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Conserved domains on  [gi|755529136|ref|XP_011240901|]
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angiopoietin-related protein 6 isoform X1 [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 ...
 259-470 6.26e-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: 336.91  E-value: 6.26e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136 259 GPWRDCAEAHGAGHWQSGVYDLRLG--RRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFGRPEGEYWLGLE 336
Cdd:cd00087    1 PLPRDCSEVLQRGGRTSGVYTIQPPgsNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136 337 PVHQVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGDSLSWHNDKPFSTVDRDRDSYSGNCAL 416
Cdd:cd00087   81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGASGNCAE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755529136 417 YHRGGWWYHACAHSNLNGVWYHGGHyRSRYQDGVYWAEFRGGAYSLKKAVMLTR 470
Cdd:cd00087  161 SYSGGWWYNSCHASNLNGRYYSGGH-RNEYDNGINWATWKGSTYSLKFTEMKIR 213
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-168 4.09e-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: 46.45  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136   48 ATQDSELATLRMRLGRHEELLRAL--QRRAAEGGALAD---EVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAA 122
Cdd:COG4913   305 ARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQlerEIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 755529136  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 ...
 259-470 6.26e-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: 336.91  E-value: 6.26e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136 259 GPWRDCAEAHGAGHWQSGVYDLRLG--RRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFGRPEGEYWLGLE 336
Cdd:cd00087    1 PLPRDCSEVLQRGGRTSGVYTIQPPgsNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136 337 PVHQVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGDSLSWHNDKPFSTVDRDRDSYSGNCAL 416
Cdd:cd00087   81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGASGNCAE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755529136 417 YHRGGWWYHACAHSNLNGVWYHGGHyRSRYQDGVYWAEFRGGAYSLKKAVMLTR 470
Cdd:cd00087  161 SYSGGWWYNSCHASNLNGRYYSGGH-RNEYDNGINWATWKGSTYSLKFTEMKIR 213
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 262-470 9.43e-90

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: 272.23  E-value: 9.43e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136   262 RDCAEAHGAGHWQSGVYDLRL--GRRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFGRPEGEYWLGLEPVH 339
Cdd:smart00186   3 RDCSDVLQNGGKTSGLYTIYPdgSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENIH 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136   340 QVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGD-SLSWHNDKPFSTVDRDRDSYSGNCALYH 418
Cdd:smart00186  83 LLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDaSLTYHNGMQFSTYDRDNDKYSGNCAEEY 162

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 755529136   419 RGGWWYHACAHSNLNGVWYHggHYrsRYQDGVYWAEFRGGAYSLKKAVMLTR 470
Cdd:smart00186 163 GGGWWYNNCHAANLNGRYYP--NN--NYDNGINWATWKGSWYSLKFTEMKIR 210
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
262-470 2.39e-75

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 235.88  E-value: 2.39e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  262 RDCAEAHGAGHWQSGVYDLRL--GRRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFG-RPEGEYWLGLEPV 338
Cdd:pfam00147   3 RDCSDVYNKGAKTSGLYTIRPdgATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGnLSPGEFWLGNDKI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  339 HQVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGD-------SLSWHNDKPFSTVDRDRDSYS 411
Cdd:pfam00147  83 HLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDAGDaldtagrSMTYHNGMQFSTWDRDNDSPD 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755529136  412 GNCALYHRGGWWYHACAHSNLNGVWYHGGHYRSryQDGVYWAEFRGGAYSLKKAVMLTR 470
Cdd:pfam00147 163 GNCALSYGGGWWYNNCHAANLNGVYYYGGTYSK--QNGIIWATWKGRWYSMKKAEMKIR 219
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-168 4.09e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136   48 ATQDSELATLRMRLGRHEELLRAL--QRRAAEGGALAD---EVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAA 122
Cdd:COG4913   305 ARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQlerEIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 755529136  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 1.52e-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: 44.29  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136   50 QDSELATLRMRlgrHEELLRAlqrrAAEGGALADEVRALREHSltlnTRLGQLRAQLQQEARAEPDLGaEPAAALGLLAE 129
Cdd:pfam05622  92 LEKEVLELQHR---NEELTSL----AEEAQALKDEMDILRESS----DKVKKLEATVETYKKKLEDLG-DLRRQVKLLEE 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 755529136  130 R-------ALDAEAEARRTTARLQQLDAQLREHAQLMSQHSS 164
Cdd:pfam05622 160 RnaeymqrTLQLEEELKKANALRGQLETYKRQVQELHGKLSE 201
PRK09039 PRK09039
peptidoglycan -binding protein;
57-154 2.45e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.03  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  57 LRMRLGRHEELLRALQRRAAEggaLADEVRALREHSLTLNTRLGQLRAQLQQeARAEPD----LGAEPAAALGLLAERA- 131
Cdd:PRK09039  44 LSREISGKDSALDRLNSQIAE---LADLLSLERQGNQDLQDSVANLRASLSA-AEAERSrlqaLLAELAGAGAAAEGRAg 119

