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Conserved domains on  [gi|1207193065|ref|XP_021329307|]
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laminin subunit beta-1 isoform X2 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
32-266 9.16e-106

Laminin N-terminal (Domain VI);


:

Pssm-ID: 459653  Cd Length: 230  Bit Score: 337.25  E-value: 9.16e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065   32 CYPATGNLLIGRAInlTTSSTCGLDGPEPYCIVSHLKDSEKCFICDSENPYDanyhrdSHRVENVIYPMDSTGElTWWQA 111
Cdd:pfam00055    1 CYPAFGNLAFGREV--SATSTCGLNGPERYCILSGLEGGKKCFICDSRDPHN------SHPPSNLTDSNNGTNE-TWWQS 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065  112 VNGE---ENVSVRLNLEAEFHFTHLIMKFKTFRPAAMIIERSSDFGRTWRIYRYFAYNCTKTFPRVPAHSLRF-IDEVIC 187
Cdd:pfam00055   72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIkDDEVIC 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065  188 EERYSDIEPSTDGEVIYKVL--DPAIHVKDpYSLDIQDLLRITNLRINFTKLHTLGDNLLDrRPDVLQKYYYALYELVVR 265
Cdd:pfam00055  152 TSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLD-DPSVLRKYYYAISDISVG 229

                   .
gi 1207193065  266 G 266
Cdd:pfam00055  230 G 230
cc_LAMB_C cd22295
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ...
1766-1835 9.10e-29

C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.


:

Pssm-ID: 411969 [Multi-domain]  Cd Length: 70  Bit Score: 110.45  E-value: 9.10e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1766 NQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNC 1835
Cdd:cd22295      1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
816-861 1.66e-14

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 69.26  E-value: 1.66e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1207193065   816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGFGPYGC 861
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1492-1818 3.37e-14

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.


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 78.14  E-value: 3.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1492 DNADEVHKNLTAVSEELQT----MAKKLRDIATLTQT---VKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEE 1564
Cdd:TIGR04523   96 DKINKLNSDLSKINSEIKNdkeqKNKLEVELNKLEKQkkeNKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1565 GADPESIEKVAQQVLAISLPVNR--TVIVNLVEQIKDsivnltnvegvfnHTSEQlAKVNDLLKKAQDAKTQADGVSDNI 1642
Cdd:TIGR04523  176 NLLEKEKLNIQKNIDKIKNKLLKleLLLSNLKKKIQK-------------NKSLE-SQISELKKQNNQLKDNIEKKQQEI 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1643 NKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNlsngvdlLKNKTEQNreMAKEA 1722
Cdd:TIGR04523  242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD-------LNNQKEQD--WNKEL 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1723 KAQSDNATREAEGLQEELTNAETLYKQLKEKV-----DSAGGTGEGNVNQKAIEMKK-EAEDLLKKATMGMETLKKLERK 1796
Cdd:TIGR04523  313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQIsqlkkELTNSESENSEKQRELEEKQnEIEKLKKENQSYKQEIKNLESQ 392
                          330       340
                   ....*....|....*....|..
gi 1207193065 1797 FNKNEQKMQQQRDELTDLEKNV 1818
Cdd:TIGR04523  393 INDLESKIQNQEKLNQQKDEQI 414
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
864-912 8.29e-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: 67.38  E-value: 8.29e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207193065  864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFPNCRQCQC 912
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
395-452 1.43e-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: 60.83  E-value: 1.43e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207193065  395 CDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGLSLDDPLGC 452
Cdd:pfam00053    1 CDCNPHGSL-SDTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1175-1215 1.89e-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: 1.89e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1207193065 1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTGN 1215
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
454-505 4.47e-10

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: 56.59  E-value: 4.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207193065  454 PCNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSHDLAGCR 505
Cdd:cd00055      1 PCDCNGHG--SLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1126-1168 7.87e-09

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: 53.13  E-value: 7.87e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1207193065 1126 PCGCVQPNALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDP 1168
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
910-954 2.62e-08

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: 51.59  E-value: 2.62e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207193065  910 CQCNSHA---ESCDPESGACyDCRDNTAGQLCERCVDGYYGNPALGSG 954
Cdd:cd00055      2 CDCNGHGslsGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
960-1016 1.33e-07

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 49.66  E-value: 1.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193065  960 CPCPGHPdsghSNGASCEvdyaSNQILCQCGQGYAGPRCDRCAPGYYGDPEHPGGSC 1016
Cdd:pfam00053    1 CDCNPHG----SLSDTCD----PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1089-1129 2.64e-07

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.89  E-value: 2.64e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1207193065 1089 QCDKQTGQCPCKQNIIGHNCDQCATNHWNFGSDCgcePCGC 1129
Cdd:pfam00053   12 TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP---PQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1019-1063 3.83e-07

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.50  E-value: 3.83e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1207193065 1019 CQCNGNIDPQDpeSCDPRTGLCLkCLYNTDGDSCSECKLGYYGNA 1063
Cdd:pfam00053    1 CDCNPHGSLSD--TCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
506-545 4.82e-07

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: 48.12  E-value: 4.82e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1207193065  506 PCNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
267-320 1.69e-06

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: 46.58  E-value: 1.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193065  267 SCFCYGHAS---ECAPVpgvttrdsgmiHGRCVCKHNTVGLNCERCRDFYHDAPWRP 320
Cdd:cd00055      1 PCDCNGHGSlsgQCDPG-----------TGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
332-384 1.48e-05

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: 43.88  E-value: 1.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193065  332 CNCNGH---SNQCHFDmavylatgnvsGGVCNnCLHNTMGRNCESCKPFYYQDPEK 384
Cdd:cd00055      2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1245-1436 7.50e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 7.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1245 DIIAMILEKGEVpgvsdkRILELEKKLAQAQELVRDGDREGTFNL--ISQTVDDLRAEIALTDGRLMGVIRDLNVTTDHN 1322
Cdd:COG4372      2 DRLGEKVGKARL------SLFGLRPKTGILIAALSEQLRKALFELdkLQEELEQLREELEQAREELEQLEEELEQARSEL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1323 NDLKQNLTALEKELKDLNNTLHQLRRELENyltaglAEQFANVLKYYQRSLNSEQrcnasvygpqspvEQSQDTRNRtea 1402
Cdd:COG4372     76 EQLEEELEELNEQLQAAQAELAQAQEELES------LQEEAEELQEELEELQKER-------------QDLEQQRKQ--- 133
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1207193065 1403 lLKDKKDSLLRTATANNKSLSELEGKAHEINRKV 1436
Cdd:COG4372    134 -LEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
32-266 9.16e-106

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 337.25  E-value: 9.16e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065   32 CYPATGNLLIGRAInlTTSSTCGLDGPEPYCIVSHLKDSEKCFICDSENPYDanyhrdSHRVENVIYPMDSTGElTWWQA 111
Cdd:pfam00055    1 CYPAFGNLAFGREV--SATSTCGLNGPERYCILSGLEGGKKCFICDSRDPHN------SHPPSNLTDSNNGTNE-TWWQS 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065  112 VNGE---ENVSVRLNLEAEFHFTHLIMKFKTFRPAAMIIERSSDFGRTWRIYRYFAYNCTKTFPRVPAHSLRF-IDEVIC 187
Cdd:pfam00055   72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIkDDEVIC 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065  188 EERYSDIEPSTDGEVIYKVL--DPAIHVKDpYSLDIQDLLRITNLRINFTKLHTLGDNLLDrRPDVLQKYYYALYELVVR 265
Cdd:pfam00055  152 TSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLD-DPSVLRKYYYAISDISVG 229

                   .
gi 1207193065  266 G 266
Cdd:pfam00055  230 G 230
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
26-266 4.58e-83

Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.


Pssm-ID: 214532  Cd Length: 238  Bit Score: 272.70  E-value: 4.58e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065    26 GCMDGSCYPATGNLLIGRAInlTTSSTCGLDGPEPYCI-VSHLKDSEKCFICDSENPYDanyhrdSHRVENVIYPmDSTG 104
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGREV--TATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPRR------SHPAENLTDG-NNPN 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065   105 ELTWWQA---VNGEENVSVRLNLEAEFHFTHLIMKFKTFRPAAMIIERSsDFGRTWRIYRYFAYNCTKTFPRVPAHSLR- 180
Cdd:smart00136   72 NPTWWQSeplSNGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITk 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065   181 -FIDEVICEERYSDIEPSTDGEVIYKVLDPAIHVKD-PYSLDIQDLLRITNLRINFTKLHTLGDNLLDRRPDVLQKYYYA 258
Cdd:smart00136  151 gNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230

                    ....*...
gi 1207193065   259 LYELVVRG 266
Cdd:smart00136  231 ISDIAVGG 238
cc_LAMB_C cd22295
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ...
1766-1835 9.10e-29

C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.


Pssm-ID: 411969 [Multi-domain]  Cd Length: 70  Bit Score: 110.45  E-value: 9.10e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1766 NQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNC 1835
Cdd:cd22295      1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
816-861 1.66e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 69.26  E-value: 1.66e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1207193065   816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGFGPYGC 861
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1492-1818 3.37e-14

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: 78.14  E-value: 3.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1492 DNADEVHKNLTAVSEELQT----MAKKLRDIATLTQT---VKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEE 1564
Cdd:TIGR04523   96 DKINKLNSDLSKINSEIKNdkeqKNKLEVELNKLEKQkkeNKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1565 GADPESIEKVAQQVLAISLPVNR--TVIVNLVEQIKDsivnltnvegvfnHTSEQlAKVNDLLKKAQDAKTQADGVSDNI 1642
Cdd:TIGR04523  176 NLLEKEKLNIQKNIDKIKNKLLKleLLLSNLKKKIQK-------------NKSLE-SQISELKKQNNQLKDNIEKKQQEI 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1643 NKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNlsngvdlLKNKTEQNreMAKEA 1722
Cdd:TIGR04523  242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD-------LNNQKEQD--WNKEL 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1723 KAQSDNATREAEGLQEELTNAETLYKQLKEKV-----DSAGGTGEGNVNQKAIEMKK-EAEDLLKKATMGMETLKKLERK 1796
Cdd:TIGR04523  313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQIsqlkkELTNSESENSEKQRELEEKQnEIEKLKKENQSYKQEIKNLESQ 392
                          330       340
                   ....*....|....*....|..
gi 1207193065 1797 FNKNEQKMQQQRDELTDLEKNV 1818
Cdd:TIGR04523  393 INDLESKIQNQEKLNQQKDEQI 414
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
816-861 5.29e-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: 5.29e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207193065  816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGFG---PYGC 861
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdpPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
864-912 8.29e-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: 67.38  E-value: 8.29e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207193065  864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFPNCRQCQC 912
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
816-862 1.22e-13

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: 66.61  E-value: 1.22e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207193065  816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGF--GPYGCT 862
Cdd:cd00055      2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
864-905 1.16e-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: 1.16e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1207193065  864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFP 905
Cdd:cd00055      2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
1493-1828 1.12e-11

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 70.63  E-value: 1.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1493 NADEVHKNLTAVSEELQTMAKKLRDIA------------TLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDF 1560
Cdd:PTZ00440  1259 IKLQVFSYLQQVIKENNKMENALHEIKnmyeflisidseKILKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQA 1338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1561 ----------LNEEGADPE--SIEKVAQQVLAIslpvnRTVIVNLVEQIKDsivNLTNVEGVFNHTSEQLAKVNDLLKKA 1628
Cdd:PTZ00440  1339 kehknkiygsLEDKQIDDEikKIEQIKEEISNK-----RKEINKYLSNIKS---NKEKCDLHVRNASRGKDKIDFLNKHE 1410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1629 QDAKTQA-----DGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNI-----TAMVDDKLLNLDNNLTDVMMRl 1698
Cdd:PTZ00440  1411 AIEPSNSkevniIKITDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNIlnnssILGKKTKLEKKKKEATNIMDD- 1489
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1699 VNLSNGVdlLKNKTEQNREMAKEAKAQSdNATREaeglQEELTNAETlyKQLKEKVDSAGGTGEGNVnQKAIEMKKEAED 1778
Cdd:PTZ00440  1490 INGEHSI--IKTKLTKSSEKLNQLNEQP-NIKRE----GDVLNNDKS--TIAYETIQYNLGRVKHNL-LNILNIKDEIET 1559
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207193065 1779 LLKKATMGMETLKKLERKF-NKNEQKMQQQRDELTDLEKNVTGIREYIRSK 1828
Cdd:PTZ00440  1560 ILNKAQDLMRDISKISKIVeNKNLENLNDKEADYVKYLDNILKEKQLMEAE 1610
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
395-452 1.43e-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: 60.83  E-value: 1.43e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207193065  395 CDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGLSLDDPLGC 452
Cdd:pfam00053    1 CDCNPHGSL-SDTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
864-905 1.74e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.40  E-value: 1.74e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1207193065   864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFP 905
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1175-1215 1.89e-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: 1.89e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1207193065 1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTGN 1215
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL 41
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1506-1819 4.44e-11

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 68.46  E-value: 4.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1506 EELQTMAKKLRDIATLTQTVKT---QAKETLDKAQNKKDMFEKSNKML----KNFIQKIKDFLNEEGADPESIEKVAQQV 1578
Cdd:pfam02463  180 EETENLAELIIDLEELKLQELKlkeQAKKALEYYQLKEKLELEEEYLLyldyLKLNEERIDLLQELLRDEQEEIESSKQE 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1579 LAISLPVNRTVIVNLVE-----------------QIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSDN 1641
Cdd:pfam02463  260 IEKEEEKLAQVLKENKEeekekklqeeelkllakEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1642 INKTKEALETSQNAIKKAEEEMStalknlkniqnitamvdDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKE 1721
Cdd:pfam02463  340 LEKELKELEIKREAEEEEEEELE-----------------KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1722 AKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNE 1801
Cdd:pfam02463  403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
                          330
                   ....*....|....*...
gi 1207193065 1802 QKMQQQRDELTDLEKNVT 1819
Cdd:pfam02463  483 QEQLELLLSRQKLEERSQ 500
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1175-1223 1.47e-10

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: 58.13  E-value: 1.47e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207193065 1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTGNFPKCVPCH 1223
Cdd:cd00055      2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1175-1219 2.66e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 57.32  E-value: 2.66e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1207193065  1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTG-NFPKC 1219
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
454-505 4.47e-10

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: 56.59  E-value: 4.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207193065  454 PCNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSHDLAGCR 505
Cdd:cd00055      1 PCDCNGHG--SLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
394-453 1.18e-09

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: 55.44  E-value: 1.18e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065  394 PCDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGLSLdDPLGCQ 453
Cdd:cd00055      1 PCDCNGHGSL-SGQCDPGT--------GQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
455-504 2.64e-09

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 54.28  E-value: 2.64e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207193065  455 CNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSHDLA-GC 504
Cdd:pfam00053    1 CDCNPHG--SLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPqGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1126-1168 7.87e-09

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: 53.13  E-value: 7.87e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1207193065 1126 PCGCVQPNALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDP 1168
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1122-1175 1.10e-08

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 52.74  E-value: 1.10e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207193065 1122 CGCEPCGcvqpnALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDPRVQCEEC 1175
Cdd:pfam00053    1 CDCNPHG-----SLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1489-1795 2.10e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 57.61  E-value: 2.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1489 KALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDK-----------AQNKKDMFEKSNKmLKNFIQKI 1557
Cdd:COG1340     19 ELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKrdelnekvkelKEERDELNEKLNE-LREELDEL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1558 KDFLNEEGADPESIEKV---------AQQVLAISLPVNRtvivNLVEQIKdsivnltnvegvfnhtseQLAKvndLLKKA 1628
Cdd:COG1340     98 RKELAELNKAGGSIDKLrkeierlewRQQTEVLSPEEEK----ELVEKIK------------------ELEK---ELEKA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1629 QDAKTQADGVSDNINKTKEaletsqnaIKKAEEEMSTALKNLKN-IQNITAmvddkllnldnnltdvmmRLVNLSNGVDL 1707
Cdd:COG1340    153 KKALEKNEKLKELRAELKE--------LRKEAEEIHKKIKELAEeAQELHE------------------EMIELYKEADE 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1708 LKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKvdsaggtgegnvnQKAIEMKKEAEDLLKKATMGM 1787
Cdd:COG1340    207 LRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKK-------------QRALKREKEKEELEEKAEEIF 273

                   ....*...
gi 1207193065 1788 ETLKKLER 1795
Cdd:COG1340    274 EKLKKGEK 281
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1127-1172 2.24e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 51.54  E-value: 2.24e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1207193065  1127 CGCVQPNALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDPRVQC 1172
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
395-452 2.55e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 51.54  E-value: 2.55e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207193065   395 CDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGlslDDPLGC 452
Cdd:smart00180    1 CDCDPGGSA-SGTCDPDT--------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
910-954 2.62e-08

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: 51.59  E-value: 2.62e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207193065  910 CQCNSHA---ESCDPESGACyDCRDNTAGQLCERCVDGYYGNPALGSG 954
Cdd:cd00055      2 CDCNGHGslsGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
910-957 2.69e-08

