE 319
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPgsNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062 320 PVHQVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGDSLSWHNDKPFSTVDRDRDSYSGNCAL 399
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGASGNCAE 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21699062 400 YHRGGWWYHACAHSNLNGVWYHGGHyRSRYQDGVYWAEFRGGAYSLKKAVMLTR 453
Cdd:cd00087 161 SYSGGWWYNSCHASNLNGRYYSGGH-RNEYDNGINWATWKGSTYSLKFTEMKIR 213
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
245-453 1.48e-89

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: 271.46  E-value: 1.48e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062    245 RDCAEAHGAGHWQSGVYDLRL--GRRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFGRPEGEYWLGLEPVH 322
Cdd:smart00186   3 RDCSDVLQNGGKTSGLYTIYPdgSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENIH 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062    323 QVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGD-SLSWHNDKPFSTVDRDRDSYSGNCALYH 401
Cdd:smart00186  83 LLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDaSLTYHNGMQFSTYDRDNDKYSGNCAEEY 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 21699062    402 RGGWWYHACAHSNLNGVWYHggHYrsRYQDGVYWAEFRGGAYSLKKAVMLTR 453
Cdd:smart00186 163 GGGWWYNNCHAANLNGRYYP--NN--NYDNGINWATWKGSWYSLKFTEMKIR 210
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
245-453 4.99e-75

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 234.34  E-value: 4.99e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062   245 RDCAEAHGAGHWQSGVYDLRL--GRRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFG-RPEGEYWLGLEPV 321
Cdd:pfam00147   3 RDCSDVYNKGAKTSGLYTIRPdgATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGnLSPGEFWLGNDKI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062   322 HQVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGD-------SLSWHNDKPFSTVDRDRDSYS 394
Cdd:pfam00147  83 HLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDAGDaldtagrSMTYHNGMQFSTWDRDNDSPD 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 21699062   395 GNCALYHRGGWWYHACAHSNLNGVWYHGGHYRSryQDGVYWAEFRGGAYSLKKAVMLTR 453
Cdd:pfam00147 163 GNCALSYGGGWWYNNCHAANLNGVYYYGGTYSK--QNGIIWATWKGRWYSMKKAEMKIR 219
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-168 5.67e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 5.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062   48 ATQDSELATLRMRLGRHEELLRAL--QRRAAEGGALAD---EVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAA 122
Cdd:COG4913  305 ARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQlerEIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 21699062  123 ALGLLAERALDAEAEARRTTARLQQLDAQL----REHAQLMSQHSSLLGR 168
Cdd:COG4913  385 LRAEAAALLEALEEELEALEEALAEAEAALrdlrRELRELEAEIASLERR 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
44-172 1.25e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062  44 RSSEATQDSELATLRMRLGRHEELLRALQRRAAEggaLADEVRALREhsltlntRLGQLRAQLQQEARAEPDLGAEPAAA 123
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEE---LEEELAELEE-------ELEELEEELEELEEELEEAEEELEEA 356
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 21699062 124 LGLLAERALDAEAEARRTTARLQQLDAQLREHAQLMSQHSSLLGRLQRA 172
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
51-157 1.32e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062  51 DSELATLRMRLGRHEELLRALQRRAAEggaLADEVRALREHSLTLNTRLGQLRAQLQQEARAEpdlgAEPAAALGLLAER 130
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAE---LEAELEELRLELEELELELEEAQAEEYELLAEL----ARLEQDIARLEER 310
                        90       100
                ....*....|....*....|....*..
gi 21699062 131 ALDAEAEARRTTARLQQLDAQLREHAQ 157
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEE 337
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
36-172 1.57e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062  36 QKATSAVCRSSEATQDSELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHsltLNTRLGQLRAQLQQEARAEPD 115
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR---LEERRRELEERLEELEEELAE 327
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21699062 116 LgaepAAALGLLAERALDAEAEARRTTARLQQLDAQLREHAQLMSQHSSLLGRLQRA 172
Cdd:COG1196 328 L----EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
50-164 2.42e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.52  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062    50 QDSELATLRMRlgrHEELLRAlqrrAAEGGALADEVRALREHSltlnTRLGQLRAQLQQEARAEPDLGaEPAAALGLLAE 129
Cdd:pfam05622  92 LEKEVLELQHR---NEELTSL----AEEAQALKDEMDILRESS----DKVKKLEATVETYKKKLEDLG-DLRRQVKLLEE 159
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 21699062   130 R-------ALDAEAEARRTTARLQQLDAQLREHAQLMSQHSS 164
Cdd:pfam05622 160 RnaeymqrTLQLEEELKKANALRGQLETYKRQVQELHGKLSE 201
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
31-172 3.01e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 3.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062  31 LVLSPQKATSAVCRSSEAtqDSELATLRMRLGRHEELLRALQRRAAEGGALADEV------RALREHSLTLNTRLGQLRA 104
Cdd:COG3206 207 LVDLSEEAKLLLQQLSEL--ESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqspviQQLRAQLAELEAELAELSA 284
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062 105 QL-----------QQEARAEPDLGAEPAAALGLLAERALDAEAEARRTTARLQQLDAQLREHAQLMSQ------------ 161
Cdd:COG3206 285 RYtpnhpdvialrAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrlerevevar 364
                       170
                ....*....|...
gi 21699062 162 --HSSLLGRLQRA 172
Cdd:COG3206 365 elYESLLQRLEEA 377
PRK09039 PRK09039
peptidoglycan -binding protein;
57-154 3.16e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.65  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062   57 LRMRLGRHEELLRALQRRAAEggaLADEVRALREHSLTLNTRLGQLRAQLQQeARAEPD----LGAEPAAALGLLAERA- 131
Cdd:PRK09039  44 LSREISGKDSALDRLNSQIAE---LADLLSLERQGNQDLQDSVANLRASLSA-AEAERSrlqaLLAELAGAGAAAEGRAg 119
                         90       100       110
                 ....*....|....*....|....*....|..
gi 21699062  132 -----LDAE----AEARRTTARLQQLDAQLRE 154
Cdd:PRK09039 120 elaqeLDSEkqvsARALAQVELLNQQIAALRR 151
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
72-178 1.03e-03

