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Conserved domains on  [gi|2217361438|ref|XP_047274725|]
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laminin subunit alpha-4 isoform X1 [Homo sapiens]

Protein Classification

Laminin_I and LamG domain-containing protein( domain architecture ID 12873424)

protein containing domains EGF_Lam, Laminin_I, ApoLp-III_like, and LamG

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 ...
298-554 1.35e-101

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: 326.68  E-value: 1.35e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  298 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDT 377
Cdd:pfam06008    1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  378 INHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRSRQpFFTQRELVDEEADEAYELLSQ 456
Cdd:pfam06008   81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  457 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLS 535
Cdd:pfam06008  160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
                          250
                   ....*....|....*....
gi 2217361438  536 TSADSLTTPRLTLSELDDI 554
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 ...
734-861 2.27e-43

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: 154.95  E-value: 2.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  734 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVNSARDAVRNLTEVVPQLLDQLRTVEQ 804
Cdd:pfam06009    1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217361438  805 KRPAS-NVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSL 861
Cdd:pfam06009   81 LEVNSsSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1492-1624 2.00e-39

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: 144.10  E-value: 2.00e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1492 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVIFIRERSSGRLVIDG 1571
Cdd:cd00110     21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 1572 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1624
Cdd:cd00110    101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1648-1799 2.83e-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: 2.83e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1648 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1726
Cdd:cd00110      1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 1727 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1799
Cdd:cd00110     78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1049-1207 8.38e-24

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: 99.41  E-value: 8.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1049 SYFFDGSGYAvvrDITRRGKFGQVTRFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLEDtl 1126
Cdd:cd00110      1 GVSFSGSSYV---RLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1127 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRALRAHlpldiNFRGCMK 1203
Cdd:cd00110     74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146

                   ....
gi 2217361438 1204 GFQF 1207
Cdd:cd00110    147 DLKV 150
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1237-1376 4.13e-19

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: 85.93  E-value: 4.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1237 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVIMDV----KGIKVQSvDKQYNDG 1310
Cdd:cd00110      2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 1311 LSHFVISSVSPTRYELIVDKSRVGSKNPTKGKIEQTqaSEKKFYFGGSPISAQ------YANFTGCISNAYF 1376
Cdd:cd00110     81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLN--LDGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
835-1012 1.78e-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: 84.01  E-value: 1.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  835 SMMFDGQSAVEVhsrTSMDDLKAFTSLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKD 914
Cdd:cd00110      1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--------TTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGS 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  915 VEIpldSKPVSSWPAYFSIVKIERVGKHgkVFLTVPSLSStaeekfikkGEFSGDDSLLDLDPEDTVfYVGGVPSNFKLP 994
Cdd:cd00110     69 LVL---SSKTPLNDGQWHSVSVERNGRS--VTLSVDGERV---------VESGSPGGSALLNLDGPL-YLGGLPEDLKSP 133
                          170
                   ....*....|....*...
gi 2217361438  995 TSLNLPGFVGCLELATLN 1012
Cdd:cd00110    134 GLPVSPGFVGCIRDLKVN 151
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
187-238 8.76e-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: 72.77  E-value: 8.76e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217361438  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 ...
131-185 1.14e-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: 63.91  E-value: 1.14e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217361438  131 PCPCPlPHlANFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNPlLIGSTCK 185
Cdd:cd00055      1 PCDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
81-130 3.23e-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: 60.06  E-value: 3.23e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217361438   81 PCDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIRGAPqfCQ 130
Cdd:cd00055      1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
529-757 2.62e-07

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


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.84  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  529 VVNMSLSTSADslTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDL--VQEAIDhaqDLQQEANELSR 606
Cdd:COG3883      5 ALAAPTPAFAD--PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  607 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 681
Cdd:COG3883     80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  682 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQA------AERGDAQQRLGQSRLITEEANRTTMEVQQATAPM 755
Cdd:COG3883    158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAqlaeleAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236

                   ..
gi 2217361438  756 AN 757
Cdd:COG3883    237 AA 238
 
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 ...
298-554 1.35e-101

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: 326.68  E-value: 1.35e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  298 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDT 377
Cdd:pfam06008    1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  378 INHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRSRQpFFTQRELVDEEADEAYELLSQ 456
Cdd:pfam06008   81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  457 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLS 535
Cdd:pfam06008  160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
                          250
                   ....*....|....*....
gi 2217361438  536 TSADSLTTPRLTLSELDDI 554
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 ...
734-861 2.27e-43

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: 154.95  E-value: 2.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  734 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVNSARDAVRNLTEVVPQLLDQLRTVEQ 804
Cdd:pfam06009    1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217361438  805 KRPAS-NVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSL 861
Cdd:pfam06009   81 LEVNSsSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1492-1624 2.00e-39

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: 144.10  E-value: 2.00e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1492 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVIFIRERSSGRLVIDG 1571
Cdd:cd00110     21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 1572 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1624
Cdd:cd00110    101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1494-1625 1.00e-35

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 132.85  E-value: 1.00e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  1494 QFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQ-EKYNDGLWHDVIFIRERSSGRLVIDGL 1572
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217361438  1573 RVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLNG 1625
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDL--KLPPLPVTPGFRGCIRNLKVNG 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1648-1799 2.83e-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: 2.83e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1648 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1726
Cdd:cd00110      1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 1727 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1799
Cdd:cd00110     78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1671-1801 3.71e-31

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 119.75  E-value: 3.71e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  1671 EIAFEVRPRSSSGTLVHGHSVNG-EYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQsLCDGRWHRITVIRDSNVVQLDVDS 1749
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2217361438  1750 EvNHVVG--PLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1801
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 ...
1499-1625 2.37e-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: 117.14  E-value: 2.37e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1499 LRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLKIRSQEK-YNDGLWHDVIFIRERSSGRLVIDGLRVLEE 1577
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKnLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2217361438 1578 SLPPTEATWKIKGPIYLGGVAPGKAVKNVQINSiySFSGCLSNLQLNG 1625
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 ...
1676-1801 1.66e-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: 1.66e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1676 VRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKqSLCDGRWHRITVIRDSNVVQLDVDSEVNH-V 1754
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVsS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2217361438 1755 VGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1801
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1049-1207 8.38e-24

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: 99.41  E-value: 8.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1049 SYFFDGSGYAvvrDITRRGKFGQVTRFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLEDtl 1126
Cdd:cd00110      1 GVSFSGSSYV---RLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1127 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRALRAHlpldiNFRGCMK 1203
Cdd:cd00110     74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146

                   ....
gi 2217361438 1204 GFQF 1207
Cdd:cd00110    147 DLKV 150
LamG smart00282
Laminin G domain;
1074-1210 2.35e-22

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 94.33  E-value: 2.35e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  1074 RFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLedTLKKAQINDAKYHEISIIyHNDKKMIL 1151
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARL--TSDPTPLNDGQWHRVAVE-RNGRSVTL 75
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438  1152 VVD---RRHVKSMDNEKMKIPFTDIYIGGAPPEILQSralraHLPLDINFRGCMKGFQFQKK 1210
Cdd:smart00282   76 SVDggnRVSGESPGGLTILNLDGPLYLGGLPEDLKLP-----PLPVTPGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1079-1207 1.55e-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: 89.02  E-value: 1.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1079 VRTPADNGLIL-LMVNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLedTLKKAQINDAKYHEISIIYhNDKKMILVVDRRH 1157
Cdd:pfam02210    1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLG--SGPESL--LSSGKNLNDGQWHSVRVER-NGNTLTLSVDGQT 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 1158 VKSMDNEKMKIPF---TDIYIGGAPPeilqsRALRAHLPLDINFRGCMKGFQF 1207
Cdd:pfam02210   76 VVSSLPPGESLLLnlnGPLYLGGLPP-----LLLLPALPVRAGFVGCIRDVRV 123
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1237-1376 4.13e-19

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: 85.93  E-value: 4.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1237 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVIMDV----KGIKVQSvDKQYNDG 1310
Cdd:cd00110      2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 1311 LSHFVISSVSPTRYELIVDKSRVGSKNPTKGKIEQTqaSEKKFYFGGSPISAQ------YANFTGCISNAYF 1376
Cdd:cd00110     81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLN--LDGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
835-1012 1.78e-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: 84.01  E-value: 1.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  835 SMMFDGQSAVEVhsrTSMDDLKAFTSLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKD 914
Cdd:cd00110      1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--------TTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGS 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  915 VEIpldSKPVSSWPAYFSIVKIERVGKHgkVFLTVPSLSStaeekfikkGEFSGDDSLLDLDPEDTVfYVGGVPSNFKLP 994
Cdd:cd00110     69 LVL---SSKTPLNDGQWHSVSVERNGRS--VTLSVDGERV---------VESGSPGGSALLNLDGPL-YLGGLPEDLKSP 133
                          170
                   ....*....|....*...
gi 2217361438  995 TSLNLPGFVGCLELATLN 1012
Cdd:cd00110    134 GLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
860-1013 3.32e-18

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 82.77  E-value: 3.32e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438   860 SLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVSswPAYFSIVKIERV 939
Cdd:smart00282    1 SISFSFR--------TTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLN--DGQWHRVAVERN 69
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438   940 GKHgkVFLTVPSLSSTAEEKFIKKgefsgddSLLDLDpedTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNN 1013
Cdd:smart00282   70 GRS--VTLSVDGGNRVSGESPGGL-------TILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1263-1376 1.45e-17

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: 80.54  E-value: 1.45e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1263 FRTLQPNGLLFYYASG-SDVFSISLDNGTVIMDVK----GIKVQSVDKQYNDGLSHFVISSVSPTRYELIVDKSRVGSKN 1337
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDlgsgPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2217361438 1338 PTKGkiEQTQASEKKFYFGG------SPISAQYANFTGCISNAYF 1376
Cdd:pfam02210   81 PPGE--SLLLNLNGPLYLGGlpplllLPALPVRAGFVGCIRDVRV 123
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
187-238 8.76e-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: 72.77  E-value: 8.76e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217361438  187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDARIAKNC 238
Cdd:cd00055      2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGC 49
LamG smart00282
Laminin G domain;
1261-1379 1.13e-14

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 72.37  E-value: 1.13e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  1261 FNFRTLQPNGLLFYYAS--GSDVFSISLDNGTVIMDVKG----IKVQSVDKQYNDGLSHFVISSVSPTRYELIVDksrvg 1334
Cdd:smart00282    4 FSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLgsgpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2217361438  1335 SKNPTKGKIEQTQA---SEKKFYFGGSP------ISAQYANFTGCISNAYFTRV 1379
Cdd:smart00282   79 GGNRVSGESPGGLTilnLDGPLYLGGLPedlklpPLPVTPGFRGCIRNLKVNGK 132
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
187-232 5.57e-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: 5.57e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2217361438  187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDA 232
Cdd:pfam00053    1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
131-185 1.14e-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: 63.91  E-value: 1.14e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217361438  131 PCPCPlPHlANFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNPlLIGSTCK 185
Cdd:cd00055      1 PCDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
187-231 4.76e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 61.94  E-value: 4.76e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2217361438   187 CDCS--GNSDPnlifeDCDEVTGQCRnCLRNTTGFKCERCAPGYYGD 231
Cdd:smart00180    1 CDCDpgGSASG-----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
347-821 9.47e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 70.45  E-value: 9.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  347 KSLLSDVEELVEKENQASRKGQL-----VQKESMDTINHASQLVEQAHDMRDKIQEINnkmlyygEEHELSPKEI----S 417
Cdd:PRK02224   186 RGSLDQLKAQIEEKEEKDLHERLnglesELAELDEEIERYEEQREQARETRDEADEVL-------EEHEERREELetleA 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  418 EKLVLAQKMLEEIRSRQPF----FTQRELVDEEADEAYELLSQAEsWQRLHNETrtlfpvVLEQLDDYNAKLSDLQEALD 493
Cdd:PRK02224   259 EIEDLRETIAETEREREELaeevRDLRERLEELEEERDDLLAEAG-LDDADAEA------VEARREELEDRDEELRDRLE 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  494 QALNYVRDAEdmNRATAARQR--DHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYA----EIDG 567
Cdd:PRK02224   332 ECRVAAQAHN--EEAESLREDadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGN 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  568 AKSELQVKLSNLSNLSHDL---------VQEAIDHAQDLQQEAN-------------------------ELSRKLhsSDM 613
Cdd:PRK02224   410 AEDFLEELREERDELREREaeleatlrtARERVEEAEALLEAGKcpecgqpvegsphvetieedrerveELEAEL--EDL 487
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  614 NGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQiiyhKDESENLLNQARELQAKAESSSDEAV-- 691
Cdd:PRK02224   488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK----RERAEELRERAAELEAEAEEKREAAAea 563
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  692 ---ADTSRRVGGAL-ARKSALKTRLsDAVKQL--QAAERGDAQQRLGqsRLITEEANRTTMEVQQatapmANNLTNWSQN 765
Cdd:PRK02224   564 eeeAEEAREEVAELnSKLAELKERI-ESLERIrtLLAAIADAEDEIE--RLREKREALAELNDER-----RERLAEKRER 635
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217361438  766 LQHFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRPA-----SNVSASIQRIREL 821
Cdd:PRK02224   636 KRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaeiGAVENELEELEEL 696
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
132-184 1.72e-11

