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Conserved domains on  [gi|1151215|gb|AAA85255|]
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laminin beta3 chain [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Laminin_N super family cl02806
Laminin N-terminal (Domain VI);
20-248 5.36e-69

Laminin N-terminal (Domain VI);


The actual alignment was detected with superfamily member smart00136:

Pssm-ID: 470680  Cd Length: 238  Bit Score: 231.10  E-value: 5.36e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215       20 ACSRGACYPPVGDLFIGRTqlLRASSTCGLTKPETYCTQ--YGQWQMKCCKCDSRLPrnYNSHRVENVASSSGP--MRWW 95
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGRE--VTATSTCGEPGPERYCKLvgHTEQGKKCDYCDARNP--RRSHPAENLTDGNNPnnPTWW 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215       96 QSQNDVSP---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSsDFGKTWRVYQYLATDCASTFPQVHQG--QPKNWQD 170
Cdd:smart00136   77 QSEPLSNGpqnVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGpiTKGNEDE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215      171 VRCRPLSQRPNGhLTGGKVQLNLMDL-ASAIPASQSKKIQELGDITNLRVNFTKLAPVPQRG-----SYPPSAYFAVSQL 244
Cdd:smart00136  156 VICTSEYSDIVP-LEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELmddrpEVTRRYYYAISDI 234


                    ....
gi 1151215      245 RLQG 248
Cdd:smart00136  235 AVGG 238
cc_LAMB_C super family cl40438
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ...
 1098-1168 1.83e-23

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.


The actual alignment was detected with superfamily member cd22303:

Pssm-ID: 424069 [Multi-domain]  Cd Length: 71  Bit Score: 94.82  E-value: 1.83e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151215  1098 GNRILSIKMEAEELFGESMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATCK 1168
Cdd:cd22303    1 GERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 376-425 4.69e-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: 4.69e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1151215     376 CECDPDGAVqGAPCDRLTGQCVCKEYVQGERCDLCKPGFTGLTFDNPKGC 425
Cdd:pfam00053    1 CDCNPHGSL-SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 530-579 6.53e-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: 61.22  E-value: 6.53e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1151215   530 ACDCDFRGTEGPACDKASGRCLCRPGFTGPRCDQCQRGHCDRYPVCVACH 579
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 427-476 1.04e-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: 55.05  E-value: 1.04e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1151215   427 ACDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKLAS-GLGCE 476
Cdd:cd00055    1 PCDCNGHGSL-SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
478-528 1.86e-09

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 54.24  E-value: 1.86e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1151215      478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVPTGC 528
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCD-----RCAPGYYGDGPPGC 46
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 829-1161 1.61e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.30  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     829 GRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQV---STSRLLMEEDVQRTRLLIQQVRGFLTDPDTDAATI 905
Cdd:TIGR02168  659 GVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     906 QQVSEAVLAlwlptdsatvlrkmkEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAE-----------QARSRAHAVEG 974
Cdd:TIGR02168  739 EAEVEQLEE---------------RIAQLSKELTELEAEIEELEERLEEAEEELAEAEaeieeleaqieQLKEELKALRE 803

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     975 QVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQ---AQEEQA 1051
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleaLLNERA 883

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    1052 QAMQARQLAEGASQQAM----NAQEGFKRLKPKYTELKDRLGQSpvlgeqGNRILSIKMEAEELFgesmemmdkmkdmes 1127
Cdd:TIGR02168  884 SLEEALALLRSELEELSeelrELESKRSELRRELEELREKLAQL------ELRLEGLEVRIDNLQ--------------- 942

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1151215    1128 ELLRGSQAIML---------RSADLSGLEKRVEQIRSYIN--GRV 1161
Cdd:TIGR02168  943 ERLSEEYSLTLeeaealenkIEDDEEEARRRLKRLENKIKelGPV 987
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 249-301 3.00e-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: 3.00e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1151215   249 SCFCHGHADRcapnpggSTTAVRVNNVCVCQHNTAAPNCDRCAPFYNNRPWRP 301
Cdd:cd00055    1 PCDCNGHGSL-------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
EGF_CA super family cl21504
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 313-367 5.83e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


The actual alignment was detected with superfamily member pfam00053:

Pssm-ID: 473889  Cd Length: 49  Bit Score: 35.79  E-value: 5.83e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1151215     313 CDCNGH---SLTCHFdpavfaasqgtNGGVCDnCRDHTEGKNCEPCQLHYFWNRRPSA 367
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPP 46
 
Name Accession Description Interval E-value
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 20-248 5.36e-69

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: 231.10  E-value: 5.36e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215       20 ACSRGACYPPVGDLFIGRTqlLRASSTCGLTKPETYCTQ--YGQWQMKCCKCDSRLPrnYNSHRVENVASSSGP--MRWW 95
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGRE--VTATSTCGEPGPERYCKLvgHTEQGKKCDYCDARNP--RRSHPAENLTDGNNPnnPTWW 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215       96 QSQNDVSP---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSsDFGKTWRVYQYLATDCASTFPQVHQG--QPKNWQD 170
Cdd:smart00136   77 QSEPLSNGpqnVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGpiTKGNEDE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215      171 VRCRPLSQRPNGhLTGGKVQLNLMDL-ASAIPASQSKKIQELGDITNLRVNFTKLAPVPQRG-----SYPPSAYFAVSQL 244
Cdd:smart00136  156 VICTSEYSDIVP-LEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELmddrpEVTRRYYYAISDI 234


                    ....
gi 1151215      245 RLQG 248
Cdd:smart00136  235 AVGG 238
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
26-248 1.69e-55

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 192.41  E-value: 1.69e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215      26 CYPPVGDLFIGRTqlLRASSTCGLTKPETYCTQ-YGQWQMKCCKCDSRLPrnYNSHRVENVASSSG--PMRWWQSQNDVS 102
Cdd:pfam00055    1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCILsGLEGGKKCFICDSRDP--HNSHPPSNLTDSNNgtNETWWQSETGVI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     103 P---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSSDFGKTWRVYQYLATDCASTFPQVHQGQPKNW-QDVRCrplSQ 178
Cdd:pfam00055   77 QyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKdDEVIC---TS 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151215     179 RPNG--HLTGGKVQLNLMDLASAIP-ASQSKKIQELGDITNLRVNFTKLA-PVPQRGSYP---PSAYFAVSQLRLQG 248
Cdd:pfam00055  154 EYSDisPLTGGEVIFSTLEGRPSANiFDYSPELQDWLTATNIRIRLLRLHtLGDELLDDPsvlRKYYYAISDISVGG 230
cc_LAMB3_C cd22303
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ...
 1098-1168 1.83e-23

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: 94.82  E-value: 1.83e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151215  1098 GNRILSIKMEAEELFGESMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATCK 1168
Cdd:cd22303    1 GERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 376-425 4.69e-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: 4.69e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1151215     376 CECDPDGAVqGAPCDRLTGQCVCKEYVQGERCDLCKPGFTGLTFDNPKGC 425
Cdd:pfam00053    1 CDCNPHGSL-SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 530-579 6.53e-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: 61.22  E-value: 6.53e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1151215   530 ACDCDFRGTEGPACDKASGRCLCRPGFTGPRCDQCQRGHCDRYPVCVACH 579
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
531-568 8.43e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.79  E-value: 8.43e-12
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1151215      531 CDCDFRGTEGPACDKASGRCLCRPGFTGPRCDQCQRGH 568
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 531-568 1.98e-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: 60.06  E-value: 1.98e-11
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1151215     531 CDCDFRGTEGPACDKASGRCLCRPGFTGPRCDQCQRGH 568
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 375-426 2.97e-11

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 59.29  E-value: 2.97e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1151215   375 PCECDPDGAVQGApCDRLTGQCVCKEYVQGERCDLCKPGFTGLTfDNPKGCH 426
Cdd:cd00055    1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
376-425 4.44e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 58.86  E-value: 4.44e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1151215      376 CECDPDGAVQGApCDRLTGQCVCKEYVQGERCDLCKPGFTGltfDNPKGC 425
Cdd:smart00180    1 CDCDPGGSASGT-CDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 427-476 1.04e-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: 55.05  E-value: 1.04e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1151215   427 ACDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKLAS-GLGCE 476
Cdd:cd00055    1 PCDCNGHGSL-SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 428-475 1.07e-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: 55.05  E-value: 1.07e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1151215     428 CDCSILGARKDmPCEEETGRCLCLPNVVGPKCDQCAPSHWKLASGLGC 475
Cdd:pfam00053    1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
478-528 1.86e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 54.24  E-value: 1.86e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1151215      478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVPTGC 528
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCD-----RCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 478-531 4.17e-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: 53.13  E-value: 4.17e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1151215     478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVPTGCRAC 531
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCD-----RCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
428-475 4.86e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.08  E-value: 4.86e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1151215      428 CDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKlASGLGC 475
Cdd:smart00180    1 CDCDPGGSA-SGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 829-1161 1.61e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.30  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     829 GRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQV---STSRLLMEEDVQRTRLLIQQVRGFLTDPDTDAATI 905
Cdd:TIGR02168  659 GVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     906 QQVSEAVLAlwlptdsatvlrkmkEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAE-----------QARSRAHAVEG 974
Cdd:TIGR02168  739 EAEVEQLEE---------------RIAQLSKELTELEAEIEELEERLEEAEEELAEAEaeieeleaqieQLKEELKALRE 803