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 51.59  E-value: 2.69e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207193065  910 CQCNSHA---ESCDPESGACyDCRDNTAGQLCERCVDGYYGNPAlGSGEHC 957
Cdd:pfam00053    1 CDCNPHGslsDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
455-498 8.09e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.00  E-value: 8.09e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1207193065   455 CNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLS 498
Cdd:smart00180    1 CDCDPGG--SASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
960-1016 1.33e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 49.66  E-value: 1.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193065  960 CPCPGHPdsghSNGASCEvdyaSNQILCQCGQGYAGPRCDRCAPGYYGDPEHPGGSC 1016
Cdd:pfam00053    1 CDCNPHG----SLSDTCD----PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1089-1129 2.64e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.89  E-value: 2.64e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1207193065 1089 QCDKQTGQCPCKQNIIGHNCDQCATNHWNFGSDCgcePCGC 1129
Cdd:pfam00053   12 TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP---PQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1019-1063 3.83e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.50  E-value: 3.83e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1207193065 1019 CQCNGNIDPQDpeSCDPRTGLCLkCLYNTDGDSCSECKLGYYGNA 1063
Cdd:pfam00053    1 CDCNPHGSLSD--TCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
506-545 4.82e-07

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: 48.12  E-value: 4.82e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1207193065  506 PCNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
910-952 7.42e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 47.31  E-value: 7.42e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1207193065   910 CQCN---SHAESCDPESGACyDCRDNTAGQLCERCVDGYYGNPALG 952
Cdd:smart00180    1 CDCDpggSASGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
507-545 7.71e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 47.31  E-value: 7.71e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1207193065   507 CNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
959-1014 8.60e-07

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: 47.35  E-value: 8.60e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193065  959 PCPCPGHPdsghSNGASCevDYASNQilCQCGQGYAGPRCDRCAPGYYGDPEHPGG 1014
Cdd:cd00055      1 PCDCNGHG----SLSGQC--DPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1070-1120 1.42e-06

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: 46.58  E-value: 1.42e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207193065 1070 RCTCVTAGTLPNsctdgvcQCDKQTGQCPCKQNIIGHNCDQCATNHWNFGS 1120
Cdd:cd00055      1 PCDCNGHGSLSG-------QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
1489-1648 1.52e-06

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 51.99  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1489 KALDNADEVHKNLTAVSEELQTMAKKLRDIAT-----LTQTVKTQAKETLDKAQNK-KDMFEKSNKMLKNFIQKIKDFLN 1562
Cdd:cd22656    132 KYQDKAAKVVDKLTDFENQTEKDQTALETLEKalkdlLTDEGGAIARKEIKDLQKElEKLNEEYAAKLKAKIDELKALIA 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1563 EEGADPESIEKVAQQVLAISlpvnrTVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQD-------AKTQA 1635
Cdd:cd22656    212 DDEAKLAAALRLIADLTAAD-----TDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISkipaailAKLEL 286
                          170
                   ....*....|...
gi 1207193065 1636 DGVSDNINKTKEA 1648
Cdd:cd22656    287 EKAIEKWNELAEK 299
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
267-320 1.69e-06

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: 46.58  E-value: 1.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193065  267 SCFCYGHAS---ECAPVpgvttrdsgmiHGRCVCKHNTVGLNCERCRDFYHDAPWRP 320
Cdd:cd00055      1 PCDCNGHGSlsgQCDPG-----------TGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1018-1069 2.02e-06

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: 46.19  E-value: 2.02e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207193065 1018 PCQCNGNIDPqdPESCDPRTGLCLkCLYNTDGDSCSECKLGYYGNALI-QDCR 1069
Cdd:cd00055      1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1071-1118 4.29e-06

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 45.38  E-value: 4.29e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1207193065  1071 CTCVTAGTLPNsctdgvcQCDKQTGQCPCKQNIIGHNCDQCATNHWNF 1118
Cdd:smart00180    1 CDCDPGGSASG-------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
332-384 1.48e-05

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: 43.88  E-value: 1.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193065  332 CNCNGH---SNQCHFDmavylatgnvsGGVCNnCLHNTMGRNCESCKPFYYQDPEK 384
Cdd:cd00055      2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
507-545 1.85e-05

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 43.50  E-value: 1.85e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1207193065  507 CNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1245-1436 7.50e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 7.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1245 DIIAMILEKGEVpgvsdkRILELEKKLAQAQELVRDGDREGTFNL--ISQTVDDLRAEIALTDGRLMGVIRDLNVTTDHN 1322
Cdd:COG4372      2 DRLGEKVGKARL------SLFGLRPKTGILIAALSEQLRKALFELdkLQEELEQLREELEQAREELEQLEEELEQARSEL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1323 NDLKQNLTALEKELKDLNNTLHQLRRELENyltaglAEQFANVLKYYQRSLNSEQrcnasvygpqspvEQSQDTRNRtea 1402
Cdd:COG4372     76 EQLEEELEELNEQLQAAQAELAQAQEELES------LQEEAEELQEELEELQKER-------------QDLEQQRKQ--- 133
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1207193065 1403 lLKDKKDSLLRTATANNKSLSELEGKAHEINRKV 1436
Cdd:COG4372    134 -LEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
332-382 7.60e-05

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 41.96  E-value: 7.60e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207193065  332 CNCNGH---SNQCHFdmavylatgnvSGGVCNnCLHNTMGRNCESCKPFYYQDP 382
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1252-1442 1.06e-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: 47.37  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1252 EKGEVPGVSDkRILELEKKLA--------------QAQELVRDGDREgtFNLISQTVDDLRAEIALTDGRLMGVIRDLNV 1317
Cdd:TIGR02169  672 EPAELQRLRE-RLEGLKRELSslqselrrienrldELSQELSDASRK--IGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1318 TTDHNNDLKQNLTALEKELKDLNNTLHQLRRELENyLTAGLAEQF-------ANVLKYYQRSLNS-----EQRCNASVYG 1385
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKLEEALND-LEARLSHSRipeiqaeLSKLEEEVSRIEArlreiEQKLNRLTLE 827
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193065 1386 PQSPVEQSQDTRNRTEAlLKDKKDSLLRTATANNKSLSELEGKAHEINRKVHHLSNK 1442
Cdd:TIGR02169  828 KEYLEKEIQELQEQRID-LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
960-1012 1.80e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 40.76  E-value: 1.80e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1207193065   960 CPCpghpDSGHSNGASCEVDYasnqILCQCGQGYAGPRCDRCAPGYYGDPEHP 1012
Cdd:smart00180    1 CDC----DPGGSASGTCDPDT----GQCECKPNVTGRRCDRCAPGYYGDGPPG 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
332-385 6.78e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.22  E-value: 6.78e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193065   332 CNCNG---HSNQCHFDmavylatgnvsGGVCNnCLHNTMGRNCESCKPFYYQDPEKD 385
Cdd:smart00180    1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
292-318 9.75e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.45  E-value: 9.75e-04
                            10        20
                    ....*....|....*....|....*..
gi 1207193065   292 HGRCVCKHNTVGLNCERCRDFYHDAPW 318
Cdd:smart00180   17 TGQCECKPNVTGRRCDRCAPGYYGDGP 43
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
291-322 2.24e-03

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 37.72  E-value: 2.24e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1207193065  291 IHGRCVCKHNTVGLNCERCRDFYHDAPWRPAE 322
Cdd:pfam00053   16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
1590-1682 3.61e-03

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 41.12  E-value: 3.61e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065  1590 IVNLVEQIKDSIVNL-TNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALK 1668
Cdd:smart00283    2 VSEAVEEIAAGAEEQaEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81
                            90       100
                    ....*....|....*....|.
gi 1207193065  1669 NLK-------NIQNITAMVDD 1682
Cdd:smart00283   82 AVEeleessdEIGEIVSVIDD 102
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
1747-1832 8.99e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.33  E-value: 8.99e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065  1747 YKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKK-ATMGMETLKKLERKFNKNEQKMQQQRDELT-DLEKNVTGIREY 1824
Cdd:smart00935   16 GKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDaATLSEAAREKKEKELQKKVQEFQRKQQKLQqDLQKRQQEELQK 95

                    ....*...
gi 1207193065  1825 IRSKVLAY 1832
Cdd:smart00935   96 ILDKINKA 103
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
32-266 9.16e-106

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 337.25  E-value: 9.16e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065   32 CYPATGNLLIGRAInlTTSSTCGLDGPEPYCIVSHLKDSEKCFICDSENPYDanyhrdSHRVENVIYPMDSTGElTWWQA 111
Cdd:pfam00055    1 CYPAFGNLAFGREV--SATSTCGLNGPERYCILSGLEGGKKCFICDSRDPHN------SHPPSNLTDSNNGTNE-TWWQS 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065  112 VNGE---ENVSVRLNLEAEFHFTHLIMKFKTFRPAAMIIERSSDFGRTWRIYRYFAYNCTKTFPRVPAHSLRF-IDEVIC 187
Cdd:pfam00055   72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIkDDEVIC 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065  188 EERYSDIEPSTDGEVIYKVL--DPAIHVKDpYSLDIQDLLRITNLRINFTKLHTLGDNLLDrRPDVLQKYYYALYELVVR 265
Cdd:pfam00055  152 TSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLD-DPSVLRKYYYAISDISVG 229

                   .
gi 1207193065  266 G 266
Cdd:pfam00055  230 G 230
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
26-266 4.58e-83

Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.


Pssm-ID: 214532  Cd Length: 238  Bit Score: 272.70  E-value: 4.58e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065    26 GCMDGSCYPATGNLLIGRAInlTTSSTCGLDGPEPYCI-VSHLKDSEKCFICDSENPYDanyhrdSHRVENVIYPmDSTG 104
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGREV--TATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPRR------SHPAENLTDG-NNPN 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065   105 ELTWWQA---VNGEENVSVRLNLEAEFHFTHLIMKFKTFRPAAMIIERSsDFGRTWRIYRYFAYNCTKTFPRVPAHSLR- 180
Cdd:smart00136   72 NPTWWQSeplSNGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITk 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065   181 -FIDEVICEERYSDIEPSTDGEVIYKVLDPAIHVKD-PYSLDIQDLLRITNLRINFTKLHTLGDNLLDRRPDVLQKYYYA 258
Cdd:smart00136  151 gNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230

                    ....*...
gi 1207193065   259 LYELVVRG 266
Cdd:smart00136  231 ISDIAVGG 238
cc_LAMB_C cd22295
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ...
1766-1835 9.10e-29

C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.


Pssm-ID: 411969 [Multi-domain]  Cd Length: 70  Bit Score: 110.45  E-value: 9.10e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1766 NQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNC 1835
Cdd:cd22295      1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
816-861 1.66e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 69.26  E-value: 1.66e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1207193065   816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGFGPYGC 861
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1492-1818 3.37e-14

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: 78.14  E-value: 3.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1492 DNADEVHKNLTAVSEELQT----MAKKLRDIATLTQT---VKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEE 1564
Cdd:TIGR04523   96 DKINKLNSDLSKINSEIKNdkeqKNKLEVELNKLEKQkkeNKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1565 GADPESIEKVAQQVLAISLPVNR--TVIVNLVEQIKDsivnltnvegvfnHTSEQlAKVNDLLKKAQDAKTQADGVSDNI 1642
Cdd:TIGR04523  176 NLLEKEKLNIQKNIDKIKNKLLKleLLLSNLKKKIQK-------------NKSLE-SQISELKKQNNQLKDNIEKKQQEI 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1643 NKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNlsngvdlLKNKTEQNreMAKEA 1722
Cdd:TIGR04523  242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD-------LNNQKEQD--WNKEL 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1723 KAQSDNATREAEGLQEELTNAETLYKQLKEKV-----DSAGGTGEGNVNQKAIEMKK-EAEDLLKKATMGMETLKKLERK 1796
Cdd:TIGR04523  313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQIsqlkkELTNSESENSEKQRELEEKQnEIEKLKKENQSYKQEIKNLESQ 392
                          330       340
                   ....*....|....*....|..
gi 1207193065 1797 FNKNEQKMQQQRDELTDLEKNV 1818
Cdd:TIGR04523  393 INDLESKIQNQEKLNQQKDEQI 414
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
816-861 5.29e-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: 5.29e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207193065  816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGFG---PYGC 861
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdpPQGC 49
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1495-1819 8.25e-14

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: 76.98  E-value: 8.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1495 DEVHKNLTAVSEELQTMAKKLRDI-ATLT-------------QTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDf 1560
Cdd:TIGR04523   36 KQLEKKLKTIKNELKNKEKELKNLdKNLNkdeekinnsnnkiKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN- 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1561 lneegaDPESIEKvaqqvlaislpvNRTVIVNLVEQIKdsivnltnvegvfnHTSEQLAKVNDLLKKAQDAKTQADGVSD 1640
Cdd:TIGR04523  115 ------DKEQKNK------------LEVELNKLEKQKK--------------ENKKNIDKFLTEIKKKEKELEKLNNKYN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1641 NINKTKEALETSQNaikKAEEEMSTALKNLKNIQNITAMVDDKLLNLD------NNLTDVMMRL----VNLSNGVDLLKN 1710
Cdd:TIGR04523  163 DLKKQKEELENELN---LLEKEKLNIQKNIDKIKNKLLKLELLLSNLKkkiqknKSLESQISELkkqnNQLKDNIEKKQQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1711 KTEQ-------NREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDsaggtgegNVNQKAIEMKKEAE-DLLKK 1782
Cdd:TIGR04523  240 EINEktteisnTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN--------QLKSEISDLNNQKEqDWNKE 311
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1207193065 1783 ATMGMETLKK----LERKFNKNEQKMQQQRDELTDLEKNVT 1819
Cdd:TIGR04523  312 LKSELKNQEKkleeIQNQISQNNKIISQLNEQISQLKKELT 352
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
864-912 8.29e-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: 67.38  E-value: 8.29e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207193065  864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFPNCRQCQC 912
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
816-862 1.22e-13

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: 66.61  E-value: 1.22e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207193065  816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGF--GPYGCT 862
Cdd:cd00055      2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1314-1828 1.04e-12

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: 73.52  E-value: 1.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1314 DLNVTTDHNNDLKQNLTALEKELKDLNNTLHQLRRELENYLTAGLA-EQFANVLKYY---QRSLNSE----QRCNASVyg 1385
Cdd:TIGR04523  153 ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKlELLLSNLKKKiqkNKSLESQiselKKQNNQL-- 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1386 pQSPVEQSQDTRNRTEALLKDKKDSLLRTATANNKSLSELEGKAHEINRKVHHLSNKvcgghaNGNVNgsceespcggag 1465
Cdd:TIGR04523  231 -KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL------EKQLN------------ 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1466 crgsdgvlkcggrgcngTVGASVKALDN--ADEVHKNLtavSEELQTMAKKLRDIAT-LTQTVK--TQAKETLdkAQNKK 1540
Cdd:TIGR04523  292 -----------------QLKSEISDLNNqkEQDWNKEL---KSELKNQEKKLEEIQNqISQNNKiiSQLNEQI--SQLKK 349
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1541 dmfEKSNKMLKNfiQKIKDFLNEEGADPESIEKVAQQVlaislpvnrtvivnlveqiKDSIVNLTNvegvfnhtseqlaK 1620
Cdd:TIGR04523  350 ---ELTNSESEN--SEKQRELEEKQNEIEKLKKENQSY-------------------KQEIKNLES-------------Q 392
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1621 VNDLLKKAQDAKtqadgvsdNINKTKealetsQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDvmmrlvn 1700
Cdd:TIGR04523  393 INDLESKIQNQE--------KLNQQK------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV------- 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1701 LSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVdsaggtgegnvnqkaIEMKKEAEDLL 1780
Cdd:TIGR04523  452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK---------------KELEEKVKDLT 516
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1781 KKATMGMETLKKLERKFNKNEQKMQQQRDELT--DLEKNVTGIREYIRSK 1828
Cdd:TIGR04523  517 KKISSLKEKIEKLESEKKEKESKISDLEDELNkdDFELKKENLEKEIDEK 566
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
864-905 1.16e-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: 1.16e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1207193065  864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFP 905
Cdd:cd00055      2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1495-1816 3.47e-12

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: 71.59  E-value: 3.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1495 DEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQaKETLdkaQNKKDMFEKSNKMLKNFIQKIKDFLNEEGADPESIEKV 1574
Cdd:TIGR04523  134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ-KEEL---ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1575 AQQVLAISLPVN-----RTVIVNLVEQIKDSIVNLTNVegvFNHTSEQLakvNDLLKKAQDAKTQADGVSDNINKTKEAL 1649
Cdd:TIGR04523  210 IQKNKSLESQISelkkqNNQLKDNIEKKQQEINEKTTE---ISNTQTQL---NQLKDEQNKIKKQLSEKQKELEQNNKKI 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1650 ETSQNAIKKAEEEMSTaLKNLKNiQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQ--------------- 1714
Cdd:TIGR04523  284 KELEKQLNQLKSEISD-LNNQKE-QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQlkkeltnsesensek 361
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1715 NREMAK-------------EAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggTGEGNVNQKAIE--------MK 1773
Cdd:TIGR04523  362 QRELEEkqneieklkkenqSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL--QQEKELLEKEIErlketiikNN 439
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193065 1774 KEAEDL-------------LKKATMGMET-LKKLERKFNKNEQKMQQQRDELTDLEK 1816
Cdd:TIGR04523  440 SEIKDLtnqdsvkeliiknLDNTRESLETqLKVLSRSINKIKQNLEQKQKELKSKEK 496
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
1493-1828 1.12e-11