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 60.44  E-value: 1.72e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217361438  132 CPCPlpHLANFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNPLLIGSTC 184
Cdd:pfam00053    1 CDCN--PHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
321-647 2.19e-11

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: 69.32  E-value: 2.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  321 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINN 400
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  401 KMLYYGEEHELSPKEISEKLVLAQKMLEEIRSRQPFFT-QRELVDEEADEAYELLSQAESWQRLHNETRTLFPVVLEQLD 479
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELEsLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  480 DYNAKLSDLQEALDQalnyvrdAEDMNRATAARQRDHEKQQERVreQMEVVNMSLSTSADSLTTprlTLSELDDIIKNAS 559
Cdd:TIGR02168  397 SLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE---LQEELERLEEALE 464
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  560 GIYAEIDGAKSELQVKLSNLSNLSH--DLVQEAIDHAQDLQQEANELsrKLHSSDMNGLVQKALDASNV---YE------ 628
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVdegYEaaieaa 542
                          330       340
                   ....*....|....*....|..
gi 2217361438  629 ---NIVNYVSEANETAEFALNT 647
Cdd:TIGR02168  543 lggRLQAVVVENLNAAKKAIAF 564
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
81-130 3.23e-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: 60.06  E-value: 3.23e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217361438   81 PCDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIRGAPqfCQ 130
Cdd:cd00055      1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
132-177 4.17e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 59.25  E-value: 4.17e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2217361438   132 CPCPLPHlaNFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNP 177
Cdd:smart00180    1 CDCDPGG--SASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
875-1013 8.80e-11

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: 61.28  E-value: 8.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  875 TETADQFILYLGSKnaKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVS--SWpayfSIVKIERVGKHgkVFLTVPSL 952
Cdd:pfam02210    3 TRQPNGLLLYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQ 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217361438  953 SSTAEEKfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNN 1013
Cdd:pfam02210   75 TVVSSLP-------PGESLLLNLN---GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
65-257 2.80e-10

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: 60.78  E-value: 2.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438   65 EKCNAGFFhTLSGECvpCDcngnsnECLDGSGYCVHCQRNTTGehCEKCLDGYIGDSIRGAPQFCQPC-PCplPHLANFA 143
Cdd:cd13416      1 EACPSGQY-TSSGEC--CE------QCPPGEGVARPCGDNQTV--CEPCLDGVTFSDVVSHTEPCQPCtRC--PGLMSMR 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  144 ESCYRKNGAVrcicnenyagpnCErCAPGYYGNPLliGSTCKKCDCsgnsdpnlifedCDEVTGQCRNC--LRNTtgfKC 221
Cdd:cd13416     68 APCTATHDTV------------CE-CAYGYYLDED--SGTCEPCTV------------CPPGQGVVQSCgpNQDT---VC 117
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2217361438  222 ERCAPGYYGDARIAKN----CAVCncggGPCDSVTGECLE 257
Cdd:cd13416    118 EACPEGTYSDEDSSTDpclpCTVC----EDGEVELRECTP 153
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
82-129 6.47e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.21  E-value: 6.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217361438   82 CDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIrGAPQFC 129
Cdd:pfam00053    1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
82-121 4.70e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.47  E-value: 4.70e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2217361438    82 CDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDS 121
Cdd:smart00180    1 CDCDPGgsaSGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
319-731 2.43e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 59.01  E-value: 2.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  319 YLLKTKLseRENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESmdtinhasQLVEQAHDMRDKIQEI 398
Cdd:COG4717     45 AMLLERL--EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--------ELEEELEELEAELEEL 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  399 NNKMLYYgeEHELSPKEISEKLVLAQKMLEEIRSRQPFFTQRELVDEEADEAYE-LLSQAESWQR-LHNETRTLFPVVLE 476
Cdd:COG4717    115 REELEKL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeLEAELAELQEeLEELLEQLSLATEE 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  477 QLDDYNAKLSDLQEALDQALNYVRDAEDmNRATAARQRD-------HEKQQERVREQMEVVN-----MSLSTSADSLTTP 544
Cdd:COG4717    193 ELQDLAEELEELQQRLAELEEELEEAQE-ELEELEEELEqleneleAAALEERLKEARLLLLiaaalLALLGLGGSLLSL 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  545 RLTL----------------------SELDDIIKNASGIYAEIDGAKSELQVKLSNL---SNLSHDLVQEAIDHAQDLQQ 599
Cdd:COG4717    272 ILTIagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQE 351
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  600 ---EANELSRKLHSSDMNGLVQKALDASNV-----YENIVNYVSEANETAEfalnttdriydAVSGIDTQIIYHKDESEN 671
Cdd:COG4717    352 llrEAEELEEELQLEELEQEIAALLAEAGVedeeeLRAALEQAEEYQELKE-----------ELEELEEQLEELLGELEE 420
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217361438  672 LLNQARELQAKAE-SSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRL 731
Cdd:COG4717    421 LLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
529-757 2.62e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.84  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  529 VVNMSLSTSADslTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDL--VQEAIDhaqDLQQEANELSR 606
Cdd:COG3883      5 ALAAPTPAFAD--PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  607 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 681
Cdd:COG3883     80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  682 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQA------AERGDAQQRLGQSRLITEEANRTTMEVQQATAPM 755
Cdd:COG3883    158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAqlaeleAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236

                   ..
gi 2217361438  756 AN 757
Cdd:COG3883    237 AA 238
growth_prot_Scy NF041483
polarized growth protein Scy;
354-855 7.63e-07

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 54.45  E-value: 7.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  354 EELVEKENQASRKgqlvQKESMDTINHASQLVEQahdmrdkiqeinnkmlyygeEHELSPKEISEKLVLAQKMLEEIRSR 433
Cdd:NF041483   699 EALAAAQEEAARR----RREAEETLGSARAEADQ--------------------ERERAREQSEELLASARKRVEEAQAE 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  434 qpffTQReLVdEEADE-AYELLSQAESwqrlhnetrtlfpvVLEQLDDynaKLSDLQEALDQALNYVRDAEDMnraTAAR 512
Cdd:NF041483   755 ----AQR-LV-EEADRrATELVSAAEQ--------------TAQQVRD---SVAGLQEQAEEEIAGLRSAAEH---AAER 808
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  513 QRDhEKQQE--RVReqmevvnmslstsADSLTTpRLTLSEldDIIKNASGIYAEIDGAKSelqvklsnlsnLSHDLVQEA 590
Cdd:NF041483   809 TRT-EAQEEadRVR-------------SDAYAE-RERASE--DANRLRREAQEETEAAKA-----------LAERTVSEA 860
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  591 IDHAQDLQQEANELSRKLHSSDMNGLVQKALDASNVYenivnyvSEANETAefalnttDRI-YDAVSGIDTQIIYHKDES 669
Cdd:NF041483   861 IAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTR-------ADAREDA-------NRIrSDAAAQADRLIGEATSEA 926
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  670 ENLLNQARelqAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQL--QAAER-GDAQQRLGQSRlitEEANRTTM 746
Cdd:NF041483   927 ERLTAEAR---AEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLraEAAETvGSAQQHAERIR---TEAERVKA 1000
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  747 EvqqaTAPMANNLTNWSQN-----LQHFDSSAYNTAVNSARDAVRNLTEVVPQlLDQLRTVEQKRPASNVSASIQRIREL 821
Cdd:NF041483  1001 E----AAAEAERLRTEAREeadrtLDEARKDANKRRSEAAEQADTLITEAAAE-ADQLTAKAQEEALRTTTEAEAQADTM 1075
                          490       500       510
                   ....*....|....*....|....*....|....
gi 2217361438  822 IAQTRSVASKIQVSMMFDGQSAVEvHSRTSMDDL 855
Cdd:NF041483  1076 VGAARKEAERIVAEATVEGNSLVE-KARTDADEL 1108
mukB PRK04863
chromosome partition protein MukB;
440-821 4.05e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 52.27  E-value: 4.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  440 RELVDEEAD---EAYELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQA---LNYVRDAEDMNRATAARQ 513
Cdd:PRK04863   282 RVHLEEALElrrELYTSRRQLAAEQYRLVEMA-------RELAELNEAESDLEQDYQAAsdhLNLVQTALRQQEKIERYQ 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  514 RDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELD-------------DIIKNASGIYAE----IDGAKSELQVKL 576
Cdd:PRK04863   355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDelksqladyqqalDVQQTRAIQYQQavqaLERAKQLCGLPD 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  577 SNLSNLShDLVQEAIDHAQDLQQEANELSRKLHSSDMnglvqkaldasnvyenivnyvseANETAEFALNTTDRIYDAVS 656
Cdd:PRK04863   435 LTADNAE-DWLEEFQAKEQEATEELLSLEQKLSVAQA-----------------------AHSQFEQAYQLVRKIAGEVS 490
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  657 GIDTQiiyhkDESENLLNQARELQAKAEsssdeavadtsrRVGGALARKSALKTRLsdavKQLQAAER--GDAQQRLGQS 734
Cdd:PRK04863   491 RSEAW-----DVARELLRRLREQRHLAE------------QLQQLRMRLSELEQRL----RQQQRAERllAEFCKRLGKN 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  735 --------RLITE-EANRTTMEVQQATA-----PMANNLTNWSQNLQHFDSSA-----YNTAVNSARDAV-------RNL 788
Cdd:PRK04863   550 lddedeleQLQEElEARLESLSESVSEArerrmALRQQLEQLQARIQRLAARApawlaAQDALARLREQSgeefedsQDV 629
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2217361438  789 TEVVPQLLDQLR--TVEQKRPASNVSASIQRIREL 821
Cdd:PRK04863   630 TEYMQQLLERERelTVERDELAARKQALDEEIERL 664
ApoLp-III_like cd13769
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ...
710-836 4.17e-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: 4.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  710 TRLSDAVKQLQAAERGDAQQRLGQSRL-ITEEANRTtmeVQQATAPMANNLTNWSQNLQHFDSSAYNTAVNSARDAVRNL 788
Cdd:cd13769      1 TQLSELIQKAQEAINNLAQQVQKQLGLqNPEEVVNT---LKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKL 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2217361438  789 TEVVPQLLDQLRTVEQkrpASNVSASIQ-RIRELIAQTRSVASKIQVSM 836
Cdd:cd13769     78 SETVPELRKSLPVEEK---AQELQAKLQsGLQTLVTESQKLAKAISENS 123
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
521-764 2.41e-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: 49.66  E-value: 2.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  521 ERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKnaSGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQD---L 597
Cdd:TIGR01612  500 MRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNIK--AKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDsihL 577
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  598 QQEAN---------------------ELSRKLHS-SDMNGLVQKALDASNVYENIVNYVSEANETAEFA----LNTTDRI 651
Cdd:TIGR01612  578 EKEIKdlfdkyleiddeiiyinklklELKEKIKNiSDKNEYIKKAIDLKKIIENNNAYIDELAKISPYQvpehLKNKDKI 657
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  652 YDAVSGIDTQI--------------IYHKDESENLLNQAR--ELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 715
Cdd:TIGR01612  658 YSTIKSELSKIyeddidalynelssIVKENAIDNTEDKAKldDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDI 737
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2217361438  716 VKQLQAAERGDaqqrlgqsrlITEEANRTTMEVQQATAPMANNLTNWSQ 764
Cdd:TIGR01612  738 IVEIKKHIHGE----------INKDLNKILEDFKNKEKELSNKINDYAK 776
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
666-824 1.39e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  666 KDESENLLNQARELQAK-AESSSDEAVADTSRR--------VGGAlaRKSALKTRLSDAVKQLQAAE--RGDAQQRLGQS 734
Cdd:COG4913    294 EAELEELRAELARLEAElERLEARLDALREELDeleaqirgNGGD--RLEQLEREIERLERELEERErrRARLEALLAAL 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  735 RLiTEEANRTTMEVQQATAPMAnnLTNWSQnlqhfDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSAS 814
Cdd:COG4913    372 GL-PLPASAEEFAALRAEAAAL--LEALEE-----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRK--SNIPAR 441
                          170
                   ....*....|
gi 2217361438  815 IQRIRELIAQ 824
Cdd:COG4913    442 LLALRDALAE 451
 