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     975 QVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQ---AQEEQA 1051
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleaLLNERA 883

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    1052 QAMQARQLAEGASQQAM----NAQEGFKRLKPKYTELKDRLGQSpvlgeqGNRILSIKMEAEELFgesmemmdkmkdmes 1127
Cdd:TIGR02168  884 SLEEALALLRSELEELSeelrELESKRSELRRELEELREKLAQL------ELRLEGLEVRIDNLQ--------------- 942

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1151215    1128 ELLRGSQAIML---------RSADLSGLEKRVEQIRSYIN--GRV 1161
Cdd:TIGR02168  943 ERLSEEYSLTLeeaealenkIEDDEEEARRRLKRLENKIKelGPV 987
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 477-529 2.24e-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: 51.20  E-value: 2.24e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 1151215   477 PCACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGH--VPTGCR 529
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCD-----RCAPGYYGLpsQGGGCQ 50
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 834-1078 2.35e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   834 QLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLlmeeDVQRTRLLIQQVRgfltdpdtdaATIQQVSEAVL 913
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQ----------AEEYELLAELA 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   914 ALwlptdSATVLRKMKEIQAIAARLpnvDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEA 993
Cdd:COG1196  299 RL-----EQDIARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   994 QDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEG 1073
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450


                 ....*
gi 1151215  1074 FKRLK 1078
Cdd:COG1196  451 EAELE 455
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 249-301 3.00e-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: 3.00e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1151215   249 SCFCHGHADRcapnpggSTTAVRVNNVCVCQHNTAAPNCDRCAPFYNNRPWRP 301
Cdd:cd00055    1 PCDCNGHGSL-------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 250-304 2.33e-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: 42.73  E-value: 2.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1151215     250 CFCHGHA---DRCAPNPGgsttavrvnnVCVCQHNTAAPNCDRCAPFYNNRPWRPAEG 304
Cdd:pfam00053    1 CDCNPHGslsDTCDPETG----------QCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 829-1073 2.85e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.97  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     829 GRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrllMEEDVQRTRLLIQQVRGFLTD----------- 897
Cdd:pfam07888   34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE----LESRVAELKEELRQSREKHEEleekykelsas 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     898 -----PDTDAATIQQVSEAVLALWLPTDSATVLRKMKEIQAIAARLPN-VDSVLSQTKQDIARARRLQAEAEQARSRAHA 971
Cdd:pfam07888  110 seelsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKErAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     972 VEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGE----------VQQVLVPAERLVKGMKEQMSGfwarMKE 1041
Cdd:pfam07888  190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEnealleelrsLQERLNASERKVEGLGEELSS----MAA 265

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1151215    1042 LRRQAQEEQAQA-MQARQLAEGASQQAMNAQEG 1073
Cdd:pfam07888  266 QRDRTQAELHQArLQAAQLTLQLADASLALREG 298
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
842-1111 3.50e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.11  E-value: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSR---LLMEEDVQRTRLLIQQVRGFLTDPDTDaatIQQVSEAVLALWLP 918
Cdd:PRK02224  330 LEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEIEELEEE---IEELRERFGDAPVD 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    919 TDSATVLRKM--KEIQAIAARLPNVDSVLSQTKQDIARARRLQA-----EAEQARSRAHAVEGQVDD--VVGNLRQGTVA 989
Cdd:PRK02224  407 LGNAEDFLEElrEERDELREREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVETIEEDreRVEELEAELED 486

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    990 LQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWA---RMKELRRQAQEEQAQAMQARQLAEGASQQ 1066
Cdd:PRK02224  487 LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEE 566

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1151215   1067 AMNAQEGFKRLKPKYTELKDRLgqspvlgEQGNRILSIKMEAEEL 1111
Cdd:PRK02224  567 AEEAREEVAELNSKLAELKERI-------ESLERIRTLLAAIADA 604
growth_prot_Scy NF041483
polarized growth protein Scy;
844-1077 7.60e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.13  E-value: 7.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    844 QTRQMIRAAEEAASRVQADAQR--LETQVSTSRLLME--------------EDVQRTRLLIQQVrgfltdpDTDAATIQ- 906
Cdd:NF041483   73 QAEQLLRNAQIQADQLRADAERelRDARAQTQRILQEhaehqarlqaelhtEAVQRRQQLDQEL-------AERRQTVEs 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    907 QVSEAVLalWlptdsATVLRKMKEIQAiaARLpnVDSVLSQTKQDIARAR------------RLQAEAEQARSRAHAVEG 974
Cdd:NF041483  146 HVNENVA--W-----AEQLRARTESQA--RRL--LDESRAEAEQALAAARaeaerlaeearqRLGSEAESARAEAEAILR 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    975 QV-DDVVGNLRQGTVALQEAqdtmqgTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQE--EQA 1051
Cdd:NF041483  215 RArKDAERLLNAASTQAQEA------TDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKvvAEA 288

                         250       260
                  ....*....|....*....|....*....
gi 1151215   1052 QAMQARQL--AEGASQQAM-NAQEGFKRL 1077
Cdd:NF041483  289 KEAAAKQLasAESANEQRTrTAKEEIARL 317
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 828-1078 2.33e-04

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: 44.20  E-value: 2.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215      828 AGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRtrllIQQVRGfltdpdtdaaTIQQ 907
Cdd:smart00283   13 AEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITA----MDQIRE----------VVEE 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215      908 VSEAVLALwlptdsatvLRKMKEIQAIAArlpNVDSVLSQTkqDI---------ARA--------------RRL----QA 960
Cdd:smart00283   79 AVSAVEEL---------EESSDEIGEIVS---VIDDIADQT--NLlalnaaieaARAgeagrgfavvadevRKLaersAE 144

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215      961 EAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLvpaERLVKGMKEQMSG---FWA 1037
Cdd:smart00283  145 SAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLV---QEIAAATDEQAAGseeVNA 221

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 1151215     1038 RMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLK 1078
Cdd:smart00283  222 AIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
growth_prot_Scy NF041483
polarized growth protein Scy;
832-1065 5.14e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.43  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    832 AEQLRNFNT-QLQQTR-----------QMIRAAEEAASRVQADAQRLETQVSTS---RLLMEEDV--QRTRLLIQQVRGF 894
Cdd:NF041483  238 AEQLRSSTAaESDQARrqaaelsraaeQRMQEAEEALREARAEAEKVVAEAKEAaakQLASAESAneQRTRTAKEEIARL 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    895 LTDPDTDAATIQQVSEAVLA------------------LWLPTDSATVLRKmkeiqaiAARlpNVDSVLSQTKQDiARAR 956
Cdd:NF041483  318 VGEATKEAEALKAEAEQALAdaraeaeklvaeaaekarTVAAEDTAAQLAK-------AAR--TAEEVLTKASED-AKAT 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    957 -----------RLQAEAEQARSRAHAVE------GQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRliQERVGE------ 1013
Cdd:NF041483  388 traaaeeaeriRREAEAEADRLRGEAADqaeqlkGAAKDDTKEYRAKTVELQEEARRLRGEAEQLR--AEAVAEgerirg 465

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151215   1014 ------VQQV---LVPAERLVKGMK----EQMSGFWA-----------RMKELRRQAQE--EQAQAMQARQLAEGASQ 1065
Cdd:NF041483  466 earreaVQQIeeaARTAEELLTKAKadadELRSTATAeservrteaieRATTLRRQAEEtlERTRAEAERLRAEAEEQ 543
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
259-299 6.02e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.83  E-value: 6.02e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1151215      259 CAPNPGGSTTAV--RVNNVCVCQHNTAAPNCDRCAPFYNNRPW 299
Cdd:smart00180    1 CDCDPGGSASGTcdPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
growth_prot_Scy NF041483
polarized growth protein Scy;
828-1088 2.63e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    828 AGRVAEQLRNFNTQLQ-QTRQMI----RAAEEAASRVQADAQ----RLETQVSTSRLLMEEDVQRTRLLIQQvrgfltdp 898
Cdd:NF041483  773 AEQTAQQVRDSVAGLQeQAEEEIaglrSAAEHAAERTRTEAQeeadRVRSDAYAERERASEDANRLRREAQE-------- 844

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    899 DTDAATI---QQVSEAVlalwlptDSATVLRKMKEIQAIAARLPNVDSvLSQTKQDIARARrlqAEA-EQA-RSRAHAVe 973
Cdd:NF041483  845 ETEAAKAlaeRTVSEAI-------AEAERLRSDASEYAQRVRTEASDT-LASAEQDAARTR---ADArEDAnRIRSDAA- 912

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    974 GQVDDVVGNLRQGTVALQEAqdtmqGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARmkeLRRQAQEEQAQA 1053
Cdd:NF041483  913 AQADRLIGEATSEAERLTAE-----ARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAER---LRAEAAETVGSA 984