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 70.63  E-value: 1.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1493 NADEVHKNLTAVSEELQTMAKKLRDIA------------TLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDF 1560
Cdd:PTZ00440  1259 IKLQVFSYLQQVIKENNKMENALHEIKnmyeflisidseKILKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQA 1338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1561 ----------LNEEGADPE--SIEKVAQQVLAIslpvnRTVIVNLVEQIKDsivNLTNVEGVFNHTSEQLAKVNDLLKKA 1628
Cdd:PTZ00440  1339 kehknkiygsLEDKQIDDEikKIEQIKEEISNK-----RKEINKYLSNIKS---NKEKCDLHVRNASRGKDKIDFLNKHE 1410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1629 QDAKTQA-----DGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNI-----TAMVDDKLLNLDNNLTDVMMRl 1698
Cdd:PTZ00440  1411 AIEPSNSkevniIKITDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNIlnnssILGKKTKLEKKKKEATNIMDD- 1489
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1699 VNLSNGVdlLKNKTEQNREMAKEAKAQSdNATREaeglQEELTNAETlyKQLKEKVDSAGGTGEGNVnQKAIEMKKEAED 1778
Cdd:PTZ00440  1490 INGEHSI--IKTKLTKSSEKLNQLNEQP-NIKRE----GDVLNNDKS--TIAYETIQYNLGRVKHNL-LNILNIKDEIET 1559
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207193065 1779 LLKKATMGMETLKKLERKF-NKNEQKMQQQRDELTDLEKNVTGIREYIRSK 1828
Cdd:PTZ00440  1560 ILNKAQDLMRDISKISKIVeNKNLENLNDKEADYVKYLDNILKEKQLMEAE 1610
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
395-452 1.43e-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: 60.83  E-value: 1.43e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207193065  395 CDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGLSLDDPLGC 452
Cdd:pfam00053    1 CDCNPHGSL-SDTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
864-905 1.74e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.40  E-value: 1.74e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1207193065   864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFP 905
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1175-1215 1.89e-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: 1.89e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1207193065 1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTGN 1215
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL 41
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1506-1819 4.44e-11

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 68.46  E-value: 4.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1506 EELQTMAKKLRDIATLTQTVKT---QAKETLDKAQNKKDMFEKSNKML----KNFIQKIKDFLNEEGADPESIEKVAQQV 1578
Cdd:pfam02463  180 EETENLAELIIDLEELKLQELKlkeQAKKALEYYQLKEKLELEEEYLLyldyLKLNEERIDLLQELLRDEQEEIESSKQE 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1579 LAISLPVNRTVIVNLVE-----------------QIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSDN 1641
Cdd:pfam02463  260 IEKEEEKLAQVLKENKEeekekklqeeelkllakEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1642 INKTKEALETSQNAIKKAEEEMStalknlkniqnitamvdDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKE 1721
Cdd:pfam02463  340 LEKELKELEIKREAEEEEEEELE-----------------KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1722 AKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNE 1801
Cdd:pfam02463  403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
                          330
                   ....*....|....*...
gi 1207193065 1802 QKMQQQRDELTDLEKNVT 1819
Cdd:pfam02463  483 QEQLELLLSRQKLEERSQ 500
cc_LAMB4_C cd22301
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ...
1766-1835 8.01e-11

C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.


Pssm-ID: 411972 [Multi-domain]  Cd Length: 70  Bit Score: 59.29  E-value: 8.01e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1766 NQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNC 1835
Cdd:cd22301      1 NERLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
1288-1821 8.40e-11

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 67.55  E-value: 8.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1288 NLISQTVDDLRAE----IALTDG---RLMGVIR-----DLNVTTDHNNDLKQNLTALEKELKDLNNTLHQLRRELENYLT 1355
Cdd:PTZ00440   684 DNIDNIIKNLKKElqnlLSLKENiikKQLNNIEqdisnSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFIL 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1356 AgLAEQFANV----------LKYYQRSLNSEQRCNASVYGPQSPVEQSQDTRNRTEAL---LKD---KKDSLLRTATA-- 1417
Cdd:PTZ00440   764 H-LYENDKDLpdgkntyeefLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILiqkLEAhteKNDEELKQLLQkf 842
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1418 ----NNKSLSELEGKAHEINRKVHHLSNKVcgGHANGNVNgsceespcggagcrgsdgVLKcggrGCNGTVGASVKALDN 1493
Cdd:PTZ00440   843 ptedENLNLKELEKEFNENNQIVDNIIKDI--ENMNKNIN------------------IIK----TLNIAINRSNSNKQL 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1494 ADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDKAQNK--KDMFEKSNKMLKNFIQKI-------------K 1558
Cdd:PTZ00440   899 VEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKEKieKQLSDTKINNLKMQIEKTleyydkskeningN 978
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1559 DFLNEEGADPESIEKVAQQVLAISLPVNRTV----IVNLVEQIKDSIVNLTN--VEGVFNHTSEQLAKVNDLLKKAQDaK 1632
Cdd:PTZ00440   979 DGTHLEKLDKEKDEWEHFKSEIDKLNVNYNIlnkkIDDLIKKQHDDIIELIDklIKEKGKEIEEKVDQYISLLEKMKT-K 1057
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1633 TQADGVSDNINKTKEAleTSQNAIKKAEEEMSTALKNLKNIQNitamvddKLLNLDNNLTDVMmrlVNLSNGVDLLKNKT 1712
Cdd:PTZ00440  1058 LSSFHFNIDIKKYKNP--KIKEEIKLLEEKVEALLKKIDENKN-------KLIEIKNKSHEHV---VNADKEKNKQTEHY 1125
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1713 EQNREMAKEAKAQSDNATREAEGLQEELT------NAETLYK---------QLKEKVDSAGGTGEgnvnqkAIEMKKEAE 1777
Cdd:PTZ00440  1126 NKKKKSLEKIYKQMEKTLKELENMNLEDItlnevnEIEIEYErilidhiveQINNEAKKSKTIME------EIESYKKDI 1199
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1207193065 1778 DLLKKaTMGMETLKKLeRKFNKNeqkmqQQRDELTDLEKNVTGI 1821
Cdd:PTZ00440  1200 DQVKK-NMSKERNDHL-TTFEYN-----AYYDKATASYENIEEL 1236
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1492-1818 1.37e-10

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: 66.58  E-value: 1.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1492 DNADEVhKNLTAVSEELQTMAKKLRDIatlTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDfLNEEGADPEsi 1571
Cdd:TIGR04523  437 KNNSEI-KDLTNQDSVKELIIKNLDNT---RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK-LNEEKKELE-- 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1572 EKVAqqvlaislpvnrtvivNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKT--QADGVSDNINKTKEAL 1649
Cdd:TIGR04523  510 EKVK----------------DLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkeNLEKEIDEKNKEIEEL 573
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1650 ETSQNAIKKAEEEMSTALKNL-KNIQNIT---AMVDDKLLNLDNNLTDVMM---RLVNLSNGVDLLKNKTEQNREMAKEa 1722
Cdd:TIGR04523  574 KQTQKSLKKKQEEKQELIDQKeKEKKDLIkeiEEKEKKISSLEKELEKAKKeneKLSSIIKNIKSKKNKLKQEVKQIKE- 652
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1723 kaqsdnatrEAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKatmgmETLKKLERKFNKNEQ 1802
Cdd:TIGR04523  653 ---------TIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRI-----KDLPKLEEKYKEIEK 718
                          330
                   ....*....|....*.
gi 1207193065 1803 KMQQQRDELTDLEKNV 1818
Cdd:TIGR04523  719 ELKKLDEFSKELENII 734
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1175-1223 1.47e-10

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: 58.13  E-value: 1.47e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207193065 1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTGNFPKCVPCH 1223
Cdd:cd00055      2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
1260-1828 1.91e-10

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: 66.15  E-value: 1.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1260 SDKRILELEKKLAQAQELVRDGDREgtfNLISQTVDDLRAEIALTDGRLMgvirdlnvttdHNNDLKQNLTALEKELKDL 1339
Cdd:TIGR00618  371 SCQQHTLTQHIHTLQQQKTTLTQKL---QSLCKELDILQREQATIDTRTS-----------AFRDLQGQLAHAKKQQELQ 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1340 NNTLHQLRRELENYLTAGLAEqfanvlkyyqrslNSEQRcnasvygpqspvEQSQDTRNRTEaLLKDKKDSLL---RTAT 1416
Cdd:TIGR00618  437 QRYAELCAAAITCTAQCEKLE-------------KIHLQ------------ESAQSLKEREQ-QLQTKEQIHLqetRKKA 490
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1417 ANNKSLSELEGKAHEINRKVHHLSNKVcggHANGNVNGSCeeSPCggagCRGSDGVLKcggrgcNGTVGASVKAldNADE 1496
Cdd:TIGR00618  491 VVLARLLELQEEPCPLCGSCIHPNPAR---QDIDNPGPLT--RRM----QRGEQTYAQ------LETSEEDVYH--QLTS 553
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1497 VHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKET---LDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEEGADPESI-- 1571
Cdd:TIGR00618  554 ERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLqniTVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRlh 633
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1572 EKVAQQVLAISLPVNRTVIVNLV-EQIKDSIVNLTNVEgvfnhtSEQLAKVNDLLKKAQDAKTQADGVsdninktKEALE 1650
Cdd:TIGR00618  634 LQQCSQELALKLTALHALQLTLTqERVREHALSIRVLP------KELLASRQLALQKMQSEKEQLTYW-------KEMLA 700
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1651 TSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVdlLKNKT---EQNRE---MAKEAKA 1724
Cdd:TIGR00618  701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTV--LKARTeahFNNNEevtAALQTGA 778
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1725 QSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLL-----KKATMGMET--LKKLERKF 1797
Cdd:TIGR00618  779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleeKSATLGEIThqLLKYEECS 858
                          570       580       590
                   ....*....|....*....|....*....|.
gi 1207193065 1798 NKNEQKMQQQRdELTDLEKNVTGIREYIRSK 1828
Cdd:TIGR00618  859 KQLAQLTQEQA-KIIQLSDKLNGINQIKIQF 888
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1175-1219 2.66e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 57.32  E-value: 2.66e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1207193065  1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTG-NFPKC 1219
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdGPPGC 46
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1488-1823 2.99e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 65.45  E-value: 2.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1488 VKALDNADEVhknLTAVSEELQTMAKKLRDIATLTQTVKtqakETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEEGAD 1567
Cdd:PRK02224   233 RETRDEADEV---LEEHEERREELETLEAEIEDLRETIA----ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1568 PESIEKVAQQVLAISlpvnrtvivNLVEQIKDSIVNLTNVEGVFNHTSEQLAK-VNDLLKKAQDAKTQADGVSDNINKTK 1646
Cdd:PRK02224   306 DADAEAVEARREELE---------DRDEELRDRLEECRVAAQAHNEEAESLREdADDLEERAEELREEAAELESELEEAR 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1647 EALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEAK--- 1723
Cdd:PRK02224   377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpe 456
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1724 -AQS----------DNATREAEGLQEELTNAETLYKQLKEKVDSAggtgegnvnQKAIEMKKEAEDLLKKATMGMETLKK 1792
Cdd:PRK02224   457 cGQPvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERA---------EDLVEAEDRIERLEERREDLEELIAE 527
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1207193065 1793 LERKFNKNEQKMQQQRDELTDLEKNVTGIRE 1823
Cdd:PRK02224   528 RRETIEEKRERAEELRERAAELEAEAEEKRE 558
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
454-505 4.47e-10

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: 56.59  E-value: 4.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207193065  454 PCNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSHDLAGCR 505
Cdd:cd00055      1 PCDCNGHG--SLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
cc_LAMB3_C cd22303
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ...
1767-1836 6.41e-10

C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called epiligrin subunit beta, kalinin B1 chain, kalinin subunit beta, laminin B1k chain, laminin-5 subunit beta, or nicein subunit beta. It is a major component of the basement membrane in most adult tissues. Mutations in LAMB3 are associated with Herlitz junctional epidermolysis bullosa (H-JEB), a severe autosomal recessive disorder characterized by blister formation within the dermal-epidermal basement membrane. LAMB3 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB3, which may be involved in the integrin binding activity.


Pssm-ID: 411974 [Multi-domain]  Cd Length: 71  Bit Score: 57.07  E-value: 6.41e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1767 QKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNCQ 1836
Cdd:cd22303      2 ERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
394-453 1.18e-09

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: 55.44  E-value: 1.18e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065  394 PCDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGLSLdDPLGCQ 453
Cdd:cd00055      1 PCDCNGHGSL-SGQCDPGT--------GQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
cc_LAMB1_C cd22300
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ...
1767-1835 1.79e-09

C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called laminin B1 chain, laminin-1 subunit beta, laminin-10 subunit beta, laminin-12 subunit beta, laminin-2 subunit beta, laminin-6 subunit beta, or laminin-8 subunit beta. It is a glycoprotein that is involved in the pathogenesis of neurodevelopmental disorders. It also plays a crucial role in both lung morphogenesis and physiological function. Mutations in LAMB1 are associated with Cobblestone brain malformation (COB) with variable muscular or ocular abnormalities. LAMB1 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB1, which is involved in the integrin binding activity.


Pssm-ID: 411971 [Multi-domain]  Cd Length: 73  Bit Score: 55.56  E-value: 1.79e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207193065 1767 QKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNC 1835
Cdd:cd22300      4 KKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTC 72
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
455-504 2.64e-09

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 54.28  E-value: 2.64e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207193065  455 CNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSHDLA-GC 504
Cdd:pfam00053    1 CDCNPHG--SLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPqGC 49
PTZ00121 PTZ00121
MAEBL; Provisional
1523-1816 4.00e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.08  E-value: 4.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1523 QTVKTQAKET--LDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEEGADPESIEKVAQQVLAISLpvNRTVIVNLVEQIKDS 1600
Cdd:PTZ00121  1233 EEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEA--KKAEEKKKADEAKKK 1310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1601 IVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKN---LKNIQNIT 1677
Cdd:PTZ00121  1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaAKKKAEEK 1390
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1678 AMVDD--KLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREmAKEAKAQSDNATR--EAEGLQEELTNAETLYKQLKEK 1753
Cdd:PTZ00121  1391 KKADEakKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK-ADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEA 1469
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207193065 1754 VDSAGGTGEGNVNQKAIEMKKEAEDLLKKATmgmETLKKLERKFNKNEQKMQQQRDELTDLEK 1816
Cdd:PTZ00121  1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKAD---EAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
1481-1824 6.59e-09

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 61.39  E-value: 6.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1481 NGTVGASVKALDNADEVHKNLTAVSEELqtmaKKLRDIATLTQTVKTQAKETLDKAQNKKDMFEKS----------NKML 1550
Cdd:PTZ00440   470 KSFYDLIISEKDSMDSKEKKESSDSNYQ----EKVDELLQIINSIKEKNNIVNNNFKNIEDYYITIeglkneieglIELI 545
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1551 KNFIQKIKDFLNEEGADPESIEKVAQQVLAIS---------LPVNRTvIVNLVEQIKDSI-VNLTNVEGVFNHTSEQLAK 1620
Cdd:PTZ00440   546 KYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEenvdhikdiISLNDE-IDNIIQQIEELInEALFNKEKFINEKNDLQEK 624
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1621 VNDLLKKAQDAKTQ--ADGVSDNINKTKEALETsqnaiKKAEEEMSTALKNLKNIQN-ITAMVDDkllNLDNNLTDVMMR 1697
Cdd:PTZ00440   625 VKYILNKFYKGDLQelLDELSHFLDDHKYLYHE-----AKSKEDLQTLLNTSKNEYEkLEFMKSD---NIDNIIKNLKKE 696
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1698 LVNLSNGVDLLKNKTEQNreMAKEAKAQSDNATREAeglqEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAE 1777
Cdd:PTZ00440   697 LQNLLSLKENIIKKQLNN--IEQDISNSLNQYTIKY----NDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDK 770
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1207193065 1778 DLLKKATMGMETLKKLERKFNKnEQKMQQQRDELTDLEKNVTGIREY 1824
Cdd:PTZ00440   771 DLPDGKNTYEEFLQYKDTILNK-ENKISNDINILKENKKNNQDLLNS 816
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1126-1168 7.87e-09

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: 53.13  E-value: 7.87e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1207193065 1126 PCGCVQPNALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDP 1168
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1612-1829 8.43e-09

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: 60.84  E-value: 8.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1612 NHTSEQLAKVNDLL--------------KKAQDAKTQADGVSD--------NINKTKEALETSQNAIKKAEEEMSTALKN 1669
Cdd:TIGR02168  182 ERTRENLDRLEDILnelerqlkslerqaEKAERYKELKAELRElelallvlRLEELREELEELQEELKEAEEELEELTAE 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1670 LKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNgvdlLKNKTEQNREMAKEAKAQSDnatREAEGLQEELTNAETLYKQ 1749
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELYALAN----EISRLEQQKQILRERLANLE---RQLEELEAQLEELESKLDE 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1750 LKEKVDSaggtgegnVNQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIR---EYIR 1826
Cdd:TIGR02168  335 LAEELAE--------LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNneiERLE 406

                   ...
gi 1207193065 1827 SKV 1829
Cdd:TIGR02168  407 ARL 409
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1122-1175 1.10e-08