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 ...
298-554 1.35e-101

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: 326.68  E-value: 1.35e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  298 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDT 377
Cdd:pfam06008    1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  378 INHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRSRQpFFTQRELVDEEADEAYELLSQ 456
Cdd:pfam06008   81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  457 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLS 535
Cdd:pfam06008  160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
                          250
                   ....*....|....*....
gi 2217361438  536 TSADSLTTPRLTLSELDDI 554
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 ...
734-861 2.27e-43

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: 154.95  E-value: 2.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  734 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVNSARDAVRNLTEVVPQLLDQLRTVEQ 804
Cdd:pfam06009    1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217361438  805 KRPAS-NVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSL 861
Cdd:pfam06009   81 LEVNSsSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1492-1624 2.00e-39

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: 144.10  E-value: 2.00e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1492 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVIFIRERSSGRLVIDG 1571
Cdd:cd00110     21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 1572 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1624
Cdd:cd00110    101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1494-1625 1.00e-35

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 132.85  E-value: 1.00e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  1494 QFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQ-EKYNDGLWHDVIFIRERSSGRLVIDGL 1572
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217361438  1573 RVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLNG 1625
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDL--KLPPLPVTPGFRGCIRNLKVNG 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1648-1799 2.83e-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: 2.83e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1648 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1726
Cdd:cd00110      1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 1727 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1799
Cdd:cd00110     78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1671-1801 3.71e-31

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 119.75  E-value: 3.71e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  1671 EIAFEVRPRSSSGTLVHGHSVNG-EYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQsLCDGRWHRITVIRDSNVVQLDVDS 1749
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2217361438  1750 EvNHVVG--PLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1801
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 ...
1499-1625 2.37e-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: 117.14  E-value: 2.37e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1499 LRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLKIRSQEK-YNDGLWHDVIFIRERSSGRLVIDGLRVLEE 1577
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKnLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2217361438 1578 SLPPTEATWKIKGPIYLGGVAPGKAVKNVQINSiySFSGCLSNLQLNG 1625
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 ...
1676-1801 1.66e-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: 1.66e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1676 VRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKqSLCDGRWHRITVIRDSNVVQLDVDSEVNH-V 1754
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVsS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2217361438 1755 VGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1801
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
Laminin_G_1 pfam00054
Laminin G domain;
1500-1628 7.33e-24

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 98.54  E-value: 7.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1500 RTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVIFIRERSSGRLVIDGLRVLE-ES 1578
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTgES 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1579 LPPTEATWKIKGPIYLGGvAPGKAVKNVQINSIYSFSGCLSNLQLNGASI 1628
Cdd:pfam00054   82 PLGATTDLDVDGPLYVGG-LPSLGVKKRRLAISPSFDGCIRDVIVNGKPL 130
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1049-1207 8.38e-24

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: 99.41  E-value: 8.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1049 SYFFDGSGYAvvrDITRRGKFGQVTRFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLEDtl 1126
Cdd:cd00110      1 GVSFSGSSYV---RLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1127 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRALRAHlpldiNFRGCMK 1203
Cdd:cd00110     74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146

                   ....
gi 2217361438 1204 GFQF 1207
Cdd:cd00110    147 DLKV 150
LamG smart00282
Laminin G domain;
1074-1210 2.35e-22

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 94.33  E-value: 2.35e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  1074 RFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLedTLKKAQINDAKYHEISIIyHNDKKMIL 1151
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARL--TSDPTPLNDGQWHRVAVE-RNGRSVTL 75
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438  1152 VVD---RRHVKSMDNEKMKIPFTDIYIGGAPPEILQSralraHLPLDINFRGCMKGFQFQKK 1210
Cdd:smart00282   76 SVDggnRVSGESPGGLTILNLDGPLYLGGLPEDLKLP-----PLPVTPGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1079-1207 1.55e-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: 89.02  E-value: 1.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1079 VRTPADNGLIL-LMVNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLedTLKKAQINDAKYHEISIIYhNDKKMILVVDRRH 1157
Cdd:pfam02210    1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLG--SGPESL--LSSGKNLNDGQWHSVRVER-NGNTLTLSVDGQT 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 1158 VKSMDNEKMKIPF---TDIYIGGAPPeilqsRALRAHLPLDINFRGCMKGFQF 1207
Cdd:pfam02210   76 VVSSLPPGESLLLnlnGPLYLGGLPP-----LLLLPALPVRAGFVGCIRDVRV 123
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1237-1376 4.13e-19

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: 85.93  E-value: 4.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1237 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVIMDV----KGIKVQSvDKQYNDG 1310
Cdd:cd00110      2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 1311 LSHFVISSVSPTRYELIVDKSRVGSKNPTKGKIEQTqaSEKKFYFGGSPISAQ------YANFTGCISNAYF 1376
Cdd:cd00110     81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLN--LDGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
835-1012 1.78e-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: 84.01  E-value: 1.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  835 SMMFDGQSAVEVhsrTSMDDLKAFTSLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKD 914
Cdd:cd00110      1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--------TTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGS 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  915 VEIpldSKPVSSWPAYFSIVKIERVGKHgkVFLTVPSLSStaeekfikkGEFSGDDSLLDLDPEDTVfYVGGVPSNFKLP 994
Cdd:cd00110     69 LVL---SSKTPLNDGQWHSVSVERNGRS--VTLSVDGERV---------VESGSPGGSALLNLDGPL-YLGGLPEDLKSP 133
                          170
                   ....*....|....*...
gi 2217361438  995 TSLNLPGFVGCLELATLN 1012
Cdd:cd00110    134 GLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
860-1013 3.32e-18

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 82.77  E-value: 3.32e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438   860 SLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVSswPAYFSIVKIERV 939
Cdd:smart00282    1 SISFSFR--------TTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLN--DGQWHRVAVERN 69
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438   940 GKHgkVFLTVPSLSSTAEEKFIKKgefsgddSLLDLDpedTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNN 1013
Cdd:smart00282   70 GRS--VTLSVDGGNRVSGESPGGL-------TILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1263-1376 1.45e-17

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: 80.54  E-value: 1.45e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1263 FRTLQPNGLLFYYASG-SDVFSISLDNGTVIMDVK----GIKVQSVDKQYNDGLSHFVISSVSPTRYELIVDKSRVGSKN 1337
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDlgsgPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2217361438 1338 PTKGkiEQTQASEKKFYFGG------SPISAQYANFTGCISNAYF 1376
Cdd:pfam02210   81 PPGE--SLLLNLNGPLYLGGlpplllLPALPVRAGFVGCIRDVRV 123
Laminin_G_1 pfam00054
Laminin G domain;
1676-1803 5.37e-16

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 76.20  E-value: 5.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1676 VRPRSSSGTLVHGHSVN-GEYLNVHMKNGQVIVKVNNGIRdfSTSVTPKQSLCDGRWHRITVIRDSNVVQLDVDSEVNHV 1754
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTeRDFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 1755 V-GPLNPK-PIDHREPVFVGGVPESLLTPRLAP-SKPFTGCIRHFVIDGHPV 1803
Cdd:pfam00054   79 GeSPLGATtDLDVDGPLYVGGLPSLGVKKRRLAiSPSFDGCIRDVIVNGKPL 130
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
187-238 8.76e-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: 72.77  E-value: 8.76e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217361438  187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDARIAKNC 238
Cdd:cd00055      2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGC 49
LamG smart00282
Laminin G domain;
1261-1379 1.13e-14

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 72.37  E-value: 1.13e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  1261 FNFRTLQPNGLLFYYAS--GSDVFSISLDNGTVIMDVKG----IKVQSVDKQYNDGLSHFVISSVSPTRYELIVDksrvg 1334
Cdd:smart00282    4 FSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLgsgpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2217361438  1335 SKNPTKGKIEQTQA---SEKKFYFGGSP------ISAQYANFTGCISNAYFTRV 1379
Cdd:smart00282   79 GGNRVSGESPGGLTilnLDGPLYLGGLPedlklpPLPVTPGFRGCIRNLKVNGK 132
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
187-232 5.57e-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: 5.57e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2217361438  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 ...
279-723 7.44e-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: 73.99  E-value: 7.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  279 DLTDDLRLAALSIEEGKsgVLSVSSGAAAHRHVNEINATIYLL----KTKLSERENQYALRKIQINNAENTMKSLLSDVE 354
Cdd:pfam05483  187 DLNNNIEKMILAFEELR--VQAENARLEMHFKLKEDHEKIQHLeeeyKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  355 ELVEKENQASRKGQLvQKESMdtinhaSQLVEQAHDMRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRSrq 434
Cdd:pfam05483  265 ESRDKANQLEEKTKL-QDENL------KELIEKKDHLTKELEDIKMSL----QRSMSTQKALEEDLQIATKTICQLTE-- 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  435 pfftQRELVDEEADEAY------------------ELLSQAEswQRLHNETRTLFPVVLEqlddYNAKLSDLQEALDQAL 496
Cdd:pfam05483  332 ----EKEAQMEELNKAKaahsfvvtefeattcsleELLRTEQ--QRLEKNEDQLKIITME----LQKKSSELEEMTKFKN 401
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  497 NYVRDAEDMNRATAARQR--DHEKQQERVREQMEVVNMSLSTsadSLTTPRLTLSELD---DIIKNASGIYA-EIDGAKS 570
Cdd:pfam05483  402 NKEVELEELKKILAEDEKllDEKKQFEKIAEELKGKEQELIF---LLQAREKEIHDLEiqlTAIKTSEEHYLkEVEDLKT 478
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  571 ELQ-VKLSNLSNLSH---------DLVQEAID-------HAQDLQQEANELSRKLhsSDMNGLVQKALDASNVYENIVNY 633
Cdd:pfam05483  479 ELEkEKLKNIELTAHcdklllenkELTQEASDmtlelkkHQEDIINCKKQEERML--KQIENLEEKEMNLRDELESVREE 556
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  634 VSEANETAEFALnttDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAEsssdeavaDTSRRVGGALARKSALKTRLS 713
Cdd:pfam05483  557 FIQKGDEVKCKL---DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE--------NKNKNIEELHQENKALKKKGS 625
                          490
                   ....*....|
gi 2217361438  714 DAVKQLQAAE 723
Cdd:pfam05483  626 AENKQLNAYE 635
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
131-185 1.14e-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: 63.91  E-value: 1.14e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217361438  131 PCPCPlPHlANFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNPlLIGSTCK 185
Cdd:cd00055      1 PCDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
187-231 4.76e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 61.94  E-value: 4.76e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2217361438   187 CDCS--GNSDPnlifeDCDEVTGQCRnCLRNTTGFKCERCAPGYYGD 231
Cdd:smart00180    1 CDCDpgGSASG-----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
347-821 9.47e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 70.45  E-value: 9.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  347 KSLLSDVEELVEKENQASRKGQL-----VQKESMDTINHASQLVEQAHDMRDKIQEINnkmlyygEEHELSPKEI----S 417
Cdd:PRK02224   186 RGSLDQLKAQIEEKEEKDLHERLnglesELAELDEEIERYEEQREQARETRDEADEVL-------EEHEERREELetleA 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  418 EKLVLAQKMLEEIRSRQPF----FTQRELVDEEADEAYELLSQAEsWQRLHNETrtlfpvVLEQLDDYNAKLSDLQEALD 493
Cdd:PRK02224   259 EIEDLRETIAETEREREELaeevRDLRERLEELEEERDDLLAEAG-LDDADAEA------VEARREELEDRDEELRDRLE 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  494 QALNYVRDAEdmNRATAARQR--DHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYA----EIDG 567
Cdd:PRK02224   332 ECRVAAQAHN--EEAESLREDadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGN 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  568 AKSELQVKLSNLSNLSHDL---------VQEAIDHAQDLQQEAN-------------------------ELSRKLhsSDM 613
Cdd:PRK02224   410 AEDFLEELREERDELREREaeleatlrtARERVEEAEALLEAGKcpecgqpvegsphvetieedrerveELEAEL--EDL 487
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  614 NGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQiiyhKDESENLLNQARELQAKAESSSDEAV-- 691
Cdd:PRK02224   488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK----RERAEELRERAAELEAEAEEKREAAAea 563
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  692 ---ADTSRRVGGAL-ARKSALKTRLsDAVKQL--QAAERGDAQQRLGqsRLITEEANRTTMEVQQatapmANNLTNWSQN 765
Cdd:PRK02224   564 eeeAEEAREEVAELnSKLAELKERI-ESLERIrtLLAAIADAEDEIE--RLREKREALAELNDER-----RERLAEKRER 635
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217361438  766 LQHFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRPA-----SNVSASIQRIREL 821
Cdd:PRK02224   636 KRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaeiGAVENELEELEEL 696
Laminin_G_1 pfam00054
Laminin G domain;
1079-1203 9.62e-12