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1151215   1054 MQA--RQLAEGASQQAMNAQEGfKRLKPKYTELKDRL 1088
Cdd:NF041483  985 QQHaeRIRTEAERVKAEAAAEA-ERLRTEAREEADRT 1020
growth_prot_Scy NF041483
polarized growth protein Scy;
827-1110 2.84e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    827 MAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRL--ETQVSTSRLLMEEdVQRTRLLIQQVRG----FLTDPDT 900
Cdd:NF041483  566 IAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIrrEAAEETERLRTEA-AERIRTLQAQAEQeaerLRTEAAA 644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    901 DAATIQQVSEAVlALWLPTDSATVLRKMK------------EIQAIAARLPN-VDSVLSQTKQDIARARR--------LQ 959
Cdd:NF041483  645 DASAARAEGENV-AVRLRSEAAAEAERLKseaqesadrvraEAAAAAERVGTeAAEALAAAQEEAARRRReaeetlgsAR 723

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    960 AEAEQARSRAHAvegQVDDVVGNLRQgtvALQEAQDTMQgtgrslRLIQERVGEVQQVLVPAERLVKGMKEQMSGfwarm 1039
Cdd:NF041483  724 AEADQERERARE---QSEELLASARK---RVEEAQAEAQ------RLVEEADRRATELVSAAEQTAQQVRDSVAG----- 786

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151215   1040 keLRRQAQEEQAqamQARQLAEGASQQA-MNAQEGFKRLKPKYTELKDRlgqspvLGEQGNRILSIKMEAEE 1110
Cdd:NF041483  787 --LQEQAEEEIA---GLRSAAEHAAERTrTEAQEEADRVRSDAYAERER------ASEDANRLRREAQEETE 847
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 313-367 5.83e-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: 35.79  E-value: 5.83e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1151215     313 CDCNGH---SLTCHFdpavfaasqgtNGGVCDnCRDHTEGKNCEPCQLHYFWNRRPSA 367
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPP 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 312-362 6.93e-03

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: 35.79  E-value: 6.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1151215   312 RCDCNGH---SLTCHFDpavfaasqgtnGGVCDnCRDHTEGKNCEPCQLHYFWN 362
Cdd:cd00055    1 PCDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
growth_prot_Scy NF041483
polarized growth protein Scy;
828-1077 7.07e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.58  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    828 AGRVAEQLRNFNTQLQQTRQMIRA--AEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQVRGfltdpDTDAATI 905
Cdd:NF041483  933 ARAEAERLRDEARAEAERVRADAAaqAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKA-----EAAAEAE 1007

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    906 QQVSEAvlalwlptdSATVLRKMKEIQAIAA--RLPNVDSVLSQTKQDIARARRLQAEA-EQARSRAHAVEGQVDDVVGN 982
Cdd:NF041483 1008 RLRTEA---------REEADRTLDEARKDANkrRSEAAEQADTLITEAAAEADQLTAKAqEEALRTTTEAEAQADTMVGA 1078

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    983 LRQGTVALqEAQDTMQGTGrslrLIQERVGEVQQVLVPAERLVKGMKEQMSGFWAR----MKELRRQAQEEQAQAMQAR- 1057
Cdd:NF041483 1079 ARKEAERI-VAEATVEGNS----LVEKARTDADELLVGARRDATAIRERAEELRDRitgeIEELHERARRESAEQMKSAg 1153

                         250       260
                  ....*....|....*....|....
gi 1151215   1058 ----QLAEGASQQAMNAQEGFKRL 1077
Cdd:NF041483 1154 ercdALVKAAEEQLAEAEAKAKEL 1177
 
Name Accession Description Interval E-value
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 20-248 5.36e-69

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: 231.10  E-value: 5.36e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215       20 ACSRGACYPPVGDLFIGRTqlLRASSTCGLTKPETYCTQ--YGQWQMKCCKCDSRLPrnYNSHRVENVASSSGP--MRWW 95
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGRE--VTATSTCGEPGPERYCKLvgHTEQGKKCDYCDARNP--RRSHPAENLTDGNNPnnPTWW 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215       96 QSQNDVSP---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSsDFGKTWRVYQYLATDCASTFPQVHQG--QPKNWQD 170
Cdd:smart00136   77 QSEPLSNGpqnVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGpiTKGNEDE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215      171 VRCRPLSQRPNGhLTGGKVQLNLMDL-ASAIPASQSKKIQELGDITNLRVNFTKLAPVPQRG-----SYPPSAYFAVSQL 244
Cdd:smart00136  156 VICTSEYSDIVP-LEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELmddrpEVTRRYYYAISDI 234


                    ....
gi 1151215      245 RLQG 248
Cdd:smart00136  235 AVGG 238
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
26-248 1.69e-55

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 192.41  E-value: 1.69e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215      26 CYPPVGDLFIGRTqlLRASSTCGLTKPETYCTQ-YGQWQMKCCKCDSRLPrnYNSHRVENVASSSG--PMRWWQSQNDVS 102
Cdd:pfam00055    1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCILsGLEGGKKCFICDSRDP--HNSHPPSNLTDSNNgtNETWWQSETGVI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     103 P---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSSDFGKTWRVYQYLATDCASTFPQVHQGQPKNW-QDVRCrplSQ 178
Cdd:pfam00055   77 QyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKdDEVIC---TS 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151215     179 RPNG--HLTGGKVQLNLMDLASAIP-ASQSKKIQELGDITNLRVNFTKLA-PVPQRGSYP---PSAYFAVSQLRLQG 248
Cdd:pfam00055  154 EYSDisPLTGGEVIFSTLEGRPSANiFDYSPELQDWLTATNIRIRLLRLHtLGDELLDDPsvlRKYYYAISDISVGG 230
cc_LAMB3_C cd22303
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ...
 1098-1168 1.83e-23

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: 94.82  E-value: 1.83e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151215  1098 GNRILSIKMEAEELFGESMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATCK 1168
Cdd:cd22303    1 GERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 376-425 4.69e-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: 4.69e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1151215     376 CECDPDGAVqGAPCDRLTGQCVCKEYVQGERCDLCKPGFTGLTFDNPKGC 425
Cdd:pfam00053    1 CDCNPHGSL-SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 530-579 6.53e-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: 61.22  E-value: 6.53e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1151215   530 ACDCDFRGTEGPACDKASGRCLCRPGFTGPRCDQCQRGHCDRYPVCVACH 579
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
531-568 8.43e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.79  E-value: 8.43e-12
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1151215      531 CDCDFRGTEGPACDKASGRCLCRPGFTGPRCDQCQRGH 568
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
cc_LAMB_C cd22295
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ...
 1100-1167 8.43e-12

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: 61.53  E-value: 8.43e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151215  1100 RILSIKMEAEELFGESMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATC 1167
Cdd:cd22295    3 RAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 531-568 1.98e-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: 60.06  E-value: 1.98e-11
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1151215     531 CDCDFRGTEGPACDKASGRCLCRPGFTGPRCDQCQRGH 568
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 375-426 2.97e-11

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 59.29  E-value: 2.97e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1151215   375 PCECDPDGAVQGApCDRLTGQCVCKEYVQGERCDLCKPGFTGLTfDNPKGCH 426
Cdd:cd00055    1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
376-425 4.44e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 58.86  E-value: 4.44e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1151215      376 CECDPDGAVQGApCDRLTGQCVCKEYVQGERCDLCKPGFTGltfDNPKGC 425
Cdd:smart00180    1 CDCDPGGSASGT-CDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 427-476 1.04e-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: 55.05  E-value: 1.04e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1151215   427 ACDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKLAS-GLGCE 476
Cdd:cd00055    1 PCDCNGHGSL-SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 428-475 1.07e-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: 55.05  E-value: 1.07e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1151215     428 CDCSILGARKDmPCEEETGRCLCLPNVVGPKCDQCAPSHWKLASGLGC 475
Cdd:pfam00053    1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
478-528 1.86e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 54.24  E-value: 1.86e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1151215      478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVPTGC 528
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCD-----RCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 478-531 4.17e-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: 53.13  E-value: 4.17e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1151215     478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVPTGCRAC 531
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCD-----RCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
428-475 4.86e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.08  E-value: 4.86e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1151215      428 CDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKlASGLGC 475
Cdd:smart00180    1 CDCDPGGSA-SGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 829-1161 1.61e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.30  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     829 GRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQV---STSRLLMEEDVQRTRLLIQQVRGFLTDPDTDAATI 905
Cdd:TIGR02168  659 GVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     906 QQVSEAVLAlwlptdsatvlrkmkEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAE-----------QARSRAHAVEG 974
Cdd:TIGR02168  739 EAEVEQLEE---------------RIAQLSKELTELEAEIEELEERLEEAEEELAEAEaeieeleaqieQLKEELKALRE 803

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     975 QVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQ---AQEEQA 1051
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleaLLNERA 883

