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Conserved domains on  [gi|387540784|gb|AFJ71019|]
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laminin subunit alpha-4 isoform 2 precursor [Macaca mulatta]

Protein Classification

LamG domain-containing protein( domain architecture ID 12873425)

LamG (Laminin G) domain-containing protein may serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules; similar to Bos taurus neurexin-1-alpha

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
291-547 1.77e-97

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


:

Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 314.74  E-value: 1.77e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   291 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDT 370
Cdd:pfam06008    1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   371 IKHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRRRQpFFTQRELVDEEADEAHELLSQ 449
Cdd:pfam06008   81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   450 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLN 528
Cdd:pfam06008  160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
                          250
                   ....*....|....*....
gi 387540784   529 TSADSLTTPRLTLSELDDI 547
Cdd:pfam06008  240 TARDSLDAANLLLQEIDDA 258
Laminin_II super family cl05515
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ...
727-854 6.00e-44

Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


The actual alignment was detected with superfamily member pfam06009:

Pssm-ID: 368703 [Multi-domain]  Cd Length: 138  Bit Score: 156.49  E-value: 6.00e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   727 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVDSARDAVRNLTEVVPQLLDQLRTVEQ 797
Cdd:pfam06009    1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784   798 KRPAS-NVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSL 854
Cdd:pfam06009   81 LEVNSsSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1485-1617 3.52e-40

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


:

Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 146.02  E-value: 3.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1485 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVVFIREKSSGRLVIDG 1564
Cdd:cd00110    21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 387540784 1565 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1617
Cdd:cd00110   101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1641-1792 2.82e-32

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


:

Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 123.68  E-value: 2.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1641 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1719
Cdd:cd00110     1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784 1720 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1792
Cdd:cd00110    78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1042-1200 1.04e-22

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


:

Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 96.33  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1042 SYFFDGSGYAAVRDitkRGKFGQVTRFDIEVRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLEDtl 1119
Cdd:cd00110     1 GVSFSGSSYVRLPT---LPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1120 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRTLRAHlpldiNFRGCMK 1196
Cdd:cd00110    74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146

                  ....
gi 387540784 1197 GFQF 1200
Cdd:cd00110   147 DLKV 150
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1230-1369 2.07e-20

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


:

Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 89.40  E-value: 2.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1230 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVVMDV----KGIKVQSvDKQYNDG 1303
Cdd:cd00110     2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387540784 1304 LSHFVIASVSPTRYELIVDKSRVGSKNPTKGKIEQTQagEKKFYFGGSPISAQ------YANFTGCISNAYF 1369
Cdd:cd00110    81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNL--DGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
853-1006 5.27e-18

Laminin G domain;


:

Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 82.00  E-value: 5.27e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784    853 SLSLYMKppvrqpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKDVEIPLDSKPVSswPAYFSIVKIERV 932
Cdd:smart00282    1 SISFSFR--------TTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLN--DGQWHRVAVERN 69
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784    933 GKHgkVFLTVPSLSSTAEEKFIKKgefsgddSLLDLDpedTVFYVGGVPSNFKLPNSLNLPGFVGCLELATLNN 1006
Cdd:smart00282   70 GRS--VTLSVDGGNRVSGESPGGL-------TILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
187-238 7.46e-16

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 73.16  E-value: 7.46e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 387540784  187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDARIAKNC 238
Cdd:cd00055     2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
132-185 1.56e-12

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 63.53  E-value: 1.56e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 387540784  132 CPCPlPHlANFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNPlLIGITCK 185
Cdd:cd00055     2 CDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
81-130 4.81e-11

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 59.29  E-value: 4.81e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 387540784   81 PCDCNGN---SNKCLDGSGFCvHCQRNTTGEHCEKCLDGYIGDSIRGAPrfCQ 130
Cdd:cd00055     1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
522-787 2.13e-07

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.22  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  522 AVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDL--VQEAIDhaqELQQEANELSR 599
Cdd:COG3883     3 ALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  600 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 674
Cdd:COG3883    80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  675 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQAA-ERGDAQQRLGQSRLITEEANRTTMEVQQATAPMANNLT 753
Cdd:COG3883   158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAQlAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
                         250       260       270
                  ....*....|....*....|....*....|....
gi 387540784  754 NWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQ 787
Cdd:COG3883   237 AAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
 
Name Accession Description Interval E-value
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
291-547 1.77e-97

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 314.74  E-value: 1.77e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   291 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDT 370
Cdd:pfam06008    1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   371 IKHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRRRQpFFTQRELVDEEADEAHELLSQ 449
Cdd:pfam06008   81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   450 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLN 528
Cdd:pfam06008  160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
                          250
                   ....*....|....*....
gi 387540784   529 TSADSLTTPRLTLSELDDI 547
Cdd:pfam06008  240 TARDSLDAANLLLQEIDDA 258
Laminin_II pfam06009
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ...
727-854 6.00e-44

Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 368703 [Multi-domain]  Cd Length: 138  Bit Score: 156.49  E-value: 6.00e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   727 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVDSARDAVRNLTEVVPQLLDQLRTVEQ 797
Cdd:pfam06009    1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784   798 KRPAS-NVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSL 854
Cdd:pfam06009   81 LEVNSsSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1485-1617 3.52e-40

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 146.02  E-value: 3.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1485 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVVFIREKSSGRLVIDG 1564
Cdd:cd00110    21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 387540784 1565 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1617
Cdd:cd00110   101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1487-1618 1.92e-36

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 134.77  E-value: 1.92e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   1487 QFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQ-EKYNDGLWHDVVFIREKSSGRLVIDGL 1565
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 387540784   1566 RVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLNG 1618
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDL--KLPPLPVTPGFRGCIRNLKVNG 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1641-1792 2.82e-32

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 123.68  E-value: 2.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1641 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1719
Cdd:cd00110     1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784 1720 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1792
Cdd:cd00110    78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1664-1794 3.59e-31

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 119.75  E-value: 3.59e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   1664 EIAFEVRPRSSSGTLVHGHSVNG-EYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQsLCDGRWHRITVIRDSNVVQLDVDS 1742
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 387540784   1743 EvNHVVG--PLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1794
Cdd:smart00282   80 G-NRVSGesPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1492-1618 5.44e-30

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 115.98  E-value: 5.44e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1492 LRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLKIRSQEK-YNDGLWHDVVFIREKSSGRLVIDGLRVLEE 1570
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKnLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 387540784  1571 SLPPTEATWKIKGPIYLGGVAPGKAVKNVQINSiySFSGCLSNLQLNG 1618
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRA--GFVGCIRDVRVNG 125
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1669-1794 1.56e-28

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 111.74  E-value: 1.56e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1669 VRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKqSLCDGRWHRITVIRDSNVVQLDVDSEVNH-V 1747
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVsS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 387540784  1748 VGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1794
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1042-1200 1.04e-22

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 96.33  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1042 SYFFDGSGYAAVRDitkRGKFGQVTRFDIEVRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLEDtl 1119
Cdd:cd00110     1 GVSFSGSSYVRLPT---LPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1120 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRTLRAHlpldiNFRGCMK 1196
Cdd:cd00110    74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146

                  ....
gi 387540784 1197 GFQF 1200
Cdd:cd00110   147 DLKV 150
LamG smart00282
Laminin G domain;
1067-1203 2.59e-21

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 91.63  E-value: 2.59e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   1067 RFDIEVRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLedTLKKAQINDAKYHEISIIyHNDKKMIL 1144
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARL--TSDPTPLNDGQWHRVAVE-RNGRSVTL 75
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387540784   1145 VVD---RRHVKSMDNEKMKIPFTDIYIGGAPPEILQSRTLRAHlpldiNFRGCMKGFQFQKK 1203
Cdd:smart00282   76 SVDggnRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTP-----GFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1230-1369 2.07e-20

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 89.40  E-value: 2.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1230 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVVMDV----KGIKVQSvDKQYNDG 1303
Cdd:cd00110     2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387540784 1304 LSHFVIASVSPTRYELIVDKSRVGSKNPTKGKIEQTQagEKKFYFGGSPISAQ------YANFTGCISNAYF 1369
Cdd:cd00110    81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNL--DGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1072-1200 7.16e-20

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 87.09  E-value: 7.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1072 VRTPADNSLIL-LMVNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLedTLKKAQINDAKYHEISIIYhNDKKMILVVDRRH 1150
Cdd:pfam02210    1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLG--SGPESL--LSSGKNLNDGQWHSVRVER-NGNTLTLSVDGQT 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 387540784  1151 VKSMDNEKMKIPF---TDIYIGGAPPeilqsRTLRAHLPLDINFRGCMKGFQF 1200
Cdd:pfam02210   76 VVSSLPPGESLLLnlnGPLYLGGLPP-----LLLLPALPVRAGFVGCIRDVRV 123
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1256-1369 8.17e-19

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 84.01  E-value: 8.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1256 FRTLQPNGLLFYYASG-SDVFSISLDNGTVVMDVK----GIKVQSVDKQYNDGLSHFVIASVSPTRYELIVDKSRVGSKN 1330
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDlgsgPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 387540784  1331 PTKGKIEQTQagEKKFYFGG------SPISAQYANFTGCISNAYF 1369
Cdd:pfam02210   81 PPGESLLLNL--NGPLYLGGlpplllLPALPVRAGFVGCIRDVRV 123
LamG smart00282
Laminin G domain;
853-1006 5.27e-18

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 82.00  E-value: 5.27e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784    853 SLSLYMKppvrqpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKDVEIPLDSKPVSswPAYFSIVKIERV 932
Cdd:smart00282    1 SISFSFR--------TTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLN--DGQWHRVAVERN 69
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784    933 GKHgkVFLTVPSLSSTAEEKFIKKgefsgddSLLDLDpedTVFYVGGVPSNFKLPNSLNLPGFVGCLELATLNN 1006
Cdd:smart00282   70 GRS--VTLSVDGGNRVSGESPGGL-------TILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
828-1005 8.98e-18

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 82.08  E-value: 8.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  828 SMMFDGQSAVEVhsrTSMDDLKAFTSLSLYMKppvrqpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKD 907
Cdd:cd00110     1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--------TTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  908 VEIpldSKPVSSWPAYFSIVKIERVGKHgkVFLTVPSLSStaeekfikkGEFSGDDSLLDLDPEDTVfYVGGVPSNFKLP 987
Cdd:cd00110    69 LVL---SSKTPLNDGQWHSVSVERNGRS--VTLSVDGERV---------VESGSPGGSALLNLDGPL-YLGGLPEDLKSP 133
                         170
                  ....*....|....*...
gi 387540784  988 NSLNLPGFVGCLELATLN 1005
Cdd:cd00110   134 GLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1254-1372 6.76e-16

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 75.84  E-value: 6.76e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   1254 FNFRTLQPNGLLFYYAS--GSDVFSISLDNGTVVMDVKG----IKVQSVDKQYNDGLSHFVIASVSPTRYELIVDksrvg 1327
Cdd:smart00282    4 FSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLgsgpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 387540784   1328 SKNPTKGKIEQTQAG---EKKFYFGGSP------ISAQYANFTGCISNAYFTRV 1372
Cdd:smart00282   79 GGNRVSGESPGGLTIlnlDGPLYLGGLPedlklpPLPVTPGFRGCIRNLKVNGK 132
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
187-238 7.46e-16

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 73.16  E-value: 7.46e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 387540784  187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDARIAKNC 238
Cdd:cd00055     2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
187-232 4.61e-14

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 67.76  E-value: 4.61e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 387540784   187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDA 232
Cdd:pfam00053    1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
318-814 8.84e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 73.54  E-value: 8.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  318 LSERENQYALRKIQINNAE--------NTMKSLLSDVEELVEKENQasrkgqliQKESMDTIKHASQLVEQAHdmRDKIQ 389
Cdd:PRK02224  182 LSDQRGSLDQLKAQIEEKEekdlherlNGLESELAELDEEIERYEE--------QREQARETRDEADEVLEEH--EERRE 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  390 EInnkmlyygEEHELSPKEISEKLVLAQKMLEEIRRRqpFFTQRELVDEEADEAHELLSQAEsWQRLHNETrtlfpvVLE 469
Cdd:PRK02224  252 EL--------ETLEAEIEDLRETIAETEREREELAEE--VRDLRERLEELEEERDDLLAEAG-LDDADAEA------VEA 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  470 QLDDYNAKLSDLQEALDQALNHVRDAEdmNRATAARQR--DHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDI 547
Cdd:PRK02224  315 RREELEDRDEELRDRLEECRVAAQAHN--EEAESLREDadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  548 IKNASGIYA----EIDGAKNELQVKLSNLSNLSHDL---------VQEAIDHAQELQQEAN------------------- 595
Cdd:PRK02224  393 IEELRERFGdapvDLGNAEDFLEELREERDELREREaeleatlrtARERVEEAEALLEAGKcpecgqpvegsphvetiee 472
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  596 ------ELSRKLhsSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQiiyhKDESENLLNQA 669
Cdd:PRK02224  473 drerveELEAEL--EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK----RERAEELRERA 546
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  670 RELQAKAESSSDEAV-----ADTSRRVGGAL-ARKSALKTRLsDAVKQL--QAAERGDAQQRLGqsRLITEEANRTTMEV 741
Cdd:PRK02224  547 AELEAEAEEKREAAAeaeeeAEEAREEVAELnSKLAELKERI-ESLERIrtLLAAIADAEDEIE--RLREKREALAELND 623
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784  742 QQatapmANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPA-----SNVSASIQRIREL 814
Cdd:PRK02224  624 ER-----RERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaeiGAVENELEELEEL 696
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
132-185 1.56e-12

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 63.53  E-value: 1.56e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 387540784  132 CPCPlPHlANFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNPlLIGITCK 185
Cdd:cd00055     2 CDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
132-184 1.96e-12

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 63.14  E-value: 1.96e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 387540784   132 CPCPlpHLANFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNPLLIGITC 184
Cdd:pfam00053    1 CDCN--PHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
132-177 2.83e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 62.71  E-value: 2.83e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 387540784    132 CPCPLPHlaNFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNP 177
Cdd:smart00180    1 CDCDPGG--SASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
187-231 3.86e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 62.33  E-value: 3.86e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 387540784    187 CDCS--GNSDPnlifeDCDEVTGQCRnCLRNTTGFKCERCAPGYYGD 231
Cdd:smart00180    1 CDCDpgGSASG-----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
314-640 4.88e-12

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: 71.63  E-value: 4.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   314 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQA--HDMRDKIQEI 391
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqiLRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   392 NNKML-YYGEEHELSPKEISEKLVLAQKMLEEIRrrqpffTQRELVDEEADEAHELLSQAESwqrlHNETRTlfpvvlEQ 470
Cdd:TIGR02168  317 QLEELeAQLEELESKLDELAEELAELEEKLEELK------EELESLEAELEELEAELEELES----RLEELE------EQ 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   471 LDDYNAKLSDLQEALDQALNHVRDAED-MNRATAARQRDHEKQQERVRE----QMEAVNMSLNTSADSLTTprlTLSELD 545
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEArLERLEDRRERLQQEIEELLKKleeaELKELQAELEELEEELEE---LQEELE 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   546 DIIKNASGIYAEIDGAKNELQVKLSNLSNLSH--DLVQEAIDHAQELQQEANELsrKLHSSDMNGLVQKALDASNV---Y 620
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVdegY 535
                          330       340
                   ....*....|....*....|....*....
gi 387540784   621 E---------NIVNYVSEANETAEFALNT 640
Cdd:TIGR02168  536 EaaieaalggRLQAVVVENLNAAKKAIAF 564
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
81-130 4.81e-11

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 59.29  E-value: 4.81e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 387540784   81 PCDCNGN---SNKCLDGSGFCvHCQRNTTGEHCEKCLDGYIGDSIRGAPrfCQ 130
Cdd:cd00055     1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
868-1006 1.55e-10

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 60.51  E-value: 1.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   868 TETADQFILYLGSKnaKKEYMGLAIKNDNLVYIYNLGTKDVEIPLDSKPVS--SWpayfSIVKIERVGKHgkVFLTVPSL 945
Cdd:pfam02210    3 TRQPNGLLLYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQ 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 387540784   946 SSTAEEKfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPNSLNLPGFVGCLELATLNN 1006
Cdd:pfam02210   75 TVVSSLP-------PGESLLLNLN---GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
314-736 2.55e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.73  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  314 LKTKLSERENQYALRKIQinNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEINN 393
Cdd:COG1196   218 LKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  394 KMLyyGEEHELSPKEisEKLVLAQKMLEEIRRRqpfftQRELVDEEADEAHELLSQAESWQRLHNETRTLfpvvLEQLDD 473
Cdd:COG1196   296 ELA--RLEQDIARLE--ERRRELEERLEELEEE-----LAELEEELEELEEELEELEEELEEAEEELEEA----EAELAE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  474 YNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASG 553
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  554 IYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMnglvqkALDASNVYENIVNYVSEANET 633
Cdd:COG1196   443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL------LLEAEADYEGFLEGVKAALLL 516
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  634 AEFALnttdriydaVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADtsRRVGGALARKSALKTRL-SDAVKQL 712
Cdd:COG1196   517 AGLRG---------LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATFLpLDKIRAR 585
                         410       420
                  ....*....|....*....|....
gi 387540784  713 QAAERGDAQQRLGQSRLITEEANR 736
Cdd:COG1196   586 AALAAALARGAIGAAVDLVASDLR 609
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
82-129 3.09e-09