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 63.88  E-value: 9.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1079 VRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLEdtlKKAQINDAKYHEISIIYhNDKKMILVVDRR 1156
Cdd:pfam00054    1 FRTTEPSGLLLYNgtQTERDFLALELRDGRLEVSYDLG--SGAAVVR---SGDKLNDGKWHSVELER-NGRSGTLSVDGE 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217361438 1157 HVKSMDNEK---MKIPF-TDIYIGGAPPEILqsraLRAHLPLDINFRGCMK 1203
Cdd:pfam00054   75 ARPTGESPLgatTDLDVdGPLYVGGLPSLGV----KKRRLAISPSFDGCIR 121
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
302-833 1.52e-11

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: 69.76  E-value: 1.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  302 SSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNA--------ENTMKSLLSDVE----ELVEKENQASRKGQL 369
Cdd:pfam15921  217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhQDRIEQLISEHEveitGLTEKASSARSQANS 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  370 VQKEsMDTI-----NHASQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRSRQPFFTQR---- 440
Cdd:pfam15921  297 IQSQ-LEIIqeqarNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnl 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  441 ---------ELVDEEADEAYELLSQAESWQRLHNETRTLfPVVLEQLDDYNAKLSDLqEALDQALNYVRDAEdMNRATAA 511
Cdd:pfam15921  376 ddqlqkllaDLHKREKELSLEKEQNKRLWDRDTGNSITI-DHLRRELDDRNMEVQRL-EALLKAMKSECQGQ-MERQMAA 452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  512 RQRDHEKQQE----------------RVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASgiyAEIDGAKSELQVK 575
Cdd:pfam15921  453 IQGKNESLEKvssltaqlestkemlrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATN---AEITKLRSRVDLK 529
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  576 LSNLSNLSHDLvqeaiDHAQDLQQEANELSRKLHSSD--MNGLVQKaldasnvYENIVNYVSEANETAefalnttdriyd 653
Cdd:pfam15921  530 LQELQHLKNEG-----DHLRNVQTECEALKLQMAEKDkvIEILRQQ-------IENMTQLVGQHGRTA------------ 585
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  654 avsgidTQIIYHKDESENLLNQAR-ELQakaESSSDEAVADTSRRvggalarksALKTRLSD----AVKQLQAaergdAQ 728
Cdd:pfam15921  586 ------GAMQVEKAQLEKEINDRRlELQ---EFKILKDKKDAKIR---------ELEARVSDleleKVKLVNA-----GS 642
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  729 QRLGQSRLITEEANRTTMEVQQATAPMaNNLTNWSQNLQ-HF--DSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVE-Q 804
Cdd:pfam15921  643 ERLRAVKDIKQERDQLLNEVKTSRNEL-NSLSEDYEVLKrNFrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgS 721
                          570       580       590
                   ....*....|....*....|....*....|
gi 2217361438  805 KRPASNVSASIQR-IRELIAQTRSVASKIQ 833
Cdd:pfam15921  722 DGHAMKVAMGMQKqITAKRGQIDALQSKIQ 751
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
132-184 1.72e-11

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 60.44  E-value: 1.72e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217361438  132 CPCPlpHLANFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNPLLIGSTC 184
Cdd:pfam00053    1 CDCN--PHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
321-647 2.19e-11

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: 69.32  E-value: 2.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  321 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINN 400
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  401 KMLYYGEEHELSPKEISEKLVLAQKMLEEIRSRQPFFT-QRELVDEEADEAYELLSQAESWQRLHNETRTLFPVVLEQLD 479
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELEsLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  480 DYNAKLSDLQEALDQalnyvrdAEDMNRATAARQRDHEKQQERVreQMEVVNMSLSTSADSLTTprlTLSELDDIIKNAS 559
Cdd:TIGR02168  397 SLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE---LQEELERLEEALE 464
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  560 GIYAEIDGAKSELQVKLSNLSNLSH--DLVQEAIDHAQDLQQEANELsrKLHSSDMNGLVQKALDASNV---YE------ 628
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVdegYEaaieaa 542
                          330       340
                   ....*....|....*....|..
gi 2217361438  629 ---NIVNYVSEANETAEFALNT 647
Cdd:TIGR02168  543 lggRLQAVVVENLNAAKKAIAF 564
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
81-130 3.23e-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: 60.06  E-value: 3.23e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217361438   81 PCDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIRGAPqfCQ 130
Cdd:cd00055      1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
132-177 4.17e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 59.25  E-value: 4.17e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2217361438   132 CPCPLPHlaNFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNP 177
Cdd:smart00180    1 CDCDPGG--SASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
875-1013 8.80e-11

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: 61.28  E-value: 8.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  875 TETADQFILYLGSKnaKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVS--SWpayfSIVKIERVGKHgkVFLTVPSL 952
Cdd:pfam02210    3 TRQPNGLLLYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQ 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217361438  953 SSTAEEKfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNN 1013
Cdd:pfam02210   75 TVVSSLP-------PGESLLLNLN---GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
65-257 2.80e-10

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: 60.78  E-value: 2.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438   65 EKCNAGFFhTLSGECvpCDcngnsnECLDGSGYCVHCQRNTTGehCEKCLDGYIGDSIRGAPQFCQPC-PCplPHLANFA 143
Cdd:cd13416      1 EACPSGQY-TSSGEC--CE------QCPPGEGVARPCGDNQTV--CEPCLDGVTFSDVVSHTEPCQPCtRC--PGLMSMR 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  144 ESCYRKNGAVrcicnenyagpnCErCAPGYYGNPLliGSTCKKCDCsgnsdpnlifedCDEVTGQCRNC--LRNTtgfKC 221
Cdd:cd13416     68 APCTATHDTV------------CE-CAYGYYLDED--SGTCEPCTV------------CPPGQGVVQSCgpNQDT---VC 117
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2217361438  222 ERCAPGYYGDARIAKN----CAVCncggGPCDSVTGECLE 257
Cdd:cd13416    118 EACPEGTYSDEDSSTDpclpCTVC----EDGEVELRECTP 153
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
82-129 6.47e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.21  E-value: 6.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217361438   82 CDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIrGAPQFC 129
Cdd:pfam00053    1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
82-121 4.70e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.47  E-value: 4.70e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2217361438    82 CDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDS 121
Cdd:smart00180    1 CDCDPGgsaSGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
319-731 2.43e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 59.01  E-value: 2.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  319 YLLKTKLseRENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESmdtinhasQLVEQAHDMRDKIQEI 398
Cdd:COG4717     45 AMLLERL--EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--------ELEEELEELEAELEEL 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  399 NNKMLYYgeEHELSPKEISEKLVLAQKMLEEIRSRQPFFTQRELVDEEADEAYE-LLSQAESWQR-LHNETRTLFPVVLE 476
Cdd:COG4717    115 REELEKL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeLEAELAELQEeLEELLEQLSLATEE 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  477 QLDDYNAKLSDLQEALDQALNYVRDAEDmNRATAARQRD-------HEKQQERVREQMEVVN-----MSLSTSADSLTTP 544
Cdd:COG4717    193 ELQDLAEELEELQQRLAELEEELEEAQE-ELEELEEELEqleneleAAALEERLKEARLLLLiaaalLALLGLGGSLLSL 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  545 RLTL----------------------SELDDIIKNASGIYAEIDGAKSELQVKLSNL---SNLSHDLVQEAIDHAQDLQQ 599
Cdd:COG4717    272 ILTIagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQE 351
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  600 ---EANELSRKLHSSDMNGLVQKALDASNV-----YENIVNYVSEANETAEfalnttdriydAVSGIDTQIIYHKDESEN 671
Cdd:COG4717    352 llrEAEELEEELQLEELEQEIAALLAEAGVedeeeLRAALEQAEEYQELKE-----------ELEELEEQLEELLGELEE 420
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217361438  672 LLNQARELQAKAE-SSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRL 731
Cdd:COG4717    421 LLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
321-743 2.67e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 2.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  321 LKTKLSERENQYALRKIQinNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINN 400
Cdd:COG1196    218 LKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  401 KMLyyGEEHELSPKEisEKLVLAQKMLEEIRSRqpfftQRELVDEEADEAYELLSQAESWQRLHNETRTLfpvvLEQLDD 480
Cdd:COG1196    296 ELA--RLEQDIARLE--ERRRELEERLEELEEE-----LAELEEELEELEEELEELEEELEEAEEELEEA----EAELAE 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  481 YNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASG 560
Cdd:COG1196    363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  561 IYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHSSDMnglvqkALDASNVYENIVNYVSEANET 640
Cdd:COG1196    443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL------LLEAEADYEGFLEGVKAALLL 516
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  641 AEFALnttdriydaVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADtsRRVGGALARKSALKTRL-SDAVKQL 719
Cdd:COG1196    517 AGLRG---------LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATFLpLDKIRAR 585
                          410       420
                   ....*....|....*....|....
gi 2217361438  720 QAAERGDAQQRLGQSRLITEEANR 743
Cdd:COG1196    586 AALAAALARGAIGAAVDLVASDLR 609
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
311-610 2.82e-08

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: 59.30  E-value: 2.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  311 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHD 390
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  391 MRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRSRqpFFTQRELVDEEADEAYELLSQAESWQRLHNETRTL 470
Cdd:TIGR02168  773 AEEELAEAEAEI----EELEAQIEQLKEELKALREALDELRAE--LTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  471 FPVVLEQLDDYNAKLSDLQEALDQAlnyvrdAEDMNRATAARQRdHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSE 550
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEEL------ESELEALLNERAS-LEEALALLRSELEELSEELRELESKRSELRRELEE 919
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  551 LDDIIKNASgiyAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHS 610
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 ...
327-749 3.31e-08

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: 58.68  E-value: 3.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  327 ERENQYALRKIqINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINhasQL-VEQAHD--MRDKIQEInnkml 403
Cdd:pfam10174  224 DPAKTKALQTV-IEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK---QMeVYKSHSkfMKNKIDQL----- 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  404 yygeEHELSPKEiSEKLVLaQKMLEEIRSRQPFFTQRELVDEEADEAYEllsqaeswQR---LHNETRTLfPVVLEQ--- 477
Cdd:pfam10174  295 ----KQELSKKE-SELLAL-QTKLETLTNQNSDCKQHIEVLKESLTAKE--------QRaaiLQTEVDAL-RLRLEEkes 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  478 -LDDYNAKLSDLQEALDQALNYVRDAEDM----NRATAARQ----------RDHEKQQERVREQMEVVNMSLSTSADSLT 542
Cdd:pfam10174  360 fLNKKTKQLQDLTEEKSTLAGEIRDLKDMldvkERKINVLQkkienlqeqlRDKDKQLAGLKERVKSLQTDSSNTDTALT 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  543 TPRLTLSELDDIIKNASGIYA--------EIDGAKSELQVKLSNLSNLSHDL------VQEAIDHAQDLQQEANELSRKL 608
Cdd:pfam10174  440 TLEEALSEKERIIERLKEQREredrerleELESLKKENKDLKEKVSALQPELtekessLIDLKEHASSLASSGLKKDSKL 519
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  609 HSSDMNglVQKALDASNVYENIVNYVSEANETAEFALNTTDRIydavSGIDTQIIYHKDES-------ENLLNQARELQA 681
Cdd:pfam10174  520 KSLEIA--VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRI----RLLEQEVARYKEESgkaqaevERLLGILREVEN 593
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217361438  682 KaESSSDEAVADTSRRVggalARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQ 749
Cdd:pfam10174  594 E-KNDKDKKIAELESLT----LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ 656
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
311-751 4.67e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 4.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  311 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHD 390
Cdd:COG1196    283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  391 MRDKIQEINNKMLyyGEEHELSpKEISEKLVLAQKMLEEIRSRQpffTQRELVDEEADEAYELLSQAESWQRLHNETRTL 470
Cdd:COG1196    363 AEEALLEAEAELA--EAEEELE-ELAEELLEALRAAAELAAQLE---ELEEAEEALLERLERLEEELEELEEALAELEEE 436
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  471 FPVVLEQLDDYNAKLSDLQEALDQALNYVRDAE------DMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTP 544
Cdd:COG1196    437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLeeaallEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  545 RLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQD-----------LQQEANELSRKLHSSDM 613
Cdd:COG1196    517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratflplDKIRARAALAAALARGA 596
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  614 NGLVQKALDASNVYENIVNYV-----------SEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAK 682
Cdd:COG1196    597 IGAAVDLVASDLREADARYYVlgdtllgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217361438  683 AESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQA 751
Cdd:COG1196    677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
318-745 2.02e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  318 IYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQE 397
Cdd:COG1196    234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  398 INNKMLYYGEEHElspkEISEKLVLAQKMLEEIRsrqpffTQRELVDEEADEAYELLSQAEswQRLHNETRTLFPVVLEQ 477
Cdd:COG1196    314 LEERLEELEEELA----ELEEELEELEEELEELE------EELEEAEEELEEAEAELAEAE--EALLEAEAELAEAEEEL 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  478 LDDYNAKLSDLQEALDQAlNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKN 557
Cdd:COG1196    382 EELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  558 ASGIYAEIDGAKSELQVKLSNLSNLSHDLVQ--EAIDHAQDLQQEANELSRKLHSSDMNGLVQKALDAsnvyENIVNYVS 635
Cdd:COG1196    461 LLELLAELLEEAALLEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV----LIGVEAAY 536
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  636 EANETAEFALNTTDRIYDAVSGIDTQIIYHKDESEN-----LLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKT 710
Cdd:COG1196    537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2217361438  711 RLSDAVkQLQAAERGDAQQRLGQSRLITEEANRTT 745
Cdd:COG1196    617 VLGDTL-LGRTLVAARLEAALRRAVTLAGRLREVT 650
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
298-753 2.41e-07