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    1052 QAMQARQLAEGASQQAM----NAQEGFKRLKPKYTELKDRLGQSpvlgeqGNRILSIKMEAEELFgesmemmdkmkdmes 1127
Cdd:TIGR02168  884 SLEEALALLRSELEELSeelrELESKRSELRRELEELREKLAQL------ELRLEGLEVRIDNLQ--------------- 942

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1151215    1128 ELLRGSQAIML---------RSADLSGLEKRVEQIRSYIN--GRV 1161
Cdd:TIGR02168  943 ERLSEEYSLTLeeaealenkIEDDEEEARRRLKRLENKIKelGPV 987
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 477-529 2.24e-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: 51.20  E-value: 2.24e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 1151215   477 PCACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGH--VPTGCR 529
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCD-----RCAPGYYGLpsQGGGCQ 50
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 834-1078 2.35e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   834 QLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLlmeeDVQRTRLLIQQVRgfltdpdtdaATIQQVSEAVL 913
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQ----------AEEYELLAELA 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   914 ALwlptdSATVLRKMKEIQAIAARLpnvDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEA 993
Cdd:COG1196  299 RL-----EQDIARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   994 QDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEG 1073
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450


                 ....*
gi 1151215  1074 FKRLK 1078
Cdd:COG1196  451 EAELE 455
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 830-1090 3.69e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 3.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrllMEEDVQRTRLLIQQVRGFLTDPDTDAATIQQVS 909
Cdd:COG1196  257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR----LEQDIARLEERRRELEERLEELEEELAELEEEL 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   910 EAvlalwlptDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVA 989
Cdd:COG1196  333 EE--------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   990 LQEAQDTMQgtGRSLRLIQERvGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMN 1069
Cdd:COG1196  405 LEEAEEALL--ERLERLEEEL-EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481

                        250       260
                 ....*....|....*....|.
gi 1151215  1070 AQEGFKRLKPKYTELKDRLGQ 1090
Cdd:COG1196  482 LLEELAEAAARLLLLLEAEAD 502
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 828-1081 1.06e-07

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: 55.54  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   828 AGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrlLMEEDVQRTRLLIQQVRgfltdpdtdAATIQQ 907
Cdd:COG4942   50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAELEAQKEELAELLR---------ALYRLG 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   908 VSEAVLALWLPTDSATVLRKMKEIQAIAarlPNVDSVLSQTKQDIARARRLQAEAEQARSRahavegqvddvvgnLRQGT 987
Cdd:COG4942  118 RQPPLALLLSPEDFLDAVRRLQYLKYLA---PARREQAEELRADLAELAALRAELEAERAE--------------LEALL 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   988 VALQEAQDTMQgtgrslRLIQERvgevqqvlvpaERLVKGMKEQMSGFWARMKELRRQAQEEQAQAmqARQLAEGASQQA 1067
Cdd:COG4942  181 AELEEERAALE------ALKAER-----------QKLLARLEKELAELAAELAELQQEAEELEALI--ARLEAEAAAAAE 241

                        250
                 ....*....|....
gi 1151215  1068 MNAQEGFKRLKPKY 1081
Cdd:COG4942  242 RTPAAGFAALKGKL 255
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 249-301 3.00e-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: 3.00e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1151215   249 SCFCHGHADRcapnpggSTTAVRVNNVCVCQHNTAAPNCDRCAPFYNNRPWRP 301
Cdd:cd00055    1 PCDCNGHGSL-------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 831-1071 5.53e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 53.30  E-value: 5.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   831 VAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRllmEEDVQRTRLLIQQVRGfltdpdtdaatiQQVSE 910
Cdd:COG3883   35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGERARA------------LYRSG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   911 AVLALWlptdsaTVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSrahavegQVDDVVGNLRQGTVAL 990
Cdd:COG3883  100 GSVSYL------DVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA-------ELEAKLAELEALKAEL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   991 QEAQDTMQgtgrslRLIQErvgevqqvlvpAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNA 1070
Cdd:COG3883  167 EAAKAELE------AQQAE-----------QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229


                 .
gi 1151215  1071 Q 1071
Cdd:COG3883  230 A 230
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
829-1078 3.76e-06

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 51.17  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   829 GRVAEQLRNFNTQLQQTRQMIR---------------AAEEAASRVQADAQRLEtQVSTSrllMEE---DVQRTRLLIQQ 890
Cdd:COG0840  238 GQLADAFNRMIENLRELVGQVResaeqvasaseelaaSAEELAAGAEEQAASLE-ETAAA---MEElsaTVQEVAENAQQ 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   891 VRGFLTDPDTDAATIQQVSEAVLALW--LPTDSATVLRKMKEIQAIAArlpNVDSVLSqTKQDI---------------A 953
Cdd:COG0840  314 AAELAEEASELAEEGGEVVEEAVEGIeeIRESVEETAETIEELGESSQ---EIGEIVD-VIDDIaeqtnllalnaaieaA 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   954 RA--------------RRLqAE-----AEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEV 1014
Cdd:COG0840  390 RAgeagrgfavvadevRKL-AErsaeaTKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEV 468

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151215  1015 ----QQVLVPAERLVKGMkEQMSgfwARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLK 1078
Cdd:COG0840  469 sdliQEIAAASEEQSAGT-EEVN---QAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFK 532
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
834-1066 4.40e-06

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 50.42  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   834 QLRNFNTQLQQTRQMIRAAEEAASRVQadaQRLETQVSTsrllmEEDVQRTRLLIQQVRGFLTDpdtdAATIQQVSEAVL 913
Cdd:COG1538   84 DLLAAQEQLALAEENLALAEELLELAR---ARYEAGLAS-----RLDVLQAEAQLAQARAQLAQ----AEAQLAQARNAL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   914 ALWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQ---DIARARrlqAEAEQARSRAHAVEGQ----VDDVVGNLRQG 986
Cdd:COG1538  152 ALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALErrpDLRAAE---AQLEAAEAEIGVARAAflpsLSLSASYGYSS 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   987 TVALQEAQDTMQGTGRSLRL-----------IQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQ 1055
Cdd:COG1538  229 SDDLFSGGSDTWSVGLSLSLplfdggrnrarVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEA 308

                        250
                 ....*....|.
gi 1151215  1056 ARQLAEGASQQ 1066
Cdd:COG1538  309 AEEALELARAR 319
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
846-1087 6.66e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 6.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   846 RQMI---RAAEEAASRVQADAQRLETqvstsrllMEEDVQRTRlliQQVRgFLTDpdtdaatIQQVSEAVLALWlptDSA 922
Cdd:COG4913  214 REYMleePDTFEAADALVEHFDDLER--------AHEALEDAR---EQIE-LLEP-------IRELAERYAAAR---ERL 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   923 TVLRKMKE---IQAIAARLPNVDSVLSQTKQDIARarrLQAEAEQARSRAHAVEGQVDDVVGNLRQ-GTVALQEAQDTMQ 998
Cdd:COG4913  272 AELEYLRAalrLWFAQRRLELLEAELEELRAELAR---LEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIE 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   999 GTGRSLRLIQERVGEVQQVL------VPAERlvkgmkeqmSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQE 1072
Cdd:COG4913  349 RLERELEERERRRARLEALLaalglpLPASA---------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419

                        250
                 ....*....|....*
gi 1151215  1073 GFKRLKPKYTELKDR 1087
Cdd:COG4913  420 ELRELEAEIASLERR 434
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
929-1111 8.59e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 8.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   929 KEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQ 1008
Cdd:COG4372   21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215  1009 ERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQE-EQAQAMQARQLAEgASQQAMNAQEGFKRLKPKYTELKDR 1087
Cdd:COG4372  101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAElQSEIAEREEELKE-LEEQLESLQEELAALEQELQALSEA 179

                        170       180
                 ....*....|....*....|....*.
gi 1151215  1088 LGQSPV--LGEQGNRILSIKMEAEEL 1111
Cdd:COG4372  180 EAEQALdeLLKEANRNAEKEEELAEA 205
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 929-1091 1.64e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   929 KEIQAIAARLpnvDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDdvvgNLRQgtvALQEAQDTMQGTGRSLRLIQ 1008
Cdd:COG1196  225 LEAELLLLKL---RELEAELEELEAELEELEAELEELEAELAELEAELE----ELRL---ELEELELELEEAQAEEYELL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215  1009 ERVGEVQQVLVPAErlvkgmkeqmsgfwARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKPKYTELKDRL 1088
Cdd:COG1196  295 AELARLEQDIARLE--------------ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360


                 ...
gi 1151215  1089 GQS 1091
Cdd:COG1196  361 AEA 363
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 250-304 2.33e-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: 42.73  E-value: 2.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1151215     250 CFCHGHA---DRCAPNPGgsttavrvnnVCVCQHNTAAPNCDRCAPFYNNRPWRPAEG 304
Cdd:pfam00053    1 CDCNPHGslsDTCDPETG----------QCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 829-1073 2.85e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.97  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     829 GRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrllMEEDVQRTRLLIQQVRGFLTD----------- 897
Cdd:pfam07888   34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE----LESRVAELKEELRQSREKHEEleekykelsas 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     898 -----PDTDAATIQQVSEAVLALWLPTDSATVLRKMKEIQAIAARLPN-VDSVLSQTKQDIARARRLQAEAEQARSRAHA 971
Cdd:pfam07888  110 seelsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKErAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     972 VEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGE----------VQQVLVPAERLVKGMKEQMSGfwarMKE 1041
Cdd:pfam07888  190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEnealleelrsLQERLNASERKVEGLGEELSS----MAA 265