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 52.74  E-value: 1.10e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207193065 1122 CGCEPCGcvqpnALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDPRVQCEEC 1175
Cdd:pfam00053    1 CDCNPHG-----SLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1262-1693 1.44e-08

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: 60.03  E-value: 1.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1262 KRILELEKKLAQAQELVRDGDR-----EGTFNLISQTVDDLRAEIAL----------TDGRLMGVIRDLNVTTDHnndLK 1326
Cdd:TIGR04523  391 SQINDLESKIQNQEKLNQQKDEqikklQQEKELLEKEIERLKETIIKnnseikdltnQDSVKELIIKNLDNTRES---LE 467
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1327 QNLTALEKELKDLNNTLHQLRRELE---------NYLTAGLAEQFANvLKYYQRSLNSEQrcnasvygpqspvEQSQDTR 1397
Cdd:TIGR04523  468 TQLKVLSRSINKIKQNLEQKQKELKskekelkklNEEKKELEEKVKD-LTKKISSLKEKI-------------EKLESEK 533
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1398 NRTEALLKDKKDSLLRTATANNKSLseLEGKAHEINRKVHHLSNkvcgghangnvngsceespcggagcrgsdgvlkcgg 1477
Cdd:TIGR04523  534 KEKESKISDLEDELNKDDFELKKEN--LEKEIDEKNKEIEELKQ------------------------------------ 575
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1478 rgcngtvgasvkalDNadevhKNLTAVSEELQTMAKKLRD--------IATLTQTVKTQAKEtLDKAqnkkdmfEKSNKM 1549
Cdd:TIGR04523  576 --------------TQ-----KSLKKKQEEKQELIDQKEKekkdlikeIEEKEKKISSLEKE-LEKA-------KKENEK 628
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1550 LKNFIQKIKdflneegadpESIEKVAQQvlaislpvnrtvivnlVEQIKDSIVNLTNvegvfnhtseqlaKVNDLLKKAQ 1629
Cdd:TIGR04523  629 LSSIIKNIK----------SKKNKLKQE----------------VKQIKETIKEIRN-------------KWPEIIKKIK 669
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207193065 1630 DAKTQadgVSDNINKTKEALETSQNAIKKAEEEMsTALKNL-------KNIQNITAMVDDKLLNLDNNLTD 1693
Cdd:TIGR04523  670 ESKTK---IDDIIELMKDWLKELSLHYKKYITRM-IRIKDLpkleekyKEIEKELKKLDEFSKELENIIKN 736
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
1483-1818 1.68e-08

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: 60.07  E-value: 1.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1483 TVGASVKALDNADEVHKNLTAVSEELQTMAKKLRDIATLT-QTVKTQAKETLDKAQNKK--DMFEKSNKMLKNF-----I 1554
Cdd:TIGR01612 1241 MIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNiSHDDDKDHHIISKKHDENisDIREKSLKIIEDFseesdI 1320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1555 QKIKDFLNEEGADPESIEKVAQQVLAISLPVNRTVIVNLVEQIKDSIVNLTN-VEGVFNHTSEQLAKVNDLLKKAQD--- 1630
Cdd:TIGR01612 1321 NDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNKIKKIIDEVKEYTKeIEENNKNIKDELDKSEKLIKKIKDdin 1400
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1631 ---AKTQADGVSD--NINKTKEALETSQNAIKKAEEEMSTALKNLK-NIQNITAMVDDklLNLDNNLTDVMMRLV--NLS 1702
Cdd:TIGR01612 1401 leeCKSKIESTLDdkDIDECIKKIKELKNHILSEESNIDTYFKNADeNNENVLLLFKN--IEMADNKSQHILKIKkdNAT 1478
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1703 NGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEeltnaetLYKQLKEKVDSAggtgegnVNQ-KAIEMKKEAEDLLK 1781
Cdd:TIGR01612 1479 NDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKE-------LFEQYKKDVTEL-------LNKySALAIKNKFAKTKK 1544
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1207193065 1782 KATMGMETLKKLERKF----NKNEQKMQQQRDELTDLEKNV 1818
Cdd:TIGR01612 1545 DSEIIIKEIKDAHKKFileaEKSEQKIKEIKKEKFRIEDDA 1585
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1496-1828 2.09e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.31  E-value: 2.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1496 EVHKNLTAVSEELQTMAKKLRDIAT----LTQTVKT--QAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEEGADPE 1569
Cdd:PRK03918   197 EKEKELEEVLREINEISSELPELREelekLEKEVKEleELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1570 SIEKVAQQVLAISLPVNRTVIvnLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADgvsdNINKTKEAL 1649
Cdd:PRK03918   277 ELEEKVKELKELKEKAEEYIK--LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKEL 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1650 ETSQNAIKKAEEEMSTALKNLKNIQNITAM--------VDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQ------- 1714
Cdd:PRK03918   351 EKRLEELEERHELYEEAKAKKEELERLKKRltgltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKElkkaiee 430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1715 -----------NREMAKEAKAQSDNA-TREAEGLQEELTNAETLYKQLKE---KVDSA-GGTGEGNVNQKAIEMKKEAED 1778
Cdd:PRK03918   431 lkkakgkcpvcGRELTEEHRKELLEEyTAELKRIEKELKEIEEKERKLRKelrELEKVlKKESELIKLKELAEQLKELEE 510
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1779 LLKKatMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSK 1828
Cdd:PRK03918   511 KLKK--YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1489-1795 2.10e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 57.61  E-value: 2.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1489 KALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDK-----------AQNKKDMFEKSNKmLKNFIQKI 1557
Cdd:COG1340     19 ELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKrdelnekvkelKEERDELNEKLNE-LREELDEL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1558 KDFLNEEGADPESIEKV---------AQQVLAISLPVNRtvivNLVEQIKdsivnltnvegvfnhtseQLAKvndLLKKA 1628
Cdd:COG1340     98 RKELAELNKAGGSIDKLrkeierlewRQQTEVLSPEEEK----ELVEKIK------------------ELEK---ELEKA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1629 QDAKTQADGVSDNINKTKEaletsqnaIKKAEEEMSTALKNLKN-IQNITAmvddkllnldnnltdvmmRLVNLSNGVDL 1707
Cdd:COG1340    153 KKALEKNEKLKELRAELKE--------LRKEAEEIHKKIKELAEeAQELHE------------------EMIELYKEADE 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1708 LKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKvdsaggtgegnvnQKAIEMKKEAEDLLKKATMGM 1787
Cdd:COG1340    207 LRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKK-------------QRALKREKEKEELEEKAEEIF 273

                   ....*...
gi 1207193065 1788 ETLKKLER 1795
Cdd:COG1340    274 EKLKKGEK 281
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1127-1172 2.24e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 51.54  E-value: 2.24e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1207193065  1127 CGCVQPNALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDPRVQC 1172
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
395-452 2.55e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 51.54  E-value: 2.55e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207193065   395 CDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGlslDDPLGC 452
Cdd:smart00180    1 CDCDPGGSA-SGTCDPDT--------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
910-954 2.62e-08

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: 51.59  E-value: 2.62e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207193065  910 CQCNSHA---ESCDPESGACyDCRDNTAGQLCERCVDGYYGNPALGSG 954
Cdd:cd00055      2 CDCNGHGslsGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
910-957 2.69e-08

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 51.59  E-value: 2.69e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207193065  910 CQCNSHA---ESCDPESGACyDCRDNTAGQLCERCVDGYYGNPAlGSGEHC 957
Cdd:pfam00053    1 CDCNPHGslsDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
1619-1810 5.05e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 57.15  E-value: 5.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1619 AKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNI---QNITAMVDDKLLNL--DNNLTD 1693
Cdd:COG3883     37 AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraLYRSGGSVSYLDVLlgSESFSD 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1694 VMMRlvnlsngVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggtgegnvNQKAIEMK 1773
Cdd:COG3883    117 FLDR-------LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL--------EAQQAEQE 181
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1207193065 1774 KEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDE 1810
Cdd:COG3883    182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1505-1816 5.46e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 56.46  E-value: 5.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1505 SEELQTMAKKLRDiatltqtvktQAKETLDKAQNKKDMFEKSNKMLKNFIQKiKDFLNEEGAdpESIEKvAQQVLAIslp 1584
Cdd:COG1340      3 TDELSSSLEELEE----------KIEELREEIEELKEKRDELNEELKELAEK-RDELNAQVK--ELREE-AQELREK--- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1585 vnRTVIVNLVEQIKDSIvnltnvegvfnhtSEQLAKVNDLLKKAQDAKTQADgvsdNINKTKEALETSQNAIKKAEEEMS 1664
Cdd:COG1340     66 --RDELNEKVKELKEER-------------DELNEKLNELREELDELRKELA----ELNKAGGSIDKLRKEIERLEWRQQ 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1665 TALKNLKN-------IQNITAMVDD--KLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEG 1735
Cdd:COG1340    127 TEVLSPEEekelvekIKELEKELEKakKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADE 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1736 LQEELTNAETLYKQLKEKVDsaggtgegNVNQKAIEMKKEAEDLLKKATMGMETLKKLERKfnKNEQKMQQQRDELtdLE 1815
Cdd:COG1340    207 LRKEADELHKEIVEAQEKAD--------ELHEEIIELQKELRELRKELKKLRKKQRALKRE--KEKEELEEKAEEI--FE 274

                   .
gi 1207193065 1816 K 1816
Cdd:COG1340    275 K 275
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
1260-1816 5.98e-08

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: 58.13  E-value: 5.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1260 SDKRILELEKKLAQAQELVRDGDREGTFNLISQ------------TVDDLRAEIALTDGRLMGVIRDLNVTTDHNNDLKQ 1327
Cdd:TIGR00606  533 TRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkkqledWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINN 612
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1328 NLTALEKEL-------------KDLNNTLHQLRRELE-----------------NYLTAgLAEQFANVLKYYQRSLNSEQ 1377
Cdd:TIGR00606  613 ELESKEEQLssyedklfdvcgsQDEESDLERLKEEIEksskqramlagatavysQFITQ-LTDENQSCCPVCQRVFQTEA 691
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1378 RCNASVYGPQSPVEQSQDTRNRTEALLKDK---KDSLLRTATANN-------KSLSELEGKAHEINRKVHHLSNKVCGGH 1447
Cdd:TIGR00606  692 ELQEFISDLQSKLRLAPDKLKSTESELKKKekrRDEMLGLAPGRQsiidlkeKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1448 AN-GNVNGScEESpcggagcrgsdgvlkcgGRGCNGTVGASVKALDNADEVHKNLTAVSEELQTmAKKLRDIATLTQTVK 1526
Cdd:TIGR00606  772 TLlGTIMPE-EES-----------------AKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG-SDLDRTVQQVNQEKQ 832
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1527 tQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEEGADPESIEKVAQQVLAislpvnrtvivnLVEQIKDSIVNLTN 1606
Cdd:TIGR00606  833 -EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ------------FEEQLVELSTEVQS 899
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1607 VEGVFNHTSEQLAKVNDLLKKAQDAKTQAdgvsdnINKTKEALETSQNAIKKAEEEMSTALKNLKNIQN-ITAMVDDKLL 1685
Cdd:TIGR00606  900 LIREIKDAKEQDSPLETFLEKDQQEKEEL------ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENkIQDGKDDYLK 973
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1686 NLDNNLTDVMMRLvnlsngvdllkNKTEQNREMAKE----AKAQSDNATREAEGLQEELTnAETLYKQLKEkVDSAGGTG 1761
Cdd:TIGR00606  974 QKETELNTVNAQL-----------EECEKHQEKINEdmrlMRQDIDTQKIQERWLQDNLT-LRKRENELKE-VEEELKQH 1040
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193065 1762 EGNVNQKAI-EMKKEAEDLlkkatmgMETLKKLERKFNKNEQKMQQQRDELTDLEK 1816
Cdd:TIGR00606 1041 LKEMGQMQVlQMKQEHQKL-------EENIDLIKRNHVLALGRQKGYEKEIKHFKK 1089
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
455-498 8.09e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.00  E-value: 8.09e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1207193065   455 CNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLS 498
Cdd:smart00180    1 CDCDPGG--SASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
1487-1818 8.75e-08

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: 57.75  E-value: 8.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1487 SVKALDNADEVHKNLTAVSEEL-----QTMAKKLRDIATLTQTVKTQAKETLDKAQNKkdmFEKSNKMLKNFIQKIKDFL 1561
Cdd:TIGR00606  270 EIKALKSRKKQMEKDNSELELKmekvfQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLLNQEKTELL 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1562 NEEGADPESIEKVAQQVLAISLPVNRTVI---VNLVEQIKDSIVNLTNVEGVFNHTSEQLAKV-----NDLLKKAQDAKT 1633
Cdd:TIGR00606  347 VEQGRLQLQADRHQEHIRARDSLIQSLATrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTaaqlcADLQSKERLKQE 426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1634 QADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLkniQNITAMVDDkLLNLDNNLTDVMMRLVNLSNGVDLlknKTE 1713
Cdd:TIGR00606  427 QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL---QQLEGSSDR-ILELDQELRKAERELSKAEKNSLT---ETL 499
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1714 QNREMA-KEAKAQSDNATREAEGLQEELTNAETLYKQL----KEKVDSaggtgegnvNQKAIEMKKEAEDLLKKATMGME 1788
Cdd:TIGR00606  500 KKEVKSlQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMemltKDKMDK---------DEQIRKIKSRHSDELTSLLGYFP 570
                          330       340       350
                   ....*....|....*....|....*....|
gi 1207193065 1789 TLKKLERKFNKNEQKMQQQRDELTDLEKNV 1818
Cdd:TIGR00606  571 NKKQLEDWLHSKSKEINQTRDRLAKLNKEL 600
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
1491-1814 9.24e-08

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 57.54  E-value: 9.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1491 LDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETL--------DKAQNKKDMFEKSNKMLKNFIQKIKDFLN 1562
Cdd:pfam12128  346 QEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnrdiagikDKLAKIREARDRQLAVAEDDLQALESELR 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1563 E--EGADPESIEKVAQQVLAISlpvNRTVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSD 1640
Cdd:pfam12128  426 EqlEAGKLEFNEEEYRLKSRLG---ELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD 502
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1641 N----INKTKEALETSQNAIKKAEEEMS----TALKNLKN-----IQNITAMVDDKLL---NLD-----------NNLTD 1693
Cdd:pfam12128  503 QaseaLRQASRRLEERQSALDELELQLFpqagTLLHFLRKeapdwEQSIGKVISPELLhrtDLDpevwdgsvggeLNLYG 582
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1694 VMMRL----VN--------LSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggTG 1761
Cdd:pfam12128  583 VKLDLkridVPewaaseeeLRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRL--FD 660
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207193065 1762 EGNVNQKAIEMKKEAEdlLKKATMGMETLKKlERKFNKNEQK--MQQQRDELTDL 1814
Cdd:pfam12128  661 EKQSEKDKKNKALAER--KDSANERLNSLEA-QLKQLDKKHQawLEEQKEQKREA 712
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
1512-1828 9.92e-08

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 56.89  E-value: 9.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1512 AKKLRDIATLTQTVKTQaketLDKAQNKKDMFEKSN---KMLKNFIQKIKDFLNEEGADPESIEKVAQQVLaiSLPVNRT 1588
Cdd:COG5185     85 ARKFLKEKKLDTKILQE----YVNSLIKLPNYEWSAdilISLLYLYKSEIVALKDELIKVEKLDEIADIEA--SYGEVET 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1589 VIVNLVEQI-KDSIVNLTNVEGVFNHTSEQLAKVNDLlKKAQDAKTQadgvsdNINKTKEALET---SQNAIKKAEEEms 1664
Cdd:COG5185    159 GIIKDIFGKlTQELNQNLKKLEIFGLTLGLLKGISEL-KKAEPSGTV------NSIKESETGNLgseSTLLEKAKEII-- 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1665 TALKNLKNIQNITAMVDDKllnldNNLTDVMMRLVNLSNgvDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAE 1744
Cdd:COG5185    230 NIEEALKGFQDPESELEDL-----AQTSDKLEKLVEQNT--DLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYT 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1745 tlykqlkEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGmetLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREY 1824
Cdd:COG5185    303 -------KSIDIKKATESLEEQLAAAEAEQELEESKRETETG---IQNLTAEIEQGQESLTENLEAIKEEIENIVGEVEL 372

                   ....
gi 1207193065 1825 IRSK 1828
Cdd:COG5185    373 SKSS 376
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
1264-1827 1.08e-07