                         90       100       110
                 ....*....|....*....|....*....|..
gi 755529136 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 4.85e-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: 39.65  E-value: 4.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136    52 SELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEpaaalgllaERA 131
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE---------LEA 365

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 755529136   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 ...
 259-470 6.26e-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: 336.91  E-value: 6.26e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136 259 GPWRDCAEAHGAGHWQSGVYDLRLG--RRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFGRPEGEYWLGLE 336
Cdd:cd00087    1 PLPRDCSEVLQRGGRTSGVYTIQPPgsNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136 337 PVHQVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGDSLSWHNDKPFSTVDRDRDSYSGNCAL 416
Cdd:cd00087   81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALSYHNGMKFSTFDRDNDGASGNCAE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755529136 417 YHRGGWWYHACAHSNLNGVWYHGGHyRSRYQDGVYWAEFRGGAYSLKKAVMLTR 470
Cdd:cd00087  161 SYSGGWWYNSCHASNLNGRYYSGGH-RNEYDNGINWATWKGSTYSLKFTEMKIR 213
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 262-470 9.43e-90

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: 272.23  E-value: 9.43e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136   262 RDCAEAHGAGHWQSGVYDLRL--GRRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFGRPEGEYWLGLEPVH 339
Cdd:smart00186   3 RDCSDVLQNGGKTSGLYTIYPdgSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENIH 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136   340 QVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGD-SLSWHNDKPFSTVDRDRDSYSGNCALYH 418
Cdd:smart00186  83 LLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDaSLTYHNGMQFSTYDRDNDKYSGNCAEEY 162

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 755529136   419 RGGWWYHACAHSNLNGVWYHggHYrsRYQDGVYWAEFRGGAYSLKKAVMLTR 470
Cdd:smart00186 163 GGGWWYNNCHAANLNGRYYP--NN--NYDNGINWATWKGSWYSLKFTEMKIR 210
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
262-470 2.39e-75

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 235.88  E-value: 2.39e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  262 RDCAEAHGAGHWQSGVYDLRL--GRRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFG-RPEGEYWLGLEPV 338
Cdd:pfam00147   3 RDCSDVYNKGAKTSGLYTIRPdgATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGnLSPGEFWLGNDKI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  339 HQVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGD-------SLSWHNDKPFSTVDRDRDSYS 411
Cdd:pfam00147  83 HLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDAGDaldtagrSMTYHNGMQFSTWDRDNDSPD 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755529136  412 GNCALYHRGGWWYHACAHSNLNGVWYHGGHYRSryQDGVYWAEFRGGAYSLKKAVMLTR 470
Cdd:pfam00147 163 GNCALSYGGGWWYNNCHAANLNGVYYYGGTYSK--QNGIIWATWKGRWYSMKKAEMKIR 219
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-168 4.09e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136   48 ATQDSELATLRMRLGRHEELLRAL--QRRAAEGGALAD---EVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAA 122
Cdd:COG4913   305 ARLEAELERLEARLDALREELDELeaQIRGNGGDRLEQlerEIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 755529136  123 ALGLLAERALDAEAEARRTTARLQQLDAQL----REHAQLMSQHSSLLGR 168
Cdd:COG4913   385 LRAEAAALLEALEEELEALEEALAEAEAALrdlrRELRELEAEIASLERR 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 51-157 8.49e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 8.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  51 DSELATLRMRLGRHEELLRALQRRAAEggaLADEVRALREHSLTLNTRLGQLRAQLQQEARAEpdlgAEPAAALGLLAER 130
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAE---LEAELEELRLELEELELELEEAQAEEYELLAEL----ARLEQDIARLEER 310

                         90       100
                 ....*....|....*....|....*..
gi 755529136 131 ALDAEAEARRTTARLQQLDAQLREHAQ 157
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEE 337
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 44-172 8.64e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 8.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  44 RSSEATQDSELATLRMRLGRHEELLRALQRRAAEggaLADEVRALREhsltlntRLGQLRAQLQQEARAEPDLGAEPAAA 123
Cdd:COG1196  287 QAEEYELLAELARLEQDIARLEERRRELEERLEE---LEEELAELEE-------ELEELEEELEELEEELEEAEEELEEA 356