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1151215    1042 LRRQAQEEQAQA-MQARQLAEGASQQAMNAQEG 1073
Cdd:pfam07888  266 QRDRTQAELHQArLQAAQLTLQLADASLALREG 298
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 929-1088 3.46e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   929 KEIQAIAARLPNVDSVLSQTKQDIARAR----RLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSL 1004
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELEleleEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215  1005 RLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKPKYTEL 1084
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412


                 ....
gi 1151215  1085 KDRL 1088
Cdd:COG1196  413 LERL 416
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
842-1111 3.50e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.11  E-value: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSR---LLMEEDVQRTRLLIQQVRGFLTDPDTDaatIQQVSEAVLALWLP 918
Cdd:PRK02224  330 LEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEIEELEEE---IEELRERFGDAPVD 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    919 TDSATVLRKM--KEIQAIAARLPNVDSVLSQTKQDIARARRLQA-----EAEQARSRAHAVEGQVDD--VVGNLRQGTVA 989
Cdd:PRK02224  407 LGNAEDFLEElrEERDELREREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVETIEEDreRVEELEAELED 486

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    990 LQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWA---RMKELRRQAQEEQAQAMQARQLAEGASQQ 1066
Cdd:PRK02224  487 LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEE 566

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1151215   1067 AMNAQEGFKRLKPKYTELKDRLgqspvlgEQGNRILSIKMEAEEL 1111
Cdd:PRK02224  567 AEEAREEVAELNSKLAELKERI-------ESLERIRTLLAAIADA 604
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 830-1161 6.32e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 6.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLEtqvstSRLLMEEDVQRTRLLIQQ--VRGFLTDPDTDAATIQQ 907
Cdd:COG1196  464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA-----DYEGFLEGVKAALLLAGLrgLAGAVAVLIGVEAAYEA 538

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   908 VSEAVLALWLPTDSATVLRKMKE-IQAIAARLPNVDSVLSQTKqdiARARRLQAEAEQARSRAHAVEGQVDD-------- 978
Cdd:COG1196  539 ALEAALAAALQNIVVEDDEVAAAaIEYLKAAKAGRATFLPLDK---IRARAALAAALARGAIGAAVDLVASDlreadary 615

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   979 -VVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQmsgfwARMKELRRQAQEEQAQAMQAR 1057
Cdd:COG1196  616 yVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE-----LLAALLEAEAELEELAERLAE 690

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215  1058 QLAEGASQQAMNAQEGFKRLKPKYTELKDRLGQSpVLGEQGNRILSIKMEAEELFGEsmemmdkmkdmesELLRGSQAIM 1137
Cdd:COG1196  691 EELELEEALLAEEEEERELAEAEEERLEEELEEE-ALEEQLEAEREELLEELLEEEE-------------LLEEEALEEL 756

                        330       340
                 ....*....|....*....|....*.
gi 1151215  1138 LRSADLSGLEKRVEQIRSYIN--GRV 1161
Cdd:COG1196  757 PEPPDLEELERELERLEREIEalGPV 782
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
827-1090 7.48e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 7.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   827 MAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQAdaqrletqvstsrllmeEDVQRTRLLIQQVRGflTDPDTDAATIQ 906
Cdd:COG3206   95 VLERVVDKLNLDEDPLGEEASREAAIERLRKNLTV-----------------EPVKGSNVIEISYTS--PDPELAAAVAN 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   907 QVSEAVLAlwlptdsATVLRKMKEIQAIAARLpnvDSVLSQTKQDIARARRlQAEAEQARSRAHAVEGQVDDVVGNLRQG 986
Cdd:COG3206  156 ALAEAYLE-------QNLELRREEARKALEFL---EEQLPELRKELEEAEA-ALEEFRQKNGLVDLSEEAKLLLQQLSEL 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   987 TVALQEAQDTMQGTGRSLRLIQERVGEVQQVL--VPAERLVKGMKEQMSGFWARMKELRRQAQEE--QAQAMQArQLAEG 1062
Cdd:COG3206  225 ESQLAEARAELAEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNhpDVIALRA-QIAAL 303

                        250       260
                 ....*....|....*....|....*...
gi 1151215  1063 ASQQAMNAQEGFKRLKPKYTELKDRLGQ 1090
Cdd:COG3206  304 RAQLQQEAQRILASLEAELEALQAREAS 331
growth_prot_Scy NF041483
polarized growth protein Scy;
844-1077 7.60e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.13  E-value: 7.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    844 QTRQMIRAAEEAASRVQADAQR--LETQVSTSRLLME--------------EDVQRTRLLIQQVrgfltdpDTDAATIQ- 906
Cdd:NF041483   73 QAEQLLRNAQIQADQLRADAERelRDARAQTQRILQEhaehqarlqaelhtEAVQRRQQLDQEL-------AERRQTVEs 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    907 QVSEAVLalWlptdsATVLRKMKEIQAiaARLpnVDSVLSQTKQDIARAR------------RLQAEAEQARSRAHAVEG 974
Cdd:NF041483  146 HVNENVA--W-----AEQLRARTESQA--RRL--LDESRAEAEQALAAARaeaerlaeearqRLGSEAESARAEAEAILR 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    975 QV-DDVVGNLRQGTVALQEAqdtmqgTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQE--EQA 1051
Cdd:NF041483  215 RArKDAERLLNAASTQAQEA------TDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKvvAEA 288

                         250       260
                  ....*....|....*....|....*....
gi 1151215   1052 QAMQARQL--AEGASQQAM-NAQEGFKRL 1077
Cdd:NF041483  289 KEAAAKQLasAESANEQRTrTAKEEIARL 317
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
936-1104 8.47e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 46.19  E-value: 8.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   936 ARLpnvDSVLSQTKQDIARARRLQAEAEQARSRA-HAVEGQVDDVVGNLRQGTVALQEAQDTMQgtgRSLRLIQERVgev 1014
Cdd:COG1566   74 ARL---DPTDLQAALAQAEAQLAAAEAQLARLEAeLGAEAEIAAAEAQLAAAQAQLDLAQRELE---RYQALYKKGA--- 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215  1015 qqvlVPAERLvkgmkEQMSgfwARMKELRRQAQEEQAQAMQARQLAEGASQQAmNAQEGFKRLKPKYTELKDRLGQ---- 1090
Cdd:COG1566  145 ----VSQQEL-----DEAR---AALDAAQAQLEAAQAQLAQAQAGLREEEELA-AAQAQVAQAEAALAQAELNLARttir 211

                        170
                 ....*....|....
gi 1151215  1091 SPVLGEQGNRILSI 1104
Cdd:COG1566  212 APVDGVVTNLNVEP 225
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
832-1076 9.36e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 9.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   832 AEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQvstsrllmeedvqrtRLLIQQVRGFLtdpdtdaatiqqvsea 911
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER---------------REALQRLAEYS---------------- 657

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   912 vlalWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQ 991
Cdd:COG4913  658 ----WDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   992 EAQDTMQGTGRSLR--LIQERVGEVQQvlvpaerlvkgmkeqmsgfWARMKELRRQAQEEQAqamQARQLAEGASQQAMN 1069
Cdd:COG4913  734 DRLEAAEDLARLELraLLEERFAAALG-------------------DAVERELRENLEERID---ALRARLNRAEEELER 791


                 ....*..
gi 1151215  1070 AQEGFKR 1076
Cdd:COG4913  792 AMRAFNR 798
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
832-1071 9.58e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 9.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   832 AEQLRNF-NTQLQQTRQMIRAAEEAASRVQADAQrletQVSTSrllmeedvQRTRLLIQQvrgfLTDPDTDAATIQQVSE 910
Cdd:COG3206  173 ARKALEFlEEQLPELRKELEEAEAALEEFRQKNG----LVDLS--------EEAKLLLQQ----LSELESQLAEARAELA 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   911 AVLALWlptdsATVLRKMKEIQAIAARLPNvDSVLSQTKQDIARARRLQAEAEQARSRAH----AVEGQVDDVVGNLRqg 986
Cdd:COG3206  237 EAEARL-----AALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHpdviALRAQIAALRAQLQ-- 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   987 tvalQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMsgfwARMKELRRQAQ--EEQAQAMQAR--QLAEG 1062
Cdd:COG3206  309 ----QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE----AELRRLEREVEvaRELYESLLQRleEARLA 380


