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Conserved domains on  [gi|157820699|ref|NP_001099996|]
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angiopoietin-4 precursor [Rattus norvegicus]

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 ...
 291-506 1.29e-117

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: 344.99  E-value: 1.29e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699 291 PLFRDCAEIKRSGANTSGVYTIHGANMTKPLKVFCDMETDGGGWTLIQRREDGSLNFQRTWEEYKEGFGNVAREHWLGNE 370
Cdd:cd00087    1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699 371 AVHSLTSRTAYLLRVELHDWEGHQTSIQYENFQLGSERQRYSLSVNDSSISArlKNSLA-PQGTKFSTKDMDNDNCMCKC 449
Cdd:cd00087   81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTA--GDALSyHNGMKFSTFDRDNDGASGNC 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157820699 450 AQMLSGGWWFDACGLSNLNGIYYPVHQHLHKINGIRWHYFRGPSYSLHGTRMMLRPM 506
Cdd:cd00087  159 AESYSGGWWYNSCHASNLNGRYYSGGHRNEYDNGINWATWKGSTYSLKFTEMKIRPK 215
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 98-233 1.02e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699    98 LEKILENNTQWLL-----KLEQSIQmNLRSDLAQAQQHtIQNQTTTMLALganlmNQTMAQTHK-LTAVEAQVLNHTS-- 169
Cdd:TIGR02169  216 LLKEKREYEGYELlkekeALERQKE-AIERQLASLEEE-LEKLTEEISEL-----EKRLEEIEQlLEELNKKIKDLGEee 288

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157820699   170 --RVKTQMLESSLSTNKLERQMLMQSRELQRLQGRNRALETRLQALEAQHQA---QLNSLQDKREQLQS 233
Cdd:TIGR02169  289 qlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTE 357
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 291-506 1.29e-117

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: 344.99  E-value: 1.29e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699 291 PLFRDCAEIKRSGANTSGVYTIHGANMTKPLKVFCDMETDGGGWTLIQRREDGSLNFQRTWEEYKEGFGNVAREHWLGNE 370
Cdd:cd00087    1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699 371 AVHSLTSRTAYLLRVELHDWEGHQTSIQYENFQLGSERQRYSLSVNDSSISArlKNSLA-PQGTKFSTKDMDNDNCMCKC 449
Cdd:cd00087   81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTA--GDALSyHNGMKFSTFDRDNDGASGNC 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157820699 450 AQMLSGGWWFDACGLSNLNGIYYPVHQHLHKINGIRWHYFRGPSYSLHGTRMMLRPM 506
Cdd:cd00087  159 AESYSGGWWYNSCHASNLNGRYYSGGHRNEYDNGINWATWKGSTYSLKFTEMKIRPK 215
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 292-506 1.54e-100

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: 301.12  E-value: 1.54e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699   292 LFRDCAEIKRSGANTSGVYTIHGANMTKPLKVFCDMETDGGGWTLIQRREDGSLNFQRTWEEYKEGFGNVAREHWLGNEA 371
Cdd:smart00186   1 LPRDCSDVLQNGGKTSGLYTIYPDGSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNEN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699   372 VHSLTSRTAYLLRVELHDWEGHQTSIQYENFQLGSERQRYSLSVNDSSISArLKNSLA-PQGTKFSTKDMDNDNCMCKCA 450
Cdd:smart00186  81 IHLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTA-GDASLTyHNGMQFSTYDRDNDKYSGNCA 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157820699   451 QMLSGGWWFDACGLSNLNGIYYPVHQHLhkiNGIRWHYFRGPSYSLHGTRMMLRPM 506
Cdd:smart00186 160 EEYGGGWWYNNCHAANLNGRYYPNNNYD---NGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
294-505 4.44e-71