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 54.28  E-value: 3.09e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 387540784    82 CDCNGN---SNKCLDGSGFCvHCQRNTTGEHCEKCLDGYIGDSIrGAPRFC 129
Cdd:pfam00053    1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
82-121 9.65e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 52.70  E-value: 9.65e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 387540784     82 CDCNGN---SNKCLDGSGFCvHCQRNTTGEHCEKCLDGYIGDS 121
Cdd:smart00180    1 CDCDPGgsaSGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
65-257 9.77e-09

Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 56.16  E-value: 9.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   65 EKCNAGFFRTlSGECvpCDcngnsnKCLDGSGFCVHCQRNTTGehCEKCLDGYIGDSIRGAPRFCQLC-PCPlpHLANFA 143
Cdd:cd13416     1 EACPSGQYTS-SGEC--CE------QCPPGEGVARPCGDNQTV--CEPCLDGVTFSDVVSHTEPCQPCtRCP--GLMSMR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  144 ESCYRKNGAVrcickenyagpnCErCAPGYYGNPLliGITCKKCDCsgnsdpnlifedCDEVTGQCRNC--LRNTtgfKC 221
Cdd:cd13416    68 APCTATHDTV------------CE-CAYGYYLDED--SGTCEPCTV------------CPPGQGVVQSCgpNQDT---VC 117
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 387540784  222 ERCAPGYYGDARIAKN----CAVCncggGPCDSVTGECLE 257
Cdd:cd13416   118 EACPEGTYSDEDSSTDpclpCTVC----EDGEVELRECTP 153
growth_prot_Scy NF041483
polarized growth protein Scy;
408-848 9.54e-08

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 57.53  E-value: 9.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  408 EISEKLVLAQKmlEEIRRRQpfftqrelvdeeadEAHELLSQA--ESWQ---RLHNETRTLFPVVLEQLDDYNAKLSDLQ 482
Cdd:NF041483  696 EAAEALAAAQE--EAARRRR--------------EAEETLGSAraEADQereRAREQSEELLASARKRVEEAQAEAQRLV 759
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  483 EALDQ-ALNHVRDAEDmnraTAARQRD-----HEKQQERVREQMEAVNMSlntsADSltTPRLTLSELDDIIKNAsgiYA 556
Cdd:NF041483  760 EEADRrATELVSAAEQ----TAQQVRDsvaglQEQAEEEIAGLRSAAEHA----AER--TRTEAQEEADRVRSDA---YA 826
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  557 EIDGA-------KNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMNGLVQKALDASNVYenivnyvSE 629
Cdd:NF041483  827 ERERAsedanrlRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTR-------AD 899
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  630 ANETAefalnttDRI-YDAVSGIDTQIIYHKDESENLLNQARelqAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 708
Cdd:NF041483  900 AREDA-------NRIrSDAAAQADRLIGEATSEAERLTAEAR---AEAERLRDEARAEAERVRADAAAQAEQLIAEATGE 969
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  709 VKQL--QAAER-GDAQQRLGQSRlitEEANRTTMEvqqaTAPMANNLTNWSQN-----LQHFDSSAYNTAVDSARDAVRN 780
Cdd:NF041483  970 AERLraEAAETvGSAQQHAERIR---TEAERVKAE----AAAEAERLRTEAREeadrtLDEARKDANKRRSEAAEQADTL 1042
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784  781 LTEVVPQlLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEvHSRTSMDDL 848
Cdd:NF041483 1043 ITEAAAE-ADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVE-KARTDADEL 1108
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
522-787 2.13e-07

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.22  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  522 AVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDL--VQEAIDhaqELQQEANELSR 599
Cdd:COG3883     3 ALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  600 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 674
Cdd:COG3883    80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  675 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQAA-ERGDAQQRLGQSRLITEEANRTTMEVQQATAPMANNLT 753
Cdd:COG3883   158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAQlAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
                         250       260       270
                  ....*....|....*....|....*....|....
gi 387540784  754 NWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQ 787
Cdd:COG3883   237 AAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
300-820 8.36e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 54.20  E-value: 8.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   300 AHRHVNEINATIYLLKTKLSERENQYALRKiqiNNAENTMKSLLSDVEELVEKENQASRKGQLiQKESMDTIKHASQLVE 379
Cdd:TIGR00618  192 LHGKAELLTLRSQLLTLCTPCMPDTYHERK---QVLEKELKHLREALQQTQQSHAYLTQKREA-QEEQLKKQQLLKQLRA 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   380 QAHDMRDKIQEINNKMlyygEEHELSPKeiSEKLVLAQKMLEEIRR---------------RQPFFTQRELVDEEADEAH 444
Cdd:TIGR00618  268 RIEELRAQEAVLEETQ----ERINRARK--AAPLAAHIKAVTQIEQqaqrihtelqskmrsRAKLLMKRAAHVKQQSSIE 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   445 ELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQ------------EALDQALNHVRDAEDMNRATA----ARQRD 508
Cdd:TIGR00618  342 EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihtlqqqkttlTQKLQSLCKELDILQREQATIdtrtSAFRD 421
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   509 HEKQQERVREQMEAvnmslntSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLshdLVQEAIDHAQ 588
Cdd:TIGR00618  422 LQGQLAHAKKQQEL-------QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI---HLQETRKKAV 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   589 ELQ--QEANELSRKLHSSDMNgLVQKALDAsnvyenivnYVSEANetaefalntTDRiydaVSGIDTQIIYHKDESENL- 665
Cdd:TIGR00618  492 VLArlLELQEEPCPLCGSCIH-PNPARQDI---------DNPGPL---------TRR----MQRGEQTYAQLETSEEDVy 548
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   666 ------LNQARELQAKAESSSDEAVADTSRRvggalARKSALKTRLSDAVKQLQaaERGDAQQRLGQSRLITEEANRTTM 739
Cdd:TIGR00618  549 hqltseRKQRASLKEQMQEIQQSFSILTQCD-----NRSKEDIPNLQNITVRLQ--DLTEKLSEAEDMLACEQHALLRKL 621
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   740 EVQQATAPMANNLTNWSQNLQ----HFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKrpASNVSASIQRIRELI 815
Cdd:TIGR00618  622 QPEQDLQDVRLHLQQCSQELAlkltALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK--MQSEKEQLTYWKEML 699

                   ....*
gi 387540784   816 AQTRS 820
Cdd:TIGR00618  700 AQCQT 704
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
331-783 8.87e-07

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 53.70  E-value: 8.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   331 QINNAENTMKSLLSDVEELVEKEnqasrkgqliqKESMDTIKHAsqlveqahdmRDKIQEINNKMLYYGeeHELSPKEis 410
Cdd:pfam06160   94 LLDDIEEDIKQILEELDELLESE-----------EKNREEVEEL----------KDKYRELRKTLLANR--FSYGPAI-- 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   411 EKLvlaQKMLEEIrrrQPFFTQRELVDEEAD--EAHELLSQaeswqrLHNETRTL------FPVVLEQL-DDYNAKLSDL 481
Cdd:pfam06160  149 DEL---EKQLAEI---EEEFSQFEELTESGDylEAREVLEK------LEEETDALeelmedIPPLYEELkTELPDQLEEL 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   482 QEALDQ------ALNHVRDAEDMNRATAARQRD----HEKQQERVREQMEAVNMSLNTSADSLTTprltlsELD---DII 548
Cdd:pfam06160  217 KEGYREmeeegyALEHLNVDKEIQQLEEQLEENlallENLELDEAEEALEEIEERIDQLYDLLEK------EVDakkYVE 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   549 KNASGIYAEIDGAK---NELQVKLSNLsNLSHDLVQEAIDHAQELQQEANELSRKLHSsdmngLVQKALDASNVYENIVN 625
Cdd:pfam06160  291 KNLPEIEDYLEHAEeqnKELKEELERV-QQSYTLNENELERVRGLEKQLEELEKRYDE-----IVERLEEKEVAYSELQE 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   626 YVSEanetaefalnttdrIYDAVSGIDTQIIYHKDESENLLNQarELQAKAESSS-DEAVADTSRRVggalaRKSAL--- 701
Cdd:pfam06160  365 ELEE--------------ILEQLEEIEEEQEEFKESLQSLRKD--ELEAREKLDEfKLELREIKRLV-----EKSNLpgl 423
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   702 ----KTRLSDAVKQLQaaergDAQQRLGQSRLITEEANRTTMEVQQAtapmannltnwsqnLQHFDSSAYNTaVDSARda 777
Cdd:pfam06160  424 pesyLDYFFDVSDEIE-----DLADELNEVPLNMDEVNRLLDEAQDD--------------VDTLYEKTEEL-IDNAT-- 481

                   ....*.
gi 387540784   778 vrnLTE 783
Cdd:pfam06160  482 ---LAE 484
ApoLp-III_like cd13769
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ...
703-829 4.11e-06

Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.


Pssm-ID: 259842 [Multi-domain]  Cd Length: 158  Bit Score: 48.47  E-value: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  703 TRLSDAVKQLQAAERGDAQQRLGQSRL-ITEEANRTtmeVQQATAPMANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNL 781
Cdd:cd13769     1 TQLSELIQKAQEAINNLAQQVQKQLGLqNPEEVVNT---LKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 387540784  782 TEVVPQLLDQLRTVEQkrpASNVSASIQ-RIRELIAQTRSVASKIQVSM 829
Cdd:cd13769    78 SETVPELRKSLPVEEK---AQELQAKLQsGLQTLVTESQKLAKAISENS 123
mukB PRK04863
chromosome partition protein MukB;
284-814 8.46e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 51.11  E-value: 8.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  284 IEEGKSGVlsvssgAAAH-RHVNEINAtiyLLKTKLSERENQYALRKiQINNAENTMKSLLSDVEELVEKEnqasrkgql 362
Cdd:PRK04863  263 ITESTNYV------AADYmRHANERRV---HLEEALELRRELYTSRR-QLAAEQYRLVEMARELAELNEAE--------- 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  363 iqkesmdtikhaSQLVEQAHDMRDKIQEINNKMLYYG--EEHELSPKEISEKLVlAQKMLeeirrrqpfftqRELVDEEA 440
Cdd:PRK04863  324 ------------SDLEQDYQAASDHLNLVQTALRQQEkiERYQADLEELEERLE-EQNEV------------VEEADEQQ 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  441 DEAHELLSQAEswqrlhnetrtlfpvvlEQLDDYNAKLSDLQEALDQAlnhvrdaedmnrATAARQRDHEKQQ-ERVReq 519
Cdd:PRK04863  379 EENEARAEAAE-----------------EEVDELKSQLADYQQALDVQ------------QTRAIQYQQAVQAlERAK-- 427
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  520 meavnmslntsadslttprlTLSELDDIiknasgiyaEIDGAKnelqvklsnlsnlshDLVQEAIDHAQELQQEANELSR 599
Cdd:PRK04863  428 --------------------QLCGLPDL---------TADNAE---------------DWLEEFQAKEQEATEELLSLEQ 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  600 KLHSSDMnglvqkaldasnvyenivnyvseANETAEFALNTTDRIYDAVSGIDTQiiyhkDESENLLNQARELQAKAEss 679
Cdd:PRK04863  464 KLSVAQA-----------------------AHSQFEQAYQLVRKIAGEVSRSEAW-----DVARELLRRLREQRHLAE-- 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  680 sdeavadtsrRVGGALARKSALKTRLsdavKQLQAAER--GDAQQRLGQS--------RLITE-EANRTTMEVQQATA-- 746
Cdd:PRK04863  514 ----------QLQQLRMRLSELEQRL----RQQQRAERllAEFCKRLGKNlddedeleQLQEElEARLESLSESVSEAre 579
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  747 ---PMANNLTNWSQNLQHFDSSAynTAVDSARDAVRNLTEVVP--------------QLLDQLR--TVEQKRPASNVSAS 807
Cdd:PRK04863  580 rrmALRQQLEQLQARIQRLAARA--PAWLAAQDALARLREQSGeefedsqdvteymqQLLERERelTVERDELAARKQAL 657

                  ....*..
gi 387540784  808 IQRIREL 814
Cdd:PRK04863  658 DEEIERL 664
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
659-817 3.73e-04

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: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  659 KDESENLLNQARELQAK-AESSSDEAVADTSRR--------VGGAlaRKSALKTRLSDAVKQLQAAE--RGDAQQRLGQS 727
Cdd:COG4913   294 EAELEELRAELARLEAElERLEARLDALREELDeleaqirgNGGD--RLEQLEREIERLERELEERErrRARLEALLAAL 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  728 RLiTEEANRTTMEVQQATAPMAnnLTNWSQnlqhfDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSAS 807
Cdd:COG4913   372 GL-PLPASAEEFAALRAEAAAL--LEALEE-----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRK--SNIPAR 441
                         170
                  ....*....|
gi 387540784  808 IQRIRELIAQ 817
Cdd:COG4913   442 LLALRDALAE 451
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
510-601 5.73e-03

Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 38.62  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  510 EKQQERVREQMEAVNMSLNtsadSLTTPRLTLSELDDI-------------------IKNA--------SGIYAE--IDG 560
Cdd:cd23160    13 EQQAEALQQQIELLQASIN----ELNRAKETLEELKKLkegteilvpigggsfvkakIKDTdkvlvnigAGVVVEktIDE 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 387540784  561 AKNELQVKLSNLSNLSHDLVQEaidhAQELQQEANELSRKL 601
Cdd:cd23160    89 AIEILEKRIKELEKALEKLQEQ----LQQIAQRLEELEAEL 125
 
Name Accession Description Interval E-value
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
291-547 1.77e-97

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 314.74  E-value: 1.77e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   291 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDT 370
Cdd:pfam06008    1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   371 IKHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRRRQpFFTQRELVDEEADEAHELLSQ 449
Cdd:pfam06008   81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   450 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLN 528
Cdd:pfam06008  160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
                          250
                   ....*....|....*....
gi 387540784   529 TSADSLTTPRLTLSELDDI 547
Cdd:pfam06008  240 TARDSLDAANLLLQEIDDA 258
Laminin_II pfam06009
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ...
727-854 6.00e-44

Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 368703 [Multi-domain]  Cd Length: 138  Bit Score: 156.49  E-value: 6.00e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   727 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVDSARDAVRNLTEVVPQLLDQLRTVEQ 797
Cdd:pfam06009    1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784   798 KRPAS-NVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSL 854
Cdd:pfam06009   81 LEVNSsSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1485-1617 3.52e-40

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 146.02  E-value: 3.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1485 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVVFIREKSSGRLVIDG 1564
Cdd:cd00110    21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 387540784 1565 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1617
Cdd:cd00110   101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1487-1618 1.92e-36

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 134.77  E-value: 1.92e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   1487 QFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQ-EKYNDGLWHDVVFIREKSSGRLVIDGL 1565
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 387540784   1566 RVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLNG 1618
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDL--KLPPLPVTPGFRGCIRNLKVNG 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1641-1792 2.82e-32

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 123.68  E-value: 2.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1641 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1719
Cdd:cd00110     1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784 1720 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1792
Cdd:cd00110    78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1664-1794 3.59e-31

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 119.75  E-value: 3.59e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   1664 EIAFEVRPRSSSGTLVHGHSVNG-EYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQsLCDGRWHRITVIRDSNVVQLDVDS 1742
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 387540784   1743 EvNHVVG--PLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1794
Cdd:smart00282   80 G-NRVSGesPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1492-1618 5.44e-30

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 115.98  E-value: 5.44e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1492 LRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLKIRSQEK-YNDGLWHDVVFIREKSSGRLVIDGLRVLEE 1570
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKnLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 387540784  1571 SLPPTEATWKIKGPIYLGGVAPGKAVKNVQINSiySFSGCLSNLQLNG 1618
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRA--GFVGCIRDVRVNG 125
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1669-1794 1.56e-28

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 111.74  E-value: 1.56e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1669 VRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKqSLCDGRWHRITVIRDSNVVQLDVDSEVNH-V 1747
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVsS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 387540784  1748 VGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1794
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
Laminin_G_1 pfam00054
Laminin G domain;
1493-1621 1.25e-24

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 100.85  E-value: 1.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1493 RTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVVFIREKSSGRLVIDGLRVLE-ES 1571
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTgES 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 387540784  1572 LPPTEATWKIKGPIYLGGvAPGKAVKNVQINSIYSFSGCLSNLQLNGASI 1621
Cdd:pfam00054   82 PLGATTDLDVDGPLYVGG-LPSLGVKKRRLAISPSFDGCIRDVIVNGKPL 130
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1042-1200 1.04e-22