                 ....*....
gi 1151215  1063 ASQQAMNAQ 1071
Cdd:COG3206  381 EALTVGNVR 389
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 843-1072 1.28e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.48  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   843 QQTR-----QMIRAAEEAASRVQAD---AQRLETQVSTSRllMEEDVQRTRLLIQQVRgfLTDPDTDAATIQQVSEAVLA 914
Cdd:COG3096  408 QQTRaiqyqQAVQALEKARALCGLPdltPENAEDYLAAFR--AKEQQATEEVLELEQK--LSVADAARRQFEKAYELVCK 483

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   915 LWLPTDSAT-------VLRKMKEIQAIAARLPNVDSVLSQTKQDIAR---ARRLQAEAEQARSRAHAVEGQVDDVvgnlr 984
Cdd:COG3096  484 IAGEVERSQawqtareLLRRYRSQQALAQRLQQLRAQLAELEQRLRQqqnAERLLEEFCQRIGQQLDAAEELEEL----- 558

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   985 qgtvaLQEAQDTMQGTGRSLRLIQERVGEVQQVLvpaerlvkgmkEQMSgfwARMKELRRQAQEEQAQAMQARQLAEGAS 1064
Cdd:COG3096  559 -----LAELEAQLEELEEQAAEAVEQRSELRQQL-----------EQLR---ARIKELAARAPAWLAAQDALERLREQSG 619


                 ....*...
gi 1151215  1065 QQAMNAQE 1072
Cdd:COG3096  620 EALADSQE 627
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 828-1078 2.33e-04

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: 44.20  E-value: 2.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215      828 AGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRtrllIQQVRGfltdpdtdaaTIQQ 907
Cdd:smart00283   13 AEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITA----MDQIRE----------VVEE 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215      908 VSEAVLALwlptdsatvLRKMKEIQAIAArlpNVDSVLSQTkqDI---------ARA--------------RRL----QA 960
Cdd:smart00283   79 AVSAVEEL---------EESSDEIGEIVS---VIDDIADQT--NLlalnaaieaARAgeagrgfavvadevRKLaersAE 144

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215      961 EAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLvpaERLVKGMKEQMSG---FWA 1037
Cdd:smart00283  145 SAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLV---QEIAAATDEQAAGseeVNA 221

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 1151215     1038 RMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLK 1078
Cdd:smart00283  222 AIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 942-1095 2.45e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 44.72  E-value: 2.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     942 DSVLSQTKQDIARARRLQAEAEQAR-----SRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERV----- 1011
Cdd:pfam00529   52 DPTDYQAALDSAEAQLAKAQAQVARlqaelDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLarrrv 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    1012 -----GEVQQVLVPAERLVKGMKEQMSGFWARMKELrrQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKPKYTELKD 1086
Cdd:pfam00529  132 lapigGISRESLVTAGALVAQAQANLLATVAQLDQI--YVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLER 209


                   ....*....
gi 1151215    1087 RLGQSPVLG 1095
Cdd:pfam00529  210 TEIRAPVDG 218
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
830-1112 3.89e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSrllmEEDVQRTRLLIQQVRgfltdpdtdaATIQQVS 909
Cdd:COG4372   42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL----NEQLQAAQAELAQAQ----------EELESLQ 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   910 EAvlalwlptdsATVLRkmKEIQAIAARLPNVDSVLSQTKQDIArarRLQAEAEQARSRAHAVEGQVDdvvgNLRQGTVA 989
Cdd:COG4372  108 EE----------AEELQ--EELEELQKERQDLEQQRKQLEAQIA---ELQSEIAEREEELKELEEQLE----SLQEELAA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   990 LQEAQDTMqgtgrslrLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAM-------QARQLAEG 1062
Cdd:COG4372  169 LEQELQAL--------SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDsleaklgLALSALLD 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 1151215  1063 ASQQAMNAQEGFKRLKPKYTELKDRLGQSPVLGEQGNRILSIKMEAEELF 1112
Cdd:COG4372  241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 830-1084 4.90e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.40  E-value: 4.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     830 RVAE-QLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVstSRLLMEEDVQ---RTRLLIQQVRGFLTDPDTDAati 905
Cdd:pfam01576  688 RALEqQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQF--ERDLQARDEQgeeKRRQLVKQVRELEAELEDER--- 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     906 QQVSEAVLA----------LWLPTDSAT--------VLRK----MKEIQ-----AIAARlpnvDSVLSQTKQDIARARRL 958
Cdd:pfam01576  763 KQRAQAVAAkkkleldlkeLEAQIDAANkgreeavkQLKKlqaqMKDLQreleeARASR----DEILAQSKESEKKLKNL 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     959 QAE----------AEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQdtmqgtgrslRLIQERVGEVQQVLVPAERLVKGM 1028
Cdd:pfam01576  839 EAEllqlqedlaaSERARRQAQQERDELADEIASGASGKSALQDEK----------RRLEARIAQLEEELEEEQSNTELL 908

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1151215    1029 KEqmsgfwaRMKELRRQAQEEQAQAMQAR---QLAEGASQQaMNAQEgfKRLKPKYTEL 1084
Cdd:pfam01576  909 ND-------RLRKSTLQVEQLTTELAAERstsQKSESARQQ-LERQN--KELKAKLQEM 957
growth_prot_Scy NF041483
polarized growth protein Scy;
832-1065 5.14e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.43  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    832 AEQLRNFNT-QLQQTR-----------QMIRAAEEAASRVQADAQRLETQVSTS---RLLMEEDV--QRTRLLIQQVRGF 894
Cdd:NF041483  238 AEQLRSSTAaESDQARrqaaelsraaeQRMQEAEEALREARAEAEKVVAEAKEAaakQLASAESAneQRTRTAKEEIARL 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    895 LTDPDTDAATIQQVSEAVLA------------------LWLPTDSATVLRKmkeiqaiAARlpNVDSVLSQTKQDiARAR 956
Cdd:NF041483  318 VGEATKEAEALKAEAEQALAdaraeaeklvaeaaekarTVAAEDTAAQLAK-------AAR--TAEEVLTKASED-AKAT 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    957 -----------RLQAEAEQARSRAHAVE------GQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRliQERVGE------ 1013
Cdd:NF041483  388 traaaeeaeriRREAEAEADRLRGEAADqaeqlkGAAKDDTKEYRAKTVELQEEARRLRGEAEQLR--AEAVAEgerirg 465

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151215   1014 ------VQQV---LVPAERLVKGMK----EQMSGFWA-----------RMKELRRQAQE--EQAQAMQARQLAEGASQ 1065
Cdd:NF041483  466 earreaVQQIeeaARTAEELLTKAKadadELRSTATAeservrteaieRATTLRRQAEEtlERTRAEAERLRAEAEEQ 543
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
259-299 6.02e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.83  E-value: 6.02e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1151215      259 CAPNPGGSTTAV--RVNNVCVCQHNTAAPNCDRCAPFYNNRPW 299
Cdd:smart00180    1 CDCDPGGSASGTcdPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 831-1069 6.27e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 6.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     831 VAEQLRNfntQLQQTRQMIraAEEAA------SRVQADAQRLETQVSTsrllMEEDVQ-----------RTRLLIQQVRG 893
Cdd:pfam01576  851 ASERARR---QAQQERDEL--ADEIAsgasgkSALQDEKRRLEARIAQ----LEEELEeeqsntellndRLRKSTLQVEQ 921

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     894 FLTDPDTDAATIQQVSEAvlalwlptdSATVLRKMKEIQAiaaRLPNVDS-VLSQTKQDIARarrLQAEAEQArsrahav 972
Cdd:pfam01576  922 LTTELAAERSTSQKSESA---------RQQLERQNKELKA---KLQEMEGtVKSKFKSSIAA---LEAKIAQL------- 979

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     973 EGQVDdvvgnlrqgtvalQEAQDTmQGTGRSLRLIQERVGEVQqVLVPAERLV-KGMKEQMSGFWARMKELRRQAQ--EE 1049
Cdd:pfam01576  980 EEQLE-------------QESRER-QAANKLVRRTEKKLKEVL-LQVEDERRHaDQYKDQAEKGNSRMKQLKRQLEeaEE 1044

                          250       260
                   ....*....|....*....|....*..
gi 1151215    1050 QAQAMQA------RQLAEGA-SQQAMN 1069
Cdd:pfam01576 1045 EASRANAarrklqRELDDATeSNESMN 1071
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
840-1063 6.88e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 6.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   840 TQLQQTRQMIRAAEEAASRVQADAQRLETqvstsrllMEEDVQRTRLLIQQVRgfltdpdTDAATIQQVSEAvLALWlpt 919
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEELEE--------LEEELEELEAELEELR-------EELEKLEKLLQL-LPLY--- 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   920 dsatvlrkmKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDdvvgnlRQGTVALQEAQDTMQG 999
Cdd:COG4717  132 ---------QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE------ELLEQLSLATEEELQD 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151215  1000 TGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWarmKELRRQAQEEQAQAMQARQLAEGA 1063
Cdd:COG4717  197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLE---NELEAAALEERLKEARLLLLIAAA 257
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
817-1158 8.81e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 8.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   817 ALPRAKGAFHMAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrllmEEDVQRTRLLIQQVRGFLT 896
Cdd:COG4717   72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPE 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   897 DPDTDAATIQQVSEAVLAlwLPTDSATVLRKMKEIQAIAARLPNVDSV-LSQTKQDI----ARARRLQAEAEQARSRAHA 971
Cdd:COG4717  147 RLEELEERLEELRELEEE--LEELEAELAELQEELEELLEQLSLATEEeLQDLAEELeelqQRLAELEEELEEAQEELEE 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   972 VEGQVDDVVGNLRQGtvALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQA 1051
Cdd:COG4717  225 LEEELEQLENELEAA--ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215  1052 QAMQARQLAEGASQQAMNAQEGFKRLKPKYTELKDRLGQSPVLGEQGNRILSikmEAEELfgESMEMMDKMKDMESELLR 1131
Cdd:COG4717  303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR---EAEEL--EEELQLEELEQEIAALLA 377