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 41.20  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062   72 QRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAAALGLLAER--------ALDAEAEArrtta 143
Cdd:PRK08269  23 PRDAAGWRALDAEARAEIERTLAALVALGRIDAAQADAVLARIAVVARDGAADALADADlvfeavpeVLDAKREA----- 97
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 21699062  144 rLQQLDAQLREHAQLMSQHSSLL-GRLQRACAGPER 178
Cdd:PRK08269  98 -LRWLGRHVDADAIIASTTSTFLvTDLQRHVAHPER 132
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-182 1.42e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062   48 ATQDSELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHS------LTLNTRLGQLRAQLQQEARAEPDLGAepa 121
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDASSDDLAA--- 689
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21699062  122 aalglLAERALDAEAEARRTTARLQQLDAQLR----EHAQLMSQHSSLLGRLQRACAGPERGQQQ 182
Cdd:COG4913  690 -----LEEQLEELEAELEELEEELDELKGEIGrlekELEQAEEELDELQDRLEAAEDLARLELRA 749
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-172 1.97e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062   48 ATQDSELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAAALGLL 127
Cdd:COG4913  671 AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 21699062  128 AERALDAEAEARRTTARLQQLDAQLREHAQLMSQHSSLLGRLQRA 172
Cdd:COG4913  751 LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
68-172 3.69e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062  68 LRALQRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQqEARAEPDLGAEPAAALGLLAERAlDAEAEARRTTARLQQ 147
Cdd:COG4717  73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE-ELREELEKLEKLLQLLPLYQELE-ALEAELAELPERLEE 150
                        90       100
                ....*....|....*....|....*
gi 21699062 148 LDAQLREHAQLMSQHSSLLGRLQRA 172
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAEL 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
52-172 6.83e-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: 6.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062     52 SELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEpaaalgllaERA 131
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE---------LEA 365
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 21699062    132 LDAEAEARRTTARlQQLDAQLREHAQLMSQHSSLLGRLQRA 172
Cdd:TIGR02168  366 ELEELESRLEELE-EQLETLRSKVAQLELQIASLNNEIERL 405
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
47-148 8.22e-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: 8.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062  47 EATQDSELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAAALGL 126
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
                        90       100
                ....*....|....*....|..
gi 21699062 127 LAERAlDAEAEARRTTARLQQL 148
Cdd:COG1196 759 PPDLE-ELERELERLEREIEAL 779
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
44-170 8.98e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 8.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21699062  44 RSSEATQ-----DSELATLRMRLGRHEELLRALQRR------AAEGGALAD-------EVRALREHSLTLNTRLGQLRAQ 105
Cdd:COG3206 169 RREEARKaleflEEQLPELRKELEEAEAALEEFRQKnglvdlSEEAKLLLQqlselesQLAEARAELAEAEARLAALRAQ 248
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21699062 106 LQQEARAEPDLGAEPaaALGLLAERALDAEAEARRTTARL-------QQLDAQLRE-HAQLMSQHSSLLGRLQ 170
Cdd:COG3206 249 LGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAAlRAQLQQEAQRILASLE 319
 
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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