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 57.16  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1264 ILELEKKLAQAQELVRDGDREGTFNLISQTvDDLRAEIALTDGRLMGVIRDLNVTTDH----NNDLKQNLTA-LEKELKD 1338
Cdd:pfam12128  267 YKSDETLIASRQEERQETSAELNQLLRTLD-DQWKEKRDELNGELSAADAAVAKDRSElealEDQHGAFLDAdIETAAAD 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1339 LNNtLHQLRRELENY--LTAGLAEQFANVLKYYQ-RSLNSEQRCNASVYGPQSPVEQSQDTRNRTEALLKDKKDSL---L 1412
Cdd:pfam12128  346 QEQ-LPSWQSELENLeeRLKALTGKHQDVTAKYNrRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeseL 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1413 RtatannkslSELEGKAHEINRKVHHLSNKVcgGHANGNVNGSCEESpcggagcrgsDGVLKcggrgcngtVGASVKALD 1492
Cdd:pfam12128  425 R---------EQLEAGKLEFNEEEYRLKSRL--GELKLRLNQATATP----------ELLLQ---------LENFDERIE 474
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1493 NADEVHKNLTAVSEELQ---TMAKKLRDIATLTQTVKTQAKETLDKA--QNKKDMFEKSNKMLknfiqkikDFLNEEGAD 1567
Cdd:pfam12128  475 RAREEQEAANAEVERLQselRQARKRRDQASEALRQASRRLEERQSAldELELQLFPQAGTLL--------HFLRKEAPD 546
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1568 -PESIEKVAQQVLaislpVNRTVIVNLV--EQIKDSIvnltNVEGVFNHTseQLAKVNDLLKKAQDAKTQADgvsdninK 1644
Cdd:pfam12128  547 wEQSIGKVISPEL-----LHRTDLDPEVwdGSVGGEL----NLYGVKLDL--KRIDVPEWAASEEELRERLD-------K 608
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1645 TKEALETSQNAIKKAEEEMSTALKNLKNIQnitAMVDDKLLNLDNNltdvMMRLVNLSNGVDLLKNKTEQNREmakEAKA 1724
Cdd:pfam12128  609 AEEALQSAREKQAAAEEQLVQANGELEKAS---REETFARTALKNA----RLDLRRLFDEKQSEKDKKNKALA---ERKD 678
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1725 QSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGMET-----LKKLERKFNK 1799
Cdd:pfam12128  679 SANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSgakaeLKALETWYKR 758
                          570       580
                   ....*....|....*....|....*...
gi 1207193065 1800 NEQKMQQQRDELTDLEknvTGIREYIRS 1827
Cdd:pfam12128  759 DLASLGVDPDVIAKLK---REIRTLERK 783
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
1506-1825 1.24e-07

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 57.15  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1506 EELQTMAKKLRDIATLTQTV-KTQAKETLD---KAQNKKDMFEKSNKML----KNF-IQKIKDFLN---------EEGAD 1567
Cdd:PTZ00440  2226 QEIENSSEKYNDISKLFNNVvETQKKKLLDnknKINNIKDKINDKEKELinvdSSFtLESIKTFNEiyddiksniGDLYK 2305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1568 PESIEKVAQQVLAISLPvNRTVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKaqdaktqadgVSDNINKTKE 1647
Cdd:PTZ00440  2306 LEDTNNDELKKVKLYIE-NITHLLNRINTLINDLDNYQDENYGKDKNIELNNENNSYIIK----------TKEKINNLKE 2374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1648 ALETSQNAIKKAEEEMSTalKNLKN-IQNITAMVDD-------------KLLNLDNNLTDV--MMRLVNLSNGVDLLKNK 1711
Cdd:PTZ00440  2375 EFSKLLKNIKRNNTLCNN--NNIKDfISNIGKSVETikqrfssnlpekeKLHQIEENLNEIknIMNETKRISNVDAFTNK 2452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1712 TEQNREMAKEakaqSDNATREAEGLQEELTNAETLYKQLKEKVDSAggtgeGNVNQKAIEMKKEAEDLLKKATMGMETLK 1791
Cdd:PTZ00440  2453 ILQDIDNEKN----KENNNMNAEKIDDLIENVTSHNEKIKSELLII-----NDALRRVKEKKDEMNKLFNSLTENNNNNN 2523
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1207193065 1792 KLERKFNKNEQKMQQQrdeltdLEKNVTGIREYI 1825
Cdd:PTZ00440  2524 NSAKNIVDNSTYIINE------LESHVSKLNELL 2551
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
960-1016 1.33e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 49.66  E-value: 1.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193065  960 CPCPGHPdsghSNGASCEvdyaSNQILCQCGQGYAGPRCDRCAPGYYGDPEHPGGSC 1016
Cdd:pfam00053    1 CDCNPHG----SLSDTCD----PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1617-1795 1.60e-07

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: 54.16  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1617 QLAKVNDLLKKA----QDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQnitamvdDKLLNLDNNlt 1692
Cdd:COG1579     18 ELDRLEHRLKELpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------EQLGNVRNN-- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1693 dvmmR-LVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggtgEGNVNQKAIE 1771
Cdd:COG1579     89 ----KeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE----LAELEAELEE 160
                          170       180
                   ....*....|....*....|....
gi 1207193065 1772 MKKEAEDLLKKatMGMETLKKLER 1795
Cdd:COG1579    161 LEAEREELAAK--IPPELLALYER 182
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1261-1828 1.90e-07

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: 56.60  E-value: 1.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1261 DKRILELEKKLAQAQelvrdgdreGTFNLISQTVDDLRAEIALTDGRLMGVIRDLNVTTDHNNDLKQNLTALEKELKDLN 1340
Cdd:TIGR02168  273 RLEVSELEEEIEELQ---------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1341 NTLHQLRRELEnyltaGLAEQFANVLKYYQrslNSEQRcnasvygpqspVEQSQDTRNRtealLKDKKDSLLRTATANNK 1420
Cdd:TIGR02168  344 EKLEELKEELE-----SLEAELEELEAELE---ELESR-----------LEELEEQLET----LRSKVAQLELQIASLNN 400
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1421 SLSELEGKAHEINRKVHHLSNKVcgghangnvngsceespcGGAGCRGSDGVLKCGGRGCNGTvgasvkaldnaDEVHKN 1500
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEI------------------EELLKKLEEAELKELQAELEEL-----------EEELEE 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1501 LTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKD-FLNEEG-------------A 1566
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAlLKNQSGlsgilgvlselisV 531
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1567 DPE---SIEKV----AQQVL---------AIS----------------------LPVNRTVIVNLVEQIKDSIVNL---- 1604
Cdd:TIGR02168  532 DEGyeaAIEAAlggrLQAVVvenlnaakkAIAflkqnelgrvtflpldsikgteIQGNDREILKNIEGFLGVAKDLvkfd 611
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1605 TNVEGVFNHTSEQLAKVNDLLKKAQDAK---------TQaDGvsDNINK----TKEALETS------QNAIKKAEEEMST 1665
Cdd:TIGR02168  612 PKLRKALSYLLGGVLVVDDLDNALELAKklrpgyrivTL-DG--DLVRPggviTGGSAKTNssilerRREIEELEEKIEE 688
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1666 ALKNLKNIQNITAMVDDKLLNLDNNLTDVMMR-------LVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQE 1738
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKEleelsrqISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1739 ELTNAETLYKQLKEKVDSAggtgEGNVNQKAIEMKKEAEDLLKKAtmgmETLKKLERKFNKNEQKMQQQRDELTDLEKNV 1818
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEEL----EAQIEQLKEELKALREALDELR----AELTLLNEEAANLRERLESLERRIAATERRL 840
                          650
                   ....*....|
gi 1207193065 1819 TGIREYIRSK 1828
Cdd:TIGR02168  841 EDLEEQIEEL 850
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1089-1129 2.64e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.89  E-value: 2.64e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1207193065 1089 QCDKQTGQCPCKQNIIGHNCDQCATNHWNFGSDCgcePCGC 1129
Cdd:pfam00053   12 TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP---PQGC 49
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
1489-1829 2.87e-07

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 55.99  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1489 KALDNADEVHKNLTAVSEELQTMAKK-----LRDIATLTQTVKTQAKETLDKAQN--KKDMFEKSNKMLKNFiQKIKDFL 1561
Cdd:PTZ00440   659 KSKEDLQTLLNTSKNEYEKLEFMKSDnidniIKNLKKELQNLLSLKENIIKKQLNniEQDISNSLNQYTIKY-NDLKSSI 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1562 NEEGADPESIEKVAQQVLAI------SLPVNRTVIV---NLVEQI---KDSIVNLTN----------------------- 1606
Cdd:PTZ00440   738 EEYKEEEEKLEVYKHQIINRknefilHLYENDKDLPdgkNTYEEFlqyKDTILNKENkisndinilkenkknnqdllnsy 817
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1607 ---VEGVFNHTSEQLAKVNDLLKK----------AQDAKT--QADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLK 1671
Cdd:PTZ00440   818 nilIQKLEAHTEKNDEELKQLLQKfptedenlnlKELEKEfnENNQIVDNIIKDIENMNKNINIIKTLNIAINRSNSNKQ 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1672 NIqnitamvdDKLLNLDNNLTDVM---MRLVNLSNGVDllknkteqnremaKEAKAQ-SDNATREAEGLQEELTNA---- 1743
Cdd:PTZ00440   898 LV--------EHLLNNKIDLKNKLeqhMKIINTDNIIQ-------------KNEKLNlLNNLNKEKEKIEKQLSDTkinn 956
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1744 ------ETL--YKQLKEKVDSAGGTGEgnvnQKAIEMKKEAEDLLKKatmgmetLKKLERKFNKNEQKM----QQQRDEL 1811
Cdd:PTZ00440   957 lkmqieKTLeyYDKSKENINGNDGTHL----EKLDKEKDEWEHFKSE-------IDKLNVNYNILNKKIddliKKQHDDI 1025
                          410
                   ....*....|....*....
gi 1207193065 1812 TDL-EKNVTGIREYIRSKV 1829
Cdd:PTZ00440  1026 IELiDKLIKEKGKEIEEKV 1044
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1616-1834 3.18e-07

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: 55.83  E-value: 3.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1616 EQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNlknIQNITAMVDDKLLNLdNNLTDVM 1695
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE---VEQLEERIAQLSKEL-TELEAEI 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1696 MRLVNLSNGVDLLKNKTEQNREmakEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAiEMKKE 1775
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIE---ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA-ATERR 839
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207193065 1776 AEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNN 1834
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1584-1832 3.60e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.52  E-value: 3.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1584 PVNRTVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQD----AKTQADGVSDNINKTKEALETSQNAIKKA 1659
Cdd:COG4372     20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEeleqARSELEQLEEELEELNEQLQAAQAELAQA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1660 EEEMSTALKNLKNIQnitamvdDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEE 1739
Cdd:COG4372    100 QEELESLQEEAEELQ-------EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1740 LTNAET--LYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKN 1817
Cdd:COG4372    173 LQALSEaeAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
                          250
                   ....*....|....*
gi 1207193065 1818 VTGIREYIRSKVLAY 1832
Cdd:COG4372    253 EEVILKEIEELELAI 267
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
1284-1821 3.63e-07

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 55.61  E-value: 3.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1284 EGTFNLISQTVDDLRAEIALTDGRLmGVIRDLNVTTDHNNDLKQNLTALEKELKDLNNTLHQLRRELENYLTAGLAEQ-- 1361
Cdd:PTZ00440   855 EKEFNENNQIVDNIIKDIENMNKNI-NIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKln 933
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1362 FANVLKYYQRSLNsEQRCNASVYGPQSPVEQSQDTRNRTEALLKDKKDSLLRTATANNKSLSELEGKAHEINRKVHHLSN 1441
Cdd:PTZ00440   934 LLNNLNKEKEKIE-KQLSDTKINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEIDKLNVNYNILNK 1012
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1442 KVcgghaNGNVNGSCEESpcggagCRGSDGVLKCGGRGCNGTVGASVKALD----------NADEVHKNLTAVS-EELQT 1510
Cdd:PTZ00440  1013 KI-----DDLIKKQHDDI------IELIDKLIKEKGKEIEEKVDQYISLLEkmktklssfhFNIDIKKYKNPKIkEEIKL 1081
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1511 MAKKLRDI--------ATLTQtVKTQAKE---TLDKAQNK-KDMFEKSNKMLKNFIQKIKDFLNE-EGADPESIekVAQQ 1577
Cdd:PTZ00440  1082 LEEKVEALlkkidenkNKLIE-IKNKSHEhvvNADKEKNKqTEHYNKKKKSLEKIYKQMEKTLKElENMNLEDI--TLNE 1158
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1578 VLAISLPVNRTVIVNLVEQIKDSIV-----------------------------NLTNVE--GVFNHTSEQLAKVNDLLK 1626
Cdd:PTZ00440  1159 VNEIEIEYERILIDHIVEQINNEAKksktimeeiesykkdidqvkknmskerndHLTTFEynAYYDKATASYENIEELTT 1238
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1627 KAQDAKTQADGvSDNINKTK----EALETSQNAIKKAEEeMSTALKNLKNIQNITAMVD------------DKLLNLDNN 1690
Cdd:PTZ00440  1239 EAKGLKGEANR-STNVDELKeiklQVFSYLQQVIKENNK-MENALHEIKNMYEFLISIDsekilkeilnstKKAEEFSND 1316
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1691 LTDVMMRLVNLSNGV--DLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAE-------TLYKQLKEKVDSA---- 1757
Cdd:PTZ00440  1317 AKKELEKTDNLIKQVeaKIEQAKEHKNKIYGSLEDKQIDDEIKKIEQIKEEISNKRkeinkylSNIKSNKEKCDLHvrna 1396
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193065 1758 --GGTGEGNVNQKAIEMKKEAEDL-LKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGI 1821
Cdd:PTZ00440  1397 srGKDKIDFLNKHEAIEPSNSKEVnIIKITDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNI 1463
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1019-1063 3.83e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.50  E-value: 3.83e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1207193065 1019 CQCNGNIDPQDpeSCDPRTGLCLkCLYNTDGDSCSECKLGYYGNA 1063
Cdd:pfam00053    1 CDCNPHGSLSD--TCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
506-545 4.82e-07

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: 48.12  E-value: 4.82e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1207193065  506 PCNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
1530-1823 4.83e-07

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: 55.44  E-value: 4.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1530 KETLDKaqNKKDM----FEKSNKMLKNFIQKI----KDFLNEEGADPESIEKVAQQVLAISLPVNRTVIVNLVEQIKDSI 1601
Cdd:TIGR01612 1006 KANLGK--NKENMlyhqFDEKEKATNDIEQKIedanKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINI 1083
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1602 VNLTNVEGVFNH-------TSEQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIkkaeEEMSTALKNLKNIQ 1674
Cdd:TIGR01612 1084 TNFNEIKEKLKHynfddfgKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYI----DEIKAQINDLEDVA 1159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1675 NiTAMVDDkllnldnNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKE-AKAQSDNAT-REAEGLQeeLTNAETLYKQLKE 1752
Cdd:TIGR01612 1160 D-KAISND-------DPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEiAEIEKDKTSlEEVKGIN--LSYGKNLGKLFLE 1229
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207193065 1753 KVDSAGGTGEGNVnqKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDL-------EKNVTGIRE 1823
Cdd:TIGR01612 1230 KIDEEKKKSEHMI--KAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHhiiskkhDENISDIRE 1305
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1490-1803 5.22e-07

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.07  E-value: 5.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1490 ALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNF---IQKIKDFLNEEGA 1566
Cdd:TIGR02169  707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELeedLHKLEEALNDLEA 786
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1567 D--PESIEKVAQQVLAIslpvnRTVIVNLVEQIKDsivnltnVEGVFN--HTSEQLA--KVNDLLKKAQDAKTQADGVS- 1639
Cdd:TIGR02169  787 RlsHSRIPEIQAELSKL-----EEEVSRIEARLRE-------IEQKLNrlTLEKEYLekEIQELQEQRIDLKEQIKSIEk 854
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1640 --DNINKTKEALETSQNAIKKAEEEMSTALKNLKNiqnitamvddKLLNLDNNLTDVMMRLVNLSNGVDLLK---NKTEQ 1714
Cdd:TIGR02169  855 eiENLNGKKEELEEELEELEAALRDLESRLGDLKK----------ERDELEAQLRELERKIEELEAQIEKKRkrlSELKA 924
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1715 NREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEgnVNQKAIEMKKEAEDLL-----KKATMGMET 1789
Cdd:TIGR02169  925 KLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP--VNMLAIQEYEEVLKRLdelkeKRAKLEEER 1002
                          330
                   ....*....|....
gi 1207193065 1790 LKKLERKFNKNEQK 1803
Cdd:TIGR02169 1003 KAILERIEEYEKKK 1016
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
1390-1830 5.86e-07

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 54.84  E-value: 5.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1390 VEQSQDTRNRTE-ALLKDKKDSLLRTATANNKSLSELEGKAHEinrkvhhlsNKVcgghangNVNGSCEESPCGGAGCRG 1468
Cdd:PTZ00440  1067 IKKYKNPKIKEEiKLLEEKVEALLKKIDENKNKLIEIKNKSHE---------HVV-------NADKEKNKQTEHYNKKKK 1130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1469 SDG-VLKcggrgcngTVGASVKALDNADEVHKNLTAVSE-ELQ-------TMAKKLRDIATLTQTVKTQAKETLDKA-QN 1538
Cdd:PTZ00440  1131 SLEkIYK--------QMEKTLKELENMNLEDITLNEVNEiEIEyerilidHIVEQINNEAKKSKTIMEEIESYKKDIdQV 1202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1539 KKDMFEKSNKMLKNFiqKIKDFLNEEGADPESIEKVAQQVLAISLPVNRTVIVNLVEQIKDSI-VNLTNVEGVFNHTSEQ 1617
Cdd:PTZ00440  1203 KKNMSKERNDHLTTF--EYNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELKEIKLQVfSYLQQVIKENNKMENA 1280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1618 LAK---VNDLL----------------KKAQDAKTQADGV---SDNINKTKEA----LETSQNAIKKAEE--EMSTALKN 1669
Cdd:PTZ00440  1281 LHEiknMYEFLisidsekilkeilnstKKAEEFSNDAKKElekTDNLIKQVEAkieqAKEHKNKIYGSLEdkQIDDEIKK 1360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1670 LKNIQ----NITAMVDDKLLNLDNNLTDVMMRLVNLSNG---VDLLKNKTEQNREMAKEAKAQsdNATREAEGLQEELTN 1742
Cdd:PTZ00440  1361 IEQIKeeisNKRKEINKYLSNIKSNKEKCDLHVRNASRGkdkIDFLNKHEAIEPSNSKEVNII--KITDNINKCKQYSNE 1438
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1743 AETLYKQLKEKVDSAggtgegnvnqkaIEMKKEAEDLLKKAT-MGMETlkKLERKfnkneqkmqqqRDELTDLEKNVTGI 1821
Cdd:PTZ00440  1439 AMETENKADENNDSI------------IKYEKEITNILNNSSiLGKKT--KLEKK-----------KKEATNIMDDINGE 1493