                        330       340
                 ....*....|....*....|....*..
gi 1151215  1132 GSQAimlrsADLSGLEKRVEQIRSYIN 1158
Cdd:COG4717  378 EAGV-----EDEEELRAALEQAEEYQE 399
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
828-969 1.11e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   828 AGRVAEQLRNFNTQLQQTRQMIRAAEeaaSRVQADAQRLETQVSTSRLLMEEDVqrtrllIQQVRGFLtdpdtdAATIQQ 907
Cdd:COG3206  214 AKLLLQQLSELESQLAEARAELAEAE---ARLAALRAQLGSGPDALPELLQSPV------IQQLRAQL------AELEAE 278

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151215   908 VSEAvLALWLPtDSATVLRKMKEIQAIAARLPN-VDSVLSQTKQDIARARR----LQAEAEQARSRA 969
Cdd:COG3206  279 LAEL-SARYTP-NHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAreasLQAQLAQLEARL 343
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 842-1150 1.15e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQVRGFL-----------TDPDTDAATIQQVSE 910
Cdd:TIGR02169  693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLssleqeienvkSELKELEARIEELEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     911 AVLALwlptdsatvlrkMKEIQAIAARL-----PNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQ 985
Cdd:TIGR02169  773 DLHKL------------EEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     986 GTVALQEAQDTMQGTGRSLRL----IQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAE 1061
Cdd:TIGR02169  841 QRIDLKEQIKSIEKEIENLNGkkeeLEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    1062 GASQQAMNAQEGFKRLKPKYTELKDRLGQSPVLG---EQGNRIL-------SIKMEAEELFGESMEMMDKMKDMESELLR 1131
Cdd:TIGR02169  921 ELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEdvqAELQRVEeeiralePVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000

                          330
                   ....*....|....*....
gi 1151215    1132 GSQAIMLRSADLSGLEKRV 1150
Cdd:TIGR02169 1001 ERKAILERIEEYEKKKREV 1019
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
830-1090 1.43e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVS--TSRLLMEEDVQRTR------------LLIQQVRGFL 895
Cdd:COG4717  189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKearlllliaaalLALLGLGGSL 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   896 TDPDTDAATIQQVSEAVLAL---WLPTDSATVLRKMKEIQAIAAR-------------------------LPNVDSVLSQ 947
Cdd:COG4717  269 LSLILTIAGVLFLVLGLLALlflLLAREKASLGKEAEELQALPALeeleeeeleellaalglppdlspeeLLELLDRIEE 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   948 TKQDIARARRLQAEAEQARSRAHAVE----GQVDDvVGNLRQGTVALQEAQDTMQgtgrSLRLIQERVGEvqQVLVPAER 1023
Cdd:COG4717  349 LQELLREAEELEEELQLEELEQEIAAllaeAGVED-EEELRAALEQAEEYQELKE----ELEELEEQLEE--LLGELEEL 421

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151215  1024 LVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEgFKRLKPKYTELKDRLGQ 1090
Cdd:COG4717  422 LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-LAELLQELEELKAELRE 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 828-1111 1.45e-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: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   828 AGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLM------------------EEDVQRTRLLIQ 889
Cdd:COG1196  468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrglagavavligveaaYEAALEAALAAA 547

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   890 QVRGFLTDPDTDAATIQQVSEAVL--ALWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAE------ 961
Cdd:COG1196  548 LQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTllgrtl 627

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   962 ----AEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGfwA 1037
Cdd:COG1196  628 vaarLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE--E 705

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151215  1038 RMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKPKYTELKDRLGQSPVLGEQGNRILSIKMEAEEL 1111
Cdd:COG1196  706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
VSP pfam03302
Giardia variant-specific surface protein;
276-581 1.97e-03

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 41.88  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     276 CVCQHNTAAPNCDRCAPfynnrpwrpaegQDTHECQRCDcNGHSLT----CHFDPA----VFAASQGTNGGVCD-----N 342
Cdd:pfam03302   17 CTSSAPCKTENCKACSN------------DKREVCEECN-SNNYLTptsqCIDDCAkignYYYTTNANNKKICKectvaN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     343 CRDHTEGKNCEPCQLHYFWNRRPSAPIHETCIPC---------ECdPDGAVQGAPCDRLTGQC--VCKEYVQGERCDLCk 411
Cdd:pfam03302   84 CKTCEDQGQCQACNDGFYKSGDACSPCHESCKTCsggtasdctEC-LTGKALRYGNDGTKGTCgeGCTTGTGAGACKTC- 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     412 pgftGLTFDNPKGCHACD----------CSILGARKDMPCEEETgrclclpnVVGPKCDQCAPSHWKLASGlgcepCACD 481
Cdd:pfam03302  162 ----GLTIDGTSYCSECAteteypqngvCTSTAARATATCKASS--------VANGMCSSCANGYFRMNGG-----CYET 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215     482 PRNSLSSQCNQFTGQCPCREGFGGLTCSSAAIRQC-PDQTYGHVPTGCRACDCDFRGTEGpACDKASGRCLCRPGFTgPR 560
Cdd:pfam03302  225 TKFPGKSVCEEANSGGTCQKEAPGYKLNNGDLVTCsPGCKTCTSNTVCTTCMDGYVKTSD-SCTKCDSSCETCTGAT-TT 302

                          330       340
                   ....*....|....*....|.
gi 1151215     561 CDQCQRGHCDRYPVCVACHSC 581
Cdd:pfam03302  303 CKTCATGYYKSGTGCVSCTSS 323
growth_prot_Scy NF041483
polarized growth protein Scy;
828-1088 2.63e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    828 AGRVAEQLRNFNTQLQ-QTRQMI----RAAEEAASRVQADAQ----RLETQVSTSRLLMEEDVQRTRLLIQQvrgfltdp 898
Cdd:NF041483  773 AEQTAQQVRDSVAGLQeQAEEEIaglrSAAEHAAERTRTEAQeeadRVRSDAYAERERASEDANRLRREAQE-------- 844

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    899 DTDAATI---QQVSEAVlalwlptDSATVLRKMKEIQAIAARLPNVDSvLSQTKQDIARARrlqAEA-EQA-RSRAHAVe 973
Cdd:NF041483  845 ETEAAKAlaeRTVSEAI-------AEAERLRSDASEYAQRVRTEASDT-LASAEQDAARTR---ADArEDAnRIRSDAA- 912

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    974 GQVDDVVGNLRQGTVALQEAqdtmqGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARmkeLRRQAQEEQAQA 1053
Cdd:NF041483  913 AQADRLIGEATSEAERLTAE-----ARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAER---LRAEAAETVGSA 984

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1151215   1054 MQA--RQLAEGASQQAMNAQEGfKRLKPKYTELKDRL 1088
Cdd:NF041483  985 QQHaeRIRTEAERVKAEAAAEA-ERLRTEAREEADRT 1020
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 852-1087 2.70e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.25  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   852 AEEAASRVQADAQRLETQVStsrllmeeDVQRTrLLIQQVRgfltdpdtdAATIQQVSEAvlalwlptdsatvLRKMKEI 931
Cdd:COG3096  380 AEARLEAAEEEVDSLKSQLA--------DYQQA-LDVQQTR---------AIQYQQAVQA-------------LEKARAL 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   932 QAIAARLP-NVDSVL--SQTKQDIARARRLQAE-----AEQARSRAHAVEGQVDDVVGNLRQGTvALQEAQDTMQgTGRS 1003
Cdd:COG3096  429 CGLPDLTPeNAEDYLaaFRAKEQQATEEVLELEqklsvADAARRQFEKAYELVCKIAGEVERSQ-AWQTARELLR-RYRS 506

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215  1004 LRLIQERVGEVQQVLVPAERLV---KGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEG------- 1073
Cdd:COG3096  507 QQALAQRLQQLRAQLAELEQRLrqqQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQrselrqq 586