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


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 55.68  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  298 VLSVSSGAAAHRHVNEINATIYLLKTklsERENQYALRKIQ--INNAENTMKS-LLSDVEELVEKENQAsrkgqlvQKES 374
Cdd:COG5278     19 LLLLVLGVLSYLSLNRLREASEWVEH---TYEVLRALEELLsaLLDAETGQRGyLLTGDESFLEPYEEA-------RAEI 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  375 MDTINHASQLVEQAHDMRDKIQEINNKMLYYGEEHELS-------PKEISEKLVLA---QKMLEEIRSRQpfFTQRELVD 444
Cdd:COG5278     89 DELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVialrragGLEAALALVRSgegKALMDEIRARL--LLLALALA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  445 EEADEAYELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVR 524
Cdd:COG5278    167 ALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLL 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  525 EQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNAsgiyAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANEL 604
Cdd:COG5278    247 AALLLALLAALALAALLAAALLALAALLLALAAA----AALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  605 SRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAE 684
Cdd:COG5278    323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217361438  685 SSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQATA 753
Cdd:COG5278    403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAV 471
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
374-851 2.45e-07

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


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 55.68  E-value: 2.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  374 SMDTINHASQLVEQAHDMRDKIQEINNKM----------LYYGEEHELspkeiseklvlaqkmleeirsrQPFFTQRELV 443
Cdd:COG5278     31 SLNRLREASEWVEHTYEVLRALEELLSALldaetgqrgyLLTGDESFL----------------------EPYEEARAEI 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  444 DEEADEAYELLSQAESWQRLhnetrtlfpvvLEQLDD-YNAKLSDLQEAL--------DQALNYVRDAEDMNRATAARQR 514
Cdd:COG5278     89 DELLAELRSLTADNPEQQAR-----------LDELEAlIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIRAR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  515 DHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHA 594
Cdd:COG5278    158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  595 QDLQQEANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLN 674
Cdd:COG5278    238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  675 QARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQATAP 754
Cdd:COG5278    318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  755 MANNLTNWSQNLQHFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASKIQV 834
Cdd:COG5278    398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
                          490
                   ....*....|....*..
gi 2217361438  835 SMMFDGQSAVEVHSRTS 851
Cdd:COG5278    478 AAAAAALAEAEAAAALA 494
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
529-757 2.62e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.84  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  529 VVNMSLSTSADslTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDL--VQEAIDhaqDLQQEANELSR 606
Cdd:COG3883      5 ALAAPTPAFAD--PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  607 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 681
Cdd:COG3883     80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  682 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQA------AERGDAQQRLGQSRLITEEANRTTMEVQQATAPM 755
Cdd:COG3883    158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAqlaeleAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236

                   ..
gi 2217361438  756 AN 757
Cdd:COG3883    237 AA 238
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
312-528 2.83e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 54.15  E-value: 2.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  312 NEINATIYLLKTKLSERENQYAlrkiQINNAENTMKSLLSDVEEL----------VEKENQ----ASRKGQLVQ--KESM 375
Cdd:COG1340     81 DELNEKLNELREELDELRKELA----ELNKAGGSIDKLRKEIERLewrqqtevlsPEEEKElvekIKELEKELEkaKKAL 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  376 DTINHASQLVEQAHDMRDKIQEINNKMlyygeehelspKEISEKlvlAQKMLEEIRSRqpfFTQRELVDEEADEAYELLS 455
Cdd:COG1340    157 EKNEKLKELRAELKELRKEAEEIHKKI-----------KELAEE---AQELHEEMIEL---YKEADELRKEADELHKEIV 219
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438  456 QA-ESWQRLHnetrtlfpvvlEQLDDYNAKLSDLQEALDQALNYVRDAEdmnrataaRQRDHEKQQERVREQME 528
Cdd:COG1340    220 EAqEKADELH-----------EEIIELQKELRELRKELKKLRKKQRALK--------REKEKEELEEKAEEIFE 274
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
418-833 4.08e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.16  E-value: 4.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  418 EKLVLAQKMLEEIRSRQPfftqrELVDEEADEAYELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQALN 497
Cdd:COG4717     49 ERLEKEADELFKPQGRKP-----ELNLKELKELEEELKEAEEKEEEYAELQ-------EELEELEEELEELEAELEELRE 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  498 YVRDAEDMNRAtaarqRDHEKQQERVREQMEvvnmSLSTSADSLTTPRLTLSELDDIIKNASgiyAEIDGAKSELQVKLS 577
Cdd:COG4717    117 ELEKLEKLLQL-----LPLYQELEALEAELA----ELPERLEELEERLEELRELEEELEELE---AELAELQEELEELLE 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  578 NLSNLSHDLVQEAIDHAQDLQQEANELSRKL---------HSSDMNGLVQKALDAsNVYENIVNY-------------VS 635
Cdd:COG4717    185 QLSLATEEELQDLAEELEELQQRLAELEEELeeaqeeleeLEEELEQLENELEAA-ALEERLKEArlllliaaallalLG 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  636 EANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSS--DEAVADTSRRVGGALARKSALKTRLS 713
Cdd:COG4717    264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELL 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  714 DAVKQLQAA--ERGDAQQRLGQSRLITE------------------------EANRTTMEVQQATAPMANNLTNWSQNLQ 767
Cdd:COG4717    344 DRIEELQELlrEAEELEEELQLEELEQEiaallaeagvedeeelraaleqaeEYQELKEELEELEEQLEELLGELEELLE 423
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217361438  768 HFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSASiQRIRELIAQTRSVASKIQ 833
Cdd:COG4717    424 ALDEEELEEELEELEEELEELEEELEELREELAELEAEL--EQLEED-GELAELLQELEELKAELR 486
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
321-677 5.39e-07

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 54.46  E-value: 5.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  321 LKTKLSERENQY--ALRKI--QINNAEntmkSLLSDVEELVEKEN-QASRKGQLVQKESMDTINH-----ASQLVEQAHD 390
Cdd:PRK04778   152 LRKSLLANRFSFgpALDELekQLENLE----EEFSQFVELTESGDyVEAREILDQLEEELAALEQimeeiPELLKELQTE 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  391 MRDKIQEINN---KML---YYGEEHELSP--KEISEKLVLAQKMLEEI---RSRQpfftQRELVDEEADEAYELLsQAES 459
Cdd:PRK04778   228 LPDQLQELKAgyrELVeegYHLDHLDIEKeiQDLKEQIDENLALLEELdldEAEE----KNEEIQERIDQLYDIL-EREV 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  460 wqRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQ-ALNYVRDAEDMnrataARQRDHEKQQERVREQMEVVnmslstsA 538
Cdd:PRK04778   303 --KARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRvKQSYTLNESEL-----ESVRQLEKQLESLEKQYDEI-------T 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  539 DSLTTPRLTLSELDDIIKNASGIYAEIDgaksELQVKLSN-LSNLSHDlVQEAIDHAQDLQQEANELSRKLHSSDMNGLV 617
Cdd:PRK04778   369 ERIAEQEIAYSELQEELEEILKQLEEIE----KEQEKLSEmLQGLRKD-ELEAREKLERYRNKLHEIKRYLEKSNLPGLP 443
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438  618 QKALDAsnvYENIVNYVSEANEtaefALNTT----DRIYDAVSGIDTQIIYHKDESENLLNQAR 677
Cdd:PRK04778   444 EDYLEM---FFEVSDEIEALAE----ELEEKpinmEAVNRLLEEATEDVETLEEETEELVENAT 500
growth_prot_Scy NF041483
polarized growth protein Scy;
354-855 7.63e-07