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 225.86  E-value: 4.44e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699  294 RDCAEIKRSGANTSGVYTIHGANMTKPLKVFCDMETDGGGWTLIQRREDGSLNFQRTWEEYKEGFGNVAR-EHWLGNEAV 372
Cdd:pfam00147   3 RDCSDVYNKGAKTSGLYTIRPDGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLSPgEFWLGNDKI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699  373 HSLTSRTAYLLRVELHDWEGHQTSIQYENFQLGSERQRYSLSVNDSSISARLKNSLAPQ------GTKFSTKDMDNDNCM 446
Cdd:pfam00147  83 HLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDAGDALDTAGRsmtyhnGMQFSTWDRDNDSPD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699  447 CKCAQMLSGGWWFDACGLSNLNGIYYpvHQ-HLHKINGIRWHYFRGPSYSLHGTRMMLRP 505
Cdd:pfam00147 163 GNCALSYGGGWWYNNCHAANLNGVYY--YGgTYSKQNGIIWATWKGRWYSMKKAEMKIRP 220
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 296-337 8.17e-14

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: 65.66  E-value: 8.17e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 157820699 296 CAEIKRSGANT-SGVYTIH--GANMTKPLKVFCDMETDGGGWTLI 337
Cdd:NF040941   2 CWEILQAGPSApSGVYWIDpdGMGGLAPFQVYCDMTTDGGGWTLV 46
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 98-233 1.02e-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: 41.98  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699    98 LEKILENNTQWLL-----KLEQSIQmNLRSDLAQAQQHtIQNQTTTMLALganlmNQTMAQTHK-LTAVEAQVLNHTS-- 169
Cdd:TIGR02169  216 LLKEKREYEGYELlkekeALERQKE-AIERQLASLEEE-LEKLTEEISEL-----EKRLEEIEQlLEELNKKIKDLGEee 288

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157820699   170 --RVKTQMLESSLSTNKLERQMLMQSRELQRLQGRNRALETRLQALEAQHQA---QLNSLQDKREQLQS 233
Cdd:TIGR02169  289 qlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTE 357
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
112-234 1.64e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699 112 LEQSIQmNLRSDLAQAQQ--HTIQNQT-TTMLALGANLMNQTMAQ-THKLTAVEAQVLNHTSRVKTqmLESSLSTNKLER 187
Cdd:COG3206  180 LEEQLP-ELRKELEEAEAalEEFRQKNgLVDLSEEAKLLLQQLSElESQLAEARAELAEAEARLAA--LRAQLGSGPDAL 256

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157820699 188 QMLMQSRELQRLQGRNRALETRLQALEAQHQAQLNSLQDKREQLQSL 234
Cdd:COG3206  257 PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
Filament pfam00038
Intermediate filament protein;
165-235 3.77e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 39.52  E-value: 3.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820699  165 LNHTSRVKTQMLESSLST-NKLERQMLMQSRELQRLQGRNRALETRLQALEAQHQAQLNSLQDKREQLQSLL 235
Cdd:pfam00038 201 LQQAAARNGDALRSAKEEiTELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAEL 272
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 291-506 1.29e-117

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: 344.99  E-value: 1.29e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699 291 PLFRDCAEIKRSGANTSGVYTIHGANMTKPLKVFCDMETDGGGWTLIQRREDGSLNFQRTWEEYKEGFGNVAREHWLGNE 370
Cdd:cd00087    1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699 371 AVHSLTSRTAYLLRVELHDWEGHQTSIQYENFQLGSERQRYSLSVNDSSISArlKNSLA-PQGTKFSTKDMDNDNCMCKC 449
Cdd:cd00087   81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTA--GDALSyHNGMKFSTFDRDNDGASGNC 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157820699 450 AQMLSGGWWFDACGLSNLNGIYYPVHQHLHKINGIRWHYFRGPSYSLHGTRMMLRPM 506
Cdd:cd00087  159 AESYSGGWWYNSCHASNLNGRYYSGGHRNEYDNGINWATWKGSTYSLKFTEMKIRPK 215
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 292-506 1.54e-100

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: 301.12  E-value: 1.54e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699   292 LFRDCAEIKRSGANTSGVYTIHGANMTKPLKVFCDMETDGGGWTLIQRREDGSLNFQRTWEEYKEGFGNVAREHWLGNEA 371
Cdd:smart00186   1 LPRDCSDVLQNGGKTSGLYTIYPDGSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNEN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699   372 VHSLTSRTAYLLRVELHDWEGHQTSIQYENFQLGSERQRYSLSVNDSSISArLKNSLA-PQGTKFSTKDMDNDNCMCKCA 450
Cdd:smart00186  81 IHLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTA-GDASLTyHNGMQFSTYDRDNDKYSGNCA 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157820699   451 QMLSGGWWFDACGLSNLNGIYYPVHQHLhkiNGIRWHYFRGPSYSLHGTRMMLRPM 506
Cdd:smart00186 160 EEYGGGWWYNNCHAANLNGRYYPNNNYD---NGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
294-505 4.44e-71