                        250
                 ....*....|....
gi 1151215  1074 FKRLKPKYTELKDR 1087
Cdd:COG3096  587 LEQLRARIKELAAR 600
growth_prot_Scy NF041483
polarized growth protein Scy;
827-1110 2.84e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    827 MAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRL--ETQVSTSRLLMEEdVQRTRLLIQQVRG----FLTDPDT 900
Cdd:NF041483  566 IAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIrrEAAEETERLRTEA-AERIRTLQAQAEQeaerLRTEAAA 644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    901 DAATIQQVSEAVlALWLPTDSATVLRKMK------------EIQAIAARLPN-VDSVLSQTKQDIARARR--------LQ 959
Cdd:NF041483  645 DASAARAEGENV-AVRLRSEAAAEAERLKseaqesadrvraEAAAAAERVGTeAAEALAAAQEEAARRRReaeetlgsAR 723

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    960 AEAEQARSRAHAvegQVDDVVGNLRQgtvALQEAQDTMQgtgrslRLIQERVGEVQQVLVPAERLVKGMKEQMSGfwarm 1039
Cdd:NF041483  724 AEADQERERARE---QSEELLASARK---RVEEAQAEAQ------RLVEEADRRATELVSAAEQTAQQVRDSVAG----- 786

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151215   1040 keLRRQAQEEQAqamQARQLAEGASQQA-MNAQEGFKRLKPKYTELKDRlgqspvLGEQGNRILSIKMEAEE 1110
Cdd:NF041483  787 --LQEQAEEEIA---GLRSAAEHAAERTrTEAQEEADRVRSDAYAERER------ASEDANRLRREAQEETE 847
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
952-1155 3.12e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   952 IARARRLQAEAEQARSRAHAVEGQVDdvvgnlrqgtvALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERL--VKGMK 1029
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLE-----------ALEAELDALQERREALQRLAEYSWDEIDVASAEREIaeLEAEL 677

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215  1030 EQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKPKYTELKDRLGQSPVLGEQGNRIlsikmEAE 1109
Cdd:COG4913  678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA-----LLE 752

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 1151215  1110 ELFGEsmemmDKMKDMESELLRG-SQAIMLRSADLSGLEKRVEQIRS 1155
Cdd:COG4913  753 ERFAA-----ALGDAVERELRENlEERIDALRARLNRAEEELERAMR 794
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
830-1105 3.20e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQVRGFLTDPDTDAATIQQVS 909
Cdd:COG4372   77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   910 EAVLALWlptDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQ-AEAEQARSRAHAVEGQVDDVVGNLRQGTV 988
Cdd:COG4372  157 EQLESLQ---EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAeAEKLIESLPRELAEELLEAKDSLEAKLGL 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   989 ALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAM 1068
Cdd:COG4372  234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 1151215  1069 NAQEGFKRLKPKYTELKDRLGQSPVLGEQGNRILSIK 1105
Cdd:COG4372  314 EDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
929-1111 3.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    929 KEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQ 1008
Cdd:PRK03918  200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   1009 ERVGEVQQVLVPAERLVKgMKEQMSGFWARMKELRRQAQ--EEQAQAMQaRQLAEGASQqamnaQEGFKRLKPKYTELKD 1086
Cdd:PRK03918  280 EKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSrlEEEINGIE-ERIKELEEK-----EERLEELKKKLKELEK 352

                         170       180
                  ....*....|....*....|....*
gi 1151215   1087 RLGQSPVLGEQGNRILSIKMEAEEL 1111
Cdd:PRK03918  353 RLEELEERHELYEEAKAKKEELERL 377
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
842-998 5.44e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.81  E-value: 5.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQ-----VRGFLTDpdtdAATIQQVSEAVLALW 916
Cdd:COG1842   32 IRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlAREALER----KAELEAQAEALEAQL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   917 lpTDSATVLRKMKE-IQAIAARLPNVdsvlsQTKQDIARARRLQAEAEQARSRAHAvEGQVDDVVGNLRQgtvaLQEAQD 995
Cdd:COG1842  108 --AQLEEQVEKLKEaLRQLESKLEEL-----KAKKDTLKARAKAAKAQEKVNEALS-GIDSDDATSALER----MEEKIE 175


                 ...
gi 1151215   996 TMQ 998
Cdd:COG1842  176 EME 178
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 313-367 5.83e-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: 35.79  E-value: 5.83e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1151215     313 CDCNGH---SLTCHFdpavfaasqgtNGGVCDnCRDHTEGKNCEPCQLHYFWNRRPSA 367
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPP 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 312-362 6.93e-03

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: 35.79  E-value: 6.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1151215   312 RCDCNGH---SLTCHFDpavfaasqgtnGGVCDnCRDHTEGKNCEPCQLHYFWN 362
Cdd:cd00055    1 PCDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
mukB PRK04863
chromosome partition protein MukB;
830-1111 7.06e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    830 RVAEQLRNFNTQL--QQTR-----QMIRAAEEAASRVQAD---AQRLETQVSTSRLLMEEDVQRTRLLIQQVRgfltdpD 899
Cdd:PRK04863  394 ELKSQLADYQQALdvQQTRaiqyqQAVQALERAKQLCGLPdltADNAEDWLEEFQAKEQEATEELLSLEQKLS------V 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    900 TDAATIQ--QVSEAVLALWLPTDSAT-------VLRKMKEIQAIAARLPNVDSVLSQTKQDIararRLQAEAEQARSRAH 970
Cdd:PRK04863  468 AQAAHSQfeQAYQLVRKIAGEVSRSEawdvareLLRRLREQRHLAEQLQQLRMRLSELEQRL----RQQQRAERLLAEFC 543

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    971 AVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRliqERVGEVQQVLvpaerlvkgmkEQMSgfwARMKELRRQAQE-E 1049
Cdd:PRK04863  544 KRLGKNLDDEDELEQLQEELEARLESLSESVSEAR---ERRMALRQQL-----------EQLQ---ARIQRLAARAPAwL 606

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151215   1050 QAQAMQARqLAE--GA----SQQAMNA-QEGFKRLKpKYTELKDRLGQspvlgeqgnRILSIKMEAEEL 1111
Cdd:PRK04863  607 AAQDALAR-LREqsGEefedSQDVTEYmQQLLERER-ELTVERDELAA---------RKQALDEEIERL 664
growth_prot_Scy NF041483
polarized growth protein Scy;
828-1077 7.07e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.58  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    828 AGRVAEQLRNFNTQLQQTRQMIRA--AEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQVRGfltdpDTDAATI 905
Cdd:NF041483  933 ARAEAERLRDEARAEAERVRADAAaqAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKA-----EAAAEAE 1007

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    906 QQVSEAvlalwlptdSATVLRKMKEIQAIAA--RLPNVDSVLSQTKQDIARARRLQAEA-EQARSRAHAVEGQVDDVVGN 982
Cdd:NF041483 1008 RLRTEA---------REEADRTLDEARKDANkrRSEAAEQADTLITEAAAEADQLTAKAqEEALRTTTEAEAQADTMVGA 1078

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    983 LRQGTVALqEAQDTMQGTGrslrLIQERVGEVQQVLVPAERLVKGMKEQMSGFWAR----MKELRRQAQEEQAQAMQAR- 1057
Cdd:NF041483 1079 ARKEAERI-VAEATVEGNS----LVEKARTDADELLVGARRDATAIRERAEELRDRitgeIEELHERARRESAEQMKSAg 1153

                         250       260
                  ....*....|....*....|....
gi 1151215   1058 ----QLAEGASQQAMNAQEGFKRL 1077
Cdd:NF041483 1154 ercdALVKAAEEQLAEAEAKAKEL 1177
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 842-1065 9.03e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.32  E-value: 9.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSRllmeEDVQRTRLLIQQVRgfLTDPDTDAATIQQVSEAVLALwlptDS 921
Cdd:COG3096  838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLK----EQLQLLNKLLPQAN--LLADETLADRLEELREELDAA----QE 907

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215   922 AtvlrkMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQV---DDVVGNLRQgtVALQEAQDtMQ 998
Cdd:COG3096  908 A-----QAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalSEVVQRRPH--FSYEDAVG-LL 979

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151215   999 GTGRSLrliqerVGEVQQVLVPAERLVKGMKEQMsgfwarmkelrRQAQEEQAQAMQARQLAEGASQ 1065
Cdd:COG3096  980 GENSDL------NEKLRARLEQAEEARREAREQL-----------RQAQAQYSQYNQVLASLKSSRD 1029
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 829-1055 9.45e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 40.17  E-value: 9.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    829 GRVAEQLRNFNTQLQQT----RQMIRAAEEAASRVQADAQRLetqvstSRLLMEEDvqRTRLLIQQV---RGFLTDPDTD 901
Cdd:PRK10246  307 AHTRQQIEEVNTRLQSTmalrARIRHHAAKQSAELQAQQQSL------NTWLAEHD--RFRQWNNELagwRAQFSQQTSD 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151215    902 AATIQQVSEAVLALwlptdsatvlrkmkeIQAIAArLPnvDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVG 981
Cdd:PRK10246  379 REQLRQWQQQLTHA---------------EQKLNA-LP--AITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQK 440

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151215    982 NLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPaerlVKGMKEQMsgfwARMKELrrQAQEEQAQAMQ 1055
Cdd:PRK10246  441 RLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD----VKTICEQE----ARIKDL--EAQRAQLQAGQ 504
 
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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