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 54.45  E-value: 7.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  354 EELVEKENQASRKgqlvQKESMDTINHASQLVEQahdmrdkiqeinnkmlyygeEHELSPKEISEKLVLAQKMLEEIRSR 433
Cdd:NF041483   699 EALAAAQEEAARR----RREAEETLGSARAEADQ--------------------ERERAREQSEELLASARKRVEEAQAE 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  434 qpffTQReLVdEEADE-AYELLSQAESwqrlhnetrtlfpvVLEQLDDynaKLSDLQEALDQALNYVRDAEDMnraTAAR 512
Cdd:NF041483   755 ----AQR-LV-EEADRrATELVSAAEQ--------------TAQQVRD---SVAGLQEQAEEEIAGLRSAAEH---AAER 808
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  513 QRDhEKQQE--RVReqmevvnmslstsADSLTTpRLTLSEldDIIKNASGIYAEIDGAKSelqvklsnlsnLSHDLVQEA 590
Cdd:NF041483   809 TRT-EAQEEadRVR-------------SDAYAE-RERASE--DANRLRREAQEETEAAKA-----------LAERTVSEA 860
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  591 IDHAQDLQQEANELSRKLHSSDMNGLVQKALDASNVYenivnyvSEANETAefalnttDRI-YDAVSGIDTQIIYHKDES 669
Cdd:NF041483   861 IAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTR-------ADAREDA-------NRIrSDAAAQADRLIGEATSEA 926
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  670 ENLLNQARelqAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQL--QAAER-GDAQQRLGQSRlitEEANRTTM 746
Cdd:NF041483   927 ERLTAEAR---AEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLraEAAETvGSAQQHAERIR---TEAERVKA 1000
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  747 EvqqaTAPMANNLTNWSQN-----LQHFDSSAYNTAVNSARDAVRNLTEVVPQlLDQLRTVEQKRPASNVSASIQRIREL 821
Cdd:NF041483  1001 E----AAAEAERLRTEAREeadrtLDEARKDANKRRSEAAEQADTLITEAAAE-ADQLTAKAQEEALRTTTEAEAQADTM 1075
                          490       500       510
                   ....*....|....*....|....*....|....
gi 2217361438  822 IAQTRSVASKIQVSMMFDGQSAVEvHSRTSMDDL 855
Cdd:NF041483  1076 VGAARKEAERIVAEATVEGNSLVE-KARTDADEL 1108
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
415-767 1.26e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  415 EISEKLVLAQKMLEEIRSR--QPFFTQRELVDEEADEAYELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEAL 492
Cdd:COG4372      3 RLGEKVGKARLSLFGLRPKtgILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------EELEQLEEELEQARSEL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  493 DQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEvvnmSLSTSADSLttprltLSELDDIIKNASGIYAEIDGAKSEL 572
Cdd:COG4372     76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE----ELQEELEEL------QKERQDLEQQRKQLEAQIAELQSEI 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  573 QVKLSNLSNLSHDLvQEAIDHAQDLQQEANELSRKLHSSDMNGLVQKAldasnvyENIVNYVSEANETAEFALNTTDRIY 652
Cdd:COG4372    146 AEREEELKELEEQL-ESLQEELAALEQELQALSEAEAEQALDELLKEA-------NRNAEKEEELAEAEKLIESLPRELA 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  653 DAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLG 732
Cdd:COG4372    218 EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2217361438  733 QSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQ 767
Cdd:COG4372    298 LALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
313-674 1.33e-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: 53.49  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  313 EINATIYLLKTKLSERENQYALRKIQINNAENTMKSL---LSDVEELVEKENQASRKGQ--LVQKESM-DTIN-HASQLV 385
Cdd:TIGR04523  430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLetqLKVLSRSINKIKQNLEQKQkeLKSKEKElKKLNeEKKELE 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  386 EQAHDMRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRSRqpffTQRELVDEEADEAYELLSQaeswqrLHN 465
Cdd:TIGR04523  510 EKVKDLTKKISSLKEKI----EKLESEKKEKESKISDLEDELNKDDFE----LKKENLEKEIDEKNKEIEE------LKQ 575
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  466 ETRTLfpvvleqlddyNAKLSDLQEALDQalnyvrdaedmnrataarqrdHEKQQERVREQMEVVNMSLSTSADSLTTPR 545
Cdd:TIGR04523  576 TQKSL-----------KKKQEEKQELIDQ---------------------KEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  546 LTLSELDDIIKNasgiyaeIDGAKSELQVKLSNLsnlsHDLVQEAIDHAQDLQQEANELSRKLhsSDMNGLVQKALDASN 625
Cdd:TIGR04523  624 KENEKLSSIIKN-------IKSKKNKLKQEVKQI----KETIKEIRNKWPEIIKKIKESKTKI--DDIIELMKDWLKELS 690
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2217361438  626 VYENivNYVSEANETAEfaLNTTDRIYDAVSGIDTQIIYHKDESENLLN 674
Cdd:TIGR04523  691 LHYK--KYITRMIRIKD--LPKLEEKYKEIEKELKKLDEFSKELENIIK 735
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
338-611 2.03e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 51.45  E-value: 2.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  338 QINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINNKMlyygEEHELSPKEIS 417
Cdd:COG1340      9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV----KELKEERDELN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  418 EKLVLAQKMLEEIRSRQPfftQRELVDEEADEAYELLSQAEsWQRlhnETRTLFP----VVLEQLDDYNAKLSDLQEALD 493
Cdd:COG1340     85 EKLNELREELDELRKELA---ELNKAGGSIDKLRKEIERLE-WRQ---QTEVLSPeeekELVEKIKELEKELEKAKKALE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  494 QALNYVrdaEDMNRATAARqrdheKQQERVREQMEvvnmSLSTSADSLTTprltlsELDDIIKNASGIYAEIDGAKSELq 573
Cdd:COG1340    158 KNEKLK---ELRAELKELR-----KEAEEIHKKIK----ELAEEAQELHE------EMIELYKEADELRKEADELHKEI- 218
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2217361438  574 VKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHSS 611
Cdd:COG1340    219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
456-831 2.25e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  456 QAESWQRLHNETRTLfpvvleQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLS 535
Cdd:COG1196    211 KAERYRELKEELKEL------EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  536 TSADSLttpRLTLSELddiiknasgiyAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHSSDMng 615
Cdd:COG1196    285 EAQAEE---YELLAEL-----------ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-- 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  616 LVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTS 695
Cdd:COG1196    349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  696 RRVGGALARKSALKTRLSDAVKQLQAAERGDAQQR----LGQSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDS 771
Cdd:COG1196    429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEllaeLLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  772 SAYNTAVNSARDAvrnltevVPQLLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASK 831
Cdd:COG1196    509 GVKAALLLAGLRG-------LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
309-573 2.78e-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: 52.76  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  309 RHVNEINATIYLLKTKLSERENQYAlrkiQINNAENTMKSLLSDVEELVEKENQAsrkgQLVQKESMDTIN-HASQLVEQ 387
Cdd:TIGR02169  702 NRLDELSQELSDASRKIGEIEKEIE----QLEQEEEKLKERLEELEEDLSSLEQE----IENVKSELKELEaRIEELEED 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  388 AHDMRDKIQEInnkmlyygeEHELSPKEISEKLVLAQKmLEEIRSRQPFFTQ---RELVDEEADEAY------ELLSQAE 458
Cdd:TIGR02169  774 LHKLEEALNDL---------EARLSHSRIPEIQAELSK-LEEEVSRIEARLReieQKLNRLTLEKEYlekeiqELQEQRI 843
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  459 SWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQALNYVRDAEDmnrataaRQRDHEKQQERVREQMEVVNMSLSTSA 538
Cdd:TIGR02169  844 DLKEQIKSIE-------KEIENLNGKKEELEEELEELEAALRDLES-------RLGDLKKERDELEAQLRELERKIEELE 909
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2217361438  539 DSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQ 573
Cdd:TIGR02169  910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
314-574 3.80e-06

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: 52.36  E-value: 3.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  314 INATIYLLKTKLSERENQYAlrkiQINNAENTMKSLLSDV---EELVEKENQASRK-GQLVQK-ESMDTINHASQLVEQA 388
Cdd:TIGR00606  756 VNRDIQRLKNDIEEQETLLG----TIMPEEESAKVCLTDVtimERFQMELKDVERKiAQQAAKlQGSDLDRTVQQVNQEK 831
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  389 HDMRDKIQEINNKmlyyGEEHELSPKEISEKLVLAQKMLEEIRS-----------RQPFFTQRELVDEEADEAYELLSQA 457
Cdd:TIGR00606  832 QEKQHELDTVVSK----IELNRKLIQDQQEQIQHLKSKTNELKSeklqigtnlqrRQQFEEQLVELSTEVQSLIREIKDA 907
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  458 --------ESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQAL-------NYVRDAED---MNRAT-----AARQR 514
Cdd:TIGR00606  908 keqdspleTFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkdieNKIQDGKDdylKQKETelntvNAQLE 987
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438  515 DHEKQQERVREQMEVVNMSLSTS--ADSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQV 574
Cdd:TIGR00606  988 ECEKHQEKINEDMRLMRQDIDTQkiQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQV 1049
mukB PRK04863
chromosome partition protein MukB;
440-821 4.05e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 52.27  E-value: 4.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  440 RELVDEEAD---EAYELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQA---LNYVRDAEDMNRATAARQ 513
Cdd:PRK04863   282 RVHLEEALElrrELYTSRRQLAAEQYRLVEMA-------RELAELNEAESDLEQDYQAAsdhLNLVQTALRQQEKIERYQ 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  514 RDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELD-------------DIIKNASGIYAE----IDGAKSELQVKL 576
Cdd:PRK04863   355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDelksqladyqqalDVQQTRAIQYQQavqaLERAKQLCGLPD 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  577 SNLSNLShDLVQEAIDHAQDLQQEANELSRKLHSSDMnglvqkaldasnvyenivnyvseANETAEFALNTTDRIYDAVS 656
Cdd:PRK04863   435 LTADNAE-DWLEEFQAKEQEATEELLSLEQKLSVAQA-----------------------AHSQFEQAYQLVRKIAGEVS 490
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  657 GIDTQiiyhkDESENLLNQARELQAKAEsssdeavadtsrRVGGALARKSALKTRLsdavKQLQAAER--GDAQQRLGQS 734
Cdd:PRK04863   491 RSEAW-----DVARELLRRLREQRHLAE------------QLQQLRMRLSELEQRL----RQQQRAERllAEFCKRLGKN 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  735 --------RLITE-EANRTTMEVQQATA-----PMANNLTNWSQNLQHFDSSA-----YNTAVNSARDAV-------RNL 788
Cdd:PRK04863   550 lddedeleQLQEElEARLESLSESVSEArerrmALRQQLEQLQARIQRLAARApawlaAQDALARLREQSgeefedsQDV 629
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2217361438  789 TEVVPQLLDQLR--TVEQKRPASNVSASIQRIREL 821
Cdd:PRK04863   630 TEYMQQLLERERelTVERDELAARKQALDEEIERL 664
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
313-718 4.15e-06

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: 51.89  E-value: 4.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  313 EINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEEL---VEKENQASRKGQLVQKESMDTINHASQLVEQAH 389
Cdd:TIGR00618  553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqdlTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  390 DMRDKIQEINNKMLY-YGEEHELSPKEISEKLVLA---QKMLEEIRSRQPFFTQRELVDEEADEayELLSQAESWQR-LH 464
Cdd:TIGR00618  633 HLQQCSQELALKLTAlHALQLTLTQERVREHALSIrvlPKELLASRQLALQKMQSEKEQLTYWK--EMLAQCQTLLReLE 710
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  465 NETRTLFPVVLEQLDDYNAKLSDLQ---EALDQALNYVR-------------DAEDMNRATAARQRDHEKQQerVREQME 528
Cdd:TIGR00618  711 THIEEYDREFNEIENASSSLGSDLAareDALNQSLKELMhqartvlkarteaHFNNNEEVTAALQTGAELSH--LAAEIQ 788
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  529 VVNMSLSTSADSLttpRLTLSEL------DDIIKNASGIyaEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEAn 602
Cdd:TIGR00618  789 FFNRLREEDTHLL---KTLEAEIgqeipsDEDILNLQCE--TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA- 862
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  603 ELSRKlhSSDMNGLVQKAldasNVYENIVNYVsEANETAEFALNTTdriYDAVsgIDTQIIYH-------KDESENllnq 675
Cdd:TIGR00618  863 QLTQE--QAKIIQLSDKL----NGINQIKIQF-DGDALIKFLHEIT---LYAN--VRLANQSEgrfhgryADSHVN---- 926
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2217361438  676 ARELQAKAE---SSSDEAVADTSRRVGGALARKS-ALKTRLSDAVKQ 718
Cdd:TIGR00618  927 ARKYQGLALlvaDAYTGSVRPSATLSGGETFLASlSLALALADLLST 973
ApoLp-III_like cd13769
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ...
710-836 4.17e-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: 4.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  710 TRLSDAVKQLQAAERGDAQQRLGQSRL-ITEEANRTtmeVQQATAPMANNLTNWSQNLQHFDSSAYNTAVNSARDAVRNL 788
Cdd:cd13769      1 TQLSELIQKAQEAINNLAQQVQKQLGLqNPEEVVNT---LKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKL 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2217361438  789 TEVVPQLLDQLRTVEQkrpASNVSASIQ-RIRELIAQTRSVASKIQVSM 836
Cdd:cd13769     78 SETVPELRKSLPVEEK---AQELQAKLQsGLQTLVTESQKLAKAISENS 123
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
339-531 4.26e-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: 4.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  339 INNAENTMKSL-----LSDVEELVEKeNQASRKGQLVQKESMDTIN-HASQLVEQAHDMRDKIQE----INNKMlyygee 408
Cdd:cd00176     16 LSEKEELLSSTdygddLESVEALLKK-HEALEAELAAHEERVEALNeLGEQLIEEGHPDAEEIQErleeLNQRW------ 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  409 helspKEISEKLVLAQKMLEEIRSRQPFFTQrelVDEEADEAYELLSQAESWQRLHNETRtlfpvVLEQLDdynaKLSDL 488
Cdd:cd00176     89 -----EELRELAEERRQRLEEALDLQQFFRD---ADDLEQWLEEKEAALASEDLGKDLES-----VEELLK----KHKEL 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2217361438  489 QEALDQALNYVRDAEDMNRATAARQrdHEKQQERVREQMEVVN 531
Cdd:cd00176    152 EEELEAHEPRLKSLNELAEELLEEG--HPDADEEIEEKLEELN 192
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
309-579 6.97e-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: 51.22  E-value: 6.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  309 RHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDvEELVEKENQASRKGQLVQKEsmDTINHASQLVEQA 388
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE-EQLRVKEKIGELEAEIASLE--RSIAEKERELEDA 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  389 HDMRDKIQEINNKMLyygEEHELSPKEISEKLVLAQKMLEEIRSRQpfftqrelvdeeaDEAYELLSQAESWQRLHNETR 468
Cdd:TIGR02169  321 EERLAKLEAEIDKLL---AEIEELEREIEEERKRRDKLTEEYAELK-------------EELEDLRAELEEVDKEFAETR 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  469 TLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEdmnrataARQRDHEKQQERVREQ-------MEVVNMSLSTSADSL 541
Cdd:TIGR02169  385 DELKDYREKLEKLKREINELKRELDRLQEELQRLS-------EELADLNAAIAGIEAKineleeeKEDKALEIKKQEWKL 457
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2217361438  542 TTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNL 579
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
Laminin_G_1 pfam00054
Laminin G domain;
1263-1376 9.65e-06