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 96.33  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1042 SYFFDGSGYAAVRDitkRGKFGQVTRFDIEVRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLEDtl 1119
Cdd:cd00110     1 GVSFSGSSYVRLPT---LPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1120 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRTLRAHlpldiNFRGCMK 1196
Cdd:cd00110    74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146

                  ....
gi 387540784 1197 GFQF 1200
Cdd:cd00110   147 DLKV 150
LamG smart00282
Laminin G domain;
1067-1203 2.59e-21

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 91.63  E-value: 2.59e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   1067 RFDIEVRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLedTLKKAQINDAKYHEISIIyHNDKKMIL 1144
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARL--TSDPTPLNDGQWHRVAVE-RNGRSVTL 75
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387540784   1145 VVD---RRHVKSMDNEKMKIPFTDIYIGGAPPEILQSRTLRAHlpldiNFRGCMKGFQFQKK 1203
Cdd:smart00282   76 SVDggnRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTP-----GFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1230-1369 2.07e-20

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 89.40  E-value: 2.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1230 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVVMDV----KGIKVQSvDKQYNDG 1303
Cdd:cd00110     2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387540784 1304 LSHFVIASVSPTRYELIVDKSRVGSKNPTKGKIEQTQagEKKFYFGGSPISAQ------YANFTGCISNAYF 1369
Cdd:cd00110    81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNL--DGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1072-1200 7.16e-20

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 87.09  E-value: 7.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1072 VRTPADNSLIL-LMVNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLedTLKKAQINDAKYHEISIIYhNDKKMILVVDRRH 1150
Cdd:pfam02210    1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLG--SGPESL--LSSGKNLNDGQWHSVRVER-NGNTLTLSVDGQT 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 387540784  1151 VKSMDNEKMKIPF---TDIYIGGAPPeilqsRTLRAHLPLDINFRGCMKGFQF 1200
Cdd:pfam02210   76 VVSSLPPGESLLLnlnGPLYLGGLPP-----LLLLPALPVRAGFVGCIRDVRV 123
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1256-1369 8.17e-19

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 84.01  E-value: 8.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1256 FRTLQPNGLLFYYASG-SDVFSISLDNGTVVMDVK----GIKVQSVDKQYNDGLSHFVIASVSPTRYELIVDKSRVGSKN 1330
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDlgsgPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 387540784  1331 PTKGKIEQTQagEKKFYFGG------SPISAQYANFTGCISNAYF 1369
Cdd:pfam02210   81 PPGESLLLNL--NGPLYLGGlpplllLPALPVRAGFVGCIRDVRV 123
LamG smart00282
Laminin G domain;
853-1006 5.27e-18

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 82.00  E-value: 5.27e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784    853 SLSLYMKppvrqpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKDVEIPLDSKPVSswPAYFSIVKIERV 932
Cdd:smart00282    1 SISFSFR--------TTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLN--DGQWHRVAVERN 69
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784    933 GKHgkVFLTVPSLSSTAEEKFIKKgefsgddSLLDLDpedTVFYVGGVPSNFKLPNSLNLPGFVGCLELATLNN 1006
Cdd:smart00282   70 GRS--VTLSVDGGNRVSGESPGGL-------TILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
828-1005 8.98e-18

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 82.08  E-value: 8.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  828 SMMFDGQSAVEVhsrTSMDDLKAFTSLSLYMKppvrqpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKD 907
Cdd:cd00110     1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--------TTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  908 VEIpldSKPVSSWPAYFSIVKIERVGKHgkVFLTVPSLSStaeekfikkGEFSGDDSLLDLDPEDTVfYVGGVPSNFKLP 987
Cdd:cd00110    69 LVL---SSKTPLNDGQWHSVSVERNGRS--VTLSVDGERV---------VESGSPGGSALLNLDGPL-YLGGLPEDLKSP 133
                         170
                  ....*....|....*...
gi 387540784  988 NSLNLPGFVGCLELATLN 1005
Cdd:cd00110   134 GLPVSPGFVGCIRDLKVN 151
Laminin_G_1 pfam00054
Laminin G domain;
1669-1796 5.35e-16

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 76.20  E-value: 5.35e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1669 VRPRSSSGTLVHGHSVN-GEYLNVHMKNGQVIVKVNNGIRdfSTSVTPKQSLCDGRWHRITVIRDSNVVQLDVDSEVNHV 1747
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTeRDFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 387540784  1748 V-GPLNPK-PIDHREPVFVGGVPESLLTPRLAP-SKPFTGCIRHFVIDGHPV 1796
Cdd:pfam00054   79 GeSPLGATtDLDVDGPLYVGGLPSLGVKKRRLAiSPSFDGCIRDVIVNGKPL 130
LamG smart00282
Laminin G domain;
1254-1372 6.76e-16

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 75.84  E-value: 6.76e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   1254 FNFRTLQPNGLLFYYAS--GSDVFSISLDNGTVVMDVKG----IKVQSVDKQYNDGLSHFVIASVSPTRYELIVDksrvg 1327
Cdd:smart00282    4 FSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLgsgpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 387540784   1328 SKNPTKGKIEQTQAG---EKKFYFGGSP------ISAQYANFTGCISNAYFTRV 1372
Cdd:smart00282   79 GGNRVSGESPGGLTIlnlDGPLYLGGLPedlklpPLPVTPGFRGCIRNLKVNGK 132
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
187-238 7.46e-16

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 73.16  E-value: 7.46e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 387540784  187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDARIAKNC 238
Cdd:cd00055     2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
187-232 4.61e-14

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 67.76  E-value: 4.61e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 387540784   187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDA 232
Cdd:pfam00053    1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
272-716 1.31e-13

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 76.30  E-value: 1.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   272 DLTDDLRLAALSIEEGKsgVLSVSSGAAAHRHVNEINATIYLL----KTKLSERENQYALRKIQINNAENTMKSLLSDVE 347
Cdd:pfam05483  187 DLNNNIEKMILAFEELR--VQAENARLEMHFKLKEDHEKIQHLeeeyKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   348 ELVEKENQASRKGQLiQKESMdtikhaSQLVEQAHDMRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRRRQ 427
Cdd:pfam05483  265 ESRDKANQLEEKTKL-QDENL------KELIEKKDHLTKELEDIKMSL----QRSMSTQKALEEDLQIATKTICQLTEEK 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   428 PffTQRELVDeEADEAH---------------ELLSQAEswQRLHNETRTLFPVVLEqlddYNAKLSDLQEALDQALNHV 492
Cdd:pfam05483  334 E--AQMEELN-KAKAAHsfvvtefeattcsleELLRTEQ--QRLEKNEDQLKIITME----LQKKSSELEEMTKFKNNKE 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   493 RDAEDMNRATAARQR--DHEKQQERVREQMEAVNMSLntsADSLTTPRLTLSELD---DIIKNASGIYA-EIDGAKNELQ 566
Cdd:pfam05483  405 VELEELKKILAEDEKllDEKKQFEKIAEELKGKEQEL---IFLLQAREKEIHDLEiqlTAIKTSEEHYLkEVEDLKTELE 481
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   567 -VKLSNLSNLSH---------DLVQEAIDHAQEL--QQE---ANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEAN 631
Cdd:pfam05483  482 kEKLKNIELTAHcdklllenkELTQEASDMTLELkkHQEdiiNCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   632 ETAEFALnttDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAEsssdeavaDTSRRVGGALARKSALKTRLSDAVKQ 711
Cdd:pfam05483  562 DEVKCKL---DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE--------NKNKNIEELHQENKALKKKGSAENKQ 630

                   ....*
gi 387540784   712 LQAAE 716
Cdd:pfam05483  631 LNAYE 635
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
318-814 8.84e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 73.54  E-value: 8.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  318 LSERENQYALRKIQINNAE--------NTMKSLLSDVEELVEKENQasrkgqliQKESMDTIKHASQLVEQAHdmRDKIQ 389
Cdd:PRK02224  182 LSDQRGSLDQLKAQIEEKEekdlherlNGLESELAELDEEIERYEE--------QREQARETRDEADEVLEEH--EERRE 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  390 EInnkmlyygEEHELSPKEISEKLVLAQKMLEEIRRRqpFFTQRELVDEEADEAHELLSQAEsWQRLHNETrtlfpvVLE 469
Cdd:PRK02224  252 EL--------ETLEAEIEDLRETIAETEREREELAEE--VRDLRERLEELEEERDDLLAEAG-LDDADAEA------VEA 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  470 QLDDYNAKLSDLQEALDQALNHVRDAEdmNRATAARQR--DHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDI 547
Cdd:PRK02224  315 RREELEDRDEELRDRLEECRVAAQAHN--EEAESLREDadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  548 IKNASGIYA----EIDGAKNELQVKLSNLSNLSHDL---------VQEAIDHAQELQQEAN------------------- 595
Cdd:PRK02224  393 IEELRERFGdapvDLGNAEDFLEELREERDELREREaeleatlrtARERVEEAEALLEAGKcpecgqpvegsphvetiee 472
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  596 ------ELSRKLhsSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQiiyhKDESENLLNQA 669
Cdd:PRK02224  473 drerveELEAEL--EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK----RERAEELRERA 546
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  670 RELQAKAESSSDEAV-----ADTSRRVGGAL-ARKSALKTRLsDAVKQL--QAAERGDAQQRLGqsRLITEEANRTTMEV 741
Cdd:PRK02224  547 AELEAEAEEKREAAAeaeeeAEEAREEVAELnSKLAELKERI-ESLERIrtLLAAIADAEDEIE--RLREKREALAELND 623
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784  742 QQatapmANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPA-----SNVSASIQRIREL 814
Cdd:PRK02224  624 ER-----RERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaeiGAVENELEELEEL 696
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
132-185 1.56e-12

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 63.53  E-value: 1.56e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 387540784  132 CPCPlPHlANFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNPlLIGITCK 185
Cdd:cd00055     2 CDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
132-184 1.96e-12

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 63.14  E-value: 1.96e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 387540784   132 CPCPlpHLANFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNPLLIGITC 184
Cdd:pfam00053    1 CDCN--PHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
132-177 2.83e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 62.71  E-value: 2.83e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 387540784    132 CPCPLPHlaNFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNP 177
Cdd:smart00180    1 CDCDPGG--SASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
187-231 3.86e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 62.33  E-value: 3.86e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 387540784    187 CDCS--GNSDPnlifeDCDEVTGQCRnCLRNTTGFKCERCAPGYYGD 231
Cdd:smart00180    1 CDCDpgGSASG-----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
314-640 4.88e-12

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: 71.63  E-value: 4.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   314 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQA--HDMRDKIQEI 391
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqiLRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   392 NNKML-YYGEEHELSPKEISEKLVLAQKMLEEIRrrqpffTQRELVDEEADEAHELLSQAESwqrlHNETRTlfpvvlEQ 470
Cdd:TIGR02168  317 QLEELeAQLEELESKLDELAEELAELEEKLEELK------EELESLEAELEELEAELEELES----RLEELE------EQ 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   471 LDDYNAKLSDLQEALDQALNHVRDAED-MNRATAARQRDHEKQQERVRE----QMEAVNMSLNTSADSLTTprlTLSELD 545
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEArLERLEDRRERLQQEIEELLKKleeaELKELQAELEELEEELEE---LQEELE 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   546 DIIKNASGIYAEIDGAKNELQVKLSNLSNLSH--DLVQEAIDHAQELQQEANELsrKLHSSDMNGLVQKALDASNV---Y 620
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVdegY 535
                          330       340
                   ....*....|....*....|....*....
gi 387540784   621 E---------NIVNYVSEANETAEFALNT 640
Cdd:TIGR02168  536 EaaieaalggRLQAVVVENLNAAKKAIAF 564
Laminin_G_1 pfam00054
Laminin G domain;
1072-1196 2.36e-11

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 63.10  E-value: 2.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1072 VRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLEdtlKKAQINDAKYHEISIIYhNDKKMILVVDRR 1149
Cdd:pfam00054    1 FRTTEPSGLLLYNgtQTERDFLALELRDGRLEVSYDLG--SGAAVVR---SGDKLNDGKWHSVELER-NGRSGTLSVDGE 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 387540784  1150 HVKSMDNEK---MKIPF-TDIYIGGAPPEIlqsrTLRAHLPLDINFRGCMK 1196
Cdd:pfam00054   75 ARPTGESPLgatTDLDVdGPLYVGGLPSLG----VKKRRLAISPSFDGCIR 121
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
81-130 4.81e-11

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 59.29  E-value: 4.81e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 387540784   81 PCDCNGN---SNKCLDGSGFCvHCQRNTTGEHCEKCLDGYIGDSIRGAPrfCQ 130
Cdd:cd00055     1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
868-1006 1.55e-10

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 60.51  E-value: 1.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   868 TETADQFILYLGSKnaKKEYMGLAIKNDNLVYIYNLGTKDVEIPLDSKPVS--SWpayfSIVKIERVGKHgkVFLTVPSL 945
Cdd:pfam02210    3 TRQPNGLLLYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQ 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 387540784   946 SSTAEEKfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPNSLNLPGFVGCLELATLNN 1006
Cdd:pfam02210   75 TVVSSLP-------PGESLLLNLN---GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
314-736 2.55e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.73  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  314 LKTKLSERENQYALRKIQinNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEINN 393
Cdd:COG1196   218 LKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  394 KMLyyGEEHELSPKEisEKLVLAQKMLEEIRRRqpfftQRELVDEEADEAHELLSQAESWQRLHNETRTLfpvvLEQLDD 473
Cdd:COG1196   296 ELA--RLEQDIARLE--ERRRELEERLEELEEE-----LAELEEELEELEEELEELEEELEEAEEELEEA----EAELAE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  474 YNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASG 553
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  554 IYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMnglvqkALDASNVYENIVNYVSEANET 633
Cdd:COG1196   443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL------LLEAEADYEGFLEGVKAALLL 516
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  634 AEFALnttdriydaVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADtsRRVGGALARKSALKTRL-SDAVKQL 712
Cdd:COG1196   517 AGLRG---------LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATFLpLDKIRAR 585
                         410       420
                  ....*....|....*....|....
gi 387540784  713 QAAERGDAQQRLGQSRLITEEANR 736
Cdd:COG1196   586 AALAAALARGAIGAAVDLVASDLR 609
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
295-826 3.09e-10

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 65.52  E-value: 3.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   295 SSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNA--------ENTMKSLLSDVE----ELVEKENQASRKGQL 362
Cdd:pfam15921  217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhQDRIEQLISEHEveitGLTEKASSARSQANS 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   363 IQKEsMDTIKHA-----SQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRRRQPFFTQRE--- 434
Cdd:pfam15921  297 IQSQ-LEIIQEQarnqnSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgnl 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   435 -------LVDEEADEAHELLSQAES---WQRLHNETRTLfPVVLEQLDDYNAKLSDLqEALDQALNHVRDAEdMNRATAA 504
Cdd:pfam15921  376 ddqlqklLADLHKREKELSLEKEQNkrlWDRDTGNSITI-DHLRRELDDRNMEVQRL-EALLKAMKSECQGQ-MERQMAA 452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   505 RQRDHEKQQE----------------RVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASgiyAEIDGAKNELQVK 568
Cdd:pfam15921  453 IQGKNESLEKvssltaqlestkemlrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATN---AEITKLRSRVDLK 529
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   569 LSNLSNLSHDLvqeaiDHAQELQQEANELSRKLHSSD--MNGLVQKaldasnvYENIVNYVSEANETAefalnttdriyd 646
Cdd:pfam15921  530 LQELQHLKNEG-----DHLRNVQTECEALKLQMAEKDkvIEILRQQ-------IENMTQLVGQHGRTA------------ 585
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   647 avsgidTQIIYHKDESENLLNQAR-ELQakaESSSDEAVADTSRRvggalarksALKTRLSD----AVKQLQAaergdAQ 721
Cdd:pfam15921  586 ------GAMQVEKAQLEKEINDRRlELQ---EFKILKDKKDAKIR---------ELEARVSDleleKVKLVNA-----GS 642
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   722 QRLGQSRLITEEANRTTMEVQQATAPMaNNLTNWSQNLQ-HF--DSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVE-Q 797
Cdd:pfam15921  643 ERLRAVKDIKQERDQLLNEVKTSRNEL-NSLSEDYEVLKrNFrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgS 721
                          570       580       590
                   ....*....|....*....|....*....|
gi 387540784   798 KRPASNVSASIQR-IRELIAQTRSVASKIQ 826
Cdd:pfam15921  722 DGHAMKVAMGMQKqITAKRGQIDALQSKIQ 751
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
304-603 6.55e-10

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: 64.31  E-value: 6.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   304 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHD 383
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   384 MRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRRRqpFFTQRELVDEEADEAHELLSQAESWQRLHNETRTL 463
Cdd:TIGR02168  773 AEEELAEAEAEI----EELEAQIEQLKEELKALREALDELRAE--LTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   464 FPVVLEQLDDYNAKLSDLQEALDQAlnhvrdAEDMNRATAARQRdHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSE 543
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEEL------ESELEALLNERAS-LEEALALLRSELEELSEELRELESKRSELRRELEE 919
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   544 LDDIIKNASgiyAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHS 603
Cdd:TIGR02168  920 LREKLAQLE---LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
320-742 1.07e-09