                   ....*....
gi 1207193065 1822 REYIRSKVL 1830
Cdd:PTZ00440  1494 HSIIKTKLT 1502
PTZ00121 PTZ00121
MAEBL; Provisional
1494-1828 5.97e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 5.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1494 ADEVHKNLTAV---SEELQTMAKKLRDIATLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDflNEEGADPES 1570
Cdd:PTZ00121  1485 ADEAKKKAEEAkkkADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK--AEELKKAEE 1562
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1571 IEKVAQQVLAISlpvNRTVIVNLVEQIKDsiVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADgvsdNINKTKEALE 1650
Cdd:PTZ00121  1563 KKKAEEAKKAEE---DKNMALRKAEEAKK--AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE----ELKKAEEEKK 1633
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1651 TSQNAIKKAEEEMSTA--LKNLKNIQNITAmvddkllnldnnltdvmmrlvnlsngvDLLKNKTEQNREMAKEAKAQSDN 1728
Cdd:PTZ00121  1634 KVEQLKKKEAEEKKKAeeLKKAEEENKIKA---------------------------AEEAKKAEEDKKKAEEAKKAEED 1686
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1729 ATREAEGLQ---EELTNAETLYKQLKEKVDSAGGT-GEGNVNQ-KAIEMKKEAEDLLKKAtmgmETLKKLERKFNKNEQK 1803
Cdd:PTZ00121  1687 EKKAAEALKkeaEEAKKAEELKKKEAEEKKKAEELkKAEEENKiKAEEAKKEAEEDKKKA----EEAKKDEEEKKKIAHL 1762
                          330       340
                   ....*....|....*....|....*.
gi 1207193065 1804 MQQQRDELTDLEKNVTG-IREYIRSK 1828
Cdd:PTZ00121  1763 KKEEEKKAEEIRKEKEAvIEEELDEE 1788
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
1494-1813 6.07e-07

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 54.58  E-value: 6.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1494 ADEVHKNLTAvSEELQTmaKKLRDIATLTQTVKTQAKETLDKAQNKKDmfEKSNKMLKNFIQKIKDFLNEEGADPESIEK 1573
Cdd:COG5185    252 SDKLEKLVEQ-NTDLRL--EKLGENAESSKRLNENANNLIKQFENTKE--KIAEYTKSIDIKKATESLEEQLAAAEAEQE 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1574 VAQQVLAISlpvnrTVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQdaktQADGVSDNINKTKEALETSQ 1653
Cdd:COG5185    327 LEESKRETE-----TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSE----ELDSFKDTIESTKESLDEIP 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1654 NAIKKAEEEmstalkNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVD-LLKNKTEQNREMAKEAKAQSDNATRE 1732
Cdd:COG5185    398 QNQRGYAQE------ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNeLISELNKVMREADEESQSRLEEAYDE 471
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1733 AE-GLQEELTNAETLYKQLKEKVDSAGGTGEGNVNqkaiEMKKEAEDLLKKATMGMETLKKLERK---FNKNEQKMQQQR 1808
Cdd:COG5185    472 INrSVRSKKEDLNEELTQIESRVSTLKATLEKLRA----KLERQLEGVRSKLDQVAESLKDFMRArgyAHILALENLIPA 547

                   ....*
gi 1207193065 1809 DELTD 1813
Cdd:COG5185    548 SELIQ 552
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
910-952 7.42e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 47.31  E-value: 7.42e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1207193065   910 CQCN---SHAESCDPESGACyDCRDNTAGQLCERCVDGYYGNPALG 952
Cdd:smart00180    1 CDCDpggSASGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
507-545 7.71e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 47.31  E-value: 7.71e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1207193065   507 CNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
959-1014 8.60e-07

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: 47.35  E-value: 8.60e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193065  959 PCPCPGHPdsghSNGASCevDYASNQilCQCGQGYAGPRCDRCAPGYYGDPEHPGG 1014
Cdd:cd00055      1 PCDCNGHG----SLSGQC--DPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1663-1829 1.39e-06

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: 51.46  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1663 MSTALKNLKNIQNItamvDDKLLNLDNNLTDVMMRLVNLsngvdllKNKTEQNREMAKEAKAQSDNATREAEGLQEELTN 1742
Cdd:COG1579      2 MPEDLRALLDLQEL----DSELDRLEHRLKELPAELAEL-------EDELAALEARLEAAKTELEDLEKEIKRLELEIEE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1743 AETLYKQLKEKVDSAGGTGEGNVNQKAIEM----KKEAEDLLKKAtmgMETLKKLERKFNKNEQKMQQQRDELTDLEKNV 1818
Cdd:COG1579     71 VEARIKKYEEQLGNVRNNKEYEALQKEIESlkrrISDLEDEILEL---MERIEELEEELAELEAELAELEAELEEKKAEL 147
                          170
                   ....*....|.
gi 1207193065 1819 TGIREYIRSKV 1829
Cdd:COG1579    148 DEELAELEAEL 158
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1070-1120 1.42e-06

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: 46.58  E-value: 1.42e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207193065 1070 RCTCVTAGTLPNsctdgvcQCDKQTGQCPCKQNIIGHNCDQCATNHWNFGS 1120
Cdd:cd00055      1 PCDCNGHGSLSG-------QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
1489-1648 1.52e-06

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 51.99  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1489 KALDNADEVHKNLTAVSEELQTMAKKLRDIAT-----LTQTVKTQAKETLDKAQNK-KDMFEKSNKMLKNFIQKIKDFLN 1562
Cdd:cd22656    132 KYQDKAAKVVDKLTDFENQTEKDQTALETLEKalkdlLTDEGGAIARKEIKDLQKElEKLNEEYAAKLKAKIDELKALIA 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1563 EEGADPESIEKVAQQVLAISlpvnrTVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQD-------AKTQA 1635
Cdd:cd22656    212 DDEAKLAAALRLIADLTAAD-----TDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISkipaailAKLEL 286
                          170
                   ....*....|...
gi 1207193065 1636 DGVSDNINKTKEA 1648
Cdd:cd22656    287 EKAIEKWNELAEK 299
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
267-320 1.69e-06

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: 46.58  E-value: 1.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193065  267 SCFCYGHAS---ECAPVpgvttrdsgmiHGRCVCKHNTVGLNCERCRDFYHDAPWRP 320
Cdd:cd00055      1 PCDCNGHGSlsgQCDPG-----------TGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
1541-1813 1.76e-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: 53.13  E-value: 1.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1541 DMFEK---SNKMLKNFIQkikdfLNEEGADPESieKVAQQVLAiSLPVNRTVIVNLVEQIKDsivNLTNVEGVFNHTSEQ 1617
Cdd:TIGR00606  380 DGFERgpfSERQIKNFHT-----LVIERQEDEA--KTAAQLCA-DLQSKERLKQEQADEIRD---EKKGLGRTIELKKEI 448
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1618 LAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMS--TALKNLKNIQNITAMVDDKLLNLDNNLTDVM 1695
Cdd:TIGR00606  449 LEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLteTLKKEVKSLQNEKADLDRKLRKLDQEMEQLN 528
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1696 MRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEkvdsaggtgegnvnqkaiemKKE 1775
Cdd:TIGR00606  529 HHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKE--------------------INQ 588
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1207193065 1776 AEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTD 1813
Cdd:TIGR00606  589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED 626
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1018-1069 2.02e-06

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: 46.19  E-value: 2.02e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207193065 1018 PCQCNGNIDPqdPESCDPRTGLCLkCLYNTDGDSCSECKLGYYGNALI-QDCR 1069
Cdd:cd00055      1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1488-1817 2.77e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 2.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1488 VKALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKtQAKETLDKAQNKKDMFEKSNKM------LKNFIQKIKDFL 1561
Cdd:PRK03918   303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELyeeakaKKEELERLKKRL 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1562 NeegadPESIEKVAQQVLAISlpvnrtvivNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQD------AKTQA 1635
Cdd:PRK03918   382 T-----GLTPEKLEKELEELE---------KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgRELTE 447
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1636 DGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMvDDKLLNLdNNLTDVMMRLVNLSNGVDL--LKNKTE 1713
Cdd:PRK03918   448 EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKL-KELAEQLKELEEKLKKYNLeeLEKKAE 525
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1714 QNREMAKEA---KAQSDNATREAEGLQE----------ELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEM-------- 1772
Cdd:PRK03918   526 EYEKLKEKLiklKGEIKSLKKELEKLEElkkklaelekKLDELEEELAELLKELEELGFESVEELEERLKELepfyneyl 605
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1773 -----KKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKN 1817
Cdd:PRK03918   606 elkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1262-1834 2.89e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 2.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1262 KRILELEKKLAQAQELVRDgdREGTFNLISQtvddLRAEIALTDGRLMGVIRDLNVTTDHNNDLKQNLTALEKELKDLNn 1341
Cdd:PRK03918   214 SELPELREELEKLEKEVKE--LEELKEEIEE----LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK- 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1342 tlhQLRRELENYLTagLAEQFANVLKYYQRSLNSEQRCNASVYGPQSPVEQSQDTRNRTEALLKDKKDSLlrtatannKS 1421
Cdd:PRK03918   287 ---ELKEKAEEYIK--LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE--------KR 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1422 LSELEGKAHEINRKVHHLSNKvcgghangnvngsceespcggagcrgsDGVLKcggRGCNGTVGASVKALDnadEVHKNL 1501
Cdd:PRK03918   354 LEELEERHELYEEAKAKKEEL---------------------------ERLKK---RLTGLTPEKLEKELE---ELEKAK 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1502 TAVSEELQTMAKKLRDIATLTQTVKTqAKETLDKAQNK-------------KDMFEKSNKMLKNFIQKIKDFLNEEgadp 1568
Cdd:PRK03918   401 EEIEEEISKITARIGELKKEIKELKK-AIEELKKAKGKcpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKE---- 475
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1569 ESIEKVAQQVlAISLPVNRTVIVN--LVEQIKdsivnltNVEgvfnhtsEQLAKVNdlLKKAQDAKTQADgvsdninKTK 1646
Cdd:PRK03918   476 RKLRKELREL-EKVLKKESELIKLkeLAEQLK-------ELE-------EKLKKYN--LEELEKKAEEYE-------KLK 531
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1647 EALETSQNAIKKAEEEmstaLKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNG-VDLLKNKTEQNREMAK---EA 1722
Cdd:PRK03918   532 EKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNeylEL 607
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1723 KaqsdNATREAEGLQEELtnaetlyKQLKEKVDSAggTGEGNVNQKAIEM-KKEAEDLLKKATMgmETLKKLERKFNKNE 1801
Cdd:PRK03918   608 K----DAEKELEREEKEL-------KKLEEELDKA--FEELAETEKRLEElRKELEELEKKYSE--EEYEELREEYLELS 672
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207193065 1802 ----------QKMQQQRDE----LTDLEKNVTGIREY----------------IRSKVLAYNN 1834
Cdd:PRK03918   673 relaglraelEELEKRREEikktLEKLKEELEEREKAkkeleklekalerveeLREKVKKYKA 735
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
1488-1825 3.48e-06

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 52.36  E-value: 3.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1488 VKALDNadEVHKNLTAVSE----------ELQTMAKKLRDIATLT------QTVKTQAKETLDKAQNKKDMFEKSNKMLk 1551
Cdd:TIGR01612 1120 IKNLDQ--KIDHHIKALEEikkksenyidEIKAQINDLEDVADKAisnddpEEIEKKIENIVTKIDKKKNIYDEIKKLL- 1196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1552 NFIQKIKDflneegaDPESIEKVAQQVLAISLPVNRTVIVNLVEQIKDS-----------------------IVNLTNVE 1608
Cdd:TIGR01612 1197 NEIAEIEK-------DKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSehmikameayiedldeikekspeIENEMGIE 1269
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1609 GVFNHTSEQLAKVNDLLKKAQD-AKTQADGVSD----------------NINKTKEALETSQNAIKKAEEEMSTALKNLK 1671
Cdd:TIGR01612 1270 MDIKAEMETFNISHDDDKDHHIiSKKHDENISDirekslkiiedfseesDINDIKKELQKNLLDAQKHNSDINLYLNEIA 1349
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1672 NIQNItamvddkllnldnnltdvmMRLVNLSNGVDLLKNKTEQNREMAKEAKaqsdnatreaeglqEELTNAETLYKQLK 1751
Cdd:TIGR01612 1350 NIYNI-------------------LKLNKIKKIIDEVKEYTKEIEENNKNIK--------------DELDKSEKLIKKIK 1396
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1752 EKV--DSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGMET-------------------LKKLERKFNKNEQKMQQQRDE 1810
Cdd:TIGR01612 1397 DDInlEECKSKIESTLDDKDIDECIKKIKELKNHILSEESnidtyfknadennenvlllFKNIEMADNKSQHILKIKKDN 1476
                          410
                   ....*....|....*.
gi 1207193065 1811 LT-DLEKNVTGIREYI 1825
Cdd:TIGR01612 1477 ATnDHDFNINELKEHI 1492
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
1487-1823 3.63e-06

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 52.53  E-value: 3.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1487 SVKALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDKaQNKKDMfEKSNKMLKNFIQKIKDflneEGA 1566
Cdd:PTZ00440  2032 SVKTLKASENIKKIVENKKTSIDAINTNIEDIEKEIESINPSLDELLKK-GHKIEI-SRYTSIIDNVQTKISN----DSK 2105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1567 DPESIEKVAQQVLAiSLPVNRTVIVNLVEQI-----KDSIVN--LTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVS 1639
Cdd:PTZ00440  2106 NINDIEKKAQIYLA-YIKNNYNSIKKDISTLneyfdEKQVSNyiLTNIDKANKLSSELSEAVTNSEEIIENIKKEIIEIN 2184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1640 DN-----INKTKEALETSQNAIKKAE---------------EEM----------STALKN---------------LKNIQ 1674
Cdd:PTZ00440  2185 ENtemntLENTADKLKELYENLKKKKniinniykkinfiklQEIenssekyndiSKLFNNvvetqkkklldnknkINNIK 2264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1675 NITAMVDDKLLNLDNNLTDVMMRLVNlsNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKV 1754
Cdd:PTZ00440  2265 DKINDKEKELINVDSSFTLESIKTFN--EIYDDIKSNIGDLYKLEDTNNDELKKVKLYIENITHLLNRINTLINDLDNYQ 2342
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207193065 1755 DsaggtgEGNVNQKAIEMKKEAEDLLKKATmgmETLKKLERKFNKNEQKMQQQ---------RDELTDLEKNVTGIRE 1823
Cdd:PTZ00440  2343 D------ENYGKDKNIELNNENNSYIIKTK---EKINNLKEEFSKLLKNIKRNntlcnnnniKDFISNIGKSVETIKQ 2411
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1071-1118 4.29e-06

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 45.38  E-value: 4.29e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1207193065  1071 CTCVTAGTLPNsctdgvcQCDKQTGQCPCKQNIIGHNCDQCATNHWNF 1118
Cdd:smart00180    1 CDCDPGGSASG-------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD 41
cc_LAMB2_C cd22299
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ...
1768-1836 4.90e-06

C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.


Pssm-ID: 411970 [Multi-domain]  Cd Length: 72  Bit Score: 45.90  E-value: 4.90e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207193065 1768 KAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNCQ 1836
Cdd:cd22299      4 KAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1492-1811 9.47e-06

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: 50.83  E-value: 9.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1492 DNADEVHKNLtavsEELQTMAKK----------LRDI-ATLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDF 1560
Cdd:TIGR02168  193 DILNELERQL----KSLERQAEKaerykelkaeLRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1561 LNE-EGADPESIEKVAQQ---VLAISLPVNRtvivnLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQAD 1636
Cdd:TIGR02168  269 LEElRLEVSELEEEIEELqkeLYALANEISR-----LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1637 GVSDNINKTKEALETSQNAIKKAEEEMSTALKNLkniqnitamvDDKLLNLDNNLTDvmmrlvnLSNGVDLLKNKTEQNR 1716
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEEL----------EEQLETLRSKVAQ-------LELQIASLNNEIERLE 406
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1717 EMAKEAKAQSDNATREAEGLQEELTNAEtlYKQLKEKVDsaggtgegnvnqkaiEMKKEAEDLLKKATMGMETLKKLERK 1796
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELE---------------ELEEELEELQEELERLEEALEELREE 469
                          330
                   ....*....|....*
gi 1207193065 1797 FNKNEQKMQQQRDEL 1811
Cdd:TIGR02168  470 LEEAEQALDAAEREL 484
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
332-384 1.48e-05

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: 43.88  E-value: 1.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193065  332 CNCNGH---SNQCHFDmavylatgnvsGGVCNnCLHNTMGRNCESCKPFYYQDPEK 384
Cdd:cd00055      2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
507-545 1.85e-05

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 43.50  E-value: 1.85e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1207193065  507 CNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
cc_DmLAMB1-like_C cd22302
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ...
1767-1835 2.19e-05

C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) and similar proteins; DmLAMB1, also called LanB1, is a glycoprotein required for nidogen (Ndg) localization to the basement membrane. It is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of DmLAMB1, which may be involved in the integrin binding activity.