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 755529136 124 LGLLAERALDAEAEARRTTARLQQLDAQLREHAQLMSQHSSLLGRLQRA 172
Cdd:COG1196  357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
31-171 1.05e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  31 LVLSPQKATSAVCRSSEAtqDSELATLRMRLGRHEELLRALQRRAAEGGALADEV------RALREHSLTLNTRLGQLRA 104
Cdd:COG3206  207 LVDLSEEAKLLLQQLSEL--ESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqspviQQLRAQLAELEAELAELSA 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136 105 QL-----------QQEARAEPDLGAEPAAALgllaeraLDAEAEARRTTARLQQLDAQLREHAQLMSQHSSL---LGRLQ 170
Cdd:COG3206  285 RYtpnhpdvialrAQIAALRAQLQQEAQRIL-------ASLEAELEALQAREASLQAQLAQLEARLAELPELeaeLRRLE 357


                 .
gi 755529136 171 R 171
Cdd:COG3206  358 R 358
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 36-172 1.08e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  36 QKATSAVCRSSEATQDSELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHsltLNTRLGQLRAQLQQEARAEPD 115
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR---LEERRRELEERLEELEEELAE 327

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755529136 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 1.52e-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: 44.29  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136   50 QDSELATLRMRlgrHEELLRAlqrrAAEGGALADEVRALREHSltlnTRLGQLRAQLQQEARAEPDLGaEPAAALGLLAE 129
Cdd:pfam05622  92 LEKEVLELQHR---NEELTSL----AEEAQALKDEMDILRESS----DKVKKLEATVETYKKKLEDLG-DLRRQVKLLEE 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 755529136  130 R-------ALDAEAEARRTTARLQQLDAQLREHAQLMSQHSS 164
Cdd:pfam05622 160 RnaeymqrTLQLEEELKKANALRGQLETYKRQVQELHGKLSE 201
PRK09039 PRK09039
peptidoglycan -binding protein;
57-154 2.45e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.03  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  57 LRMRLGRHEELLRALQRRAAEggaLADEVRALREHSLTLNTRLGQLRAQLQQeARAEPD----LGAEPAAALGLLAERA- 131
Cdd:PRK09039  44 LSREISGKDSALDRLNSQIAE---LADLLSLERQGNQDLQDSVANLRASLSA-AEAERSrlqaLLAELAGAGAAAEGRAg 119

                         90       100       110
                 ....*....|....*....|....*....|..
gi 755529136 132 -----LDAE----AEARRTTARLQQLDAQLRE 154
Cdd:PRK09039 120 elaqeLDSEkqvsARALAQVELLNQQIAALRR 151
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 44-157 3.73e-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: 42.83  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  44 RSSEATQDSELATLRMRLGRHEELLRALQRRAAEggaLADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAAA 123
Cdd:COG4942   47 KKEEKALLKQLAALERRIAALARRIRALEQELAA---LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755529136 124 LGLLAERALDAE-----------------AEARRTTARLQQLDAQLREHAQ 157
Cdd:COG4942  124 LLLSPEDFLDAVrrlqylkylaparreqaEELRADLAELAALRAELEAERA 174
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-188 8.00e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 8.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136   48 ATQDSELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHS------LTLNTRLGQLRAQLQQEARAEPDLGAepa 121
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDASSDDLAA--- 689

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755529136  122 aalglLAERALDAEAEARRTTARLQQLDAQLREHAQLMSQHSSLLGRLQRACAGPERGQQQVAVPRA 188
Cdd:COG4913   690 -----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 72-178 1.05e-03

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 41.20  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  72 QRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAAALGLLAER--------ALDAEAEArrtta 143
Cdd:PRK08269  23 PRDAAGWRALDAEARAEIERTLAALVALGRIDAAQADAVLARIAVVARDGAADALADADlvfeavpeVLDAKREA----- 97

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755529136 144 rLQQLDAQLREHAQLMSQHSSLL-GRLQRACAGPER 178
Cdd:PRK08269  98 -LRWLGRHVDADAIIASTTSTFLvTDLQRHVAHPER 132
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-172 1.62e-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: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136   48 ATQDSELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAAALGLL 127
Cdd:COG4913   671 AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755529136  128 AERALDAEAEARRTTARLQQLDAQLREHAQLMSQHSSLLGRLQRA 172
Cdd:COG4913   751 LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
68-172 2.48e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  68 LRALQRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQqEARAEPDLGAEPAAALGLLAERAlDAEAEARRTTARLQQ 147
Cdd:COG4717   73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE-ELREELEKLEKLLQLLPLYQELE-ALEAELAELPERLEE 150