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 46.93  E-value: 9.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1263 FRTLQPNGLLFYYAS--GSDVFSISLDNG--TVIMDV-KGIKVQSVDKQYNDGLSHFVISSVSPTRYELIVDK-SRVGSK 1336
Cdd:pfam00054    1 FRTTEPSGLLLYNGTqtERDFLALELRDGrlEVSYDLgSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2217361438 1337 NPTKGKieQTQASEKKFYFGGSPISAQYA-------NFTGCISNAYF 1376
Cdd:pfam00054   81 SPLGAT--TDLDVDGPLYVGGLPSLGVKKrrlaispSFDGCIRDVIV 125
PTZ00121 PTZ00121
MAEBL; Provisional
320-608 9.92e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 9.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  320 LLKTKLSERENQYALRKiqinNAENTMKsllsdVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEIN 399
Cdd:PTZ00121  1680 AKKAEEDEKKAAEALKK----EAEEAKK-----AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  400 NkmlyygEEHElsPKEISEKLVLAQKMLEEIRSRQPFFTQRELVDEEADEAYELlsqaeswQRLHNETRTLFPVVLEQLD 479
Cdd:PTZ00121  1751 K------DEEE--KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV-------DKKIKDIFDNFANIIEGGK 1815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  480 DYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKnas 559
Cdd:PTZ00121  1816 EGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEK--- 1892
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2217361438  560 giyaeIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKL 608
Cdd:PTZ00121  1893 -----IDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEI 1936
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
321-678 2.29e-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: 49.66  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  321 LKTKLS--ERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEI 398
Cdd:TIGR01612 2049 IKEKIDnyEKEKEKFGIDFDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKII 2128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  399 NNKMLyygEEHELSPKeiseklvlaqkmLEEIRSRQPFFTQRELVDEeadeayeLLSQAESWQRLHNETRTLFPVVLEQL 478
Cdd:TIGR01612 2129 EDKII---EKNDLIDK------------LIEMRKECLLFSYATLVET-------LKSKVINHSEFITSAAKFSKDFFEFI 2186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  479 DDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNM--------SLSTSADSLTTPRLTL-- 548
Cdd:TIGR01612 2187 EDISDSLNDDIDALQIKYNLNQTKKHMISILADATKDHNNLIEKEKEATKIINNltelftidFNNADADILHNNKIQIiy 2266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  549 --SELDDIIKNASGIYAEIDGakselqVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHssDMNGLVQKALDASNV 626
Cdd:TIGR01612 2267 fnSELHKSIESIKKLYKKINA------FKLLNISHINEKYFDISKEFDNIIQLQKHKLTENLN--DLKEIDQYISDKKNI 2338
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217361438  627 YENIVNyvseanETAEFALNTTDRIYDAVSGIDTQIiyhkDESENLLNQARE 678
Cdd:TIGR01612 2339 FLHALN------ENTNFNFNALKEIYDDIINRENKA----DEIENINNKENE 2380
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
521-764 2.41e-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: 49.66  E-value: 2.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  521 ERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKnaSGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQD---L 597
Cdd:TIGR01612  500 MRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNIK--AKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDsihL 577
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  598 QQEAN---------------------ELSRKLHS-SDMNGLVQKALDASNVYENIVNYVSEANETAEFA----LNTTDRI 651
Cdd:TIGR01612  578 EKEIKdlfdkyleiddeiiyinklklELKEKIKNiSDKNEYIKKAIDLKKIIENNNAYIDELAKISPYQvpehLKNKDKI 657
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  652 YDAVSGIDTQI--------------IYHKDESENLLNQAR--ELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 715
Cdd:TIGR01612  658 YSTIKSELSKIyeddidalynelssIVKENAIDNTEDKAKldDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDI 737
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2217361438  716 VKQLQAAERGDaqqrlgqsrlITEEANRTTMEVQQATAPMANNLTNWSQ 764
Cdd:TIGR01612  738 IVEIKKHIHGE----------INKDLNKILEDFKNKEKELSNKINDYAK 776
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
321-611 3.06e-05

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: 49.30  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  321 LKTKLSEREnQYALRKiQINNAENTMKSLLSDVEELvEKEnQASRKGQLvqkesmdtinhaSQLVEQAHDMRDKIQEINN 400
Cdd:TIGR02169  216 LLKEKREYE-GYELLK-EKEALERQKEAIERQLASL-EEE-LEKLTEEI------------SELEKRLEEIEQLLEELNK 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  401 KMLYYGEEHELSPKE---------------ISEKLVLAQKMLEEirsRQPFFTQRELVDEEADeayELLSQAESWQRlhn 465
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEkigeleaeiaslersIAEKERELEDAEER---LAKLEAEIDKLLAEIE---ELEREIEEERK--- 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  466 ETRTLFPVVLEQLDDYNAKLSDLQEAldqalnyvrDAEdmNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPR 545
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEV---------DKE--FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  546 LTLSELDDIIKNASGIYAEIDGAKSELQVKLS----NLSNLSHDLVQEAIDHaQDLQQEANELSRKLHSS 611
Cdd:TIGR02169  420 EELADLNAAIAGIEAKINELEEEKEDKALEIKkqewKLEQLAADLSKYEQEL-YDLKEEYDRVEKELSKL 488
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
310-766 3.47e-05

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: 48.70  E-value: 3.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  310 HVNEINATIYLLKTKLSERenqyALRKI--QINNAENTMKSLLSDVEELVEKEnqasrkgqlvqKESMDTINHAsqlveq 387
Cdd:pfam06160   68 LLFEAEELNDKYRFKKAKK----ALDEIeeLLDDIEEDIKQILEELDELLESE-----------EKNREEVEEL------ 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  388 ahdmRDKIQEINNKMLYYGeeHELSPKEisEKLvlaQKMLEEIRSRqpfFTQRELVDEEAD--EAYELLSQaeswqrLHN 465
Cdd:pfam06160  127 ----KDKYRELRKTLLANR--FSYGPAI--DEL---EKQLAEIEEE---FSQFEELTESGDylEAREVLEK------LEE 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  466 ETRTL------FPVVLEQL-DDYNAKLSDLQEALDQAL--NYVRD----AEDMNRATAARQRD----HEKQQERVREQME 528
Cdd:pfam06160  187 ETDALeelmedIPPLYEELkTELPDQLEELKEGYREMEeeGYALEhlnvDKEIQQLEEQLEENlallENLELDEAEEALE 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  529 VVNMSLSTSADSLTTprltlsELD---DIIKNASGIYAEIDGAKS---ELQVKLSNLsNLSHDLVQEAIDHAQDLQQEAN 602
Cdd:pfam06160  267 EIEERIDQLYDLLEK------EVDakkYVEKNLPEIEDYLEHAEEqnkELKEELERV-QQSYTLNENELERVRGLEKQLE 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  603 ELSRKLHSsdmngLVQKALDASNVYENIVNYVSEanetaefalnttdrIYDAVSGIDTQIIYHKDESENLLNQarELQAK 682
Cdd:pfam06160  340 ELEKRYDE-----IVERLEEKEVAYSELQEELEE--------------ILEQLEEIEEEQEEFKESLQSLRKD--ELEAR 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  683 AESSS-DEAVADTSRRVggalaRKSAL-------KTRLSDAVKQLQaaergDAQQRLGQSRLITEEANRttmEVQQATAP 754
Cdd:pfam06160  399 EKLDEfKLELREIKRLV-----EKSNLpglpesyLDYFFDVSDEIE-----DLADELNEVPLNMDEVNR---LLDEAQDD 465
                          490
                   ....*....|..
gi 2217361438  755 MaNNLTNWSQNL 766
Cdd:pfam06160  466 V-DTLYEKTEEL 476
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
313-579 4.80e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 4.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  313 EINATIYLLKTKLSERENQyalrKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKEsmdtinhasqlVEQAHDMR 392
Cdd:PRK03918   173 EIKRRIERLEKFIKRTENI----EELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----------VKELEELK 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  393 DKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRSRqpfftQRELvDEEADEAYELLSQAESWQRL---HNETRT 469
Cdd:PRK03918   238 EEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKE-----IEEL-EEKVKELKELKEKAEEYIKLsefYEEYLD 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  470 LFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVvnMSLSTSADSLTTpRLTLS 549
Cdd:PRK03918   308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA--KAKKEELERLKK-RLTGL 384
                          250       260       270
                   ....*....|....*....|....*....|
gi 2217361438  550 ELDDIIKNasgiYAEIDGAKSELQVKLSNL 579
Cdd:PRK03918   385 TPEKLEKE----LEELEKAKEEIEEEISKI 410
Laminin_G_1 pfam00054
Laminin G domain;
882-1013 8.34e-05

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 44.23  E-value: 8.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  882 ILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKDVEIPldSKPVSSwPAYFSIVKIERVGKHGkvFLTV---PSLSSTAEe 958
Cdd:pfam00054   10 LLYNGTQT-ERDFLALELRDGRLEVSYDLGSGAAVVR--SGDKLN-DGKWHSVELERNGRSG--TLSVdgeARPTGESP- 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217361438  959 kfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPTSL-NLPGFVGCLELATLNN 1013
Cdd:pfam00054   83 --------LGATTDLDVD---GPLYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNG 127
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
284-665 1.13e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  284 LRLAALSIEEGKSGVLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELvEKENQA 363
Cdd:COG4372     13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL-NEQLQA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  364 SRKGQLVQKESMDTINhasqlvEQAHDMRDKIQEINnkmlyygeehelspKEISEKLVLAQKMLEEIRSRQPFFTQRElv 443
Cdd:COG4372     92 AQAELAQAQEELESLQ------EEAEELQEELEELQ--------------KERQDLEQQRKQLEAQIAELQSEIAERE-- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  444 deeaDEAYELLSQAESWQRLhnetrtlfpvvLEQLDDYNAKLSD--LQEALDQALNYVRDAEDMNRATAARQRDHEKQQE 521
Cdd:COG4372    150 ----EELKELEEQLESLQEE-----------LAALEQELQALSEaeAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  522 RVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEA 601
Cdd:COG4372    215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438  602 NELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYH 665
Cdd:COG4372    295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
PRK01156 PRK01156
chromosome segregation protein; Provisional
311-725 3.93e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 45.28  E-value: 3.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  311 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRkgqlvqkesmdtinhasqLVEQAHD 390
Cdd:PRK01156   199 LENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNR------------------YESEIKT 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  391 MRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEE-IRSRQPFFTQREL---VDEEADEAYELLSQAESWQRLHNE 466
Cdd:PRK01156   261 AESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDyFKYKNDIENKKQIlsnIDAEINKYHAIIKKLSVLQKDYND 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  467 trtlFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRataaRQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRL 546
Cdd:PRK01156   341 ----YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKK----KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELN 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  547 TL-SELDDIIKNASGIYAEIDGAKSELQVKLSNLSNL-----------------SHDLVQEAIDHAQDLQQEANELSRKL 608
Cdd:PRK01156   413 EInVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEV 492
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  609 HSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDrIYDAVSgidtQIIYHKDESENLLNQAR-----ELQAKA 683
Cdd:PRK01156   493 KDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLED-IKIKIN----ELKDKHDKYEEIKNRYKslkleDLDSKR 567
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2217361438  684 ESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERG 725
Cdd:PRK01156   568 TSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIG 609
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
313-575 3.97e-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: 45.44  E-value: 3.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  313 EINATIYLLKTKLSERENQYALRKIQINNAE-NTMKSLLSDVEELVE----KENQASRKGQLVQKESMDTINHASQLVEQ 387
Cdd:TIGR02169  769 ELEEDLHKLEEALNDLEARLSHSRIPEIQAElSKLEEEVSRIEARLReieqKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  388 AHDMRDKIQEIN---NKMLYYGEEHELSPKEISEKLVLAQKMLEEIRS--RQPFFTQRELvDEEADEAYELLSQ-AESWQ 461
Cdd:TIGR02169  849 IKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKERDELEAqlRELERKIEEL-EAQIEKKRKRLSElKAKLE 927
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  462 RLHNETRTLFPVVLEQLDDYNAKLS--DLQEALDQALNYVRDAEDMN-RA------TAARQRDHEKQQERVREQMEvvnm 532
Cdd:TIGR02169  928 ALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEPVNmLAiqeyeeVLKRLDELKEKRAKLEEERK---- 1003
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2217361438  533 SLSTSADSLTTPR--LTLSELDDIIKNASGIYAEIDGAKSELQVK 575
Cdd:TIGR02169 1004 AILERIEEYEKKKreVFMEAFEAINENFNEIFAELSGGTGELILE 1048
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
311-609 4.45e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 4.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  311 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHD 390
Cdd:COG4372     82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  391 MRDKIQEINNkmlyygEEHELSPKEISEKLvlaQKMLEEIRSRQPFFTQRELVDEEADEAYELLSQAESwQRLHNETRTL 470
Cdd:COG4372    162 LQEELAALEQ------ELQALSEAEAEQAL---DELLKEANRNAEKEEELAEAEKLIESLPRELAEELL-EAKDSLEAKL 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  471 FPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSAdslTTPRLTLSE 550
Cdd:COG4372    232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA---LLLNLAALS 308
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217361438  551 LDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLH 609
Cdd:COG4372    309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
366-682 8.13e-04