Pssm-ID: 411973 [Multi-domain]  Cd Length: 70  Bit Score: 44.15  E-value: 2.19e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207193065 1767 QKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNC 1835
Cdd:cd22302      2 ERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
1516-1833 2.66e-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: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1516 RDIATLTQTVKTQAKETLDKAQNKKDMFEKSNKMlKNFIQKIKDFLNEEGADPESIEKVAQQVLAISLPVNRTV------ 1589
Cdd:TIGR01612  751 KDLNKILEDFKNKEKELSNKINDYAKEKDELNKY-KSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTIsikede 829
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1590 ---IVNLVEQIKDSIVNLTNV---------EGVfNHTSEQLAKVNDLLKkAQDAKTQADGVSDNINKTKEALETSQNAIK 1657
Cdd:TIGR01612  830 ifkIINEMKFMKDDFLNKVDKfinfennckEKI-DSEHEQFAELTNKIK-AEISDDKLNDYEKKFNDSKSLINEINKSIE 907
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1658 KAEEEMSTalknLKNIqnitamvdDKLLNLDNNLTDvmmRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEG-L 1736
Cdd:TIGR01612  908 EEYQNINT----LKKV--------DEYIKICENTKE---SIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNtL 972
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1737 QEELTNAETLYKqlkekvDSAGGTGEGNVNqkaiEMKKEAEDLlkKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEK 1816
Cdd:TIGR01612  973 IDKINELDKAFK------DASLNDYEAKNN----ELIKYFNDL--KANLGKNKENMLYHQFDEKEKATNDIEQKIEDANK 1040
                          330
                   ....*....|....*..
gi 1207193065 1817 NVTGIREYIRSKVlaYN 1833
Cdd:TIGR01612 1041 NIPNIEIAIHTSI--YN 1055
PRK12704 PRK12704
phosphodiesterase; Provisional
1707-1823 3.48e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.62  E-value: 3.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1707 LLKNKTE-QNREMAKEAKAQSDNATREAEGLQEE-LTNAETLYKQLKEKVdsaggtgEGNVNQKAIEMKK------EAED 1778
Cdd:PRK12704    24 VRKKIAEaKIKEAEEEAKRILEEAKKEAEAIKKEaLLEAKEEIHKLRNEF-------EKELRERRNELQKlekrllQKEE 96
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1207193065 1779 LLKKAtmgMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIRE 1823
Cdd:PRK12704    97 NLDRK---LELLEKREEELEKKEKELEQKQQELEKKEEELEELIE 138
OspD pfam03207
Borrelia outer surface protein D (OspD);
1603-1793 3.52e-05

Borrelia outer surface protein D (OspD);


Pssm-ID: 367392 [Multi-domain]  Cd Length: 254  Bit Score: 47.54  E-value: 3.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1603 NLTNVEGVF-------NHTSEQ---LAKVNDLLKKAQDAKTQADGVSDNIN------KTKEALETSQNAIKKAEEEMSTA 1666
Cdd:pfam03207   32 NLNNQKGYLdnegansNYESKKqsiLSELNQLLKQTTNSLKEAKNTTDNLNasneanKVVEAVINAVNLISSAADQVKSA 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1667 LKNLKNIQNITAMVDDKLlnldNNLTDVMMRLVNLSNGVDLLKNKTEQN-----REMAK--EAKAQSD------------ 1727
Cdd:pfam03207  112 TKNMHDLAQMAEIDLEKI----KNSSDKAIFASNLAKEAYSLTKAAEQNmqklyKEQQKisESESESDysdsaeikqake 187
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207193065 1728 ------NATREAeglQEELTNAETLYKQLKEKVDSaggtgEGNVNQKAIEMKKEAEDLLKKATMGMETLKKL 1793
Cdd:pfam03207  188 aveiawKATVEA---KDKLIDVENTVKETLDKIKT-----ETTNNTKLADIKEAAELVLQIAKNAKEIVQEV 251
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1567-1820 3.69e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 3.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1567 DPESIEKVAQQVLAIslpvnrtvivnlvEQIKDSIVNLTNVEGVFNHTSEQLAK-------VNDLLKKAQDAKTQadgVS 1639
Cdd:PRK03918   143 SDESREKVVRQILGL-------------DDYENAYKNLGEVIKEIKRRIERLEKfikrtenIEELIKEKEKELEE---VL 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1640 DNINKTKEALETSQNAIKKAEEEmstaLKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMA 1719
Cdd:PRK03918   207 REINEISSELPELREELEKLEKE----VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1720 KEAK-------------AQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggtgeGNVNQKAIEMKKEAEDLLKKatmg 1786
Cdd:PRK03918   283 KELKelkekaeeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL-----EEKEERLEELKKKLKELEKR---- 353
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1207193065 1787 METLKKLERKFNKNEQKMqqqrDELTDLEKNVTG 1820
Cdd:PRK03918   354 LEELEERHELYEEAKAKK----EELERLKKRLTG 383
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
1488-1821 3.92e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 48.29  E-value: 3.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1488 VKALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDKAQN-KKDMFEKS----------NKMLKNFIQK 1556
Cdd:PRK04778   101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRElRKSLLANRfsfgpaldelEKQLENLEEE 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1557 IKDF--LNEEGaDP----ESIEKVAQQVLAISlpvnrtvivNLVEQIKDSIVNLTNVegvFnhtSEQLAKVNDLLKKAQD 1630
Cdd:PRK04778   181 FSQFveLTESG-DYvearEILDQLEEELAALE---------QIMEEIPELLKELQTE---L---PDQLQELKAGYRELVE 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1631 AKTQADgvSDNINKTkeaLETSQNAIKKAEEEMSTaLKnLKNIQNITAMVDDKLlnldNNLTDVMMRLV--------NLS 1702
Cdd:PRK04778   245 EGYHLD--HLDIEKE---IQDLKEQIDENLALLEE-LD-LDEAEEKNEEIQERI----DQLYDILEREVkarkyvekNSD 313
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1703 NGVDLLKNKTEQNREMAKEAK--AQS----DNATREAEGLQEELTNAETLYKQLKEKVDsaggtgEGNV-------NQKA 1769
Cdd:PRK04778   314 TLPDFLEHAKEQNKELKEEIDrvKQSytlnESELESVRQLEKQLESLEKQYDEITERIA------EQEIayselqeELEE 387
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207193065 1770 I-----EMKKEAEDLLkkatmgmETLKKLERKFNKNEQKMQQQRDELTD----LEK-NVTGI 1821
Cdd:PRK04778   388 IlkqleEIEKEQEKLS-------EMLQGLRKDELEAREKLERYRNKLHEikryLEKsNLPGL 442
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1676-1827 4.49e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 4.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1676 ITAMVDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNA-----------E 1744
Cdd:COG4372      4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArseleqleeelE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1745 TLYKQLKEKVDSAGGTGE--GNVNQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIR 1822
Cdd:COG4372     84 ELNEQLQAAQAELAQAQEelESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163

                   ....*
gi 1207193065 1823 EYIRS 1827
Cdd:COG4372    164 EELAA 168
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1245-1436 7.50e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 7.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1245 DIIAMILEKGEVpgvsdkRILELEKKLAQAQELVRDGDREGTFNL--ISQTVDDLRAEIALTDGRLMGVIRDLNVTTDHN 1322
Cdd:COG4372      2 DRLGEKVGKARL------SLFGLRPKTGILIAALSEQLRKALFELdkLQEELEQLREELEQAREELEQLEEELEQARSEL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1323 NDLKQNLTALEKELKDLNNTLHQLRRELENyltaglAEQFANVLKYYQRSLNSEQrcnasvygpqspvEQSQDTRNRtea 1402
Cdd:COG4372     76 EQLEEELEELNEQLQAAQAELAQAQEELES------LQEEAEELQEELEELQKER-------------QDLEQQRKQ--- 133
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1207193065 1403 lLKDKKDSLLRTATANNKSLSELEGKAHEINRKV 1436
Cdd:COG4372    134 -LEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
332-382 7.60e-05

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 41.96  E-value: 7.60e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207193065  332 CNCNGH---SNQCHFdmavylatgnvSGGVCNnCLHNTMGRNCESCKPFYYQDP 382
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
ApoLp-III_like cd13769
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ...
1689-1807 8.09e-05

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: 45.01  E-value: 8.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1689 NNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQ-LKEKVDSAggtgegnvnQ 1767
Cdd:cd13769     15 NNLAQQVQKQLGLQNPEEVVNTLKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTkLSETVPEL---------R 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1207193065 1768 KAIEMKKEAEDLLKKATMGMETL----KKLERKFNKNEQKMQQQ 1807
Cdd:cd13769     86 KSLPVEEKAQELQAKLQSGLQTLvtesQKLAKAISENSQKAQEE 129
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1593-1828 8.75e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 8.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1593 LVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKA----QDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALK 1668
Cdd:COG4942     32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALarriRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1669 NLKNIQNITAMvddKLLNLDNNLTDVMMRLvnlsngvDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYK 1748
Cdd:COG4942    112 ALYRLGRQPPL---ALLLSPEDFLDAVRRL-------QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1749 QLKEKvdsaggtgegnvnQKAIEMKKEAEDllkkatmgmETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSK 1828
Cdd:COG4942    182 ELEEE-------------RAALEALKAERQ---------KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1252-1442 1.06e-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: 47.37  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1252 EKGEVPGVSDkRILELEKKLA--------------QAQELVRDGDREgtFNLISQTVDDLRAEIALTDGRLMGVIRDLNV 1317
Cdd:TIGR02169  672 EPAELQRLRE-RLEGLKRELSslqselrrienrldELSQELSDASRK--IGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1318 TTDHNNDLKQNLTALEKELKDLNNTLHQLRRELENyLTAGLAEQF-------ANVLKYYQRSLNS-----EQRCNASVYG 1385
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKLEEALND-LEARLSHSRipeiqaeLSKLEEEVSRIEArlreiEQKLNRLTLE 827
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193065 1386 PQSPVEQSQDTRNRTEAlLKDKKDSLLRTATANNKSLSELEGKAHEINRKVHHLSNK 1442
Cdd:TIGR02169  828 KEYLEKEIQELQEQRID-LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1616-1826 1.09e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1616 EQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQnaikkaeeEMSTALKNLkniqnitAMVDDKLLNLDNNLTdvm 1695
Cdd:COG4913    617 AELAELEEELAEAEERLEALEAELDALQERREALQRLA--------EYSWDEIDV-------ASAEREIAELEAELE--- 678
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1696 mRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKE 1775
Cdd:COG4913    679 -RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207193065 1776 A--EDLLKKAtmgmetLKKLERKFNKNEQKMQQQRDELTDLeknvtgIREYIR 1826
Cdd:COG4913    758 AlgDAVEREL------RENLEERIDALRARLNRAEEELERA------MRAFNR 798
PRK01156 PRK01156
chromosome segregation protein; Provisional
1546-1833 1.74e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.43  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1546 SNKMLKNFIQKIKD-FLNE----EG-------ADPESIEKVAQQVLAI-SLPVNRTVIVNLVEQIKDSIVNLTNVEGVFN 1612
Cdd:PRK01156   114 TKYIEKNILGISKDvFLNSifvgQGemdslisGDPAQRKKILDEILEInSLERNYDKLKDVIDMLRAEISNIDYLEEKLK 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1613 HTSEQLAKVNDLLkkAQDAKTQADgvsdnINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLT 1692
Cdd:PRK01156   194 SSNLELENIKKQI--ADDEKSHSI-----TLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1693 DVMMRLVNlsngvdlLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNaetlYKQLKEKVDSAGGTGEGNVNQKA--- 1769
Cdd:PRK01156   267 MELEKNNY-------YKELEERHMKIINDPVYKNRNYINDYFKYKNDIEN----KKQILSNIDAEINKYHAIIKKLSvlq 335
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1770 ------IEMKKEAEDLLKK-------------ATMGMETLKKLERKFNKNEQKMQQQRDELTDLE----KNVTGIREYIR 1826
Cdd:PRK01156   336 kdyndyIKKKSRYDDLNNQilelegyemdynsYLKSIESLKKKIEEYSKNIERMSAFISEILKIQeidpDAIKKELNEIN 415

                   ....*..
gi 1207193065 1827 SKVLAYN 1833
Cdd:PRK01156   416 VKLQDIS 422
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
960-1012 1.80e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 40.76  E-value: 1.80e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1207193065   960 CPCpghpDSGHSNGASCEVDYasnqILCQCGQGYAGPRCDRCAPGYYGDPEHP 1012
Cdd:smart00180    1 CDC----DPGGSASGTCDPDT----GQCECKPNVTGRRCDRCAPGYYGDGPPG 45
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
1621-1751 1.98e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 45.44  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1621 VNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMvddkllnldnnltdvmmrlvn 1700
Cdd:cd22656    123 LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIARKEI--------------------- 181
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207193065 1701 lsngVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLK 1751
Cdd:cd22656    182 ----KDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
1546-1757 2.80e-04

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 45.10  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1546 SNKMLKnFIQKIKDFLNEEGA-----DPESIEKVAQQV--------LAISLPVNRTVIVN-LVEQIKDSIVNLTNVEG-- 1609
Cdd:TIGR04320  118 TEGSLD-FAQAVAKAYKKDNSgtgghDETAINKAAAENgldntyenLGSISSNNENTTMDdLKRAIYDSILGMLFNDAds 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1610 VFNHTsEQLAKVNDLLKKA------QDAK--------TQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQN 1675
Cdd:TIGR04320  197 NWGHA-QNLLGDDKINAGAylgvsiSNDGgvtihfvnFNDSYIADGNKFDKTPIPNPPNSLAALQAKLATAQADLAAAQT 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1676 ITAMVDDKLLNLDNNLTDvmmrlvnlsngvdLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVD 1755
Cdd:TIGR04320  276 ALNTAQAALTSAQTAYAA-------------AQAALATAQKELANAQAQALQTAQNNLATAQAALANAEARLAKAKEALA 342

                   ..
gi 1207193065 1756 SA 1757
Cdd:TIGR04320  343 NL 344
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1641-1827 2.94e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 2.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1641 NINKTKEALETSQNAIKKAEEEMstalKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSngvDLLKNKTEQNREMAK 1720
Cdd:PRK03918   156 GLDDYENAYKNLGEVIKEIKRRI----ERLEKFIKRTENIEELIKEKEKELEEVLREINEIS---SELPELREELEKLEK 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1721 EAKaqsdnatrEAEGLQEELTNAEtlyKQLKEKVDSAGGTGEGNVN-QKAIEMKKEAEDLLKKATMGMETLKKLERKFNK 1799
Cdd:PRK03918   229 EVK--------ELEELKEEIEELE---KELESLEGSKRKLEEKIRElEERIEELKKEIEELEEKVKELKELKEKAEEYIK 297
                          170       180
                   ....*....|....*....|....*...
gi 1207193065 1800 NEQKMQQQRDELTDLEKNVTGIREYIRS 1827
Cdd:PRK03918   298 LSEFYEEYLDELREIEKRLSRLEEEING 325
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
1626-1771 3.15e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 45.38  E-value: 3.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1626 KKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQN---ITAMVDDKLLNLDNNLTDVMMRLVNLS 1702
Cdd:pfam05262  213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKpadTSSPKEDKQVAENQKREIEKAQIEIKK 292
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207193065 1703 NGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGegnvNQKAIE 1771
Cdd:pfam05262  293 NDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSL----NEDAID 357
46 PHA02562
endonuclease subunit; Provisional
1618-1816 4.05e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.01  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1618 LAKVNDLLK-KAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMS-----------TALKNLKNIQNITAMVDDKLL 1685
Cdd:PHA02562   165 LSEMDKLNKdKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGeniarkqnkydELVEEAKTIKAEIEELTDELL 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1686 NLDNNLTDVMMRLVNLSNGVDLLKNKTEQnreMAKEAKAQSDNA-----TREAEGLQEELTNAETLYKQLKEKVDSAggt 1760
Cdd:PHA02562   245 NLVMDIEDPSAALNKLNTAAAKIKSKIEQ---FQKVIKMYEKGGvcptcTQQISEGPDRITKIKDKLKELQHSLEKL--- 318
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193065 1761 gegnvnQKAIEMKKEAEDLLKKATMgmeTLKKLERKFNKNEQKMQQQRDELTDLEK 1816
Cdd:PHA02562   319 ------DTAIDELEEIMDEFNEQSK---KLLELKNKISTNKQSLITLVDKAKKVKA 365
ApoLp-III_like cd13769
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ...
1550-1745 5.60e-04