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 63.69  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   320 ERENQYALRKIqINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKhasQL-VEQAHD--MRDKIQEInnkml 396
Cdd:pfam10174  224 DPAKTKALQTV-IEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK---QMeVYKSHSkfMKNKIDQL----- 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   397 yygeEHELSPKEiSEKLVLaQKMLEEIRRRQPFFTQRELVDEEADEAHEllsqaeswQR---LHNETRTLfPVVLEQ--- 470
Cdd:pfam10174  295 ----KQELSKKE-SELLAL-QTKLETLTNQNSDCKQHIEVLKESLTAKE--------QRaaiLQTEVDAL-RLRLEEkes 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   471 -LDDYNAKLSDLQEALDQALNHVRDAEDM----NRATAARQ----------RDHEKQQERVREQMEAVNMSLNTSADSLT 535
Cdd:pfam10174  360 fLNKKTKQLQDLTEEKSTLAGEIRDLKDMldvkERKINVLQkkienlqeqlRDKDKQLAGLKERVKSLQTDSSNTDTALT 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   536 TPRLTLSELDDIIKNASGIYA--------EIDGAKNELQVKLSNLSNLSHDL------VQEAIDHAQELQQEANELSRKL 601
Cdd:pfam10174  440 TLEEALSEKERIIERLKEQREredrerleELESLKKENKDLKEKVSALQPELtekessLIDLKEHASSLASSGLKKDSKL 519
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   602 HSSDMNglVQKALDASNVYENIVNYVSEANETAEFALNTTDRIydavSGIDTQIIYHKDES-------ENLLNQARELQA 674
Cdd:pfam10174  520 KSLEIA--VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRI----RLLEQEVARYKEESgkaqaevERLLGILREVEN 593
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784   675 KaESSSDEAVADTSRRVggalARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQ 742
Cdd:pfam10174  594 E-KNDKDKKIAELESLT----LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ 656
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
304-744 1.88e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  304 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHD 383
Cdd:COG1196   283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  384 MRDKIQEINNKMLyyGEEHELSpKEISEKLVLAQKMLEEIRRRQpffTQRELVDEEADEAHELLSQAESWQRLHNETRTL 463
Cdd:COG1196   363 AEEALLEAEAELA--EAEEELE-ELAEELLEALRAAAELAAQLE---ELEEAEEALLERLERLEEELEELEEALAELEEE 436
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  464 FPVVLEQLDDYNAKLSDLQEALDQALNHVRDAE------DMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTP 537
Cdd:COG1196   437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLeeaallEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  538 RLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQE-----------LQQEANELSRKLHSSDM 606
Cdd:COG1196   517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratflplDKIRARAALAAALARGA 596
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  607 NGLVQKALDASNVYENIVNYV-----------SEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAK 675
Cdd:COG1196   597 IGAAVDLVASDLREADARYYVlgdtllgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 387540784  676 AESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQA 744
Cdd:COG1196   677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
82-129 3.09e-09

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 54.28  E-value: 3.09e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 387540784    82 CDCNGN---SNKCLDGSGFCvHCQRNTTGEHCEKCLDGYIGDSIrGAPRFC 129
Cdd:pfam00053    1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
311-738 4.65e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 4.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  311 IYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQE 390
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  391 INNKMLYYGEEHElspkEISEKLVLAQKMLEEIrrrqpfftQRELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQ 470
Cdd:COG1196   314 LEERLEELEEELA----ELEEELEELEEELEEL--------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  471 LDDYNAKLSDLQEALDQAlNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKN 550
Cdd:COG1196   382 EELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  551 ASGIYAEIDGAKNELQVKLSNLSNLSHDLVQ--EAIDHAQELQQEANELSRKLHSSDMNGLVQKALDAsnvyENIVNYVS 628
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV----LIGVEAAY 536
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  629 EANETAEFALNTTDRIYDAVSGIDTQIIYHKDESEN-----LLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKT 703
Cdd:COG1196   537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 387540784  704 RLSDAVkQLQAAERGDAQQRLGQSRLITEEANRTT 738
Cdd:COG1196   617 VLGDTL-LGRTLVAARLEAALRRAVTLAGRLREVT 650
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
82-121 9.65e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 52.70  E-value: 9.65e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 387540784     82 CDCNGN---SNKCLDGSGFCvHCQRNTTGEHCEKCLDGYIGDS 121
Cdd:smart00180    1 CDCDPGgsaSGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
65-257 9.77e-09

Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 56.16  E-value: 9.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   65 EKCNAGFFRTlSGECvpCDcngnsnKCLDGSGFCVHCQRNTTGehCEKCLDGYIGDSIRGAPRFCQLC-PCPlpHLANFA 143
Cdd:cd13416     1 EACPSGQYTS-SGEC--CE------QCPPGEGVARPCGDNQTV--CEPCLDGVTFSDVVSHTEPCQPCtRCP--GLMSMR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  144 ESCYRKNGAVrcickenyagpnCErCAPGYYGNPLliGITCKKCDCsgnsdpnlifedCDEVTGQCRNC--LRNTtgfKC 221
Cdd:cd13416    68 APCTATHDTV------------CE-CAYGYYLDED--SGTCEPCTV------------CPPGQGVVQSCgpNQDT---VC 117
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 387540784  222 ERCAPGYYGDARIAKN----CAVCncggGPCDSVTGECLE 257
Cdd:cd13416   118 EACPEGTYSDEDSSTDpclpCTVC----EDGEVELRECTP 153
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
305-521 1.84e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 58.00  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  305 NEINATIYLLKTKLSERENQYAlrkiQINNAENTMKSLLSDVEEL----------VEKENQ----ASRKGQLIQ--KESM 368
Cdd:COG1340    81 DELNEKLNELREELDELRKELA----ELNKAGGSIDKLRKEIERLewrqqtevlsPEEEKElvekIKELEKELEkaKKAL 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  369 DTIKHASQLVEQAHDMRDKIQEINNKMlyygeehelspKEISEKlvlAQKMLEEIrrrQPFFTQRELVDEEADEAHELLS 448
Cdd:COG1340   157 EKNEKLKELRAELKELRKEAEEIHKKI-----------KELAEE---AQELHEEM---IELYKEADELRKEADELHKEIV 219
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784  449 QA-ESWQRLHnetrtlfpvvlEQLDDYNAKLSDLQEALDQALNHVRDAEdmnrataaRQRDHEKQQERVREQME 521
Cdd:COG1340   220 EAqEKADELH-----------EEIIELQKELRELRKELKKLRKKQRALK--------REKEKEELEEKAEEIFE 274
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
312-724 1.89e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 59.40  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  312 YLLKTKLseRENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESmdtikhasQLVEQAHDMRDKIQEI 391
Cdd:COG4717    45 AMLLERL--EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--------ELEEELEELEAELEEL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  392 NNKMLYYGEEHELSP-----KEISEKLVLAQKMLEEIRRRQPFFTQRElvdEEADEAHELLSQAEswQRLHNETRTLFPV 466
Cdd:COG4717   115 REELEKLEKLLQLLPlyqelEALEAELAELPERLEELEERLEELRELE---EELEELEAELAELQ--EELEELLEQLSLA 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  467 VLEQLDDYNAKLSDLQEALDQALNHVRDAEDmNRATAARQRD-------HEKQQERVREQM-----EAVNMSLNTSADSL 534
Cdd:COG4717   190 TEEELQDLAEELEELQQRLAELEEELEEAQE-ELEELEEELEqleneleAAALEERLKEARlllliAAALLALLGLGGSL 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  535 TTPRLTL----------------------SELDDIIKNASGIYAEIDGAKNELQVKLSNL---SNLSHDLVQEAIDHAQE 589
Cdd:COG4717   269 LSLILTIagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEE 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  590 LQQ---EANELSRKLHSSDMNGLVQKALDASNV-----YENIVNYVSEANETAEfalnttdriydAVSGIDTQIIYHKDE 661
Cdd:COG4717   349 LQEllrEAEELEEELQLEELEQEIAALLAEAGVedeeeLRAALEQAEEYQELKE-----------ELEELEEQLEELLGE 417
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784  662 SENLLNQARELQAKAE-SSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRL 724
Cdd:COG4717   418 LEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
418-824 2.05e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  418 KMLEEI--------RRRQpffTQRELvdEEADE--------AHELLSQ----------AESWQRLHNETRtlfpvVLE-- 469
Cdd:COG1196   159 AIIEEAagiskykeRKEE---AERKL--EATEEnlerlediLGELERQleplerqaekAERYRELKEELK-----ELEae 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  470 ----QLDDYNAKLSDLQEALDQALNHVRDAEdmnrataARQRDHEKQQERVREQMEAVNMSLNTSADSLttpRLTLSELd 545
Cdd:COG1196   229 llllKLRELEAELEELEAELEELEAELEELE-------AELAELEAELEELRLELEELELELEEAQAEE---YELLAEL- 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  546 diiknasgiyAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMngLVQKALDASNVYENIVN 625
Cdd:COG1196   298 ----------ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE--AEEELEEAEAELAEAEE 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  626 YVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRL 705
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  706 SDAVKQLQAAERGDAQQR----LGQSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSAyntavdsARDAVRNL 781
Cdd:COG1196   446 EAAEEEAELEEEEEALLEllaeLLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV-------KAALLLAG 518
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 387540784  782 TEVVPQLLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASK 824
Cdd:COG1196   519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
419-878 4.74e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.86  E-value: 4.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  419 MLEEI--RRRQPFFT----QRELVDEEADEAHELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQALNHV 492
Cdd:COG4717    46 MLLERleKEADELFKpqgrKPELNLKELKELEEELKEAEEKEEEYAELQ-------EELEELEEELEELEAELEELREEL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  493 RDAEDMNRAtaarqRDHEKQQERVREQMEavnmSLNTSADSLTTPRLTLSELDDIIKNASgiyAEIDGAKNELQVKLSNL 572
Cdd:COG4717   119 EKLEKLLQL-----LPLYQELEALEAELA----ELPERLEELEERLEELRELEEELEELE---AELAELQEELEELLEQL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  573 SNLSHDLVQEAIDHAQELQQEANELSRKL---------HSSDMNGLVQKALDAsNVYENIVNY-------------VSEA 630
Cdd:COG4717   187 SLATEEELQDLAEELEELQQRLAELEEELeeaqeeleeLEEELEQLENELEAA-ALEERLKEArlllliaaallalLGLG 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  631 NETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSS--DEAVADTSRRVGGALARKSALKTRLSDA 708
Cdd:COG4717   266 GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELLDR 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  709 VKQLQAA--ERGDAQQRLGQSRLITE------------------------EANRTTMEVQQATAPMANNLTNWSQNLQHF 762
Cdd:COG4717   346 IEELQELlrEAEELEEELQLEELEQEiaallaeagvedeeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEAL 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  763 DSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQK----RPASNVSASIQRIRELIAQTRSVASKIQVSMMfdGQSAVE 838
Cdd:COG4717   426 DEEELEEELEELEEELEELEEELEELREELAELEAEleqlEEDGELAELLQELEELKAELRELAEEWAALKL--ALELLE 503
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 387540784  839 VHSRTSMDDlkaftslslymkppvRQPELTETADQFILYL 878
Cdd:COG4717   504 EAREEYREE---------------RLPPVLERASEYFSRL 528
growth_prot_Scy NF041483
polarized growth protein Scy;
408-848 9.54e-08

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 57.53  E-value: 9.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  408 EISEKLVLAQKmlEEIRRRQpfftqrelvdeeadEAHELLSQA--ESWQ---RLHNETRTLFPVVLEQLDDYNAKLSDLQ 482
Cdd:NF041483  696 EAAEALAAAQE--EAARRRR--------------EAEETLGSAraEADQereRAREQSEELLASARKRVEEAQAEAQRLV 759
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  483 EALDQ-ALNHVRDAEDmnraTAARQRD-----HEKQQERVREQMEAVNMSlntsADSltTPRLTLSELDDIIKNAsgiYA 556
Cdd:NF041483  760 EEADRrATELVSAAEQ----TAQQVRDsvaglQEQAEEEIAGLRSAAEHA----AER--TRTEAQEEADRVRSDA---YA 826
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  557 EIDGA-------KNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMNGLVQKALDASNVYenivnyvSE 629
Cdd:NF041483  827 ERERAsedanrlRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTR-------AD 899
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  630 ANETAefalnttDRI-YDAVSGIDTQIIYHKDESENLLNQARelqAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 708
Cdd:NF041483  900 AREDA-------NRIrSDAAAQADRLIGEATSEAERLTAEAR---AEAERLRDEARAEAERVRADAAAQAEQLIAEATGE 969
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  709 VKQL--QAAER-GDAQQRLGQSRlitEEANRTTMEvqqaTAPMANNLTNWSQN-----LQHFDSSAYNTAVDSARDAVRN 780
Cdd:NF041483  970 AERLraEAAETvGSAQQHAERIR---TEAERVKAE----AAAEAERLRTEAREeadrtLDEARKDANKRRSEAAEQADTL 1042
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784  781 LTEVVPQlLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEvHSRTSMDDL 848
Cdd:NF041483 1043 ITEAAAE-ADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVE-KARTDADEL 1108
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
314-593 2.09e-07

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: 56.23  E-value: 2.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   314 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKEsmdtikhASQLVEQAHDMRDKIQEINN 393
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE-------EEKLKERLEELEEDLSSLEQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   394 KMLYYGEEHELSPKEIS---EKLVLAQKMLEEIRRR---QPFFTQRELVDEEADEAHELLSQAESWQRLHNEtRTLFPVV 467
Cdd:TIGR02169  752 EIENVKSELKELEARIEeleEDLHKLEEALNDLEARlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   468 LE----------------------QLDDYNAKLSDLQEALDQALNHVRDAEDmnrataaRQRDHEKQQERVREQMEAVNM 525
Cdd:TIGR02169  831 LEkeiqelqeqridlkeqiksiekEIENLNGKKEELEEELEELEAALRDLES-------RLGDLKKERDELEAQLRELER 903
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784   526 SLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLsnLSHDLVQEAIdhaQELQQE 593
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE--LSLEDVQAEL---QRVEEE 966
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
522-787 2.13e-07

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.22  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  522 AVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDL--VQEAIDhaqELQQEANELSR 599
Cdd:COG3883     3 ALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  600 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 674
Cdd:COG3883    80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  675 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQAA-ERGDAQQRLGQSRLITEEANRTTMEVQQATAPMANNLT 753
Cdd:COG3883   158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAQlAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
                         250       260       270
                  ....*....|....*....|....*....|....
gi 387540784  754 NWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQ 787
Cdd:COG3883   237 AAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
431-900 2.55e-07

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 55.68  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  431 TQRELVDEEADEAHELLSQAESWQR------------LHNETRTLFPVVLEQLDDYNA-------KLSDLQEALDQ---A 488
Cdd:COG5278    43 EHTYEVLRALEELLSALLDAETGQRgylltgdesflePYEEARAEIDELLAELRSLTAdnpeqqaRLDELEALIDQwlaE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  489 LNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVK 568
Cdd:COG5278   123 LEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  569 LSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMNGLVQKALDAsnvyenIVNYVSEANETAEFALNTTDRIYDAV 648
Cdd:COG5278   203 LLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALL------LALLAALALAALLAAALLALAALLLA 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  649 SGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSR 728
Cdd:COG5278   277 LAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAA 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  729 LITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSASI 808
Cdd:COG5278   357 AAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAE 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  809 QRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSLSLYMKPPVRQPELTETADQFILYLGSKNAKKEYM 888
Cdd:COG5278   437 EEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAA 516
                         490
                  ....*....|..
gi 387540784  889 GLAIKNDNLVYI 900
Cdd:COG5278   517 LAAALAAALASA 528
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
300-820 8.36e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 54.20  E-value: 8.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   300 AHRHVNEINATIYLLKTKLSERENQYALRKiqiNNAENTMKSLLSDVEELVEKENQASRKGQLiQKESMDTIKHASQLVE 379
Cdd:TIGR00618  192 LHGKAELLTLRSQLLTLCTPCMPDTYHERK---QVLEKELKHLREALQQTQQSHAYLTQKREA-QEEQLKKQQLLKQLRA 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   380 QAHDMRDKIQEINNKMlyygEEHELSPKeiSEKLVLAQKMLEEIRR---------------RQPFFTQRELVDEEADEAH 444
Cdd:TIGR00618  268 RIEELRAQEAVLEETQ----ERINRARK--AAPLAAHIKAVTQIEQqaqrihtelqskmrsRAKLLMKRAAHVKQQSSIE 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   445 ELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQ------------EALDQALNHVRDAEDMNRATA----ARQRD 508
Cdd:TIGR00618  342 EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihtlqqqkttlTQKLQSLCKELDILQREQATIdtrtSAFRD 421
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   509 HEKQQERVREQMEAvnmslntSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLshdLVQEAIDHAQ 588
Cdd:TIGR00618  422 LQGQLAHAKKQQEL-------QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI---HLQETRKKAV 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   589 ELQ--QEANELSRKLHSSDMNgLVQKALDAsnvyenivnYVSEANetaefalntTDRiydaVSGIDTQIIYHKDESENL- 665
Cdd:TIGR00618  492 VLArlLELQEEPCPLCGSCIH-PNPARQDI---------DNPGPL---------TRR----MQRGEQTYAQLETSEEDVy 548
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   666 ------LNQARELQAKAESSSDEAVADTSRRvggalARKSALKTRLSDAVKQLQaaERGDAQQRLGQSRLITEEANRTTM 739
Cdd:TIGR00618  549 hqltseRKQRASLKEQMQEIQQSFSILTQCD-----NRSKEDIPNLQNITVRLQ--DLTEKLSEAEDMLACEQHALLRKL 621
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   740 EVQQATAPMANNLTNWSQNLQ----HFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKrpASNVSASIQRIRELI 815
Cdd:TIGR00618  622 QPEQDLQDVRLHLQQCSQELAlkltALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK--MQSEKEQLTYWKEML 699