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: 43.92  E-value: 8.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  366 KGQLVQKESMDTINHASQLVEQAHDMRDKIQEINnkmlyygeehelspKEISEKLVLAQKMLEEIRSRqpfftqRELVDE 445
Cdd:pfam04108    4 SAQDLCRWANELLTDARSLLEELVVLLAKIAFLR--------------RGLSVQLANLEKVREGLEKV------LNELKK 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  446 EADEAYELLSQA-ESWQR-LHNETRTLFPVVLEQLDDYNAKLSDL--QEALDQALNYVRdaedmnrataarqrdheKQQE 521
Cdd:pfam04108   64 DFKQLLKDLDAAlERLEEtLDKLRNTPVEPALPPGEEKQKTLLDFidEDSVEILRDALK-----------------ELID 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  522 RVREQMEvvnmSLSTSADSLTTprlTLSELDDIIKNASGIYAEIDGAKSELQvklsNLSNLSHDLVQ--EAIDHAQDLQQ 599
Cdd:pfam04108  127 ELQAAQE----SLDSDLKRFDD---DLRDLQKELESLSSPSESISLIPTLLK----ELESLEEEMASllESLTNHYDQCV 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  600 EANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAvsgidtqiiyhKDESENLLNQAREL 679
Cdd:pfam04108  196 TAVKLTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSL-----------IDELLSALQLIAEI 264

                   ...
gi 2217361438  680 QAK 682
Cdd:pfam04108  265 QSR 267
46 PHA02562
endonuclease subunit; Provisional
476-679 9.60e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 9.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  476 EQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAarqRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDII 555
Cdd:PHA02562   195 QQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA---KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKI 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  556 KNASGI----------------YAEIDGAKSELQVKLSNLsNLSHDLVQEAIDHAQDLQQEANELSRKLHssDMNGlvqk 619
Cdd:PHA02562   272 EQFQKVikmyekggvcptctqqISEGPDRITKIKDKLKEL-QHSLEKLDTAIDELEEIMDEFNEQSKKLL--ELKN---- 344
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  620 alDASNVYENIVNYVSEAnetaefalnttDRIYDAVSGIDTQIIYHKDESENLLNQAREL 679
Cdd:PHA02562   345 --KISTNKQSLITLVDKA-----------KKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
VSP pfam03302
Giardia variant-specific surface protein;
87-212 1.00e-03

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 43.80  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438   87 NSNECLDGSGYCVHCQRNTTgehCEKCLDGYIGDSirgapQFCQPCpcplphlanfAESCYRKNGAVRcicnenyagpNC 166
Cdd:pfam03302  252 NNGDLVTCSPGCKTCTSNTV---CTTCMDGYVKTS-----DSCTKC----------DSSCETCTGATT----------TC 303
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2217361438  167 ERCAPGYYGNplliGSTCKKCDCSgNSDPNLIfedcdEVTGqCRNC 212
Cdd:pfam03302  304 KTCATGYYKS----GTGCVSCTSS-ESDNGIT-----GVKG-CLNC 338
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
666-824 1.39e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  666 KDESENLLNQARELQAK-AESSSDEAVADTSRR--------VGGAlaRKSALKTRLSDAVKQLQAAE--RGDAQQRLGQS 734
Cdd:COG4913    294 EAELEELRAELARLEAElERLEARLDALREELDeleaqirgNGGD--RLEQLEREIERLERELEERErrRARLEALLAAL 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  735 RLiTEEANRTTMEVQQATAPMAnnLTNWSQnlqhfDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSAS 814
Cdd:COG4913    372 GL-PLPASAEEFAALRAEAAAL--LEALEE-----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRK--SNIPAR 441
                          170
                   ....*....|
gi 2217361438  815 IQRIRELIAQ 824
Cdd:COG4913    442 LLALRDALAE 451
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
323-550 1.48e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  323 TKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKEsMDT----INHASQLVEQAhdmRDKIQEI 398
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE-IDKlqaeIAEAEAEIEER---REELGER 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  399 NNKMlyYGEEHELSPKEIseklVLAQKMLEEirsrqpFFTQRELVDEEADEAYELLSQAESWQRLHNETRTLfpvVLEQL 478
Cdd:COG3883     92 ARAL--YRSGGSVSYLDV----LLGSESFSD------FLDRLSALSKIADADADLLEELKADKAELEAKKAE---LEAKL 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438  479 DDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSE 550
Cdd:COG3883    157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
405-608 1.77e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  405 YGEEHELSPKEISEKLvlaqKMLEEIRSRQpffTQRELVDEEADEAYELLSQAESWQRLHNETRTLFPVVLEQLDDYN-- 482
Cdd:COG4717    328 LGLPPDLSPEELLELL----DRIEELQELL---REAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQel 400
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  483 -AKLSDLQEALDQALNYVRDAEDMNrataarqrdhekQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNA--S 559
Cdd:COG4717    401 kEELEELEEQLEELLGELEELLEAL------------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLeeD 468
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  560 GIYAEIDGAKSELQVKLSNLS------NLSHDLVQEAIDHAQD-----LQQEANELSRKL 608
Cdd:COG4717    469 GELAELLQELEELKAELRELAeewaalKLALELLEEAREEYREerlppVLERASEYFSRL 528
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
476-687 2.14e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  476 EQLDDYNAKLSDLQEALD--QALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELdd 553
Cdd:COG3206    182 EQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-- 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  554 iikNASGIYAEIDGAKSELQVKLSNLSNL---SHDLVQEAIDHAQDLQQE-ANELSRKLHS--SDMNGLVQKALDASNVY 627
Cdd:COG3206    260 ---LQSPVIQQLRAQLAELEAELAELSARytpNHPDVIALRAQIAALRAQlQQEAQRILASleAELEALQAREASLQAQL 336
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  628 ENIVNYVSEANETaEFALNTTDRIYDAvsgidTQIIYhkdesENLLNQARELQAKAESSS 687
Cdd:COG3206    337 AQLEARLAELPEL-EAELRRLEREVEV-----ARELY-----ESLLQRLEEARLAEALTV 385
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
324-458 2.90e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.82  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  324 KLSERENQYALRKiQINNAENTMKSLLSDVEELVEKENQASRK-GQLVQK-----ESMDTI-NHASQLVEQAHDMRDKIQ 396
Cdd:COG1340    141 KIKELEKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKiKELAEEaqelhEEMIELyKEADELRKEADELHKEIV 219
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217361438  397 EINNKMlyyGEEHEL------SPKEISEKLVLAQKMLEEIRSRQpfftQRELVDEEADEAYELLSQAE 458
Cdd:COG1340    220 EAQEKA---DELHEEiielqkELRELRKELKKLRKKQRALKREK----EKEELEEKAEEIFEKLKKGE 280
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
383-467 5.03e-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: 39.09  E-value: 5.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  383 QLVEQAHDMRDKIQEINNKMLYYGEEHElspkEISEKLVLAQKMLEEIRSRQPffTQRELVDEEA-DEAYELLSQAES-W 460
Cdd:pfam05103   36 ALIRENAELKEKIEELEEKLAHYKNLEE----TLQNTLILAQETAEEVKANAQ--KEAELIIKEAeAKAERIVDDANNeV 109

                   ....*..
gi 2217361438  461 QRLHNET 467
Cdd:pfam05103  110 KKINDEI 116
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
346-607 5.98e-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: 5.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  346 MKSLlSDVEELVekenqasRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINNKMlyygeehelspkeiseklvlaqK 425
Cdd:COG4913    203 FKPI-GDLDDFV-------REYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQI----------------------E 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  426 MLEEIRSRQpffTQRELVDEEADEAYELLSQAESWQR------LHNETRTLfpvvLEQLDDYNAKLSDLQEALDQALNYV 499
Cdd:COG4913    253 LLEPIRELA---ERYAAARERLAELEYLRAALRLWFAqrrlelLEAELEEL----RAELARLEAELERLEARLDALREEL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  500 RDAE----------------DMNRATAARQRdHEKQQERVREQMEVVNMSLSTSADslttprltlsELDDIIKNASGIYA 563
Cdd:COG4913    326 DELEaqirgnggdrleqlerEIERLERELEE-RERRRARLEALLAALGLPLPASAE----------EFAALRAEAAALLE 394
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2217361438  564 EIDGAKSELQVKLSNLSNLSHDLVQEaidhAQDLQQEANELSRK 607
Cdd:COG4913    395 ALEEELEALEEALAEAEAALRDLRRE----LRELEAEIASLERR 434
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
414-693 6.50e-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: 6.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  414 KEISEKLVLAQKMLEEIRsrqpffTQRELVDEEADEAYELLSQAES---WQRLHNETRTLfPVVLEQLDDYNAKLSDLQE 490
Cdd:COG4913    620 AELEEELAEAEERLEALE------AELDALQERREALQRLAEYSWDeidVASAEREIAEL-EAELERLDASSDDLAALEE 692
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  491 ALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLST-SADSLTTPRLTLSE-LDDIIKNASG------IY 562
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEErFAAALGDAVErelrenLE 772
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  563 AEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQ------QEANELSRKLHSSDMNGLVQKALDA--SNVYENIVNYV 634
Cdd:COG4913    773 ERIDALRARLNRAEEELERAMRAFNREWPAETADLDadleslPEYLALLDRLEEDGLPEYEERFKELlnENSIEFVADLL 852
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217361438  635 SEANETAEFALNTTDRIYDAVSGIDtqiiYHKDesenllnqaRELQAKAESSSDEAVAD 693
Cdd:COG4913    853 SKLRRAIREIKERIDPLNDSLKRIP----FGPG---------RYLRLEARPRPDPEVRE 898
TNFRSF6_teleost cd13423
Tumor necrosis factor receptor superfamily member 6 (TNFRSF6) in teleosts; also known as fas ...
157-249 7.88e-03

Tumor necrosis factor receptor superfamily member 6 (TNFRSF6) in teleosts; also known as fas cell surface death receptor (FasR); This subfamily of TNFRSF6 (also known as fas cell surface death receptor (FasR) or Fas; APT1; CD95; FAS1; APO-1; FASTM; ALPS1A) is found in teleosts. It contains a death domain and plays a central role in the physiological regulation of programmed cell death. In humans, it has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The receptor interactions with the Fas ligand (FasL), allowing the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10; autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, leading to apoptosis. This receptor has also been shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is involved in transducing the proliferating signals in normal diploid fibroblast and T cells. In channel catfish and the Japanese rice fish, medaka, homologs of Fas receptor (FasR), as well as FADD and caspase 8, have been identified and characterized, and likely constitute the teleost equivalent of the death-inducing signaling complex (DISC). FasL/FasR are involved in the initiation of apoptosis and suggest that mechanisms of cell-mediated cytotoxicity in teleosts are similar to those used by mammals; presumably, the mechanism of apoptosis induction via death receptors was evolutionarily established during the appearance of vertebrates.


Pssm-ID: 276928 [Multi-domain]  Cd Length: 103  Bit Score: 37.79  E-value: 7.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  157 CNENYAGPNCERCAPGYYGNPLLIGSTCKKCD-CSGNSdpNLIFED-CdeVTGQCRNClrnttgfkceRCAPGYYGDARi 234
Cdd:cd13423     27 CTNNGTDGECEACEDGTYNSHPNSLDSCEPCTsCDPNA--NLEVEErC--TPSSDTVC----------RCKEGHYCDKG- 91
                           90
                   ....*....|....*
gi 2217361438  235 aKNCAVCNcgggPCD 249
Cdd:cd13423     92 -EECKVCY----PCD 101
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
476-607 8.38e-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: 39.91  E-value: 8.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438  476 EQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSlstsaDSLTTPRLTLSELDDII 555
Cdd:COG1579     38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ-----KEIESLKRRISDLEDEI 112
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217361438  556 KNasgIYAEIDGAKSELQVKLSNLSNLSHDL--VQEAIDHA-QDLQQEANELSRK 607
Cdd:COG1579    113 LE---LMERIEELEEELAELEAELAELEAELeeKKAELDEElAELEAELEELEAE 164
 
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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