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 225.86  E-value: 4.44e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699  294 RDCAEIKRSGANTSGVYTIHGANMTKPLKVFCDMETDGGGWTLIQRREDGSLNFQRTWEEYKEGFGNVAR-EHWLGNEAV 372
Cdd:pfam00147   3 RDCSDVYNKGAKTSGLYTIRPDGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLSPgEFWLGNDKI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699  373 HSLTSRTAYLLRVELHDWEGHQTSIQYENFQLGSERQRYSLSVNDSSISARLKNSLAPQ------GTKFSTKDMDNDNCM 446
Cdd:pfam00147  83 HLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDAGDALDTAGRsmtyhnGMQFSTWDRDNDSPD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699  447 CKCAQMLSGGWWFDACGLSNLNGIYYpvHQ-HLHKINGIRWHYFRGPSYSLHGTRMMLRP 505
Cdd:pfam00147 163 GNCALSYGGGWWYNNCHAANLNGVYY--YGgTYSKQNGIIWATWKGRWYSMKKAEMKIRP 220
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 296-337 8.17e-14

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: 65.66  E-value: 8.17e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 157820699 296 CAEIKRSGANT-SGVYTIH--GANMTKPLKVFCDMETDGGGWTLI 337
Cdd:NF040941   2 CWEILQAGPSApSGVYWIDpdGMGGLAPFQVYCDMTTDGGGWTLV 46
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 98-233 1.02e-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: 41.98  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699    98 LEKILENNTQWLL-----KLEQSIQmNLRSDLAQAQQHtIQNQTTTMLALganlmNQTMAQTHK-LTAVEAQVLNHTS-- 169
Cdd:TIGR02169  216 LLKEKREYEGYELlkekeALERQKE-AIERQLASLEEE-LEKLTEEISEL-----EKRLEEIEQlLEELNKKIKDLGEee 288

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157820699   170 --RVKTQMLESSLSTNKLERQMLMQSRELQRLQGRNRALETRLQALEAQHQA---QLNSLQDKREQLQS 233
Cdd:TIGR02169  289 qlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTE 357
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
112-234 1.64e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699 112 LEQSIQmNLRSDLAQAQQ--HTIQNQT-TTMLALGANLMNQTMAQ-THKLTAVEAQVLNHTSRVKTqmLESSLSTNKLER 187
Cdd:COG3206  180 LEEQLP-ELRKELEEAEAalEEFRQKNgLVDLSEEAKLLLQQLSElESQLAEARAELAEAEARLAA--LRAQLGSGPDAL 256

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157820699 188 QMLMQSRELQRLQGRNRALETRLQALEAQHQAQLNSLQDKREQLQSL 234
Cdd:COG3206  257 PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
Filament pfam00038
Intermediate filament protein;
165-235 3.77e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 39.52  E-value: 3.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820699  165 LNHTSRVKTQMLESSLST-NKLERQMLMQSRELQRLQGRNRALETRLQALEAQHQAQLNSLQDKREQLQSLL 235
Cdd:pfam00038 201 LQQAAARNGDALRSAKEEiTELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAEL 272
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-232 8.15e-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: 8.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820699    96 SQLEKILENntqwLLKLE---QSIQMNLRSDLAQAQQ----HTIQNQ-TTTMLALGANLMNQTMAQTHKL----TAVEAQ 163
Cdd:TIGR02168  179 RKLERTREN----LDRLEdilNELERQLKSLERQAEKaeryKELKAElRELELALLVLRLEELREELEELqeelKEAEEE 254

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820699   164 VLNHTSRVktQMLESSLSTNKLERQMLmqSRELQRLQGRNRALETRLQALEAQ---HQAQLNSLQDKREQLQ 232
Cdd:TIGR02168  255 LEELTAEL--QELEEKLEELRLEVSEL--EEEIEELQKELYALANEISRLEQQkqiLRERLANLERQLEELE 322
 
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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