                   ....*
gi 387540784   816 AQTRS 820
Cdd:TIGR00618  700 AQCQT 704
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
331-783 8.87e-07

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 53.70  E-value: 8.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   331 QINNAENTMKSLLSDVEELVEKEnqasrkgqliqKESMDTIKHAsqlveqahdmRDKIQEINNKMLYYGeeHELSPKEis 410
Cdd:pfam06160   94 LLDDIEEDIKQILEELDELLESE-----------EKNREEVEEL----------KDKYRELRKTLLANR--FSYGPAI-- 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   411 EKLvlaQKMLEEIrrrQPFFTQRELVDEEAD--EAHELLSQaeswqrLHNETRTL------FPVVLEQL-DDYNAKLSDL 481
Cdd:pfam06160  149 DEL---EKQLAEI---EEEFSQFEELTESGDylEAREVLEK------LEEETDALeelmedIPPLYEELkTELPDQLEEL 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   482 QEALDQ------ALNHVRDAEDMNRATAARQRD----HEKQQERVREQMEAVNMSLNTSADSLTTprltlsELD---DII 548
Cdd:pfam06160  217 KEGYREmeeegyALEHLNVDKEIQQLEEQLEENlallENLELDEAEEALEEIEERIDQLYDLLEK------EVDakkYVE 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   549 KNASGIYAEIDGAK---NELQVKLSNLsNLSHDLVQEAIDHAQELQQEANELSRKLHSsdmngLVQKALDASNVYENIVN 625
Cdd:pfam06160  291 KNLPEIEDYLEHAEeqnKELKEELERV-QQSYTLNENELERVRGLEKQLEELEKRYDE-----IVERLEEKEVAYSELQE 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   626 YVSEanetaefalnttdrIYDAVSGIDTQIIYHKDESENLLNQarELQAKAESSS-DEAVADTSRRVggalaRKSAL--- 701
Cdd:pfam06160  365 ELEE--------------ILEQLEEIEEEQEEFKESLQSLRKD--ELEAREKLDEfKLELREIKRLV-----EKSNLpgl 423
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   702 ----KTRLSDAVKQLQaaergDAQQRLGQSRLITEEANRTTMEVQQAtapmannltnwsqnLQHFDSSAYNTaVDSARda 777
Cdd:pfam06160  424 pesyLDYFFDVSDEIE-----DLADELNEVPLNMDEVNRLLDEAQDD--------------VDTLYEKTEEL-IDNAT-- 481

                   ....*.
gi 387540784   778 vrnLTE 783
Cdd:pfam06160  482 ---LAE 484
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
408-760 1.41e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  408 EISEKLVLAQKMLEEIRRR--QPFFTQRELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEAL 485
Cdd:COG4372     3 RLGEKVGKARLSLFGLRPKtgILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  486 DQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNmslntsadslttprltlSELDDIIKNASGIYAEIDGAKNEL 565
Cdd:COG4372    83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ-----------------KERQDLEQQRKQLEAQIAELQSEI 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  566 QVKLSNLSNLSHDLvQEAIDHAQELQQEANELSRKLHSSDMNGLVQKAldasnvyENIVNYVSEANETAEFALNTTDRIY 645
Cdd:COG4372   146 AEREEELKELEEQL-ESLQEELAALEQELQALSEAEAEQALDELLKEA-------NRNAEKEEELAEAEKLIESLPRELA 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  646 DAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLG 725
Cdd:COG4372   218 EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 387540784  726 QSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQ 760
Cdd:COG4372   298 LALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
Laminin_G_1 pfam00054
Laminin G domain;
1256-1369 2.28e-06

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 48.47  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1256 FRTLQPNGLLFYYAS--GSDVFSISLDNG--TVVMDV-KGIKVQSVDKQYNDGLSHFVIASVSPTRYELIVDK-SRVGSK 1329
Cdd:pfam00054    1 FRTTEPSGLLLYNGTqtERDFLALELRDGrlEVSYDLgSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 387540784  1330 NPTKGKieQTQAGEKKFYFGGSPISAQYA-------NFTGCISNAYF 1369
Cdd:pfam00054   81 SPLGAT--TDLDVDGPLYVGGLPSLGVKKrrlaispSFDGCIRDVIV 125
PTZ00121 PTZ00121
MAEBL; Provisional
313-601 2.84e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  313 LLKTKLSERENQYALRKiqinNAENTMKsllsdVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEIN 392
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKK----EAEEAKK-----AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  393 nkmlyygeehelspKEISEKLVLAQKMLEEIRRRQPFFTQRELV-DEEADEAHEllSQAESWQRLHNETRTLFPVVLEQL 471
Cdd:PTZ00121 1751 --------------KDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEELDEEDE--KRRMEVDKKIKDIFDNFANIIEGG 1814
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  472 DDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKna 551
Cdd:PTZ00121 1815 KEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEK-- 1892
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 387540784  552 sgiyaeIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKL 601
Cdd:PTZ00121 1893 ------IDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEI 1936
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
306-667 2.97e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.33  E-value: 2.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   306 EINATIYLLKTKLSERENQYALRKIQINNAENTMKSL---LSDVEELVEKENQASRKGQ--LIQKESM-DTIK-HASQLV 378
Cdd:TIGR04523  430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLetqLKVLSRSINKIKQNLEQKQkeLKSKEKElKKLNeEKKELE 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   379 EQAHDMRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRrrqpFFTQRELVDEEADEAHELLSQaeswqrLHN 458
Cdd:TIGR04523  510 EKVKDLTKKISSLKEKI----EKLESEKKEKESKISDLEDELNKDD----FELKKENLEKEIDEKNKEIEE------LKQ 575
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   459 ETRTLfpvvleqlddyNAKLSDLQEALDQalnhvrdaedmnrataarqrdHEKQQERVREQMEAVNMSLNTSADSLTTPR 538
Cdd:TIGR04523  576 TQKSL-----------KKKQEEKQELIDQ---------------------KEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   539 LTLSELDDIIKNasgiyaeIDGAKNELQVKLSNLsnlsHDLVQEAIDHAQELQQEANELSRKLhsSDMNGLVQKALDASN 618
Cdd:TIGR04523  624 KENEKLSSIIKN-------IKSKKNKLKQEVKQI----KETIKEIRNKWPEIIKKIKESKTKI--DDIIELMKDWLKELS 690
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 387540784   619 VYENivNYVSEANETAEfaLNTTDRIYDAVSGIDTQIIYHKDESENLLN 667
Cdd:TIGR04523  691 LHYK--KYITRMIRIKD--LPKLEEKYKEIEKELKKLDEFSKELENIIK 735
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
314-604 3.25e-06

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: 52.38  E-value: 3.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   314 LKTKLSEREnQYALrkiqinnaentMKSLLSDVEELVEKENQASRkgqlIQKESMDTIKHASQLVEQAHDMRDKIQEINN 393
Cdd:TIGR02169  216 LLKEKREYE-GYEL-----------LKEKEALERQKEAIERQLAS----LEEELEKLTEEISELEKRLEEIEQLLEELNK 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   394 KMLYYGEEHELspkEISEKLVLAQKMLEEIRRRQPfFTQRELVDEEADEA------HELLSQAESWQRLHNETRTlfpvv 467
Cdd:TIGR02169  280 KIKDLGEEEQL---RVKEKIGELEAEIASLERSIA-EKERELEDAEERLAkleaeiDKLLAEIEELEREIEEERK----- 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   468 leQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDI 547
Cdd:TIGR02169  351 --RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 387540784   548 IKNASGIYAEIDGAKNELQVKLS----NLSNLSHDLVQEAIDHAQeLQQEANELSRKLHSS 604
Cdd:TIGR02169  429 IAGIEAKINELEEEKEDKALEIKkqewKLEQLAADLSKYEQELYD-LKEEYDRVEKELSKL 488
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
302-573 3.36e-06

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: 52.38  E-value: 3.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   302 RHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDvEELVEKENQASRKGQLIQKEsmDTIKHASQLVEQA 381
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE-EQLRVKEKIGELEAEIASLE--RSIAEKERELEDA 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   382 HDMRDKIQEINNKMLyygEEHELSPKEISEKLVLAQKMLEEIrrrqpfftqrelvDEEADEAHELLSQAESWQRLHNETR 461
Cdd:TIGR02169  321 EERLAKLEAEIDKLL---AEIEELEREIEEERKRRDKLTEEY-------------AELKEELEDLRAELEEVDKEFAETR 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   462 TLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEdmnrataARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTL 541
Cdd:TIGR02169  385 DELKDYREKLEKLKREINELKRELDRLQEELQRLS-------EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
                          250       260       270
                   ....*....|....*....|....*....|..
gi 387540784   542 SELDDIIKNASGIYAEIDGAKNELQVKLSNLS 573
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
314-671 4.10e-06

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 52.36  E-value: 4.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   314 LKTKLS--ERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEI 391
Cdd:TIGR01612 2049 IKEKIDnyEKEKEKFGIDFDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKII 2128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   392 NNKMLyygEEHELSPKeiseklvlaqkmLEEIRRRQPFFTQRELVDEeadeaheLLSQAESWQRLHNETRTLFPVVLEQL 471
Cdd:TIGR01612 2129 EDKII---EKNDLIDK------------LIEMRKECLLFSYATLVET-------LKSKVINHSEFITSAAKFSKDFFEFI 2186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   472 DDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNM--------SLNTSADSLTTPRLTL-- 541
Cdd:TIGR01612 2187 EDISDSLNDDIDALQIKYNLNQTKKHMISILADATKDHNNLIEKEKEATKIINNltelftidFNNADADILHNNKIQIiy 2266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   542 --SELDDIIKNASGIYAEIDGAKnelqvklsnLSNLSHdLVQEAIDHAQE----LQQEANELSRKLHssDMNGLVQKALD 615
Cdd:TIGR01612 2267 fnSELHKSIESIKKLYKKINAFK---------LLNISH-INEKYFDISKEfdniIQLQKHKLTENLN--DLKEIDQYISD 2334
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 387540784   616 ASNVYENIVNyvseanETAEFALNTTDRIYDAVSGIDTQIiyhkDESENLLNQARE 671
Cdd:TIGR01612 2335 KKNIFLHALN------ENTNFNFNALKEIYDDIINRENKA----DEIENINNKENE 2380
ApoLp-III_like cd13769
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ...
703-829 4.11e-06

Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.


Pssm-ID: 259842 [Multi-domain]  Cd Length: 158  Bit Score: 48.47  E-value: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  703 TRLSDAVKQLQAAERGDAQQRLGQSRL-ITEEANRTtmeVQQATAPMANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNL 781
Cdd:cd13769     1 TQLSELIQKAQEAINNLAQQVQKQLGLqNPEEVVNT---LKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 387540784  782 TEVVPQLLDQLRTVEQkrpASNVSASIQ-RIRELIAQTRSVASKIQVSM 829
Cdd:cd13769    78 SETVPELRKSLPVEEK---AQELQAKLQsGLQTLVTESQKLAKAISENS 123
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
332-524 4.53e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 49.75  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  332 INNAENTMKSL-----LSDVEELVEKeNQASRKGQLIQKESMDTI-KHASQLVEQAHDMRDKIQE----INNKMlyygee 401
Cdd:cd00176    16 LSEKEELLSSTdygddLESVEALLKK-HEALEAELAAHEERVEALnELGEQLIEEGHPDAEEIQErleeLNQRW------ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  402 helspKEISEKLVLAQKMLEEIRRRQPFFTQrelVDEEADEAHELLSQAESWQRLHNETRtlfpvVLEQLDdynaKLSDL 481
Cdd:cd00176    89 -----EELRELAEERRQRLEEALDLQQFFRD---ADDLEQWLEEKEAALASEDLGKDLES-----VEELLK----KHKEL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 387540784  482 QEALDQALNHVRDAEDMNRATAARQrdHEKQQERVREQMEAVN 524
Cdd:cd00176   152 EEELEAHEPRLKSLNELAEELLEEG--HPDADEEIEEKLEELN 192
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
314-670 7.85e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 50.60  E-value: 7.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  314 LKTKLSERENQY--ALRKI--QINNAEntmkSLLSDVEELVEKEN--QASR-----KGQLIQ-KESMDTIKhaSQLVEQA 381
Cdd:PRK04778  152 LRKSLLANRFSFgpALDELekQLENLE----EEFSQFVELTESGDyvEAREildqlEEELAAlEQIMEEIP--ELLKELQ 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  382 HDMRDKIQEINN---KML---YYGEEHELSP--KEISEKLVLAQKMLEEIrrrqpfftqrelvdeEADEAHELLSQAESw 453
Cdd:PRK04778  226 TELPDQLQELKAgyrELVeegYHLDHLDIEKeiQDLKEQIDENLALLEEL---------------DLDEAEEKNEEIQE- 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  454 qRL-------------HNETRTLFPVVLEQLDDYNAKLSDLQEALDQ-----ALNHvRDAEdmnrataaRQRDHEKQQER 515
Cdd:PRK04778  290 -RIdqlydilerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRvkqsyTLNE-SELE--------SVRQLEKQLES 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  516 VREQMEAVnmslntsADSLTTPRLTLSELDDIIKNASGIYAEIdgakNELQVKLSN-LSNLSHDlVQEAIDHAQELQQEA 594
Cdd:PRK04778  360 LEKQYDEI-------TERIAEQEIAYSELQEELEEILKQLEEI----EKEQEKLSEmLQGLRKD-ELEAREKLERYRNKL 427
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  595 NELSRKLHSSDMNGLVQKALDAsnvYENIVNYVSEANEtaefALNTT----DRIYDAVSGIDTQIIYHKDESENLLNQAR 670
Cdd:PRK04778  428 HEIKRYLEKSNLPGLPEDYLEM---FFEVSDEIEALAE----ELEEKpinmEAVNRLLEEATEDVETLEEETEELVENAT 500
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
332-822 7.93e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 50.99  E-value: 7.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   332 INNAENTMKSLLSDVE----ELVEKENQASRKgQLIQKESMDTIKhaSQLVEQAHDMRDKIQEINNkmlyygeehELSPK 407
Cdd:pfam12128  246 LQQEFNTLESAELRLShlhfGYKSDETLIASR-QEERQETSAELN--QLLRTLDDQWKEKRDELNG---------ELSAA 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   408 EisEKLVLAQKMLEEIRRRQpfftqRELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQ 487
Cdd:pfam12128  314 D--AAVAKDRSELEALEDQH-----GAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   488 ALNhvRDAEDMN------RATAARQR-----DHEKQQERVREQMEAVNMSLNTSADSLttpRLTLSELDDIIKNASgiya 556
Cdd:pfam12128  387 QNN--RDIAGIKdklakiREARDRQLavaedDLQALESELREQLEAGKLEFNEEEYRL---KSRLGELKLRLNQAT---- 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   557 eidgAKNELQVKLSNLsnlshdlvQEAIDHAQELQQEANELSRKLHSSD--MNGLVQKALDASNVYENIVNYVSEANETA 634
Cdd:pfam12128  458 ----ATPELLLQLENF--------DERIERAREEQEAANAEVERLQSELrqARKRRDQASEALRQASRRLEERQSALDEL 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   635 EFALnttdriyDAVSG-----IDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGA------------LAR 697
Cdd:pfam12128  526 ELQL-------FPQAGtllhfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVkldlkridvpewAAS 598
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   698 KSALKTRLSDAVKQLQAAERGDAQQ--RLGQSRLITEEANRttmEVQQATAPMANN------LTNWSQNLQHFDSSAYNT 769
Cdd:pfam12128  599 EEELRERLDKAEEALQSAREKQAAAeeQLVQANGELEKASR---EETFARTALKNArldlrrLFDEKQSEKDKKNKALAE 675
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 387540784   770 AVDSARDAVRNLTEVVPQLLDQLRTV--EQKRPASNVSASIQRIRELIAQTRSVA 822
Cdd:pfam12128  676 RKDSANERLNSLEAQLKQLDKKHQAWleEQKEQKREARTEKQAYWQVVEGALDAQ 730
mukB PRK04863
chromosome partition protein MukB;
284-814 8.46e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 51.11  E-value: 8.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  284 IEEGKSGVlsvssgAAAH-RHVNEINAtiyLLKTKLSERENQYALRKiQINNAENTMKSLLSDVEELVEKEnqasrkgql 362
Cdd:PRK04863  263 ITESTNYV------AADYmRHANERRV---HLEEALELRRELYTSRR-QLAAEQYRLVEMARELAELNEAE--------- 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  363 iqkesmdtikhaSQLVEQAHDMRDKIQEINNKMLYYG--EEHELSPKEISEKLVlAQKMLeeirrrqpfftqRELVDEEA 440
Cdd:PRK04863  324 ------------SDLEQDYQAASDHLNLVQTALRQQEkiERYQADLEELEERLE-EQNEV------------VEEADEQQ 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  441 DEAHELLSQAEswqrlhnetrtlfpvvlEQLDDYNAKLSDLQEALDQAlnhvrdaedmnrATAARQRDHEKQQ-ERVReq 519
Cdd:PRK04863  379 EENEARAEAAE-----------------EEVDELKSQLADYQQALDVQ------------QTRAIQYQQAVQAlERAK-- 427
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  520 meavnmslntsadslttprlTLSELDDIiknasgiyaEIDGAKnelqvklsnlsnlshDLVQEAIDHAQELQQEANELSR 599
Cdd:PRK04863  428 --------------------QLCGLPDL---------TADNAE---------------DWLEEFQAKEQEATEELLSLEQ 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  600 KLHSSDMnglvqkaldasnvyenivnyvseANETAEFALNTTDRIYDAVSGIDTQiiyhkDESENLLNQARELQAKAEss 679
Cdd:PRK04863  464 KLSVAQA-----------------------AHSQFEQAYQLVRKIAGEVSRSEAW-----DVARELLRRLREQRHLAE-- 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  680 sdeavadtsrRVGGALARKSALKTRLsdavKQLQAAER--GDAQQRLGQS--------RLITE-EANRTTMEVQQATA-- 746
Cdd:PRK04863  514 ----------QLQQLRMRLSELEQRL----RQQQRAERllAEFCKRLGKNlddedeleQLQEElEARLESLSESVSEAre 579
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  747 ---PMANNLTNWSQNLQHFDSSAynTAVDSARDAVRNLTEVVP--------------QLLDQLR--TVEQKRPASNVSAS 807
Cdd:PRK04863  580 rrmALRQQLEQLQARIQRLAARA--PAWLAAQDALARLREQSGeefedsqdvteymqQLLERERelTVERDELAARKQAL 657