                         90       100
                 ....*....|....*....|....*
gi 755529136 148 LDAQLREHAQLMSQHSSLLGRLQRA 172
Cdd:COG4717  151 LEERLEELRELEEELEELEAELAEL 175
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
50-184 2.68e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  50 QDSELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHSLTLnTRLGQLRAQLQQEARAEPDLGAEPAAALGLLAE 129
Cdd:COG4717   76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEER 154

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755529136 130 RA--LDAEAEARRTTARLQQLDAQLREHAQLMSQHSslLGRLQRACAGPERGQQQVA 184
Cdd:COG4717  155 LEelRELEEELEELEAELAELQEELEELLEQLSLAT--EEELQDLAEELEELQQRLA 209
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
51-184 4.74e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  51 DSELATLRMRLGRHEELLRALqRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLgaepAAALGLLAER 130
Cdd:COG4717  101 EEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEEL----EELEAELAEL 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755529136 131 ALDAEAEARRTTAR-LQQLDAQLREHAQLMSQHSSLLGRLQRACAGPERGQQQVA 184
Cdd:COG4717  176 QEELEELLEQLSLAtEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-172 4.85e-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: 39.65  E-value: 4.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136    52 SELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEpaaalgllaERA 131
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE---------LEA 365

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 755529136   132 LDAEAEARRTTARlQQLDAQLREHAQLMSQHSSLLGRLQRA 172
Cdd:TIGR02168  366 ELEELESRLEELE-EQLETLRSKVAQLELQIASLNNEIERL 405
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
44-170 5.79e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 5.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  44 RSSEATQ-----DSELATLRMRLGRHEELLRALQRR------AAEGGALAD-------EVRALREHSLTLNTRLGQLRAQ 105
Cdd:COG3206  169 RREEARKaleflEEQLPELRKELEEAEAALEEFRQKnglvdlSEEAKLLLQqlselesQLAEARAELAEAEARLAALRAQ 248

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755529136 106 LQQEARAEPDLGAEPaaALGLLAERALDAEAEARRTTARL-------QQLDAQLRE-HAQLMSQHSSLLGRLQ 170
Cdd:COG3206  249 LGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAAlRAQLQQEAQRILASLE 319
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 47-148 6.42e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  47 EATQDSELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAAALGL 126
Cdd:COG1196  679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758

                         90       100
                 ....*....|....*....|..
gi 755529136 127 LAERAlDAEAEARRTTARLQQL 148
Cdd:COG1196  759 PPDLE-ELERELERLEREIEAL 779
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 38-170 6.67e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.00  E-value: 6.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136    38 ATSAVCRSSEATQDSELATLRMRLGRHEELLRALQRRA-AEGGALADEVRALREhsltLNTRLGQLRAQLQQE----ARA 112
Cdd:pfam01576  215 GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLeEETAQKNNALKKIRE----LEAQISELQEDLESEraarNKA 290

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755529136   113 EP---DLGAEPAAALGLLaERALDA-----EAEARRTT--ARLQQ-LDAQLREH-AQL--MSQ-HSSLLGRLQ 170
Cdd:pfam01576  291 EKqrrDLGEELEALKTEL-EDTLDTtaaqqELRSKREQevTELKKaLEEETRSHeAQLqeMRQkHTQALEELT 362
PRK13889 PRK13889
conjugal transfer relaxase TraA; Provisional
 22-157 9.60e-03

conjugal transfer relaxase TraA; Provisional


Pssm-ID: 237546 [Multi-domain]  Cd Length: 988  Bit Score: 38.52  E-value: 9.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136  22 GGAARCRVTLVLSPQKATSAVCRSSEATQDSELATLRMR-LGRHEELLRALQR-RAAEGGALADEVRALREHSltlnTRL 99
Cdd:PRK13889 775 PGPEAGRRPERESAAATTDAPARTVAADPEAALRQARTRaLVRHARAVDAIFRmQEQGGPVLPHQVKELQEAR----KAF 850

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755529136 100 GQLRAQLQQEARA----EPDLGAEPAAALGLLAERALDAEAEAR--------RTTARLQQLDAQLREHAQ 157
Cdd:PRK13889 851 EEVRPYGSHDAEAaykkNPELAAEAASGRPARAIRALQLETELRtdparradRFVERWQKLDRASQRQYQ 920
 
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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