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: 42.31  E-value: 5.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1550 LKNFIQKIKDFLNEegadpesiekVAQQVL-AISLPVNRTVivnlVEQIKDsivnltNVEGVFNHTSEQLAKVNDLLKKA 1628
Cdd:cd13769      3 LSELIQKAQEAINN----------LAQQVQkQLGLQNPEEV----VNTLKE------QSDNFANNLQEVSSSLKEEAKKK 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1629 Q-DAKTQADGVSDNINKTKEALETSQNAIKKAEEemstalknlknIQNitamvddkllNLDNNLTDVMMRLVNLSNGVDl 1707
Cdd:cd13769     63 QgEVEEAWNEFKTKLSETVPELRKSLPVEEKAQE-----------LQA----------KLQSGLQTLVTESQKLAKAIS- 120
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1207193065 1708 lKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAET 1745
Cdd:cd13769    121 -ENSQKAQEELQKATKQAYDIAVEAAQNLQNQLQTATQ 157
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
332-385 6.78e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.22  E-value: 6.78e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207193065   332 CNCNG---HSNQCHFDmavylatgnvsGGVCNnCLHNTMGRNCESCKPFYYQDPEKD 385
Cdd:smart00180    1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
1675-1810 7.75e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 44.22  E-value: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1675 NITAMVDDKLLN--LDNNLTDVMMRlvnlSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEEL----TNAETLYK 1748
Cdd:pfam05262  173 DTDSISDKKVVEalREDNEKGVNFR----RDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKAdfaqDNADKQRD 248
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207193065 1749 QLKEKVDSA------GGTGEGNVNQK-AIEMKKEAEDLLKKATMGMETLKKLE-------RKFNKNEQKMQQQRDE 1810
Cdd:pfam05262  249 EVRQKQQEAknlpkpADTSSPKEDKQvAENQKREIEKAQIEIKKNDEEALKAKdhkafdlKQESKASEKEAEDKEL 324
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1261-1439 8.57e-04

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: 44.28  E-value: 8.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1261 DKRILELEKKLAQAQELVRDGDREGT-----FNLISQTVDDLRAEIALTDGRLMGVIRDLNVTTDHNNDLKQNLTALEKE 1335
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTeleaeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1336 LKDLNNTLHQLRRELENYLT-AGLAEQFANVLKyYQRSLNSEQ--RCNASVYGPQSPVEQSQDTRNRtealLKDKKDSLL 1412
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERrIAATERRLEDLE-EQIEELSEDieSLAAEIEELEELIEELESELEA----LLNERASLE 886
                          170       180
                   ....*....|....*....|....*..
gi 1207193065 1413 RTATANNKSLSELEGKAHEINRKVHHL 1439
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSEL 913
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
292-318 9.75e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.45  E-value: 9.75e-04
                            10        20
                    ....*....|....*....|....*..
gi 1207193065   292 HGRCVCKHNTVGLNCERCRDFYHDAPW 318
Cdd:smart00180   17 TGQCECKPNVTGRRCDRCAPGYYGDGP 43
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
1709-1815 1.06e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1709 KNKTEQNREM-AKEAKAQSdnATREAEGLQEELtnaetlyKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGM 1787
Cdd:cd16269    191 QALTEKEKEIeAERAKAEA--AEQERKLLEEQQ-------RELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERAL 261
                           90       100       110
                   ....*....|....*....|....*....|
gi 1207193065 1788 ETLKKLERKFNK--NEQKMQQQRDELTDLE 1815
Cdd:cd16269    262 ESKLKEQEALLEegFKEQAELLQEEIRSLK 291
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1261-1442 1.19e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1261 DKRILELEKKLAQAQELVRD-------GDREGTFNLISQTVDDLRAEIALTDGRLmgvirdlnvttdhnNDLKQNLTALE 1333
Cdd:COG3206    181 EEQLPELRKELEEAEAALEEfrqknglVDLSEEAKLLLQQLSELESQLAEARAEL--------------AEAEARLAALR 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1334 KELKDLNNTLHQLrreLENYLTAGLAEQFANVlkyyQRSLNSEQrcnaSVYGPQSP-VEQSQDTRNRTEALLKDKKDSLL 1412
Cdd:COG3206    247 AQLGSGPDALPEL---LQSPVIQQLRAQLAEL----EAELAELS----ARYTPNHPdVIALRAQIAALRAQLQQEAQRIL 315
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1207193065 1413 RTATANNKSL----SELEGKAHEINRKVHHLSNK 1442
Cdd:COG3206    316 ASLEAELEALqareASLQAQLAQLEARLAELPEL 349
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1262-1442 1.19e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1262 KRILELEKKLAQAQELVRDGDREgtFNLISQTVDDLRAEIALTDGRLMGVIRDLNVTTDHNNDLKQNLTALEKELKDLNN 1341
Cdd:COG4372     80 EELEELNEQLQAAQAELAQAQEE--LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1342 TLHQLRRE---LENYLTAGLAEQFANVLKYYQRSLNSEQRCNASVYGPQSPVEQSQDTRNRTEALLKDKKDSLLRTATAN 1418
Cdd:COG4372    158 QLESLQEElaaLEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
                          170       180
                   ....*....|....*....|....
gi 1207193065 1419 NKSLSELEGKAHEINRKVHHLSNK 1442
Cdd:COG4372    238 LLDALELEEDKEELLEEVILKEIE 261
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1489-1806 1.20e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1489 KALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKT---QAKETLDKAQNKKDMFEKSNKMLKN---FIQKIKDFLN 1562
Cdd:COG4372     56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAelaQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLE 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1563 EEGADPESIEKVAQQVLAiSLpvnRTVIVNLVEQIKDSIVNLTNVEgvfnhTSEQLAKVNDLLKKAQDAKTQAdgvsdNI 1642
Cdd:COG4372    136 AQIAELQSEIAEREEELK-EL---EEQLESLQEELAALEQELQALS-----EAEAEQALDELLKEANRNAEKE-----EE 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1643 NKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEA 1722
Cdd:COG4372    202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1723 KAQSDNATREAEGLQEEltnaetlYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQ 1802
Cdd:COG4372    282 ALELEALEEAALELKLL-------ALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354

                   ....
gi 1207193065 1803 KMQQ 1806
Cdd:COG4372    355 VLEL 358
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
1505-1829 1.45e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 43.67  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1505 SEELQTMAKKLRDIATLTQTVKTQAKETLDkaqNKKDMFEKsnkmlkNFIQK-IKDFLNEEGADPESIEKVAQQVLAISl 1583
Cdd:PTZ00440   260 SNNYDNYLNRAKELLESGSDLINKIKKELG---DNKTIYSI------NFIQEeIGDIIKRYNFHLKKIEKGKEYIKRIQ- 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1584 PVNRTVIVNLVEqIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQ------------DAKTQADGVSDN---------- 1641
Cdd:PTZ00440   330 NNNIPPQVKKDE-LKKKYFESAKHYASFKFSLEMLSMLDSLLIKKEkilnnlfnklfgDLKEKIETLLDSeyfiskytni 408
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1642 INKTKEALETSQNAIKKAEEEMS--TALKNLKnIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVDLlkNKTEQNREMA 1719
Cdd:PTZ00440   409 ISLSEHTLKAAEDVLKENSQKIAdyALYSNLE-IIEIKKKYDEKINELKKSINQLKTLISIMKSFYDL--IISEKDSMDS 485
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1720 KEAKAQSDNATreaeglQEELTNAETLYKQLKEKVdsaggtgeGNVNQKAIEMKKEAEDLlkkatmgmETLKKLERKFNK 1799
Cdd:PTZ00440   486 KEKKESSDSNY------QEKVDELLQIINSIKEKN--------NIVNNNFKNIEDYYITI--------EGLKNEIEGLIE 543
                          330       340       350
                   ....*....|....*....|....*....|
gi 1207193065 1800 NEQKMQQQRDELTDLEKNVTGIREYIRSKV 1829
Cdd:PTZ00440   544 LIKYYLQSIETLIKDEKLKRSMKNDIKNKI 573
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1261-1373 1.54e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1261 DKRILELEKKLAQAQELVRDGDRegtfnlISQTVDDLRAEIA-LTDGRLMGVIRDLNVTTDHNNDLKQNLTALEKELKDL 1339
Cdd:COG4717    145 PERLEELEERLEELRELEEELEE------LEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1207193065 1340 NNTLHQLRRELENYLTAGLAEQFANVLKYYQRSL 1373
Cdd:COG4717    219 QEELEELEEELEQLENELEAAALEERLKEARLLL 252
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1616-1823 1.77e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1616 EQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNitamvddkllnldnnltdvm 1695
Cdd:COG1196    236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-------------------- 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1696 mRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggtgegnvNQKAIEMKKE 1775
Cdd:COG1196    296 -ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA--------EAELAEAEEA 366
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207193065 1776 AEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIRE 1823
Cdd:COG1196    367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1616-1816 2.20e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1616 EQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVM 1695
Cdd:COG1196    243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1696 MRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggtgegnvNQKAIEMKKE 1775
Cdd:COG1196    323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL--------AEELLEALRA 394
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1207193065 1776 AEDLLKKATmgmETLKKLERKFNKNEQKMQQQRDELTDLEK 1816
Cdd:COG1196    395 AAELAAQLE---ELEEAEEALLERLERLEEELEELEEALAE 432
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
291-322 2.24e-03

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 37.72  E-value: 2.24e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1207193065  291 IHGRCVCKHNTVGLNCERCRDFYHDAPWRPAE 322
Cdd:pfam00053   16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1587-1829 2.37e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1587 RTVIVNLVEQI-----KDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEE 1661
Cdd:PRK02224   186 RGSLDQLKAQIeekeeKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRE 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1662 EMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRL-------VNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAE 1734
Cdd:PRK02224   266 TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1735 GLQEELTNAETLYKQLKEkvdsaggtgegnvnqKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQ---QQRDEL 1811
Cdd:PRK02224   346 SLREDADDLEERAEELRE---------------EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapVDLGNA 410
                          250
                   ....*....|....*...
gi 1207193065 1812 TDLEKNVTGIREYIRSKV 1829
Cdd:PRK02224   411 EDFLEELREERDELRERE 428
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
1589-1814 2.67e-03

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


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 41.99  E-value: 2.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1589 VIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKV---NDLLKKAQDAKTQADGVS-DNINKTKEALETSQNAIKKAEEEMS 1664
Cdd:pfam04108   57 VLNELKKDFKQLLKDLDAALERLEETLDKLRNTpvePALPPGEEKQKTLLDFIDeDSVEILRDALKELIDELQAAQESLD 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1665 TALKNlkniqnitamVDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEAKAQSD------NATREAEGLQE 1738
Cdd:pfam04108  137 SDLKR----------FDDDLRDLQKELESLSSPSESISLIPTLLKELESLEEEMASLLESLTNhydqcvTAVKLTEGGRA 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1739 ELTN-----AETLYKQLKEKVDSAG--GTGEGNVnQKAIEMKKEAEDLLKKATMGMETLK-----------KLERKFNKN 1800
Cdd:pfam04108  207 EMLEvlendARELDDVVPELQDRLDemENNYERL-QKLLEQKNSLIDELLSALQLIAEIQsrlpeylaalkEFEERWEEE 285
                          250
                   ....*....|....
gi 1207193065 1801 EQKMQQQRDELTDL 1814
Cdd:pfam04108  286 KETIEDYLSELEDL 299
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
1499-1563 3.32e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 39.87  E-value: 3.32e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207193065 1499 KNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDKAQNK---------KDMFEKSNKMLKNFIQKIKDFLNE 1563
Cdd:pfam03938   33 AELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQElqqlqqkaqQELQKKQQELLQPIQDKINKAIKE 106
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
1590-1682 3.61e-03

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 41.12  E-value: 3.61e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065  1590 IVNLVEQIKDSIVNL-TNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALK 1668
Cdd:smart00283    2 VSEAVEEIAAGAEEQaEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81
                            90       100
                    ....*....|....*....|.
gi 1207193065  1669 NLK-------NIQNITAMVDD 1682
Cdd:smart00283   82 AVEeleessdEIGEIVSVIDD 102
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
1503-1682 3.68e-03

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 41.93  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1503 AVSEELQTMAKKLRDIAT--LTQTVKTQAKETLDkaqnkkDMFEKSNKMLKNF---IQKIKDFLNEEGADPESIEKVAQQ 1577
Cdd:COG0840    205 SITRPLRELLEVLERIAEgdLTVRIDVDSKDEIG------QLADAFNRMIENLrelVGQVRESAEQVASASEELAASAEE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1578 VLAISLPVNRTV--IVNLVEQIKDSIvnltnvegvfNHTSEQLAKVNDLlkkAQDAKTQADGVSDNINKTKEALETSQNA 1655
Cdd:COG0840    279 LAAGAEEQAASLeeTAAAMEELSATV----------QEVAENAQQAAEL---AEEASELAEEGGEVVEEAVEGIEEIRES 345
                          170       180
                   ....*....|....*....|....*..
gi 1207193065 1656 IKKAEEEMSTALKNLKNIQNITAMVDD 1682
Cdd:COG0840    346 VEETAETIEELGESSQEIGEIVDVIDD 372
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
1509-1673 4.20e-03

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 40.86  E-value: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1509 QTMAKKLRDIA-TLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNeegadpesiekvaqqvlaiSLPVNR 1587
Cdd:cd21116     72 QSYYPDLIELAdNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKN-------------------DLDDDS 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1588 TVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDA----KTQADGVSDNINKTKEALET--SQNAIKKAEE 1661
Cdd:cd21116    133 RNLQTDATKAQAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDwqtlDSDIKELITDLEDAESSIDAafLQADLKAAKA 212
                          170
                   ....*....|..
gi 1207193065 1662 EMSTALKNLKNI 1673
Cdd:cd21116    213 DWNQLYEQAKSL 224
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
1487-1816 4.44e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 42.13  E-value: 4.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1487 SVKALDNA-DEVHKNLTAVSEELQTMAKKLRDIATLTQTVkTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEEG 1565
Cdd:PTZ00440  2285 SIKTFNEIyDDIKSNIGDLYKLEDTNNDELKKVKLYIENI-THLLNRINTLINDLDNYQDENYGKDKNIELNNENNSYII 2363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1566 ADPESIEKVAQQVLAISLPVNRTVIVNLVEQIKDSIVNLTN-VEGVFNHTSEQLAKvNDLLKKAQDAKTQADGVSDNINK 1644
Cdd:PTZ00440  2364 KTKEKINNLKEEFSKLLKNIKRNNTLCNNNNIKDFISNIGKsVETIKQRFSSNLPE-KEKLHQIEENLNEIKNIMNETKR 2442
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1645 TKEALETSQNAIKKAEEEMSTAlKNLKNIQNITAMVDdkllNLDNNLTDVMMRLVNLSNGVDLLKNKTEqnrEMAKEAKA 1724
Cdd:PTZ00440  2443 ISNVDAFTNKILQDIDNEKNKE-NNNMNAEKIDDLIE----NVTSHNEKIKSELLIINDALRRVKEKKD---EMNKLFNS 2514
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1725 QSDNATREAEGLQEELTNAETLYKQLKEKVdSAGGTGEGNVNQKAIEMKKEAEDLLKKATM-----GMETLKKLERKFNK 1799
Cdd:PTZ00440  2515 LTENNNNNNNSAKNIVDNSTYIINELESHV-SKLNELLSYIDNEIKELENEKLKLLEKAKIeesrkERERIESETQEDNT 2593
                          330
                   ....*....|....*...
gi 1207193065 1800 NE-QKMQQQRDELTDLEK 1816
Cdd:PTZ00440  2594 DEeQINRQQQERLQKEEE 2611
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1262-1435 4.51e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1262 KRILELEKKLAQAQELVRDgdregtfnlISQTVDDLRAEIALTDGRLmgvirdlnvttdhnNDLKQNLTALEKELKDLNN 1341
Cdd:COG4942     34 QEIAELEKELAALKKEEKA---------LLKQLAALERRIAALARRI--------------RALEQELAALEAELAELEK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1342 TLHQLRRELENyltagLAEQFANVLKYYQRslNSEQRCNASVYGPQSPVEQSqdtrnRTEALLKDKKDSLLRTATANNKS 1421
Cdd:COG4942     91 EIAELRAELEA-----QKEELAELLRALYR--LGRQPPLALLLSPEDFLDAV-----RRLQYLKYLAPARREQAEELRAD 158
                          170
                   ....*....|....
gi 1207193065 1422 LSELEGKAHEINRK 1435
Cdd:COG4942    159 LAELAALRAELEAE 172
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
1622-1733 5.70e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 41.25  E-value: 5.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065 1622 NDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNItamvddKLLNLDNNLTDVmmrlvnl 1701
Cdd:TIGR04320  257 AALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQ------ALQTAQNNLATA------- 323
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1207193065 1702 sngVDLLKNKTEQNREmAKEAKA--QSDNATREA 1733
Cdd:TIGR04320  324 ---QAALANAEARLAK-AKEALAnlNADLAKKQA 353
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
1747-1832 8.99e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.33  E-value: 8.99e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207193065  1747 YKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKK-ATMGMETLKKLERKFNKNEQKMQQQRDELT-DLEKNVTGIREY 1824
Cdd:smart00935   16 GKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDaATLSEAAREKKEKELQKKVQEFQRKQQKLQqDLQKRQQEELQK 95

                    ....*...
gi 1207193065  1825 IRSKVLAY 1832
Cdd:smart00935   96 ILDKINKA 103
 
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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