                  ....*..
gi 387540784  808 IQRIREL 814
Cdd:PRK04863  658 DEEIERL 664
VSP pfam03302
Giardia variant-specific surface protein;
67-300 9.91e-06

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 49.97  E-value: 9.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784    67 CNAGFFRTlSGECVPCD-----CNGNS----NKCLDG-----------------------SGFCVHCQRNTTG-EHCEKC 113
Cdd:pfam03302   96 CNDGFYKS-GDACSPCHescktCSGGTasdcTECLTGkalrygndgtkgtcgegcttgtgAGACKTCGLTIDGtSYCSEC 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   114 -------LDGYIGDSIRGAPRFCQLCPCPLPHLANFAESCYRKNGAV--------RCICKENYAGPNCERCAPGYYGNPL 178
Cdd:pfam03302  175 ateteypQNGVCTSTAARATATCKASSVANGMCSSCANGYFRMNGGCyettkfpgKSVCEEANSGGTCQKEAPGYKLNNG 254
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   179 LIGITCKKCD-CSGNSDPNLIFED-------CDEVTGQCRNCLRNTTgfKCERCAPGYYGDARIAKNCAVCNCGGGpcds 250
Cdd:pfam03302  255 DLVTCSPGCKtCTSNTVCTTCMDGyvktsdsCTKCDSSCETCTGATT--TCKTCATGYYKSGTGCVSCTSSESDNG---- 328
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 387540784   251 VTG--ECLEegLEPPTGCDKCVwdltddlrLAALSIEEGKSGVLSVSSGAAA 300
Cdd:pfam03302  329 ITGvkGCLN--CAPPSNNKGSV--------LCYLIKDSGSTNKSGLSTGAIA 370
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
314-567 1.26e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 50.43  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   314 LKTKLSERENQYA--LRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTikhasqlVEQAHDMRDKIQEI 391
Cdd:TIGR00606  797 FQMELKDVERKIAqqAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ-------QEQIQHLKSKTNEL 869
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   392 NNKMLYYGEehelspkEISEKLVLAQKMLEEIRRRQpfftqrELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQL 471
Cdd:TIGR00606  870 KSEKLQIGT-------NLQRRQQFEEQLVELSTEVQ------SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN 936
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   472 DDYNAKLSDLQEALDQALNHVRDAED----------MNRAT-----AARQRDHEKQQERVREQMEAVNMSLNTS--ADSL 534
Cdd:TIGR00606  937 KKAQDKVNDIKEKVKNIHGYMKDIENkiqdgkddylKQKETelntvNAQLEECEKHQEKINEDMRLMRQDIDTQkiQERW 1016
                          250       260       270
                   ....*....|....*....|....*....|...
gi 387540784   535 TTPRLTLSELDDIIKNASGIYAEIDGAKNELQV 567
Cdd:TIGR00606 1017 LQDNLTLRKRENELKEVEEELKQHLKEMGQMQV 1049
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
467-700 1.53e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.44  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  467 VLEQLDDYNAKLSDLQEALDQALNHVRDAE----DMNRATAARQRDHEKQQERVREQMEAVNMSLNT--------SADSL 534
Cdd:COG3883    35 AQAELDALQAELEELNEEYNELQAELEALQaeidKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvllGSESF 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  535 TT--PRLTLseLDDIIKNASGIYAEIDGAKNELQVKLSNLSnlshDLVQEAIDHAQELQQEANELSRKLhsSDMNGLVQK 612
Cdd:COG3883   115 SDflDRLSA--LSKIADADADLLEELKADKAELEAKKAELE----AKLAELEALKAELEAAKAELEAQQ--AEQEALLAQ 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  613 ALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVG 692
Cdd:COG3883   187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266

                  ....*...
gi 387540784  693 GALARKSA 700
Cdd:COG3883   267 AAAGAAGA 274
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
277-658 1.72e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  277 LRLAALSIEEGKSGVLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELvEKENQA 356
Cdd:COG4372    13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL-NEQLQA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  357 SRKGQLIQKESMDTIKhasqlvEQAHDMRDKIQEINnkmlyygeehelspKEISEKLVLAQKMLEEIRRRQPFFTQRElv 436
Cdd:COG4372    92 AQAELAQAQEELESLQ------EEAEELQEELEELQ--------------KERQDLEQQRKQLEAQIAELQSEIAERE-- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  437 deeaDEAHELLSQAESWQRLhnetrtlfpvvLEQLDDYNAKLSD--LQEALDQALNHVRDAEDMNRATAARQRDHEKQQE 514
Cdd:COG4372   150 ----EELKELEEQLESLQEE-----------LAALEQELQALSEaeAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  515 RVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEA 594
Cdd:COG4372   215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784  595 NELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYH 658
Cdd:COG4372   295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
PLU-1 pfam08429
PLU-1-like protein; Sequences in this family bear similarity to the central region of PLU-1. ...
314-597 2.54e-05

PLU-1-like protein; Sequences in this family bear similarity to the central region of PLU-1. This is a nuclear protein that may have a role in DNA-binding and transcription, and is closely associated with the malignant phenotype of breast cancer. This region is found in various other Jumonji/ARID domain-containing proteins (see pfam02373, pfam01388).


Pssm-ID: 462475 [Multi-domain]  Cd Length: 336  Bit Score: 48.36  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   314 LKTKLSERENqyalRKIQINNAENTMKSLLSDVEELVEKENQ-------ASRKGQLIQKE---SMDTIKHASQLVEQAHD 383
Cdd:pfam08429   21 LRALLNEAEK----IKFPLPELLQDLRAFVQRANKWVEEAQQllsrkqqTRRKNEAEEDErerEKRTVEELRKLLEEADN 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   384 MRDKIQEInnkmlyygeeHELspKEISEKLV----LAQKMLEEirrrqpfftqrELVDEEADEAHELLSQAESwqrlhne 459
Cdd:pfam08429   97 LPFDCPEI----------EQL--KELLEEIEefqkRAREALSE-----------EPPSLSIEELEELLEEGKS------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   460 trtlFPVVLEQLDDynaklsdLQEALDQA--LNHVRDAEDMNRAT-------------AARQRDHEKQQERVREQMEAVN 524
Cdd:pfam08429  147 ----FNVDLPELEE-------LEKVLEQLkwLEEVRETSRKKSLTledvrelieegveLGIPPPYEDLMAELQELLTAGE 215
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 387540784   525 MSLNTSADSLTTPRLTLSELDDIIKNASGIyaeidgaknelQVKLSNLSNLshdlvQEAIDHAQELQQEANEL 597
Cdd:pfam08429  216 RWEEKAKELLSRERVSLAQLEALSKEAQEI-----------PVSLPNLAAL-----DEILKKAREWQRQIEAL 272
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
433-819 3.96e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 48.80  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  433 RELVDEEADEAHELLSQAESW---QRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQA---LNHVRDAEDMNRATAARQ 506
Cdd:COG3096   281 RELSERALELRRELFGARRQLaeeQYRLVEMA-------RELEELSARESDLEQDYQAAsdhLNLVQTALRQQEKIERYQ 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  507 RDHEKQQERVREQMEAVnmslNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVK----------------LS 570
Cdd:COG3096   354 EDLEELTERLEEQEEVV----EEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyqqavqalekaraLC 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  571 NLSNLS----HDLVQEAIDHAQELQQEANELSRKLHSSDM-NGLVQKALDAsnvYENIVNYV--SEANETAEFALnTTDR 643
Cdd:COG3096   430 GLPDLTpenaEDYLAAFRAKEQQATEEVLELEQKLSVADAaRRQFEKAYEL---VCKIAGEVerSQAWQTARELL-RRYR 505
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  644 IYDAVSGIDTQIIYHKDESENLLNQarelQAKAESSSDEavadTSRRVGGALARKSALKTRLSDAVKQLQ--AAERGDAQ 721
Cdd:COG3096   506 SQQALAQRLQQLRAQLAELEQRLRQ----QQNAERLLEE----FCQRIGQQLDAAEELEELLAELEAQLEelEEQAAEAV 577
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  722 QRLGQSRLiTEEANRTTMEVQQATAPM-------ANNLTNwsQNLQHFDSSAyntAVDSARDavrnltevvpQLLDQLRT 794
Cdd:COG3096   578 EQRSELRQ-QLEQLRARIKELAARAPAwlaaqdaLERLRE--QSGEALADSQ---EVTAAMQ----------QLLERERE 641
                         410       420
                  ....*....|....*....|....*
gi 387540784  795 VEQKRpasnvSASIQRIRELIAQTR 819
Cdd:COG3096   642 ATVER-----DELAARKQALESQIE 661
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
514-757 4.07e-05

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 48.89  E-value: 4.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   514 ERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKnaSGIYAEIDGAKNELQVKLSNLSNLSHDL---VQEAIDHAQEL 590
Cdd:TIGR01612  500 MRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNIK--AKLYKEIEAGLKESYELAKNWKKLIHEIkkeLEEENEDSIHL 577
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   591 QQEAN---------------------ELSRKLHS-SDMNGLVQKALDASNVYENIVNYVSEANETAEFA----LNTTDRI 644
Cdd:TIGR01612  578 EKEIKdlfdkyleiddeiiyinklklELKEKIKNiSDKNEYIKKAIDLKKIIENNNAYIDELAKISPYQvpehLKNKDKI 657
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   645 YDAVSGIDTQI--------------IYHKDESENLLNQAR--ELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 708
Cdd:TIGR01612  658 YSTIKSELSKIyeddidalynelssIVKENAIDNTEDKAKldDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDI 737
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 387540784   709 VKQLQAAERGDaqqrlgqsrlITEEANRTTMEVQQATAPMANNLTNWSQ 757
Cdd:TIGR01612  738 IVEIKKHIHGE----------INKDLNKILEDFKNKEKELSNKINDYAK 776
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
314-824 4.28e-05

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: 48.63  E-value: 4.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   314 LKTKLSERENqyalRKIQINNAENTMKSLLSDVEELVEKENQASRKGQL--------IQKESMDTIKHASQ---LVEQAH 382
Cdd:pfam01576   80 LESRLEEEEE----RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLekvtteakIKKLEEDILLLEDQnskLSKERK 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   383 DMRDKIQEINNKMlyyGEEHELSpKEISeKLVLAQKML---EEIRRRQPFFTQREL------VDEEADEAHE----LLSQ 449
Cdd:pfam01576  156 LLEERISEFTSNL---AEEEEKA-KSLS-KLKNKHEAMisdLEERLKKEEKGRQELekakrkLEGESTDLQEqiaeLQAQ 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   450 AE----SWQRLHNETRTLfpvvLEQLDDYNAKLSDLQEALDQALNHVRDA-EDMNRATAARQRdHEKQQERVREQMEAVN 524
Cdd:pfam01576  231 IAelraQLAKKEEELQAA----LARLEEETAQKNNALKKIRELEAQISELqEDLESERAARNK-AEKQRRDLGEELEALK 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   525 MSLNTSADS------LTTPRLT------------------------------LSELDDIIKNASGIYAEIDGAK------ 562
Cdd:pfam01576  306 TELEDTLDTtaaqqeLRSKREQevtelkkaleeetrsheaqlqemrqkhtqaLEELTEQLEQAKRNKANLEKAKqalese 385
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   563 -NELQVKLSNLSNLSHDLVQ---EAIDHAQELQQEANELSRklHSSDMNGLVQKaldASNVYENIVNYVSEANETAEfal 638
Cdd:pfam01576  386 nAELQAELRTLQQAKQDSEHkrkKLEGQLQELQARLSESER--QRAELAEKLSK---LQSELESVSSLLNEAEGKNI--- 457
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   639 nttdRIYDAVSGIDTQIiyhkDESENLLNQarELQAKAESSSdeavadtsrRVGGALARKSALKTRLSDAVKQLQAAER- 717
Cdd:pfam01576  458 ----KLSKDVSSLESQL----QDTQELLQE--ETRQKLNLST---------RLRQLEDERNSLQEQLEEEEEAKRNVERq 518
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   718 -GDAQQRLGQSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHfDSSAYNTaVDSARDAVRnltevvpQLLDQLrTVE 796
Cdd:pfam01576  519 lSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE-KAAAYDK-LEKTKNRLQ-------QELDDL-LVD 588
                          570       580       590
                   ....*....|....*....|....*....|.
gi 387540784   797 QKRPASNVSASIQRIR---ELIAQTRSVASK 824
Cdd:pfam01576  589 LDHQRQLVSNLEKKQKkfdQMLAEEKAISAR 619
Laminin_G_1 pfam00054
Laminin G domain;
875-1006 9.23e-05

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 43.84  E-value: 9.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   875 ILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKDVEIPldSKPVSSwPAYFSIVKIERVGKHGkvFLTV---PSLSSTAEe 951
Cdd:pfam00054   10 LLYNGTQT-ERDFLALELRDGRLEVSYDLGSGAAVVR--SGDKLN-DGKWHSVELERNGRSG--TLSVdgeARPTGESP- 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 387540784   952 kfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPNSL-NLPGFVGCLELATLNN 1006
Cdd:pfam00054   83 --------LGATTDLDVD---GPLYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNG 127
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
347-600 1.31e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 46.61  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  347 EELVEKENQASRKGQLIQKEsMDTIKHASQLVEQAHDM-RDKIQEINNKMLYYGEEHELSpKEIsEKLVLAQKMLEEIRR 425
Cdd:COG0497   154 EELLEEYREAYRAWRALKKE-LEELRADEAERARELDLlRFQLEELEAAALQPGEEEELE-EER-RRLSNAEKLREALQE 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  426 rqpfftQRELVDEEADEAHELLSQAESWqrlhnetrtlfpvvLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAAR 505
Cdd:COG0497   231 ------ALEALSGGEGGALDLLGQALRA--------------LERLAEYDPSLAELAERLESALIELEEAASELRRYLDS 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  506 QRDHEKQQERVREQMEAVNmslntsadslttpRLTL---SELDDIIKnasgiYAEidgaknELQVKLSNLSNLSHDL--V 580
Cdd:COG0497   291 LEFDPERLEEVEERLALLR-------------RLARkygVTVEELLA-----YAE------ELRAELAELENSDERLeeL 346
                         250       260
                  ....*....|....*....|.
gi 387540784  581 QEAIDHA-QELQQEANELSRK 600
Cdd:COG0497   347 EAELAEAeAELLEAAEKLSAA 367
PRK01156 PRK01156
chromosome segregation protein; Provisional
304-826 1.36e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.82  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  304 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIqKESMDTIKHASQLVEQAHD 383
Cdd:PRK01156  199 LENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-KTAESDLSMELEKNNYYKE 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  384 MRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIrrrqpfftqrelvDEEADEAHELLSQAESWQRLHNEtrtl 463
Cdd:PRK01156  278 LEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNI-------------DAEINKYHAIIKKLSVLQKDYND---- 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  464 FPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRataaRQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTL-S 542
Cdd:PRK01156  341 YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKK----KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEInV 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  543 ELDDIIKNASGIYAEIDGAKNELQVKLSNLSNL-----------------SHDLVQEAIDHAQELQQEANELSRKLHSSD 605
Cdd:PRK01156  417 KLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEVKDID 496
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  606 MNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDrIYDAVSgidtQIIYHKDESENLLNQAR-----ELQAKAESSS 680
Cdd:PRK01156  497 EKIVDLKKRKEYLESEEINKSINEYNKIESARADLED-IKIKIN----ELKDKHDKYEEIKNRYKslkleDLDSKRTSWL 571
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  681 DEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERG--DAQQRLGQS-RLITEEANRTTMEVQQATAPMAnNLTNWSQ 757
Cdd:PRK01156  572 NALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpDDKSYIDKSiREIENEANNLNNKYNEIQENKI-LIEKLRG 650
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 387540784  758 NLQHFDSSAynTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSASiqRIRELIAQTRSVASKIQ 826
Cdd:PRK01156  651 KIDNYKKQI--AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA--RLESTIEILRTRINELS 715
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
469-680 1.56e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  469 EQLDDYNAKLSDLQEALD--QALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELdd 546
Cdd:COG3206   182 EQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-- 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  547 iikNASGIYAEIDGAKNELQVKLSNLSNL---SHDLVQEAIDHAQELQQE-ANELSRKLHS--SDMNGLVQKALDASNVY 620
Cdd:COG3206   260 ---LQSPVIQQLRAQLAELEAELAELSARytpNHPDVIALRAQIAALRAQlQQEAQRILASleAELEALQAREASLQAQL 336
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  621 ENIVNYVSEANETaEFALNTTDRIYDAvsgidTQIIYhkdesENLLNQARELQAKAESSS 680
Cdd:COG3206   337 AQLEARLAELPEL-EAELRRLEREVEV-----ARELY-----ESLLQRLEEARLAEALTV 385
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
337-600 1.57e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 45.67  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  337 NTMKSLLSDVEELVEKENQASRK-GQLIQKESmdtikhasQLVEQAHDMRDKIQEINNKMlyygeehelspKEISEKlvl 415
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEiEELKEKRD--------ELNEELKELAEKRDELNAQV-----------KELREE--- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  416 AQKMleeirrrqpfftqRELVDEEADEAHELLSQAESWQrlhNETRTLFpvvlEQLDDYNAKLSDLQ------EALDQAL 489
Cdd:COG1340    59 AQEL-------------REKRDELNEKVKELKEERDELN---EKLNELR----EELDELRKELAELNkaggsiDKLRKEI 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  490 NHVRDAEDmnraTAARQRDHEKQ----QERVREQMEAVNMSLNTSadslttprltlSELDDIIKNASGIYAEIDGAKNEL 565
Cdd:COG1340   119 ERLEWRQQ----TEVLSPEEEKElvekIKELEKELEKAKKALEKN-----------EKLKELRAELKELRKEAEEIHKKI 183
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 387540784  566 QvKLSNLSNLSHDLVQEAIDHAQELQQEANELSRK 600
Cdd:COG1340   184 K-ELAEEAQELHEEMIELYKEADELRKEADELHKE 217
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
306-568 2.64e-04

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: 46.21  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   306 EINATIYLLKTKLSERENQYALRKIQINNAE-NTMKSLLSDVEELVE----KENQASRKGQLIQKESMDTIKHASQLVEQ 380
Cdd:TIGR02169  769 ELEEDLHKLEEALNDLEARLSHSRIPEIQAElSKLEEEVSRIEARLReieqKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   381 AHDMRDKIQEIN---NKMLYYGEEHELSPKEISEKLV-------LAQKMLEEIRRRQpfftqRELvDEEADEAHELLSQ- 449
Cdd:TIGR02169  849 IKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGdlkkerdELEAQLRELERKI-----EEL-EAQIEKKRKRLSEl 922
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   450 AESWQRLHNETRTLFPVVLEQLDDYNAKLS--DLQEALDQALNHVRDAEDMN-RA------TAARQRDHEKQQERVREQM 520
Cdd:TIGR02169  923 KAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEPVNmLAiqeyeeVLKRLDELKEKRAKLEEER 1002
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 387540784   521 EAVnmsLNTSADSLTTPRLTLSE-LDDIIKNASGIYAEIDGAKNELQVK 568
Cdd:TIGR02169 1003 KAI---LERIEEYEKKKREVFMEaFEAINENFNEIFAELSGGTGELILE 1048
46 PHA02562
endonuclease subunit; Provisional
469-672 3.15e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.39  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  469 EQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAarqRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDII 548
Cdd:PHA02562  195 QQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA---KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKI 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  549 KNASGI---YAE----------IDGAKNELQVKLSNLSNLSH--DLVQEAIDHAQELQQEANELSRKLHssDMNGlvqka 613
Cdd:PHA02562  272 EQFQKVikmYEKggvcptctqqISEGPDRITKIKDKLKELQHslEKLDTAIDELEEIMDEFNEQSKKLL--ELKN----- 344
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 387540784  614 lDASNVYENIVNYVSEAnetaefalnttDRIYDAVSGIDTQIIYHKDESENLLNQAREL 672
Cdd:PHA02562  345 -KISTNKQSLITLVDKA-----------KKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
361-601 3.33e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  361 QLIQKESMDTIKHASQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLvlaqKMLEEIRRRQpffTQRELVDEEA 440
Cdd:COG4717   291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL----DRIEELQELL---REAEELEEEL 363
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  441 DEAHELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATaarqrdhekQQERVREQM 520
Cdd:COG4717   364 QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL---------DEEELEEEL 434
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  521 EAVNMSLNTSADSLTTPRLTLSELDDIIKNA--SGIYAEIDGAKNELQVKLSNLS------NLSHDLVQEAIDHAQE--- 589
Cdd:COG4717   435 EELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAeewaalKLALELLEEAREEYREerl 514
                         250
                  ....*....|....
gi 387540784  590 --LQQEANELSRKL 601
Cdd:COG4717   515 ppVLERASEYFSRL 528
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
299-760 3.64e-04

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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.73  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   299 AAHRHVNEINATIYLLKTKLSERENQYA-LRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKhASQL 377
Cdd:pfam02463  227 LYLDYLKLNEERIDLLQELLRDEQEEIEsSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE-LLKL 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   378 VEQAHDMRDKIQEinnkmlyygeeHELSPKEISEKLVLAQK--------MLEEIRRRQPF-----FTQRELVDEEADEAH 444
Cdd:pfam02463  306 ERRKVDDEEKLKE-----------SEKEKKKAEKELKKEKEeieelekeLKELEIKREAEeeeeeELEKLQEKLEQLEEE 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   445 ELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEAldqalnhvRDAEDMNRATAARQRDHEKQQERVREQMEAvn 524
Cdd:pfam02463  375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA--------RQLEDLLKEEKKEELEILEEEEESIELKQG-- 444
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   525 mSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLsnlsnLSHDLVQEAIDHAQELQQEANELSRKLHSS 604
Cdd:pfam02463  445 -KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL-----LLSRQKLEERSQKESKARSGLKVLLALIKD 518
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   605 DMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRI--------YDAVSGIDTQIIYHKDESENLLNQARELQ--- 673
Cdd:pfam02463  519 GVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADeveerqklVRALTELPLGARKLRLLIPKLKLPLKSIAvle 598
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   674 -------AKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQaaERGDAQQRLGQSRLITEEANRTTMEVQQATA 746
Cdd:pfam02463  599 idpilnlAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE--SGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
                          490
                   ....*....|....
gi 387540784   747 PMANNLTNWSQNLQ 760
Cdd:pfam02463  677 EIQELQEKAESELA 690
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
659-817 3.73e-04

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: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  659 KDESENLLNQARELQAK-AESSSDEAVADTSRR--------VGGAlaRKSALKTRLSDAVKQLQAAE--RGDAQQRLGQS 727
Cdd:COG4913   294 EAELEELRAELARLEAElERLEARLDALREELDeleaqirgNGGD--RLEQLEREIERLERELEERErrRARLEALLAAL 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  728 RLiTEEANRTTMEVQQATAPMAnnLTNWSQnlqhfDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSAS 807
Cdd:COG4913   372 GL-PLPASAEEFAALRAEAAAL--LEALEE-----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRK--SNIPAR 441
                         170
                  ....*....|
gi 387540784  808 IQRIRELIAQ 817
Cdd:COG4913   442 LLALRDALAE 451
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
316-543 3.99e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  316 TKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKEsMDT----IKHASQLVEQAhdmRDKIQEI 391
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE-IDKlqaeIAEAEAEIEER---REELGER 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  392 NNKMlyYGEEHELSPKEIseklVLAQKMLEEirrrqpFFTQRELVDEEADEAHELLSQAESWQRLHNETRTLfpvVLEQL 471
Cdd:COG3883    92 ARAL--YRSGGSVSYLDV----LLGSESFSD------FLDRLSALSKIADADADLLEELKADKAELEAKKAE---LEAKL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387540784  472 DDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSE 543
Cdd:COG3883   157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
407-603 4.17e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  407 KEISEKLVLAQKMLEEIRRrqpfftQRELVDEEADEAHELLSQAES---WQRLHNETRTLfPVVLEQLDDYNAKLSDLQE 483
Cdd:COG4913   620 AELEEELAEAEERLEALEA------ELDALQERREALQRLAEYSWDeidVASAEREIAEL-EAELERLDASSDDLAALEE 692
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  484 ALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNT-SADSLTTPRLTLSELddiiknasgiYAEIDGAK 562
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEER----------FAAALGDA 762
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 387540784  563 NELQVKlsnlSNLSHDLVQEaidhAQELQQEANELSRKLHS 603
Cdd:COG4913   763 VERELR----ENLEERIDAL----RARLNRAEEELERAMRA 795
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
501-807 4.90e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  501 ATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLsnlsnlshdlv 580
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----------- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  581 qeaidhaQELQQEANELSRKLHSsdmnglvQKALDASNVYeniVNYVSEANETAEFALNTTDriydaVSGIDTQIIYHKD 660
Cdd:COG4942    86 -------AELEKEIAELRAELEA-------QKEELAELLR---ALYRLGRQPPLALLLSPED-----FLDAVRRLQYLKY 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  661 ESENLLNQARELQAKaesssdeavadtsrrvggaLARKSALKTRLSDAVKQLQAAErgdAQQRLGQSRLITEEANRTTME 740
Cdd:COG4942   144 LAPARREQAEELRAD-------------------LAELAALRAELEAERAELEALL---AELEEERAALEALKAERQKLL 201
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387540784  741 VQQATapmannltnwsqnlqhfDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSAS 807
Cdd:COG4942   202 ARLEK-----------------ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
mukB PRK04863
chromosome partition protein MukB;
336-675 5.25e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.33  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  336 ENTMKSLLSDVEELVEKENQASRKGQLIQKesmdTIKHASQLV------------EQA-HDMRDKIQEINNKMlyygEEH 402
Cdd:PRK04863  785 EKRIEQLRAEREELAERYATLSFDVQKLQR----LHQAFSRFIgshlavafeadpEAElRQLNRRRVELERAL----ADH 856
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  403 ELSPKEISEKLVLAQKMLEEIRRRQPFFT--QRELVDEEADEAHELLSQAESWQR-LHNETRTLfpvvlEQLDDYNAKLS 479
Cdd:PRK04863  857 ESQEQQQRSQLEQAKEGLSALNRLLPRLNllADETLADRVEEIREQLDEAEEAKRfVQQHGNAL-----AQLEPIVSVLQ 931
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  480 DLQEALDQAlnhvrdaedmnrataarQRDH---EKQQERVREQMEAVnmslntsaDSLTTPRLTLSelddiIKNASGIYA 556
Cdd:PRK04863  932 SDPEQFEQL-----------------KQDYqqaQQTQRDAKQQAFAL--------TEVVQRRAHFS-----YEDAAEMLA 981
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  557 EIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQeANELSRKLHSSdMNGLVQKALDASNVYENI-VNYVSEANETAE 635
Cdd:PRK04863  982 KNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ-YNQVLASLKSS-YDAKRQMLQELKQELQDLgVPADSGAEERAR 1059
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 387540784  636 falNTTDRIYDAVSG-------IDTQIIYHKDESENLLNQARELQAK 675
Cdd:PRK04863 1060 ---ARRDELHARLSAnrsrrnqLEKQLTFCEAEMDNLTKKLRKLERD 1103
PRK01156 PRK01156
chromosome segregation protein; Provisional
305-671 5.44e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.89  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  305 NEINATIYLLKTKLSerenqyalrkiqinNAENTMKSLLSDVEELveKENQASRKGQ---------LIQKESMDTIKHAS 375
Cdd:PRK01156  412 NEINVKLQDISSKVS--------------SLNQRIRALRENLDEL--SRNMEMLNGQsvcpvcgttLGEEKSNHIINHYN 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  376 qlvEQAHDMRDKIQEINNKMlyygeehelspKEISEKLVLAQKMLE-----EIRRRQPFFTQ-----RELVDEEADEAhE 445
Cdd:PRK01156  476 ---EKKSRLEEKIREIEIEV-----------KDIDEKIVDLKKRKEyleseEINKSINEYNKiesarADLEDIKIKIN-E 540
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  446 LLSQAESWQRLHNETRTLFPVVLEQ-LDDYNAKLS--------DLQEALDQALNHVRDAED-MNRATAARQRDHEKQQER 515
Cdd:PRK01156  541 LKDKHDKYEEIKNRYKSLKLEDLDSkRTSWLNALAvislidieTNRSRSNEIKKQLNDLESrLQEIEIGFPDDKSYIDKS 620
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  516 VREQMEAVNmSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDG---AKNELQVKLSNlSNLSHDLVQEAIDHAQELQQ 592
Cdd:PRK01156  621 IREIENEAN-NLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSiipDLKEITSRIND-IEDNLKKSRKALDDAKANRA 698
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 387540784  593 EANELSRKLHSsDMNGLVQKALDasnvyeniVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARE 671
Cdd:PRK01156  699 RLESTIEILRT-RINELSDRIND--------INETLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRK 768
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
304-602 6.10e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  304 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHD 383
Cdd:COG4372    82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  384 MRDKIQEINNkmlyygEEHELSPKEISEKLvlaQKMLEEIRRRQPFFTQRELVDEEADEAHELLSQAESwQRLHNETRTL 463
Cdd:COG4372   162 LQEELAALEQ------ELQALSEAEAEQAL---DELLKEANRNAEKEEELAEAEKLIESLPRELAEELL-EAKDSLEAKL 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  464 FPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNmslNTSADSLTTPRLTLSE 543
Cdd:COG4372   232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA---LELKLLALLLNLAALS 308
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 387540784  544 LDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLH 602
Cdd:COG4372   309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
298-596 6.99e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  298 AAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKEnqasrkgqliqKESMDTIKHASQL 377
Cdd:PRK02224  373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE-----------AELEATLRTARER 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  378 VEQAHDMRD--KIQEInnkmlyyGEEHELSP--KEISEKLVLAQKM---LEEIRrrqpffTQRELVDEEADEAHELLSQA 450
Cdd:PRK02224  442 VEEAEALLEagKCPEC-------GQPVEGSPhvETIEEDRERVEELeaeLEDLE------EEVEEVEERLERAEDLVEAE 508
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  451 ESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDmNRATAARQRDhekQQERVREQMEAVN---MSL 527
Cdd:PRK02224  509 DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEE-KREAAAEAEE---EAEEAREEVAELNsklAEL 584
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 387540784  528 NTSADSLTTPRLTLSELDDIIKNASGI------YAEI-DGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANE 596
Cdd:PRK02224  585 KERIESLERIRTLLAAIADAEDEIERLrekreaLAELnDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEE 660
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
417-677 1.06e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.98  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  417 QKMLEEIRRrqpfftQRELVDEEADEA----HELLSQAESW--QR--LHNETRTL---FPVVLEQLDDYNAKLSDLQEAL 485
Cdd:COG1340     7 SSSLEELEE------KIEELREEIEELkekrDELNEELKELaeKRdeLNAQVKELreeAQELREKRDELNEKVKELKEER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  486 D---QALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSAdslttprLTLSELDDIIKNASGIYAEIDGAK 562
Cdd:COG1340    81 DelnEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV-------LSPEEEKELVEKIKELEKELEKAK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  563 --NELQVKLSNLSNLS----------HDLVQEAIDHAQELQQEANELSRKLhssdmNGLVQKALDAsnvYENIVNYVSEA 630
Cdd:COG1340   154 kaLEKNEKLKELRAELkelrkeaeeiHKKIKELAEEAQELHEEMIELYKEA-----DELRKEADEL---HKEIVEAQEKA 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 387540784  631 NET-AEFalnttDRIYDAVSGIDTQIIYHKDESENLL--NQARELQAKAE 677
Cdd:COG1340   226 DELhEEI-----IELQKELRELRKELKKLRKKQRALKreKEKEELEEKAE 270
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
469-600 1.08e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  469 EQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVR--EQMEAVNMSLntsaDSLttpRLTLSELDD 546
Cdd:COG1579    38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEI----ESL---KRRISDLED 110
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 387540784  547 IIKNasgIYAEIDGAKNELQVKLSNLSNLSHDL--VQEAIDHA-QELQQEANELSRK 600
Cdd:COG1579   111 EILE---LMERIEELEEELAELEAELAELEAELeeKKAELDEElAELEAELEELEAE 164
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
525-744 1.08e-03

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 42.78  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   525 MSLNTSADSLTTPRLTLSELDDIIKNASgiyaEIDGAKNELQVKLSNLSNLSHDLVQEaidhAQELQQEANELSRK--LH 602
Cdd:pfam06008    2 LSLNSLTGALPAPYKINYNLENLTKQLQ----EYLSPENAHKIQIEILEKELSSLAQE----TEELQKKATQTLAKaqQV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   603 SSDMNGLVQKALDASNVYENIVNYVSEANETAEfALNTTDriyDAVSGidTQIIYHKDESENLLNQARELQAKAESSSDE 682
Cdd:pfam06008   74 NAESERTLGHAKELAEAIKNLIDNIKEINEKVA-TLGEND---FALPS--SDLSRMLAEAQRMLGEIRSRDFGTQLQNAE 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387540784   683 AVADTSRRVggaLAR---------------KSALKTRLSDAVKQLQaaergDAQQRLGQSRLITEEANRTTMEVQQA 744
Cdd:pfam06008  148 AELKAAQDL---LSRiqtwfqspqeenkalANALRDSLAEYEAKLS-----DLRELLREAAAKTRDANRLNLANQAN 216
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
339-601 1.90e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  339 MKSLLSDVEELVEKENQASRKGQLIQKEsmdtIKHASQLVEQaHDMRDKIQEINNKMLYYGEEhELSPK-----EISEKL 413
Cdd:PRK03918  461 LKRIEKELKEIEEKERKLRKELRELEKV----LKKESELIKL-KELAEQLKELEEKLKKYNLE-ELEKKaeeyeKLKEKL 534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  414 VLAQK----MLEEIRRRQPFFTQRELVDEEADEAHELLSQaeswqrLHNETRTLFpvvLEQLDDYNAKLSDLQEALDQAL 489
Cdd:PRK03918  535 IKLKGeiksLKKELEKLEELKKKLAELEKKLDELEEELAE------LLKELEELG---FESVEELEERLKELEPFYNEYL 605
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  490 NhVRDAEDmnrataaRQRDHEKQQERVREqmeavnmslntsadslttprltlsELDDIIKNASGIYAEIDGAKNELQVKL 569
Cdd:PRK03918  606 E-LKDAEK-------ELEREEKELKKLEE------------------------ELDKAFEELAETEKRLEELRKELEELE 653
                         250       260       270
                  ....*....|....*....|....*....|..
gi 387540784  570 SNLSNLSHdlvqeaidhaQELQQEANELSRKL 601
Cdd:PRK03918  654 KKYSEEEY----------EELREEYLELSREL 675
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
366-599 2.03e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  366 ESMDTIKHASQLVEQAHDMRDKIQ------EINNKMLYYGEEHElspKEISEKLVLAQKmLEEIRRRQPFFTQRelVDEE 439
Cdd:COG4717   341 ELLDRIEELQELLREAEELEEELQleeleqEIAALLAEAGVEDE---EELRAALEQAEE-YQELKEELEELEEQ--LEEL 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  440 ADEAHELLSQA--ESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQrdhekQQERVR 517
Cdd:COG4717   415 LGELEELLEALdeEELEEELEELE-------EELEELEEELEELREELAELEAELEQLEEDGELAELLQ-----ELEELK 482
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  518 EQMEAV---NMSLNTSADSLTTPRLTLSE--LDDIIKNASGIYAEI-DGAKNELQVklsnlsNLSHDLVqeaIDHAQELQ 591
Cdd:COG4717   483 AELRELaeeWAALKLALELLEEAREEYREerLPPVLERASEYFSRLtDGRYRLIRI------DEDLSLK---VDTEDGRT 553

                  ....*...
gi 387540784  592 QEANELSR 599
Cdd:COG4717   554 RPVEELSR 561
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
359-675 2.68e-03

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 41.99  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   359 KGQLIQKESMDTIKHASQLVEQAHDMRDKIQEINnkmlyygeehelspKEISEKLVLAQKMLEEIRRRqpfftQRELVDE 438
Cdd:pfam04108    4 SAQDLCRWANELLTDARSLLEELVVLLAKIAFLR--------------RGLSVQLANLEKVREGLEKV-----LNELKKD 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   439 EADEAHELLSQAESWQR-LHNETRTLFPVVLEQLDDYNAKLSDL--QEALDQALNHVRdaedmnrataarqrdheKQQER 515
Cdd:pfam04108   65 FKQLLKDLDAALERLEEtLDKLRNTPVEPALPPGEEKQKTLLDFidEDSVEILRDALK-----------------ELIDE 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   516 VREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYaeidgaknelqVKLSNLSNLSHDLVQ--EAIDHAQELQQE 593
Cdd:pfam04108  128 LQAAQESLDSDLKRFDDDLRDLQKELESLSSPSESISLIP-----------TLLKELESLEEEMASllESLTNHYDQCVT 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   594 ANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAvsgidtqiiyhKDESENLLNQARELQ 673
Cdd:pfam04108  197 AVKLTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSL-----------IDELLSALQLIAEIQ 265

                   ..
gi 387540784   674 AK 675
Cdd:pfam04108  266 SR 267
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
376-460 2.84e-03

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


Pssm-ID: 428304 [Multi-domain]  Cd Length: 131  Bit Score: 39.86  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   376 QLVEQAHDMRDKIQEINNKMLYYGEEHElspkEISEKLVLAQKMLEEIRRRQPffTQRELVDEEA-DEAHELLSQAES-W 453
Cdd:pfam05103   36 ALIRENAELKEKIEELEEKLAHYKNLEE----TLQNTLILAQETAEEVKANAQ--KEAELIIKEAeAKAERIVDDANNeV 109

                   ....*..
gi 387540784   454 QRLHNET 460
Cdd:pfam05103  110 KKINDEI 116
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
1490-1612 4.16e-03

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 39.67  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  1490 IRLRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLK-IRSQEKYNDGLWHDVVFIREKSSGRLVIDGLRVL 1568
Cdd:pfam13385   25 VKPDSLPGWARAIISSSGG-GGYSLGLDGDGRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAVTYDGGTLRLYVNGVLVG 103
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 387540784  1569 EESLPPTeATWKIKGPIYLGGVAPGKAVKNVQINSIYSFSGCLS 1612
Cdd:pfam13385  104 SSTLTGG-PPPGTGGPLYIGRSPGGDDYFNGLIDEVRIYDRALS 146
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
407-601 4.27e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  407 KEISEKLVLAQKMLEEIRRRQPFFTqrelVDEEADEAHELLSQAESwQRlhNETRTlfpvvleQLDDYNAKLSDLQEALD 486
Cdd:COG3206   185 PELRKELEEAEAALEEFRQKNGLVD----LSEEAKLLLQQLSELES-QL--AEARA-------ELAEAEARLAALRAQLG 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  487 QALNHVRDAEDMNRATAARQRDHEKQQERVReqmeavnMSLNTSADSlttPRLT-----LSELDDIIKN-ASGIYAEIDG 560
Cdd:COG3206   251 SGPDALPELLQSPVIQQLRAQLAELEAELAE-------LSARYTPNH---PDVIalraqIAALRAQLQQeAQRILASLEA 320
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 387540784  561 AKNELQVKLSNLSNLSHDLvQEAIDHAQELQQEANELSRKL 601
Cdd:COG3206   321 ELEALQAREASLQAQLAQL-EARLAELPELEAELRRLEREV 360
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
317-451 4.52e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  317 KLSERENQYALRKiQINNAENTMKSLLSDVEELVEKENQASRK----GQLIQK--ESMDTI-KHASQLVEQAHDMRDKIQ 389
Cdd:COG1340   141 KIKELEKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKikelAEEAQElhEEMIELyKEADELRKEADELHKEIV 219
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784  390 EINNKMlyyGEEHEL------SPKEISEKLVLAQKMLEEIRRRQpfftQRELVDEEADEAHELLSQAE 451
Cdd:COG1340   220 EAQEKA---DELHEEiielqkELRELRKELKKLRKKQRALKREK----EKEELEEKAEEIFEKLKKGE 280
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
469-727 4.73e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  469 EQLDDYNAKLSDLQEALDQalnhvrdaedmnraTAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDII 548
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAE--------------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  549 KNASgiyAEIDGAKNELQVKLSNLSNLshdlvqeaIDHAQELQQeANELSRKLHSSDMNGLVQKAldasnvyeNIVNYVS 628
Cdd:COG4942    86 AELE---KEIAELRAELEAQKEELAEL--------LRALYRLGR-QPPLALLLSPEDFLDAVRRL--------QYLKYLA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  629 EANETAEFALNTTdriYDAVSGIDTQIIYHKDESENLLNQARELQA---KAESSSDEAVADTSRRVGGALARKSALK--- 702
Cdd:COG4942   146 PARREQAEELRAD---LAELAALRAELEAERAELEALLAELEEERAaleALKAERQKLLARLEKELAELAAELAELQqea 222
                         250       260
                  ....*....|....*....|....*
gi 387540784  703 TRLSDAVKQLQAAERGDAQQRLGQS 727
Cdd:COG4942   223 EELEALIARLEAEAAAAAERTPAAG 247
Rcc_KIF21A cd22263
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ...
328-395 4.84e-03

regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


Pssm-ID: 410204 [Multi-domain]  Cd Length: 82  Bit Score: 37.98  E-value: 4.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784  328 RKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEINNKM 395
Cdd:cd22263     1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSI 68
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
314-678 5.32e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 5.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   314 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEEL------VEKENQaSRKGQLIQKES-MDTIKHASQ-LVEQAHDMR 385
Cdd:TIGR04523  312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLkkeltnSESENS-EKQRELEEKQNeIEKLKKENQsYKQEIKNLE 390
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   386 DKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRRrqpfftQRELVDEEADEAHELLSQAESWQRLHNETRTLFP 465
Cdd:TIGR04523  391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER------LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   466 VVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEavnmSLNTSADSLTTprlTLSELD 545
Cdd:TIGR04523  465 SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS----SLKEKIEKLES---EKKEKE 537
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784   546 DiiknasgiyaEIDGAKNELqvkLSNLSNLSHDLVQEAIDhaqELQQEANELSrklhssdmngLVQKALDASN--VYENI 623
Cdd:TIGR04523  538 S----------KISDLEDEL---NKDDFELKKENLEKEID---EKNKEIEELK----------QTQKSLKKKQeeKQELI 591
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 387540784   624 VNYVSEANE-TAEFALNTTdriydAVSGIDTQIIYHKDESENLLNQARELQAKAES 678
Cdd:TIGR04523  592 DQKEKEKKDlIKEIEEKEK-----KISSLEKELEKAKKENEKLSSIIKNIKSKKNK 642
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
510-601 5.73e-03

Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 38.62  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  510 EKQQERVREQMEAVNMSLNtsadSLTTPRLTLSELDDI-------------------IKNA--------SGIYAE--IDG 560
Cdd:cd23160    13 EQQAEALQQQIELLQASIN----ELNRAKETLEELKKLkegteilvpigggsfvkakIKDTdkvlvnigAGVVVEktIDE 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 387540784  561 AKNELQVKLSNLSNLSHDLVQEaidhAQELQQEANELSRKL 601
Cdd:cd23160    89 AIEILEKRIKELEKALEKLQEQ----LQQIAQRLEELEAEL 125
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
376-463 6.17e-03

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 38.68  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  376 QLVEQAHDMRDKIQEINNKMLYYGEEHElspkEISEKLVLAQKMLEEIRR--RQpfftQRELVDEEAD-EAHELLSQAES 452
Cdd:COG3599    38 RLIRENKELKEKLEELEEELEEYRELEE----TLQKTLVVAQETAEEVKEnaEK----EAELIIKEAElEAEKIIEEAQE 109
                          90
                  ....*....|..
gi 387540784  453 -WQRLHNETRTL 463
Cdd:COG3599   110 kARKIVREIEEL 121
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
302-717 6.42e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  302 RHVNEIN--ATIYLlktKLSERENQYALRKIQINNAENTMKSLLSDVEELVEK-ENQASRKGQLIQKESmDTIKHASQLV 378
Cdd:PRK03918  283 KELKELKekAEEYI---KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKElEEKEERLEELKKKLK-ELEKRLEELE 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  379 EQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRRRQPFFTQR--ELVDEEAD--EAHELLSQAES-- 452
Cdd:PRK03918  359 ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARigELKKEIKElkKAIEELKKAKGkc 438
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  453 ---WQRLHNETRtlfpvvLEQLDDYNAKLSDLQEALDQALNHVRDAED---------MNRATAARQRDHEKQQERVREQM 520
Cdd:PRK03918  439 pvcGRELTEEHR------KELLEEYTAELKRIEKELKEIEEKERKLRKelrelekvlKKESELIKLKELAEQLKELEEKL 512
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  521 EAVNMS-LNTSADSLttpRLTLSELDDIIKNASGIYAEID------GAKNELQVKLSN----LSNLSHDLVQEAIDHAQE 589
Cdd:PRK03918  513 KKYNLEeLEKKAEEY---EKLKEKLIKLKGEIKSLKKELEkleelkKKLAELEKKLDEleeeLAELLKELEELGFESVEE 589
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  590 LQQEANELsRKLHSSDMnglvqKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQI-----IYHKDESEN 664
Cdd:PRK03918  590 LEERLKEL-EPFYNEYL-----ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELeelekKYSEEEYEE 663
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 387540784  665 LLNQARELqakaesssdeavadtSRRVGGALARKSALKTRLSDAVKQLQAAER 717
Cdd:PRK03918  664 LREEYLEL---------------SRELAGLRAELEELEKRREEIKKTLEKLKE 701
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
469-726 6.93e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 6.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  469 EQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQER---------VREQMEAVNMSLntsaDSLTTPRL 539
Cdd:COG4913   610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAEL----ERLDASSD 685
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  540 TLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNlSHDLVQEAIDHAQELQQEANELSRKLHSSDMNGLVQKALDasnv 619
Cdd:COG4913   686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEK-ELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG---- 760
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  620 yENIVNYVSEanetaefalnttdRIYDAVSGIDTQIIYHKDESENLLNQ--------ARELQAKAESSSD-EAVADTSRR 690
Cdd:COG4913   761 -DAVERELRE-------------NLEERIDALRARLNRAEEELERAMRAfnrewpaeTADLDADLESLPEyLALLDRLEE 826
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 387540784  691 VGgaLAR-----KSALKTRLSDAVKQLQAA---ERGDAQQRLGQ 726
Cdd:COG4913   827 DG--LPEyeerfKELLNENSIEFVADLLSKlrrAIREIKERIDP 868
PRK11281 PRK11281
mechanosensitive channel MscK;
364-596 7.65e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.44  E-value: 7.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  364 QKESMDTIKHASQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEklvlAQKMLEEIRrrqpfftqrELVDEEADEA 443
Cdd:PRK11281   51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQ----AQAELEALK---------DDNDEETRET 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  444 HELLSQAESWQRLhNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVrdaedmnraTAARQRdhekqqervreqMEAV 523
Cdd:PRK11281  118 LSTLSLRQLESRL-AQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAAL---------YANSQR------------LQQI 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784  524 NMSLNTSADSLTTPRLTLSELddiiknasgIYAEID--GAKNELQVK-------LSNLSNLSHDLVQEAIDHAQE----L 590
Cdd:PRK11281  176 RNLLKGGKVGGKALRPSQRVL---------LQAEQAllNAQNDLQRKslegntqLQDLLQKQRDYLTARIQRLEHqlqlL 246

                  ....*.
gi 387540784  591 QQEANE 596
Cdd:PRK11281  247 QEAINS 252
 
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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